Year |
Citation |
Score |
2024 |
Chen SW, Barritt JD, Cascella R, Bigi A, Cecchi C, Banchelli M, Gallo A, Jarvis JA, Chiti F, Dobson CM, Fusco G, De Simone A. Structure-Toxicity Relationship in Intermediate Fibrils from α-Synuclein Condensates. Journal of the American Chemical Society. PMID 38567991 DOI: 10.1021/jacs.3c14703 |
0.359 |
|
2023 |
Miller A, Wei J, Meehan S, Dobson CM, Welland ME, Klenerman D, Vendruscolo M, Ruggeri FS, Knowles TPJ. Formation of amyloid loops in brain tissues is controlled by the flexibility of protofibril chains. Proceedings of the National Academy of Sciences of the United States of America. 120: e2216234120. PMID 37186840 DOI: 10.1073/pnas.2216234120 |
0.663 |
|
2022 |
Fusco G, Bemporad F, Chiti F, Dobson CM, De Simone A. The role of structural dynamics in the thermal adaptation of hyperthermophilic enzymes. Frontiers in Molecular Biosciences. 9: 981312. PMID 36158582 DOI: 10.3389/fmolb.2022.981312 |
0.303 |
|
2022 |
Bell R, Thrush RJ, Castellana-Cruz M, Oeller M, Staats R, Nene A, Flagmeier P, Xu CK, Satapathy S, Galvagnion C, Wilson MR, Dobson CM, Kumita JR, Vendruscolo M. N-Terminal Acetylation of α-Synuclein Slows down Its Aggregation Process and Alters the Morphology of the Resulting Aggregates. Biochemistry. PMID 35944093 DOI: 10.1021/acs.biochem.2c00104 |
0.498 |
|
2021 |
Williams DM, Thorn DC, Dobson CM, Meehan S, Jackson SE, Woodcock JM, Carver JA. The Amyloid Fibril-Forming β-Sheet Regions of Amyloid β and α-Synuclein Preferentially Interact with the Molecular Chaperone 14-3-3ζ. Molecules (Basel, Switzerland). 26. PMID 34684701 DOI: 10.3390/molecules26206120 |
0.32 |
|
2021 |
Schneider MM, Gautam S, Herling TW, Andrzejewska E, Krainer G, Miller AM, Trinkaus VA, Peter QAE, Ruggeri FS, Vendruscolo M, Bracher A, Dobson CM, Hartl FU, Knowles TPJ. The Hsc70 disaggregation machinery removes monomer units directly from α-synuclein fibril ends. Nature Communications. 12: 5999. PMID 34650037 DOI: 10.1038/s41467-021-25966-w |
0.525 |
|
2021 |
Scheidt T, Carozza JA, Kolbe CC, Aprile FA, Tkachenko O, Bellaiche MMJ, Meisl G, Peter QAE, Herling TW, Ness S, Castellana-Cruz M, Benesch JLP, Vendruscolo M, Dobson CM, Arosio P, et al. The binding of the small heat-shock protein αB-crystallin to fibrils of α-synuclein is driven by entropic forces. Proceedings of the National Academy of Sciences of the United States of America. 118. PMID 34518228 DOI: 10.1073/pnas.2108790118 |
0.514 |
|
2021 |
Joshi P, Perni M, Limbocker R, Mannini B, Casford S, Chia S, Habchi J, Labbadia J, Dobson CM, Vendruscolo M. Publisher Correction: Two human metabolites rescue a C. elegans model of Alzheimer's disease via a cytosolic unfolded protein response. Communications Biology. 4: 930. PMID 34312490 DOI: 10.1038/s42003-021-02457-8 |
0.431 |
|
2021 |
Nowicka U, Chroscicki P, Stroobants K, Sladowska M, Turek M, Uszczynska-Ratajczak B, Kundra R, Goral T, Perni M, Dobson CM, Vendruscolo M, Chacinska A. Cytosolic aggregation of mitochondrial proteins disrupts cellular homeostasis by stimulating the aggregation of other proteins. Elife. 10. PMID 34292154 DOI: 10.7554/eLife.65484 |
0.48 |
|
2021 |
Perni M, Mannini B, Xu CK, Kumita JR, Dobson CM, Chiti F, Vendruscolo M. Exogenous misfolded protein oligomers can cross the intestinal barrier and cause a disease phenotype in C. elegans. Scientific Reports. 11: 14391. PMID 34257326 DOI: 10.1038/s41598-021-93527-8 |
0.507 |
|
2021 |
Joshi P, Perni M, Limbocker R, Mannini B, Casford S, Chia S, Habchi J, Labbadia J, Dobson CM, Vendruscolo M. Two human metabolites rescue a C. elegans model of Alzheimer's disease via a cytosolic unfolded protein response. Communications Biology. 4: 843. PMID 34234268 DOI: 10.1038/s42003-021-02218-7 |
0.498 |
|
2021 |
Limbocker R, Staats R, Chia S, Ruggeri FS, Mannini B, Xu CK, Perni M, Cascella R, Bigi A, Sasser LR, Block NR, Wright AK, Kreiser RP, Custy ET, Meisl G, ... ... Dobson CM, et al. Squalamine and Its Derivatives Modulate the Aggregation of Amyloid-β and α-Synuclein and Suppress the Toxicity of Their Oligomers. Frontiers in Neuroscience. 15: 680026. PMID 34220435 DOI: 10.3389/fnins.2021.680026 |
0.502 |
|
2021 |
Leal-Lasarte M, Mannini B, Chiti F, Vendruscolo M, Dobson CM, Roodveldt C, Pozo D. Distinct responses of human peripheral blood cells to different misfolded protein oligomers. Immunology. PMID 34043816 DOI: 10.1111/imm.13377 |
0.424 |
|
2021 |
Perni M, van der Goot A, Limbocker R, van Ham TJ, Aprile FA, Xu CK, Flagmeier P, Thijssen K, Sormanni P, Fusco G, Chen SW, Challa PK, Kirkegaard JB, Laine RF, Ma KY, ... ... Dobson CM, et al. Comparative Studies in the A30P and A53T α-Synuclein Strains to Investigate the Molecular Origins of Parkinson's Disease. Frontiers in Cell and Developmental Biology. 9: 552549. PMID 33829010 DOI: 10.3389/fcell.2021.552549 |
0.358 |
|
2021 |
Vettore N, Moray J, Brans A, Herman R, Charlier P, Kumita JR, Kerff F, Dobson CM, Dumoulin M. Characterisation of the structural, dynamic and aggregation properties of the W64R amyloidogenic variant of human lysozyme. Biophysical Chemistry. 271: 106563. PMID 33640796 DOI: 10.1016/j.bpc.2021.106563 |
0.833 |
|
2021 |
Fani G, Mannini B, Vecchi G, Cascella R, Cecchi C, Dobson CM, Vendruscolo M, Chiti F. Aβ Oligomers Dysregulate Calcium Homeostasis by Mechanosensitive Activation of AMPA and NMDA Receptors. Acs Chemical Neuroscience. PMID 33538575 DOI: 10.1021/acschemneuro.0c00811 |
0.385 |
|
2021 |
Cataldi R, Chia S, Pisani K, Ruggeri FS, Xu CK, Šneideris T, Perni M, Sarwat S, Joshi P, Kumita JR, Linse S, Habchi J, Knowles TPJ, Mannini B, Dobson CM, et al. Publisher Correction: A dopamine metabolite stabilizes neurotoxic amyloid-β oligomers. Communications Biology. 4: 154. PMID 33500508 DOI: 10.1038/s42003-021-01680-7 |
0.384 |
|
2021 |
Cataldi R, Chia S, Pisani K, Ruggeri FS, Xu CK, Šneideris T, Perni M, Sarwat S, Joshi P, Kumita JR, Linse S, Habchi J, Knowles TPJ, Mannini B, Dobson CM, et al. A dopamine metabolite stabilizes neurotoxic amyloid-β oligomers. Communications Biology. 4: 19. PMID 33398040 DOI: 10.1038/s42003-020-01490-3 |
0.466 |
|
2021 |
Hardenberg MC, Sinnige T, Casford S, Dada S, Poudel C, Robinson EA, Fuxreiter M, Kaminksi C, Kaminski-Schierle GS, Nollen EAA, Dobson CM, Vendruscolo M. Observation of an α-synuclein liquid droplet state and its maturation into Lewy body-like assemblies. Journal of Molecular Cell Biology. PMID 33386842 DOI: 10.1093/jmcb/mjaa075 |
0.45 |
|
2020 |
Staats R, Michaels TCT, Flagmeier P, Chia S, Horne RI, Habchi J, Linse S, Knowles TPJ, Dobson CM, Vendruscolo M. Screening of small molecules using the inhibition of oligomer formation in α-synuclein aggregation as a selection parameter. Communications Chemistry. 3: 191. PMID 36703335 DOI: 10.1038/s42004-020-00412-y |
0.452 |
|
2020 |
Needham LM, Weber J, Varela JA, Fyfe JWB, Do DT, Xu CK, Tutton L, Cliffe R, Keenlyside B, Klenerman D, Dobson CM, Hunter CA, Müller KH, O'Holleran K, Bohndiek SE, et al. ThX - a next-generation probe for the early detection of amyloid aggregates. Chemical Science. 11: 4578-4583. PMID 34122915 DOI: 10.1039/c9sc04730a |
0.326 |
|
2020 |
Needham LM, Weber J, Varela JA, Fyfe JWB, Do DT, Xu CK, Tutton L, Cliffe R, Keenlyside B, Klenerman D, Dobson CM, Hunter CA, Müller KH, O'Holleran K, Bohndiek SE, et al. ThX - a next-generation probe for the early detection of amyloid aggregates. Chemical Science. 11: 4578-4583. PMID 34122915 DOI: 10.1039/c9sc04730a |
0.326 |
|
2020 |
Camino JD, Gracia P, Chen SW, Sot J, de la Arada I, Sebastián V, Arrondo JLR, Goñi FM, Dobson CM, Cremades N. The extent of protein hydration dictates the preference for heterogeneous or homogeneous nucleation generating either parallel or antiparallel β-sheet α-synuclein aggregates. Chemical Science. 11: 11902-11914. PMID 33520152 DOI: 10.1039/d0sc05297c |
0.319 |
|
2020 |
Lindstedt PR, Aprile FA, Sormanni P, Rakoto R, Dobson CM, Bernardes GJL, Vendruscolo M. Systematic Activity Maturation of a Single-Domain Antibody with Non-canonical Amino Acids through Chemical Mutagenesis. Cell Chemical Biology. PMID 33217338 DOI: 10.1016/j.chembiol.2020.11.002 |
0.412 |
|
2020 |
Sinnige T, Stroobants K, Dobson CM, Vendruscolo M. Biophysical studies of protein misfolding and aggregation in models of Alzheimer's and Parkinson's diseases - ERRATUM. Quarterly Reviews of Biophysics. 53: e13. PMID 33203502 DOI: 10.1017/S0033583520000104 |
0.465 |
|
2020 |
Heller GT, Aprile FA, Michaels TCT, Limbocker R, Perni M, Ruggeri FS, Mannini B, Löhr T, Bonomi M, Camilloni C, De Simone A, Felli IC, Pierattelli R, Knowles TPJ, Dobson CM, et al. Small-molecule sequestration of amyloid-β as a drug discovery strategy for Alzheimer's disease. Science Advances. 6. PMID 33148639 DOI: 10.1126/sciadv.abb5924 |
0.695 |
|
2020 |
Arter WE, Xu CK, Castellana-Cruz M, Herling TW, Krainer G, Saar KL, Kumita JR, Dobson CM, Knowles TPJ. Rapid Structural, Kinetic, and Immunochemical Analysis of Alpha-Synuclein Oligomers in Solution. Nano Letters. PMID 33079553 DOI: 10.1021/acs.nanolett.0c03260 |
0.32 |
|
2020 |
Linse S, Scheidt T, Bernfur K, Vendruscolo M, Dobson CM, Cohen SIA, Sileikis E, Lundqvist M, Qian F, O'Malley T, Bussiere T, Weinreb PH, Xu CK, Meisl G, Devenish SRA, et al. Kinetic fingerprints differentiate the mechanisms of action of anti-Aβ antibodies. Nature Structural & Molecular Biology. PMID 32989305 DOI: 10.1038/s41594-020-0505-6 |
0.446 |
|
2020 |
Ikenoue T, Aprile FA, Sormanni P, Ruggeri FS, Perni M, Heller GT, Haas CP, Middel C, Limbocker R, Mannini B, Michaels TCT, Knowles TPJ, Dobson CM, Vendruscolo M. A rationally designed bicyclic peptide remodels Aβ42 aggregation in vitro and reduces its toxicity in a worm model of Alzheimer's disease. Scientific Reports. 10: 15280. PMID 32943652 DOI: 10.1038/S41598-020-69626-3 |
0.548 |
|
2020 |
Michaels TCT, Šarić A, Meisl G, Heller GT, Curk S, Arosio P, Linse S, Dobson CM, Vendruscolo M, Knowles TPJ. Thermodynamic and kinetic design principles for amyloid-aggregation inhibitors. Proceedings of the National Academy of Sciences of the United States of America. 117: 24251-24257. PMID 32929030 DOI: 10.1073/Pnas.2006684117 |
0.571 |
|
2020 |
Chrabąszczewska M, Sieradzan AK, Rodziewicz-Motowidło S, Grubb A, Dobson CM, Kumita JR, Kozak M. Structural Characterization of Covalently Stabilized Human Cystatin C Oligomers. International Journal of Molecular Sciences. 21. PMID 32824145 DOI: 10.3390/Ijms21165860 |
0.346 |
|
2020 |
Du Z, Chakrabarti S, Kulaberoglu Y, Smith ESJ, Dobson CM, Itzhaki LS, Kumita JR. Probing the unfolded protein response in long-lived naked mole-rats. Biochemical and Biophysical Research Communications. 529: 1151-1157. PMID 32819579 DOI: 10.1016/J.Bbrc.2020.06.118 |
0.341 |
|
2020 |
Yang J, Dear AJ, Yao QQ, Liu Z, Dobson CM, Knowles TPJ, Wu S, Perrett S. Amelioration of aggregate cytotoxicity by catalytic conversion of protein oligomers into amyloid fibrils. Nanoscale. PMID 32794533 DOI: 10.1039/D0Nr01481H |
0.461 |
|
2020 |
Limbocker R, Mannini B, Ruggeri FS, Cascella R, Xu CK, Perni M, Chia S, Chen SW, Habchi J, Bigi A, Kreiser RP, Wright AK, Albright JA, Kartanas T, Kumita JR, ... ... Dobson CM, et al. Trodusquemine displaces protein misfolded oligomers from cell membranes and abrogates their cytotoxicity through a generic mechanism. Communications Biology. 3: 435. PMID 32792544 DOI: 10.1038/s42003-020-01140-8 |
0.53 |
|
2020 |
Flagmeier P, De S, Michaels TCT, Yang X, Dear AJ, Emanuelsson C, Vendruscolo M, Linse S, Klenerman D, Knowles TPJ, Dobson CM. Direct measurement of lipid membrane disruption connects kinetics and toxicity of Aβ42 aggregation. Nature Structural & Molecular Biology. PMID 32778821 DOI: 10.1038/S41594-020-0471-Z |
0.578 |
|
2020 |
Ke PC, Zhou R, Serpell LC, Riek R, Knowles TPJ, Lashuel HA, Gazit E, Hamley IW, Davis TP, Fändrich M, Otzen DE, Chapman MR, Dobson CM, Eisenberg DS, Mezzenga R. Half a century of amyloids: past, present and future. Chemical Society Reviews. PMID 32632432 DOI: 10.1039/C9Cs00199A |
0.353 |
|
2020 |
Limbocker R, Mannini B, Cataldi R, Chhangur S, Wright AK, Kreiser RP, Albright JA, Chia S, Habchi J, Sormanni P, Kumita JR, Ruggeri FS, Dobson CM, Chiti F, Aprile FA, et al. Rationally Designed Antibodies as Research Tools to Study the Structure-Toxicity Relationship of Amyloid-β Oligomers. International Journal of Molecular Sciences. 21. PMID 32630615 DOI: 10.3390/Ijms21124542 |
0.559 |
|
2020 |
Aprile FA, Sormanni P, Podpolny M, Chhangur S, Needham LM, Ruggeri FS, Perni M, Limbocker R, Heller GT, Sneideris T, Scheidt T, Mannini B, Habchi J, Lee SF, Salinas PC, ... ... Dobson CM, et al. Rational design of a conformation-specific antibody for the quantification of Aβ oligomers. Proceedings of the National Academy of Sciences of the United States of America. PMID 32493749 DOI: 10.1073/Pnas.1919464117 |
0.533 |
|
2020 |
Sinnige T, Stroobants K, Dobson CM, Vendruscolo M. Biophysical studies of protein misfolding and aggregation in models of Alzheimer's and Parkinson's diseases. Quarterly Reviews of Biophysics. 49: e22. PMID 32493529 DOI: 10.1017/S0033583520000025 |
0.563 |
|
2020 |
Koopman M, Peter Q, Seinstra RI, Perni M, Vendruscolo M, Dobson CM, Knowles TPJ, Nollen EAA. Assessing motor-related phenotypes of Caenorhabditis elegans with the wide field-of-view nematode tracking platform. Nature Protocols. PMID 32433626 DOI: 10.1038/S41596-020-0321-9 |
0.434 |
|
2020 |
Dear AJ, Michaels TCT, Meisl G, Klenerman D, Wu S, Perrett S, Linse S, Dobson CM, Knowles TPJ. Kinetic diversity of amyloid oligomers. Proceedings of the National Academy of Sciences of the United States of America. PMID 32414930 DOI: 10.1073/Pnas.1922267117 |
0.435 |
|
2020 |
Michaels TCT, Šarić A, Curk S, Bernfur K, Arosio P, Meisl G, Dear AJ, Cohen SIA, Dobson CM, Vendruscolo M, Linse S, Knowles TPJ. Author Correction: Dynamics of oligomer populations formed during the aggregation of Alzheimer's Aβ42 peptide. Nature Chemistry. PMID 32303714 DOI: 10.1038/S41557-020-0468-6 |
0.507 |
|
2020 |
Michaels TCT, Šarić A, Curk S, Bernfur K, Arosio P, Meisl G, Dear AJ, Cohen SIA, Dobson CM, Vendruscolo M, Linse S, Knowles TPJ. Dynamics of oligomer populations formed during the aggregation of Alzheimer's Aβ42 peptide. Nature Chemistry. PMID 32284577 DOI: 10.1038/S41557-020-0452-1 |
0.573 |
|
2020 |
Ruggeri FS, Flagmeier P, Kumita JR, Meisl G, Chirgadze DY, Bongiovanni MN, Knowles TPJ, Dobson CM. The Influence of Pathogenic Mutations in α-Synuclein on Biophysical and Structural Characteristics of Amyloid Fibrils. Acs Nano. PMID 32159944 DOI: 10.1021/Acsnano.9B09676 |
0.405 |
|
2020 |
Kundra R, Dobson CM, Vendruscolo M. A Cell- and Tissue-Specific Weakness of the Protein Homeostasis System Underlies Brain Vulnerability to Protein Aggregation. Iscience. 23: 100934. PMID 32146327 DOI: 10.1016/J.Isci.2020.100934 |
0.543 |
|
2020 |
Man WK, De Simone A, Barritt JD, Vendruscolo M, Dobson CM, Fusco G. A Role of Cholesterol in Modulating the Binding of α-Synuclein to Synaptic-Like Vesicles. Frontiers in Neuroscience. 14: 18. PMID 32063829 DOI: 10.3389/Fnins.2020.00018 |
0.508 |
|
2020 |
Ghadami SA, Chia S, Ruggeri FS, Meisl G, Bemporad F, Habchi J, Cascella R, Dobson CM, Vendruscolo M, Knowles TPJ, Chiti F. Transthyretin inhibits primary and secondary nucleation of amyloid-β peptide aggregation and reduces the toxicity of its oligomers. Biomacromolecules. PMID 32011129 DOI: 10.1021/Acs.Biomac.9B01475 |
0.559 |
|
2020 |
Runfola M, De Simone A, Vendruscolo M, Dobson CM, Fusco G. The N-terminal Acetylation of α-Synuclein Changes the Affinity for Lipid Membranes but not the Structural Properties of the Bound State. Scientific Reports. 10: 204. PMID 31937832 DOI: 10.1038/S41598-019-57023-4 |
0.519 |
|
2020 |
Needham L, Weber J, Varela JA, Fyfe JWB, Do DT, Xu CK, Tutton L, Cliffe R, Keenlyside B, Klenerman D, Dobson CM, Hunter CA, Müller KH, O'Holleran K, Bohndiek SE, et al. ThX – a next-generation probe for the early detection of amyloid aggregates Chemical Science. 11: 4578-4583. DOI: 10.1039/C9Sc04730A |
0.364 |
|
2020 |
Schneider MM, Scheidt T, Dobson CM, Knowles TP. Microfluidic Diffusional Sizing for Studying Protein-Protein Interactions Biophysical Journal. 118: 512a. DOI: 10.1016/J.Bpj.2019.11.2818 |
0.342 |
|
2020 |
Callaghan KL, Peter Q, Kumita JR, Knowles TP, Dobson CM. Quantifying the Thermodynamic Stability of Amyloid Fibrils Biophysical Journal. 118: 492a. DOI: 10.1016/J.Bpj.2019.11.2725 |
0.359 |
|
2019 |
Vecchi G, Sormanni P, Mannini B, Vandelli A, Tartaglia GG, Dobson CM, Hartl FU, Vendruscolo M. Proteome-wide observation of the phenomenon of life on the edge of solubility. Proceedings of the National Academy of Sciences of the United States of America. PMID 31892536 DOI: 10.1073/Pnas.1910444117 |
0.546 |
|
2019 |
Ciryam P, Antalek M, Cid F, Tartaglia GG, Dobson CM, Guettsches AK, Eggers B, Vorgerd M, Marcus K, Kley RA, Morimoto RI, Vendruscolo M, Weihl CC. A metastable subproteome underlies inclusion formation in muscle proteinopathies. Acta Neuropathologica Communications. 7: 197. PMID 31796104 DOI: 10.1186/S40478-019-0853-9 |
0.566 |
|
2019 |
Galvagnion C, Topgaard D, Makasewicz K, Buell AK, Linse S, Sparr E, Dobson CM. Lipid Dynamics and Phase Transition within α-Synuclein Amyloid Fibrils. The Journal of Physical Chemistry Letters. 7872-7877. PMID 31790267 DOI: 10.1021/Acs.Jpclett.9B03005 |
0.655 |
|
2019 |
Freer R, Sormanni P, Ciryam P, Rammner B, Rizzoli SO, Dobson CM, Vendruscolo M. Supersaturated proteins are enriched at synapses and underlie cell and tissue vulnerability in Alzheimer's disease. Heliyon. 5: e02589. PMID 31768427 DOI: 10.1016/J.Heliyon.2019.E02589 |
0.513 |
|
2019 |
Meisl G, Michaels TCT, Arosio P, Vendruscolo M, Dobson CM, Knowles TPJ. Dynamics and Control of Peptide Self-Assembly and Aggregation. Advances in Experimental Medicine and Biology. 1174: 1-33. PMID 31713195 DOI: 10.1007/978-981-13-9791-2_1 |
0.589 |
|
2019 |
Delivoria DC, Chia S, Habchi J, Perni M, Matis I, Papaevgeniou N, Reczko M, Chondrogianni N, Dobson CM, Vendruscolo M, Skretas G. Bacterial production and direct functional screening of expanded molecular libraries for discovering inhibitors of protein aggregation. Science Advances. 5: eaax5108. PMID 31663025 DOI: 10.1126/Sciadv.Aax5108 |
0.553 |
|
2019 |
Wang X, Kirkpatrick JP, Launay HMM, de Simone A, Häussinger D, Dobson CM, Vendruscolo M, Cabrita LD, Waudby CA, Christodoulou J. Probing the dynamic stalk region of the ribosome using solution NMR. Scientific Reports. 9: 13528. PMID 31537834 DOI: 10.1038/S41598-019-49190-1 |
0.519 |
|
2019 |
Ng JSW, Hanspal MA, Matharu NS, Barros TP, Esbjörner EK, Wilson MR, Yerbury JJ, Dobson CM, Kumita JR. Using Tetracysteine-Tagged TDP-43 with a Biarsenical Dye To Monitor Real-Time Trafficking in a Cell Model of Amyotrophic Lateral Sclerosis. Biochemistry. PMID 31529970 DOI: 10.1021/Acs.Biochem.9B00592 |
0.31 |
|
2019 |
Lindstedt PR, Aprile FA, Matos MJ, Perni M, Bertoldo JB, Bernardim B, Peter Q, Jiménez-Osés G, Knowles TPJ, Dobson CM, Corzana F, Vendruscolo M, Bernardes GJL. Enhancement of the Anti-Aggregation Activity of a Molecular Chaperone Using a Rationally Designed Post-Translational Modification. Acs Central Science. 5: 1417-1424. PMID 31482124 DOI: 10.1021/Acscentsci.9B00467 |
0.568 |
|
2019 |
Agerschou ED, Flagmeier P, Saridaki T, Galvagnion C, Komnig D, Heid L, Prasad V, Shaykhalishahi H, Willbold D, Dobson CM, Voigt A, Falkenbürger B, Hoyer W, Buell AK. An engineered monomer binding-protein for α-synuclein efficiently inhibits the proliferation of amyloid fibrils. Elife. 8. PMID 31389332 DOI: 10.7554/Elife.46112 |
0.644 |
|
2019 |
Mannini B, Vecchi G, Labrador-Garrido A, Fabre B, Fani G, Munoz Franco J, Lilley KS, Pozo D, Vendruscolo M, Chiti F, Dobson CM, Roodveldt C. Differential interactome and innate immune response activation of two structurally distinct misfolded protein oligomers. Acs Chemical Neuroscience. PMID 31313906 DOI: 10.1021/Acschemneuro.9B00088 |
0.534 |
|
2019 |
Waudby CA, Dobson CM, Christodoulou J. Nature and Regulation of Protein Folding on the Ribosome. Trends in Biochemical Sciences. PMID 31301980 DOI: 10.1016/J.Tibs.2019.06.008 |
0.388 |
|
2019 |
Laine RF, Sinnige T, Ma KY, Haack AJ, Poudel C, Gaida P, Curry N, Perni M, Nollen EAA, Dobson CM, Vendruscolo M, Kaminski Schierle GS, Kaminski CF. Fast Fluorescence Lifetime Imaging Reveals the Aggregation Processes of α-Synuclein and Polyglutamine in Aging Caenorhabditis elegans. Acs Chemical Biology. PMID 31246415 DOI: 10.1021/Acschembio.9B00354 |
0.585 |
|
2019 |
Sinnige T, Ciryam P, Casford S, Dobson CM, de Bono M, Vendruscolo M. Expression of the amyloid-β peptide in a single pair of C. elegans sensory neurons modulates the associated behavioural response. Plos One. 14: e0217746. PMID 31150491 DOI: 10.1371/Journal.Pone.0217746 |
0.513 |
|
2019 |
Froula JM, Castellana-Cruz M, Anabtawi NM, Camino JD, Chen SW, Thrasher DR, Freire J, Yazdi AA, Fleming S, Dobson CM, Kumita JR, Cremades N, Volpicelli-Daley LA. Defining α-synuclein species responsible for Parkinson disease phenotypes in mice. The Journal of Biological Chemistry. PMID 31142553 DOI: 10.1074/Jbc.Ra119.007743 |
0.333 |
|
2019 |
Vivoli Vega M, Cascella R, Chen SW, Fusco G, De Simone A, Dobson CM, Cecchi C, Chiti F. The toxicity of misfolded protein oligomers is independent of their secondary structure. Acs Chemical Biology. PMID 31074957 DOI: 10.1021/Acschembio.9B00324 |
0.46 |
|
2019 |
Cascella R, Perni M, Chen SW, Fusco G, Cecchi C, Vendruscolo M, Chiti F, Dobson CM, De Simone A. Probing the origin of the toxicity of oligomeric aggregates of α-synuclein with antibodies. Acs Chemical Biology. PMID 31050886 DOI: 10.1021/Acschembio.9B00312 |
0.542 |
|
2019 |
Scheidt T, Łapińska U, Kumita JR, Whiten DR, Klenerman D, Wilson MR, Cohen SIA, Linse S, Vendruscolo M, Dobson CM, Knowles TPJ, Arosio P. Secondary nucleation and elongation occur at different sites on Alzheimer's amyloid-β aggregates. Science Advances. 5: eaau3112. PMID 31001578 DOI: 10.1126/Sciadv.Aau3112 |
0.576 |
|
2019 |
Ahmed N, Sormanni P, Ciryam P, Vendruscolo M, Dobson CM, O'Brien EP. Identifying A- and P-site locations on ribosome-protected mRNA fragments using Integer Programming. Scientific Reports. 9: 6256. PMID 31000737 DOI: 10.1038/S41598-019-42348-X |
0.429 |
|
2019 |
Dobson CM. Biophysical Techniques in Structural Biology. Annual Review of Biochemistry. PMID 30986087 DOI: 10.1146/Annurev-Biochem-013118-111947 |
0.321 |
|
2019 |
Shimizu M, Kajikawa Y, Kuwajima K, Dobson CM, Okamoto Y. Determination of the Structural Ensemble of the Molten Globule State of a Protein by Computer Simulations. Proteins. PMID 30958596 DOI: 10.1002/Prot.25688 |
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2019 |
Yerbury JJ, Ooi L, Blair IP, Ciryam P, Dobson CM, Vendruscolo M. The metastability of the proteome of spinal motor neurons underlies their selective vulnerability in ALS. Neuroscience Letters. PMID 30953736 DOI: 10.1016/J.Neulet.2019.04.001 |
0.488 |
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2019 |
De S, Wirthensohn DC, Flagmeier P, Hughes C, Aprile FA, Ruggeri FS, Whiten DR, Emin D, Xia Z, Varela JA, Sormanni P, Kundel F, Knowles TPJ, Dobson CM, Bryant C, et al. Different soluble aggregates of Aβ42 can give rise to cellular toxicity through different mechanisms. Nature Communications. 10: 1541. PMID 30948723 DOI: 10.1038/S41467-019-09477-3 |
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2019 |
Dobson CM, Knowles TPJ, Vendruscolo M. The Amyloid Phenomenon and Its Significance in Biology and Medicine. Cold Spring Harbor Perspectives in Biology. PMID 30936117 DOI: 10.1101/Cshperspect.A033878 |
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2019 |
Cater JH, Kumita JR, Zeineddine Abdallah R, Zhao G, Bernardo-Gancedo A, Henry A, Winata W, Chi M, Grenyer BSF, Townsend ML, Ranson M, Buhimschi CS, Charnock-Jones DS, Dobson CM, Wilson MR, et al. Human pregnancy zone protein stabilizes misfolded proteins including preeclampsia- and Alzheimer's-associated amyloid beta peptide. Proceedings of the National Academy of Sciences of the United States of America. PMID 30850528 DOI: 10.1073/Pnas.1817298116 |
0.409 |
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2019 |
Liu X, Toprakcioglu Z, Dear AJ, Levin A, Ruggeri FS, Taylor CG, Hu M, Kumita JR, Andreasen M, Dobson CM, Shimanovich U, Knowles TPJ. Fabrication and Characterization of Reconstituted Silk Microgels for the Storage and Release of Small Molecules. Macromolecular Rapid Communications. e1800898. PMID 30840348 DOI: 10.1002/Marc.201800898 |
0.333 |
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2019 |
Weiffert T, Meisl G, Flagmeier P, De S, Dunning CJR, Frohm B, Zetterberg H, Blennow K, Portelius E, Klenerman D, Dobson CM, Knowles TPJ, Linse S. Increased secondary nucleation underlies accelerated aggregation of the four-residue N-terminally truncated Aβ42 species Aβ5-42. Acs Chemical Neuroscience. PMID 30793584 DOI: 10.1021/Acschemneuro.8B00676 |
0.392 |
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2019 |
Limbocker R, Chia S, Ruggeri FS, Perni M, Cascella R, Heller GT, Meisl G, Mannini B, Habchi J, Michaels TCT, Challa PK, Ahn M, Casford ST, Fernando N, Xu CK, ... ... Dobson CM, et al. Trodusquemine enhances Aβ aggregation but suppresses its toxicity by displacing oligomers from cell membranes. Nature Communications. 10: 225. PMID 30644384 DOI: 10.1038/S41467-018-07699-5 |
0.545 |
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2019 |
Ahn M, Lee BI, Chia S, Habchi J, Kumita JR, Vendruscolo M, Dobson CM, Park CB. Chemical and mechanistic analysis of photodynamic inhibition of Alzheimer's β-amyloid aggregation. Chemical Communications (Cambridge, England). PMID 30632567 DOI: 10.1039/C8Cc09288E |
0.553 |
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2019 |
Andreasen M, Meisl G, Taylor JD, Michaels TCT, Levin A, Otzen DE, Chapman MR, Dobson CM, Matthews SJ, Knowles TPJ. Physical Determinants of Amyloid Assembly in Biofilm Formation. Mbio. 10. PMID 30622185 DOI: 10.1128/Mbio.02279-18 |
0.371 |
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2019 |
Agerschou ED, Flagmeier P, Saridaki T, Galvagnion C, Komnig D, Heid L, Prasad V, Shaykhalishahi H, Willbold D, Dobson CM, Voigt A, Falkenburger B, Hoyer W, Buell AK. Author response: An engineered monomer binding-protein for α-synuclein efficiently inhibits the proliferation of amyloid fibrils Elife. DOI: 10.7554/Elife.46112.035 |
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2019 |
Wang X, Kirkpatrick J, Launay H, Simone Ad, Haussinger D, Dobson C, Vendruscolo M, Cabrita L, Waudby C, Christodoulou J. Backbone 1H, 13C, and 15N Chemical Shift Assignments for ribosomal protein bL12 S89C and with LBT tag Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr27948 |
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2019 |
Aprile FA, Sormanni P, Perni M, Arosio P, Linse S, Knowles TP, Dobson CM, Vendruscolo M. Targeting the Formation of Amyloid Oligomers using Rationally Designed Antibodies Biophysical Journal. 116: 28a. DOI: 10.1016/J.Bpj.2018.11.196 |
0.466 |
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2018 |
Perni M, Casford S, Aprile FA, Nollen EA, Knowles TPJ, Vendruscolo M, Dobson CM. Automated Behavioral Analysis of Large C. elegans Populations Using a Wide Field-of-view Tracking Platform. Journal of Visualized Experiments : Jove. PMID 30582580 DOI: 10.3791/58643 |
0.449 |
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2018 |
Lee JE, Sang JC, Rodrigues M, Carr AR, Horrocks MH, De S, Bongiovanni MN, Flagmeier P, Dobson CM, Wales DJ, Lee SF, Klenerman D. Mapping Surface Hydrophobicity of α-Synuclein Oligomers at the Nanoscale. Nano Letters. PMID 30380895 DOI: 10.1021/Acs.Nanolett.8B02916 |
0.452 |
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2018 |
Iljina M, Dear AJ, Garcia GA, De S, Tosatto L, Flagmeier P, Whiten DR, Michaels TCT, Frenkel D, Dobson CM, Knowles TPJ, Klenerman D. Quantifying Co-Oligomer Formation by α-Synuclein. Acs Nano. PMID 30371053 DOI: 10.1021/Acsnano.8B03575 |
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2018 |
Dear AJ, Šarić A, Michaels TCT, Dobson CM, Knowles TPJ. Statistical Mechanics of Globular Oligomer Formation by Protein Molecules. The Journal of Physical Chemistry. B. PMID 30336667 DOI: 10.1021/Acs.Jpcb.8B07805 |
0.454 |
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2018 |
Chia S, Habchi J, Michaels TCT, Cohen SIA, Linse S, Dobson CM, Knowles TPJ, Vendruscolo M. SAR by kinetics for drug discovery in protein misfolding diseases. Proceedings of the National Academy of Sciences of the United States of America. PMID 30257937 DOI: 10.1073/Pnas.1807884115 |
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2018 |
Ruggeri FS, Charmet J, Kartanas T, Peter Q, Chia S, Habchi J, Dobson CM, Vendruscolo M, Knowles TPJ. Microfluidic deposition for resolving single-molecule protein architecture and heterogeneity. Nature Communications. 9: 3890. PMID 30250131 DOI: 10.1038/S41467-018-06345-4 |
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2018 |
Chatterjee D, Bhatt M, Butler D, De Genst E, Dobson CM, Messer A, Kordower JH. Proteasome-targeted nanobodies alleviate pathology and functional decline in an α-synuclein-based Parkinson's disease model. Npj Parkinson's Disease. 4: 25. PMID 30155513 DOI: 10.1038/S41531-018-0062-4 |
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2018 |
Matagne A, Dobson CM. Obituary: Nico van Nuland 1961-2017. European Biophysics Journal : Ebj. 47: 597-600. PMID 30116857 DOI: 10.1007/S00249-018-1326-Y |
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2018 |
van der Wateren IM, Knowles TPJ, Buell AK, Dobson CM, Galvagnion C. C-terminal truncation of α-synuclein promotes amyloid fibril amplification at physiological pH. Chemical Science. 9: 5506-5516. PMID 30061982 DOI: 10.1039/C8Sc01109E |
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2018 |
Horrocks M, Whiten DR, Zuo Y, Calo L, Choi ML, De S, Flagmeier P, Wirthensohn DC, Kundel F, Lee SF, Dobson C, Gandhi S, Spillantini M, Klenerman D, Ranasinghe RT, et al. Nanoscopic characterization of individual endogenous protein aggregates in human neuronal cells. Chembiochem : a European Journal of Chemical Biology. PMID 30051958 DOI: 10.1002/Cbic.201800209 |
0.453 |
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2018 |
Månsson C, van Cruchten RTP, Weininger U, Yang X, Cukalevski R, Arosio P, Dobson CM, Knowles TPJ, Akke M, Linse S, Emanuelsson C. Conserved S/T-residues of the human chaperone DNAJB6 are required for effective inhibition of Aβ42 amyloid fibril formation. Biochemistry. PMID 30024736 DOI: 10.1021/Acs.Biochem.8B00353 |
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2018 |
Capitini C, Patel JR, Natalello A, D'Andrea C, Relini A, Jarvis JA, Birolo L, Peduzzo A, Vendruscolo M, Matteini P, Dobson CM, De Simone A, Chiti F. Structural differences between toxic and nontoxic HypF-N oligomers. Chemical Communications (Cambridge, England). PMID 30020284 DOI: 10.1039/C8Cc03446J |
0.811 |
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2018 |
Mannini B, Habchi J, Chia SKR, Ruggeri FS, Perni M, Knowles TPJ, Dobson CM, Vendruscolo M. Stabilization and characterization of cytotoxic Aβ40 oligomers isolated from an aggregation reaction in the presence of zinc ions. Acs Chemical Neuroscience. PMID 29986583 DOI: 10.1021/Acschemneuro.8B00141 |
0.58 |
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2018 |
Perni M, Flagmeier P, Limbocker R, Cascella R, Aprile FA, Galvagnion C, Heller GT, Meisl G, Chen SW, Kumita JR, Challa PK, Kirkegaard JB, Cohen SIA, Mannini B, Barbut D, ... ... Dobson CM, et al. Multistep Inhibition of α-Synuclein Aggregation and Toxicity in Vitro and in Vivo by Trodusquemine. Acs Chemical Biology. PMID 29953201 DOI: 10.1021/Acschembio.8B00466 |
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2018 |
Brown JWP, Meisl G, Knowles TPJ, Buell AK, Dobson CM, Galvagnion C. Kinetic barriers to α-synuclein protofilament formation and conversion into mature fibrils. Chemical Communications (Cambridge, England). PMID 29951679 DOI: 10.1039/C8Cc03002B |
0.67 |
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2018 |
Whiten DR, Cox D, Horrocks MH, Taylor CG, De S, Flagmeier P, Tosatto L, Kumita JR, Ecroyd H, Dobson CM, Klenerman D, Wilson MR. Single-Molecule Characterization of the Interactions between Extracellular Chaperones and Toxic α-Synuclein Oligomers. Cell Reports. 23: 3492-3500. PMID 29924993 DOI: 10.1016/J.Celrep.2018.05.074 |
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2018 |
Zhang Y, Yates EV, Hong L, Saar KL, Meisl G, Dobson CM, Knowles TPJ. On-chip measurements of protein unfolding from direct observations of micron-scale diffusion. Chemical Science. 9: 3503-3507. PMID 29780480 DOI: 10.1039/C7Sc04331G |
0.39 |
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2018 |
Wright MA, Aprile FA, Bellaiche MM, Michaels TCT, Müller T, Arosio P, Vendruscolo M, Dobson CM, Knowles TPJ. Cooperative assembly of Hsp70 subdomain clusters. Biochemistry. PMID 29763298 DOI: 10.1021/Acs.Biochem.8B00151 |
0.522 |
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2018 |
Habchi J, Chia S, Galvagnion C, Michaels TCT, Bellaiche MMJ, Ruggeri FS, Sanguanini M, Idini I, Kumita JR, Sparr E, Linse S, Dobson CM, Knowles TPJ, Vendruscolo M. Cholesterol catalyses Aβ42 aggregation through a heterogeneous nucleation pathway in the presence of lipid membranes. Nature Chemistry. PMID 29736006 DOI: 10.1038/S41557-018-0031-X |
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2018 |
El Turk F, De Genst E, Guilliams T, Fauvet B, Hejjaoui M, Di Trani J, Chiki A, Mittermaier A, Vendruscolo M, Lashuel HA, Dobson CM. Exploring the role of post-translational modifications in regulating α-synuclein interactions by studying the effects of phosphorylation on nanobody binding. Protein Science : a Publication of the Protein Society. PMID 29603451 DOI: 10.1002/Pro.3412 |
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2018 |
Fusco G, Sanz-Hernandez M, Ruggeri FS, Vendruscolo M, Dobson CM, De Simone A. Molecular determinants of the interaction of EGCG with ordered and disordered proteins. Biopolymers. e23117. PMID 29603125 DOI: 10.1002/Bip.23117 |
0.596 |
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2018 |
Cohen SIA, Cukalevski R, Michaels TCT, Šarić A, Törnquist M, Vendruscolo M, Dobson CM, Buell AK, Knowles TPJ, Linse S. Distinct thermodynamic signatures of oligomer generation in the aggregation of the amyloid-β peptide. Nature Chemistry. PMID 29581486 DOI: 10.1038/S41557-018-0023-X |
0.728 |
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2018 |
Herling TW, Levin A, Saar KL, Dobson CM, Knowles TPJ. Microfluidic approaches for probing amyloid assembly and behaviour. Lab On a Chip. PMID 29527600 DOI: 10.1039/C7Lc01241A |
0.461 |
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2018 |
Needham LM, Weber J, Fyfe JWB, Kabia OM, Do DT, Klimont E, Zhang Y, Rodrigues M, Dobson CM, Ghandi S, Bohndiek SE, Snaddon TN, Lee SF. Bifunctional fluorescent probes for detection of amyloid aggregates and reactive oxygen species. Royal Society Open Science. 5: 171399. PMID 29515860 DOI: 10.1098/Rsos.171399 |
0.362 |
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2018 |
Michaels TCT, Šarić A, Habchi J, Chia S, Meisl G, Vendruscolo M, Dobson CM, Knowles TPJ. Chemical Kinetics for Bridging Molecular Mechanisms and Macroscopic Measurements of Amyloid Fibril Formation. Annual Review of Physical Chemistry. PMID 29490200 DOI: 10.1146/Annurev-Physchem-050317-021322 |
0.577 |
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2018 |
Perni M, Challa PK, Kirkegaard JB, Limbocker R, Koopman M, Hardenberg MC, Sormanni P, Müller T, Saar KL, Roode LWY, Habchi J, Vecchi G, Fernando NW, Casford S, Nollen EAA, ... ... Dobson CM, et al. Massively parallel C. elegans tracking provides multi-dimensional fingerprints for phenotypic discovery. Journal of Neuroscience Methods. PMID 29452179 DOI: 10.1016/J.Jneumeth.2018.02.005 |
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2018 |
Cox D, Whiten DR, Brown J, Horrocks MH, San Gil R, Dobson CM, Klenerman D, van Oijen AM, Ecroyd H. The small heat shock protein Hsp27 binds α-synuclein fibrils, preventing elongation and cytotoxicity. The Journal of Biological Chemistry. PMID 29382725 DOI: 10.1074/Jbc.M117.813865 |
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2018 |
Shimanovich U, Pinotsi D, Shimanovich K, Yu N, Bolisetty S, Adamcik J, Mezzenga R, Charmet J, Vollrath F, Gazit E, Dobson CM, Schierle GK, Holland C, Kaminski CF, Knowles TPJ. Biophotonics of Native Silk Fibrils. Macromolecular Bioscience. PMID 29377575 DOI: 10.1002/Mabi.201700295 |
0.315 |
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2018 |
Yang J, Dear AJ, Michaels TCT, Dobson CM, Knowles TPJ, Wu S, Perrett S. Direct observation of oligomerization by single molecule fluorescence reveals a multi-step aggregation mechanism for the yeast prion protein Ure2. Journal of the American Chemical Society. PMID 29357227 DOI: 10.1021/Jacs.7B10439 |
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2018 |
Varela JA, Rodrigues M, De S, Flagmeier P, Gandhi S, Dobson CM, Klenerman D, Lee S. Optical structural analysis of individual α-synuclein oligomers. Angewandte Chemie (International Ed. in English). PMID 29342318 DOI: 10.1002/Anie.201710779 |
0.42 |
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2018 |
Gang H, Galvagnion C, Meisl G, Müller T, Buell AK, Levin A, Dobson CM, Mu BZ, Knowles TPJ. A microfluidic diffusion platform for characterizing the size of lipid vesicles and the thermodynamics of protein-lipid interactions. Analytical Chemistry. PMID 29313342 DOI: 10.1021/Acs.Analchem.7B04820 |
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2018 |
Kundel F, De S, Flagmeier P, Horrocks MH, Kjaergaard M, Shammas SL, Jackson SE, Dobson CM, Klenerman D. Hsp70 inhibits the nucleation and elongation of tau and sequesters tau aggregates with high affinity. Acs Chemical Biology. PMID 29300447 DOI: 10.1021/Acschembio.7B01039 |
0.398 |
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2018 |
Turk FE, Genst ED, Guilliams T, Fauvet B, Hejjaoui M, Vendruscolo M, Lashuel H, Dobson C. 1H and 15N Chemical Shift Assignments for wild-type alpha-synuclein Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr27074 |
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2018 |
Yang J, Dear AJ, Michaels TC, Dobson CM, Knowles TP, Perrett S, Wu S. Revealing the Mechanism of Amyloid Fibril Formation by Combined Single Molecule FRET and Kinetic Modeling Biophysical Journal. 114: 685a. DOI: 10.1016/J.Bpj.2017.11.3693 |
0.358 |
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2018 |
Limbocker R, Mannini B, Chia S, Ruggeri FS, Perni M, Cascella R, Xu C, Habchi J, Kumita JR, Chiti F, Knowles TP, Vendruscolo M, Dobson CM. Modulating Amyloid-Beta Aggregation to Reduce the Toxicity of its Oligomeric Aggregates Biophysical Journal. 114: 430a. DOI: 10.1016/J.Bpj.2017.11.2382 |
0.516 |
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2018 |
Sinnige T, Laine RF, Yu Ma K, Haack AJ, Gaida P, Curry N, Perni M, Nollen EA, Dobson CM, Vendruscolo M, Kaminski Schierle GS, Kaminski CF. Fast Fluorescence Lifetime Imaging for Longitudinal Studies of Protein Aggregation in Living C. Elegans Biophysical Journal. 114: 350a. DOI: 10.1016/J.Bpj.2017.11.1949 |
0.499 |
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2018 |
Chia S, Habchi J, Limbocker R, Mannini B, Ahn M, Perni M, Hansson O, Arosio P, Kumita JR, Kumar Challa P, Cohen SI, Linse S, Dobson CM, Knowles TP, Vendruscolo M. Systematic Development of Small Molecules to Inhibit Specific Microscopic Steps of Amyloid-Beta42 Aggregation in Alzheimer's Disease Biophysical Journal. 114: 225a. DOI: 10.1016/J.Bpj.2017.11.1253 |
0.516 |
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2018 |
Whiten DR, Zuo Y, Calo L, Choi M, De S, Flagmeier P, Wirthensohn DC, Kundel F, Ranasinghe RT, Sanchez SE, Athauda D, Lee SF, Dobson CM, Gandhi S, Spillantini M, et al. Cover Feature: Nanoscopic Characterisation of Individual Endogenous Protein Aggregates in Human Neuronal Cells (ChemBioChem 19/2018) Chembiochem. 19: 2001-2001. DOI: 10.1002/Cbic.201800547 |
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2017 |
Fusco G, Chen SW, Williamson PTF, Cascella R, Perni M, Jarvis JA, Cecchi C, Vendruscolo M, Chiti F, Cremades N, Ying L, Dobson CM, De Simone A. Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers. Science (New York, N.Y.). 358: 1440-1443. PMID 29242346 DOI: 10.1126/Science.Aan6160 |
0.509 |
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2017 |
Drews A, De S, Flagmeier P, Wirthensohn DC, Chen WH, Whiten DR, Rodrigues M, Vincke C, Muyldermans S, Paterson RW, Slattery CF, Fox NC, Schott JM, Zetterberg H, Dobson CM, et al. Inhibiting the Ca2+ Influx Induced by Human CSF. Cell Reports. 21: 3310-3316. PMID 29241555 DOI: 10.1016/J.Celrep.2017.11.057 |
0.332 |
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2017 |
Meisl G, Rajah L, Cohen SAI, Pfammatter M, Šarić A, Hellstrand E, Buell AK, Aguzzi A, Linse S, Vendruscolo M, Dobson CM, Knowles TPJ. Scaling behaviour and rate-determining steps in filamentous self-assembly. Chemical Science. 8: 7087-7097. PMID 29147538 DOI: 10.1039/C7Sc01965C |
0.715 |
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2017 |
Perni M, Aprile FA, Casford S, Mannini B, Sormanni P, Dobson CM, Vendruscolo M. Delivery of Native Proteins into C. elegans Using a Transduction Protocol Based on Lipid Vesicles. Scientific Reports. 7: 15045. PMID 29118344 DOI: 10.1038/S41598-017-13755-9 |
0.521 |
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2017 |
Gregory JM, Whiten DR, Brown RA, Barros TP, Kumita JR, Yerbury JJ, Satapathy S, McDade K, Smith C, Luheshi LM, Dobson CM, Wilson MR. Clusterin protects neurons against intracellular proteotoxicity. Acta Neuropathologica Communications. 5: 81. PMID 29115989 DOI: 10.1186/S40478-017-0481-1 |
0.314 |
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2017 |
Ahn M, Waudby CA, Bernardo-Gancedo A, De Genst E, Dhulesia A, Salvatella X, Christodoulou J, Dobson CM, Kumita JR. Application of Lysine-specific Labeling to Detect Transient Interactions Present During Human Lysozyme Amyloid Fibril Formation. Scientific Reports. 7: 15018. PMID 29101328 DOI: 10.1038/S41598-017-14739-5 |
0.408 |
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2017 |
Mason TO, Michaels TCT, Levin A, Dobson CM, Gazit E, Knowles TPJ, Buell AK. Thermodynamics of polypeptide supramolecular assembly in the short chain limit. Journal of the American Chemical Society. PMID 28994295 DOI: 10.1021/Jacs.7B00229 |
0.665 |
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2017 |
Meisl G, Yang X, Dobson CM, Linse S, Knowles TPJ. Modulation of electrostatic interactions to reveal a reaction network unifying the aggregation behaviour of the Aβ42 peptide and its variants. Chemical Science. 8: 4352-4362. PMID 28979758 DOI: 10.1039/C7Sc00215G |
0.375 |
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2017 |
Pfammatter M, Andreasen M, Meisl G, Taylor CG, Adamcik J, Bolisetty S, Sanchez-Ferrer A, Klenerman D, Dobson CM, Mezzenga R, Knowles TPJ, Aguzzi AA, Hornemann S. Absolute Quantification of Amyloid Propagons by Digital Microfluidics. Analytical Chemistry. PMID 28972786 DOI: 10.1021/Acs.Analchem.7B03279 |
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2017 |
Łapińska U, Saar KL, Yates EV, Herling TW, Müller T, Challa PK, Dobson CM, Knowles TPJ. Gradient-free determination of isoelectric points of proteins on chip. Physical Chemistry Chemical Physics : Pccp. PMID 28817152 DOI: 10.1039/C7Cp01503H |
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2017 |
Shimanovich U, Michaels TCT, de Genst EJ, Matak-Vinkovic D, Dobson CM, Knowles TPJ. Sequential release of proteins from structured multishell microcapsules. Biomacromolecules. PMID 28792742 DOI: 10.1021/Acs.Biomac.7B00351 |
0.393 |
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2017 |
Shimanovich U, Ruggeri FS, De Genst E, Adamcik J, Barros TP, Porter D, Müller T, Mezzenga R, Dobson CM, Vollrath F, Holland C, Knowles TPJ. Silk micrococoons for protein stabilisation and molecular encapsulation. Nature Communications. 8: 15902. PMID 28722016 DOI: 10.1038/Ncomms15902 |
0.384 |
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2017 |
Hanspal MA, Dobson CM, Yerbury JJ, Kumita JR. The relevance of contact-independent cell-to-cell transfer of TDP-43 and SOD1 in amyotrophic lateral sclerosis. Biochimica Et Biophysica Acta. PMID 28711596 DOI: 10.1016/J.Bbadis.2017.07.007 |
0.386 |
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2017 |
Cremades N, Dobson CM. The contribution of biophysical and structural studies of protein self-assembly to the design of therapeutic strategies for amyloid diseases. Neurobiology of Disease. PMID 28709995 DOI: 10.1016/J.Nbd.2017.07.009 |
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2017 |
Chia S, Flagmeier P, Habchi J, Lattanzi V, Linse S, Dobson CM, Knowles TPJ, Vendruscolo M. Monomeric and fibrillar α-synuclein exert opposite effects on the catalytic cycle that promotes the proliferation of Aβ42 aggregates. Proceedings of the National Academy of Sciences of the United States of America. PMID 28698377 DOI: 10.1073/Pnas.1700239114 |
0.537 |
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2017 |
Aprile FA, Sormanni P, Perni M, Arosio P, Linse S, Knowles TPJ, Dobson CM, Vendruscolo M. Selective targeting of primary and secondary nucleation pathways in Aβ42 aggregation using a rational antibody scanning method. Science Advances. 3: e1700488. PMID 28691099 DOI: 10.1126/Sciadv.1700488 |
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2017 |
Iljina M, Hong L, Horrocks MH, Ludtmann MH, Choi ML, Hughes CD, Ruggeri FS, Guilliams T, Buell AK, Lee JE, Gandhi S, Lee SF, Bryant CE, Vendruscolo M, Knowles TPJ, ... Dobson CM, et al. Nanobodies raised against monomeric ɑ-synuclein inhibit fibril formation and destabilize toxic oligomeric species. Bmc Biology. 15: 57. PMID 28673288 DOI: 10.1186/S12915-017-0390-6 |
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2017 |
Kundra R, Ciryam P, Morimoto RI, Dobson CM, Vendruscolo M. Protein homeostasis of a metastable subproteome associated with Alzheimer's disease. Proceedings of the National Academy of Sciences of the United States of America. PMID 28652376 DOI: 10.1073/Pnas.1618417114 |
0.569 |
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2017 |
Elia F, Cantini F, Chiti F, Dobson CM, Bemporad F. Direct Conversion of an Enzyme from Native-like to Amyloid-like Aggregates within Inclusion Bodies. Biophysical Journal. 112: 2540-2551. PMID 28636911 DOI: 10.1016/J.Bpj.2017.05.011 |
0.483 |
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2017 |
Munke A, Persson J, Weiffert T, De Genst E, Meisl G, Arosio P, Carnerup A, Dobson CM, Vendruscolo M, Knowles TPJ, Linse S. Phage display and kinetic selection of antibodies that specifically inhibit amyloid self-replication. Proceedings of the National Academy of Sciences of the United States of America. PMID 28584111 DOI: 10.1073/Pnas.1700407114 |
0.555 |
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2017 |
Chiti F, Dobson CM. Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade. Annual Review of Biochemistry. PMID 28498720 DOI: 10.1146/Annurev-Biochem-061516-045115 |
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2017 |
Stroobants K, Kumita JR, Harris N, Chirgadze D, Dobson CM, Booth PJ, Vendruscolo M. Amyloid-like fibrils from an α-helical transmembrane protein. Biochemistry. PMID 28493669 DOI: 10.1021/Acs.Biochem.7B00157 |
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2017 |
Fusco G, Pape T, Stephens AD, Mahou P, Costa AR, Kaminski CF, Schierle GSK, Vendruscolo M, Veglia G, Dobson CM, De Simone A. Corrigendum: Structural basis of synaptic vesicle assembly promoted by α-synuclein. Nature Communications. 8: 15667. PMID 28492274 DOI: 10.1038/Ncomms15667 |
0.446 |
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2017 |
Flagmeier P, De S, Wirthensohn DC, Lee SF, Vincke C, Muyldermans S, Knowles TPJ, Gandhi S, Dobson CM, Klenerman D. Ultrasensitive Measurement of Ca(2+) Influx into Lipid Vesicles Induced by Protein Aggregates. Angewandte Chemie (International Ed. in English). PMID 28474754 DOI: 10.1002/Anie.201700966 |
0.372 |
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2017 |
Ciryam P, Lambert-Smith IA, Bean DM, Freer R, Cid F, Tartaglia GG, Saunders DN, Wilson MR, Oliver SG, Morimoto RI, Dobson CM, Vendruscolo M, Favrin G, Yerbury JJ. Spinal motor neuron protein supersaturation patterns are associated with inclusion body formation in ALS. Proceedings of the National Academy of Sciences of the United States of America. PMID 28396410 DOI: 10.1073/Pnas.1613854114 |
0.531 |
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2017 |
Perni M, Galvagnion C, Maltsev A, Meisl G, Mueller MBD, Challa PK, Kirkegaard JB, Flagmeier P, Cohen SIA, Cascella R, Chen SW, Limboker R, Sormanni P, Heller GT, Aprile FA, ... ... Dobson CM, et al. Correction for Perni et al., A natural product inhibits the initiation of alpha-synuclein aggregation and suppresses its toxicity (vol 114, pg E1009, 2017) Proceedings of the National Academy of Sciences of the United States of America. 114. PMID 28265088 DOI: 10.1073/Pnas.1701964114 |
0.449 |
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2017 |
Walther DM, Kasturi P, Zheng M, Pinkert S, Vecchi G, Ciryam P, Morimoto RI, Dobson CM, Vendruscolo M, Mann M, Hartl FU. Widespread Proteome Remodeling and Aggregation in Aging C. elegans. Cell. 168: 944. PMID 28235202 DOI: 10.1016/J.Cell.2016.12.041 |
0.479 |
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2017 |
Aprile FA, Arosio P, Fusco G, Chen SW, Kumita JR, Dhulesia A, Tortora P, Knowles TP, Vendruscolo M, Dobson CM, Cremades N. Inhibition of α-Synuclein Fibril Elongation by Hsp70 Is Governed by a Kinetic Binding Competition between α-Synuclein Species. Biochemistry. PMID 28230968 DOI: 10.1021/Acs.Biochem.6B01178 |
0.563 |
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2017 |
Cremades N, Chen SW, Dobson CM. Structural Characteristics of α-Synuclein Oligomers. International Review of Cell and Molecular Biology. 329: 79-143. PMID 28109332 DOI: 10.1016/Bs.Ircmb.2016.08.010 |
0.425 |
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2017 |
Perni M, Galvagnion C, Maltsev A, Meisl G, Müller MB, Challa PK, Kirkegaard JB, Flagmeier P, Cohen SI, Cascella R, Chen SW, Limboker R, Sormanni P, Heller GT, Aprile FA, ... ... Dobson CM, et al. A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity. Proceedings of the National Academy of Sciences of the United States of America. PMID 28096355 DOI: 10.1073/Pnas.1610586114 |
0.509 |
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2017 |
Dobson CM. The Amyloid Phenomenon and Its Links with Human Disease. Cold Spring Harbor Perspectives in Biology. PMID 28062560 DOI: 10.1101/Cshperspect.A023648 |
0.448 |
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2017 |
Sinnige T, Ciryam P, Dobson CM, de Bono M, Vendruscolo M. Effects of Amyloid-Beta Expression on Neuronal Signalling Pathways in a Novel C. elegans Model of Alzheimer's Disease Biophysical Journal. 112: 159a-160a. DOI: 10.1016/J.Bpj.2016.11.878 |
0.548 |
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2017 |
Limbocker R, Mannini B, Perni M, Chia S, Heller G, Ruggeri FS, Habchi J, Meisl G, Challa PK, Zasloff M, Knowles TP, Vendruscolo M, Dobson CM. Attenuating the Toxicity of Amyloid-Beta Aggregation with Specific Species Biophysical Journal. 112: 494a. DOI: 10.1016/J.Bpj.2016.11.2673 |
0.495 |
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2016 |
Šarić A, Buell AK, Meisl G, Michaels TCT, Dobson CM, Linse S, Knowles TPJ, Frenkel D. Physical determinants of the self-replication of protein fibrils. Nature Physics. 12: 874-880. PMID 31031819 DOI: 10.1038/Nphys3828 |
0.692 |
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2016 |
Habchi J, Chia S, Limbocker R, Mannini B, Ahn M, Perni M, Hansson O, Arosio P, Kumita JR, Challa PK, Cohen SI, Linse S, Dobson CM, Knowles TP, Vendruscolo M. Systematic development of small molecules to inhibit specific microscopic steps of Aβ42 aggregation in Alzheimer's disease. Proceedings of the National Academy of Sciences of the United States of America. PMID 28011763 DOI: 10.1073/Pnas.1615613114 |
0.537 |
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2016 |
Ahn M, Hagan CL, Bernardo-Gancedo A, De Genst E, Newby FN, Christodoulou J, Dhulesia A, Dumoulin M, Robinson CV, Dobson CM, Kumita JR. The Significance of the Location of Mutations for the Native-State Dynamics of Human Lysozyme. Biophysical Journal. 111: 2358-2367. PMID 27926837 DOI: 10.1016/J.Bpj.2016.10.028 |
0.493 |
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2016 |
Butler DC, Joshi SN, Genst E, Baghel AS, Dobson CM, Messer A. Bifunctional Anti-Non-Amyloid Component α-Synuclein Nanobodies Are Protective In Situ. Plos One. 11: e0165964. PMID 27824888 DOI: 10.1371/Journal.Pone.0165964 |
0.33 |
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2016 |
Brown JW, Buell AK, Michaels TC, Meisl G, Carozza J, Flagmeier P, Vendruscolo M, Knowles TP, Dobson CM, Galvagnion C. β-Synuclein suppresses both the initiation and amplification steps of α-synuclein aggregation via competitive binding to surfaces. Scientific Reports. 6: 36010. PMID 27808107 DOI: 10.1038/Srep36010 |
0.706 |
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2016 |
Fusco G, Pape T, Stephens AD, Mahou P, Costa AR, Kaminski CF, Kaminski Schierle GS, Vendruscolo M, Veglia G, Dobson CM, De Simone A. Structural basis of synaptic vesicle assembly promoted by α-synuclein. Nature Communications. 7: 12563. PMID 27640673 DOI: 10.1038/Ncomms12563 |
0.498 |
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2016 |
Evangelisti E, Cascella R, Becatti M, Marrazza G, Dobson CM, Chiti F, Stefani M, Cecchi C. Binding affinity of amyloid oligomers to cellular membranes is a generic indicator of cellular dysfunction in protein misfolding diseases. Scientific Reports. 6: 32721. PMID 27619987 DOI: 10.1038/Srep32721 |
0.402 |
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2016 |
Flagmeier P, Meisl G, Vendruscolo M, Knowles TP, Dobson CM, Buell AK, Galvagnion C. Mutations associated with familial Parkinson's disease alter the initiation and amplification steps of α-synuclein aggregation. Proceedings of the National Academy of Sciences of the United States of America. PMID 27573854 DOI: 10.1073/Pnas.1604645113 |
0.704 |
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2016 |
Freer R, Sormanni P, Vecchi G, Ciryam P, Dobson CM, Vendruscolo M. A protein homeostasis signature in healthy brains recapitulates tissue vulnerability to Alzheimer's disease. Science Advances. 2: e1600947. PMID 27532054 DOI: 10.1126/Sciadv.1600947 |
0.516 |
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2016 |
Zhang Y, Buell AK, Müller T, De Genst E, Benesch J, Dobson CM, Knowles TP. Protein aggregate-ligand binding assays based on microfluidic diffusional separation. Chembiochem : a European Journal of Chemical Biology. PMID 27472818 DOI: 10.1002/Cbic.201600384 |
0.686 |
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2016 |
Crippa V, Cicardi ME, Ramesh N, Seguin SJ, Ganassi M, Bigi I, Diacci C, Zelotti E, Baratashvili M, Gregory JM, Dobson CM, Cereda C, Pandey UB, Poletti A, Carra S. The Chaperone HSPB8 Reduces the Accumulation of Truncated TDP-43 Species in Cells and Protects Against TDP-43-Mediated Toxicity. Human Molecular Genetics. PMID 27466192 DOI: 10.1093/Hmg/Ddw232 |
0.319 |
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2016 |
Camilloni C, Bonetti D, Morrone A, Giri R, Dobson CM, Brunori M, Gianni S, Vendruscolo M. Towards a structural biology of the hydrophobic effect in protein folding. Scientific Reports. 6: 28285. PMID 27461719 DOI: 10.1038/Srep28285 |
0.714 |
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2016 |
Cascella R, Capitini C, Fani G, Dobson CM, Cecchi C, Chiti F. Quantification of the relative contributions of loss-of-function and gain-of-function mechanisms in TDP-43 proteinopathies. The Journal of Biological Chemistry. PMID 27445339 DOI: 10.1074/Jbc.M116.737726 |
0.308 |
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2016 |
Mason TO, Michaels TC, Levin A, Gazit E, Dobson CM, Buell AK, Knowles TP. Synthesis of non-equilibrium supra-molecular peptide polymers on a microfluidic platform. Journal of the American Chemical Society. PMID 27387359 DOI: 10.1021/Jacs.6B04136 |
0.618 |
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2016 |
Iljina M, Garcia GA, Dear AJ, Flint J, Narayan P, Michaels TC, Dobson CM, Frenkel D, Knowles TP, Klenerman D. Quantitative analysis of co-oligomer formation by amyloid-beta peptide isoforms. Scientific Reports. 6: 28658. PMID 27346247 DOI: 10.1038/Srep28658 |
0.421 |
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2016 |
Galvagnion C, Brown JW, Ouberai MM, Flagmeier P, Vendruscolo M, Buell AK, Sparr E, Dobson CM. Chemical properties of lipids strongly affect the kinetics of the membrane-induced aggregation of α-synuclein. Proceedings of the National Academy of Sciences of the United States of America. PMID 27298346 DOI: 10.1073/Pnas.1601899113 |
0.702 |
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2016 |
Fusco G, De Simone A, Arosio P, Vendruscolo M, Veglia G, Dobson CM. Structural Ensembles of Membrane-bound α-Synuclein Reveal the Molecular Determinants of Synaptic Vesicle Affinity. Scientific Reports. 6: 27125. PMID 27273030 DOI: 10.1038/Srep27125 |
0.541 |
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2016 |
Kakkar V, Månsson C, de Mattos EP, Bergink S, van der Zwaag M, van Waarde MA, Kloosterhuis NJ, Melki R, van Cruchten RT, Al-Karadaghi S, Arosio P, Dobson CM, Knowles TP, Bates GP, van Deursen JM, et al. The S/T-Rich Motif in the DNAJB6 Chaperone Delays Polyglutamine Aggregation and the Onset of Disease in a Mouse Model. Molecular Cell. PMID 27151442 DOI: 10.1016/J.Molcel.2016.03.017 |
0.417 |
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2016 |
El-Turk F, Newby F, de Genst EJ, Guilliams T, Sprules T, Mittermaier AK, Dobson CM, Vendruscolo M. Structural effects of two camelid nanobodies directed to distinct C-terminal epitopes on α-synuclein. Biochemistry. PMID 27096466 DOI: 10.1021/Acs.Biochem.6B00149 |
0.546 |
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2016 |
Deckert A, Waudby CA, Wlodarski T, Wentink AS, Wang X, Kirkpatrick JP, Paton JF, Camilloni C, Kukic P, Dobson CM, Vendruscolo M, Cabrita LD, Christodoulou J. Structural characterization of the interaction of α-synuclein nascent chains with the ribosomal surface and trigger factor. Proceedings of the National Academy of Sciences of the United States of America. PMID 27092002 DOI: 10.1073/Pnas.1519124113 |
0.71 |
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2016 |
Ciryam P, Kundra R, Freer R, Morimoto RI, Dobson CM, Vendruscolo M. A transcriptional signature of Alzheimer's disease is associated with a metastable subproteome at risk for aggregation. Proceedings of the National Academy of Sciences of the United States of America. PMID 27071083 DOI: 10.1073/Pnas.1516604113 |
0.526 |
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2016 |
Arosio P, Michaels TC, Linse S, Månsson C, Emanuelsson C, Presto J, Johansson J, Vendruscolo M, Dobson CM, Knowles TP. Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation. Nature Communications. 7: 10948. PMID 27009901 DOI: 10.1038/Ncomms10948 |
0.578 |
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2016 |
Pinotsi D, Michel CH, Buell AK, Laine RF, Mahou P, Dobson CM, Kaminski CF, Kaminski Schierle GS. Nanoscopic insights into seeding mechanisms and toxicity of α-synuclein species in neurons. Proceedings of the National Academy of Sciences of the United States of America. PMID 26993805 DOI: 10.1073/Pnas.1516546113 |
0.675 |
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2016 |
Wolff M, Mittag JJ, Herling TW, Genst ED, Dobson CM, Knowles TP, Braun D, Buell AK. Quantitative thermophoretic study of disease-related protein aggregates. Scientific Reports. 6: 22829. PMID 26984748 DOI: 10.1038/Srep22829 |
0.695 |
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2016 |
Pedersen JT, Chen SW, Borg CB, Ness S, Bahl JM, Heegard NH, Dobson CM, Hemmingsen L, Cremades N, Teilum K. Amyloid-β and α-Synuclein Decrease the Level of Metal-Catalyzed Reactive Oxygen Species by Radical Scavenging and Redox Silencing. Journal of the American Chemical Society. PMID 26967463 DOI: 10.1021/Jacs.5B13577 |
0.363 |
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2016 |
Habchi J, Arosio P, Perni M, Costa AR, Yagi-Utsumi M, Joshi P, Chia S, Cohen SI, Müller MB, Linse S, Nollen EA, Dobson CM, Knowles TP, Vendruscolo M. An anticancer drug suppresses the primary nucleation reaction that initiates the production of the toxic Aβ42 aggregates linked with Alzheimer's disease. Science Advances. 2: e1501244. PMID 26933687 DOI: 10.1126/Sciadv.1501244 |
0.541 |
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2016 |
Cabrita LD, Cassaignau AM, Launay HM, Waudby CA, Wlodarski T, Camilloni C, Karyadi ME, Robertson AL, Wang X, Wentink AS, Goodsell LS, Woolhead CA, Vendruscolo M, Dobson CM, Christodoulou J. A structural ensemble of a ribosome-nascent chain complex during cotranslational protein folding. Nature Structural & Molecular Biology. PMID 26926436 DOI: 10.1038/Nsmb.3182 |
0.701 |
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2016 |
Joshi P, Chia S, Habchi J, Knowles TP, Dobson CM, Vendruscolo M. A Fragment-Based Method of Creating Small-Molecule Libraries to Target the Aggregation of Intrinsically Disordered Proteins. Acs Combinatorial Science. PMID 26923286 DOI: 10.1021/Acscombsci.5B00129 |
0.526 |
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2016 |
Iljina M, Garcia GA, Horrocks MH, Tosatto L, Choi ML, Ganzinger KA, Abramov AY, Gandhi S, Wood NW, Cremades N, Dobson CM, Knowles TP, Klenerman D. Kinetic model of the aggregation of alpha-synuclein provides insights into prion-like spreading. Proceedings of the National Academy of Sciences of the United States of America. PMID 26884195 DOI: 10.1073/Pnas.1524128113 |
0.447 |
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2016 |
Yates EV, Meisl G, Knowles TP, Dobson CM. An Environmentally Sensitive Fluorescent Dye as a Multidimensional Probe of Amyloid Formation. The Journal of Physical Chemistry. B. PMID 26865546 DOI: 10.1021/Acs.Jpcb.5B09663 |
0.37 |
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2016 |
Michaels TC, Cohen SI, Vendruscolo M, Dobson CM, Knowles TP. Hamiltonian Dynamics of Protein Filament Formation. Physical Review Letters. 116: 038101. PMID 26849615 DOI: 10.1103/Physrevlett.116.038101 |
0.526 |
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2016 |
Saar KL, Yates EV, Müller T, Saunier S, Dobson CM, Knowles TP. Automated Ex Situ Assays of Amyloid Formation on a Microfluidic Platform. Biophysical Journal. 110: 555-560. PMID 26840721 DOI: 10.1016/J.Bpj.2015.11.3523 |
0.423 |
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2016 |
Cappelli S, Penco A, Mannini B, Cascella R, Wilson M, Ecroyd H, Li X, Buxbaum J, Dobson CM, Cecchi C, Relini A, Chiti F. Effect of molecular chaperones on aberrant protein oligomers in vitro: super- versus sub-stoichiometric chaperone concentrations. Biological Chemistry. PMID 26812789 DOI: 10.1515/Hsz-2015-0250 |
0.403 |
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2016 |
Horrocks MH, Lee SF, Gandhi S, Magdalinou NK, Chen SW, Devine MJ, Tosatto L, Kjaergaard M, Beckwith JS, Zetterberg H, Iljina M, Cremades N, Dobson CM, Wood NW, Klenerman D. Single-molecule imaging of individual amyloid protein aggregates in human biofluids. Acs Chemical Neuroscience. PMID 26800462 DOI: 10.1021/Acschemneuro.5B00324 |
0.426 |
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2016 |
Meisl G, Kirkegaard JB, Arosio P, Michaels TC, Vendruscolo M, Dobson CM, Linse S, Knowles TP. Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nature Protocols. 11: 252-72. PMID 26741409 DOI: 10.1038/Nprot.2016.010 |
0.565 |
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2016 |
Müller T, Arosio P, Rajah L, Cohen SIA, Yates EV, Vendruscolo M, Dobson CM, Knowles TPJ. Particle-Based Monte-Carlo Simulations of Steady-State Mass Transport at Intermediate Péclet Numbers International Journal of Nonlinear Sciences and Numerical Simulation. 17: 175-183. DOI: 10.1515/Ijnsns-2015-0056 |
0.422 |
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2016 |
Pietralik Z, Murawska M, Szymanska A, Kumita JR, Dobson CM, Kozak M. Structural Studies of the Oligomerization Process of Human Cystatin C Variants Biophysical Journal. 110: 26a. DOI: 10.1016/J.Bpj.2015.11.205 |
0.341 |
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2015 |
Arosio P, Müller T, Rajah L, Yates EV, Aprile FA, Zhang Y, Cohen SI, White DA, Herling TW, de Genst EJ, Linse S, Vendruscolo M, Dobson CM, Knowles TP. Microfluidic Diffusion Analysis of the Sizes and Interactions of Proteins Under Native Solution Conditions. Acs Nano. PMID 26678709 DOI: 10.1021/Acsnano.5B04713 |
0.475 |
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2015 |
Tosatto L, Horrocks MH, Dear AJ, Knowles TP, Dalla Serra M, Cremades N, Dobson CM, Klenerman D. Single-molecule FRET studies on alpha-synuclein oligomerization of Parkinson's disease genetically related mutants. Scientific Reports. 5: 16696. PMID 26582456 DOI: 10.1038/Srep16696 |
0.378 |
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2015 |
Deas E, Cremades N, Angelova PR, Ludtmann M, Yao Z, Chen S, Horrocks M, Banushi B, Little D, Devine M, Gissen P, Klenerman D, Dobson C, Wood N, Gandhi S, et al. Alpha-synuclein oligomers interact with metal ions to induce oxidative stress and neuronal death in Parkinson's disease. Antioxidants & Redox Signaling. PMID 26564470 DOI: 10.1089/Ars.2015.6343 |
0.329 |
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2015 |
Terol PA, Kumita JR, Hook SC, Dobson CM, Esbjörner EK. Solvent exposure of Tyr10 as a probe of structural differences between monomeric and aggregated forms of the amyloid-β peptide. Biochemical and Biophysical Research Communications. PMID 26551456 DOI: 10.1016/J.Bbrc.2015.11.018 |
0.408 |
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2015 |
Michaels TC, Yde P, Willis JC, Jensen MH, Otzen D, Dobson CM, Buell AK, Knowles TP. The length distribution of frangible biofilaments. The Journal of Chemical Physics. 143: 164901. PMID 26520548 DOI: 10.1063/1.4933230 |
0.646 |
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2015 |
Zeineddine R, Pundavela JF, Corcoran L, Stewart EM, Do-Ha D, Bax M, Guillemin G, Vine KL, Hatters DM, Ecroyd H, Dobson CM, Turner BJ, Ooi L, Wilson MR, Cashman NR, et al. SOD1 protein aggregates stimulate macropinocytosis in neurons to facilitate their propagation. Molecular Neurodegeneration. 10: 57. PMID 26520394 DOI: 10.1186/S13024-015-0053-4 |
0.376 |
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2015 |
Pickhardt M, Neumann T, Schwizer D, Callaway K, Vendruscolo M, Schenk D, George-Hyslop PS, Mandelkow EM, Dobson CM, McConlogue L, Mandelkow E, Toth G. Identification of Small Molecule Inhibitors of Tau Aggregation by Targeting Monomeric Tau As a Potential Therapeutic Approach for Tauopathies. Current Alzheimer Research. 12: 814-28. PMID 26510979 DOI: 10.2174/156720501209151019104951 |
0.546 |
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2015 |
Newby FN, De Simone A, Yagi-Utsumi M, Salvatella X, Dobson CM, Vendruscolo M. Structure-Free Validation of Residual Dipolar Coupling and Paramagnetic Relaxation Enhancement Measurements of Disordered Proteins. Biochemistry. PMID 26479087 DOI: 10.1021/Acs.Biochem.5B00670 |
0.573 |
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2015 |
Labrador-Garrido A, Cejudo-Guillén M, Daturpalli S, Leal MM, Klippstein R, De Genst EJ, Villadiego J, Toledo-Aral JJ, Dobson CM, Jackson SE, Pozo D, Roodveldt C. Chaperome screening leads to identification of Grp94/Gp96 and FKBP4/52 as modulators of the α-synuclein-elicited immune response. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. PMID 26443817 DOI: 10.1096/Fj.15-275131 |
0.314 |
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2015 |
Yagi-Utsumi M, Dobson CM. Conformational Effects of the A21G Flemish Mutation on the Aggregation of Amyloid β Peptide. Biological & Pharmaceutical Bulletin. 38: 1668-72. PMID 26424029 DOI: 10.1248/Bpb.B15-00466 |
0.383 |
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2015 |
Yates EV, Müller T, Rajah L, De Genst EJ, Arosio P, Linse S, Vendruscolo M, Dobson CM, Knowles TP. Latent analysis of unmodified biomolecules and their complexes in solution with attomole detection sensitivity. Nature Chemistry. 7: 802-9. PMID 26391079 DOI: 10.1038/Nchem.2344 |
0.465 |
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2015 |
Wright MA, Aprile FA, Arosio P, Vendruscolo M, Dobson CM, Knowles TP. Biophysical approaches for the study of interactions between molecular chaperones and protein aggregates. Chemical Communications (Cambridge, England). 51: 14425-34. PMID 26328629 DOI: 10.1039/C5Cc03689E |
0.594 |
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2015 |
Horrocks MH, Tosatto L, Dear AJ, Garcia GA, Iljina M, Cremades N, Dalla Serra M, Knowles TP, Dobson CM, Klenerman D. Fast Flow Microfluidics and Single-Molecule Fluorescence for the Rapid Characterization of α-Synuclein Oligomers. Analytical Chemistry. 87: 8818-26. PMID 26258431 DOI: 10.1021/Acs.Analchem.5B01811 |
0.381 |
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2015 |
Herling TW, Garcia GA, Michaels TC, Grentz W, Dean J, Shimanovich U, Gang H, Müller T, Kav B, Terentjev EM, Dobson CM, Knowles TP. Force generation by the growth of amyloid aggregates. Proceedings of the National Academy of Sciences of the United States of America. 112: 9524-9. PMID 26195762 DOI: 10.1073/Pnas.1417326112 |
0.335 |
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2015 |
Wyatt AR, Kumita JR, Farrawell NE, Dobson CM, Wilson MR. Alpha-2-Macroglobulin Is Acutely Sensitive to Freezing and Lyophilization: Implications for Structural and Functional Studies. Plos One. 10: e0130036. PMID 26103636 DOI: 10.1371/Journal.Pone.0130036 |
0.312 |
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2015 |
Dworzak J, Renvoisé B, Habchi J, Yates EV, Combadière C, Knowles TP, Dobson CM, Blackstone C, Paulsen O, Murphy PM. Neuronal Cx3cr1 Deficiency Protects against Amyloid β-Induced Neurotoxicity. Plos One. 10: e0127730. PMID 26038823 DOI: 10.1371/Journal.Pone.0127730 |
0.308 |
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2015 |
Zhou XM, Shimanovich U, Herling TW, Wu S, Dobson CM, Knowles TP, Perrett S. Enzymatically Active Microgels from Self-Assembling Protein Nanofibrils for Microflow Chemistry. Acs Nano. 9: 5772-81. PMID 26030507 DOI: 10.1021/Acsnano.5B00061 |
0.361 |
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2015 |
Walther DM, Kasturi P, Zheng M, Pinkert S, Vecchi G, Ciryam P, Morimoto RI, Dobson CM, Vendruscolo M, Mann M, Hartl FU. Widespread Proteome Remodeling and Aggregation in Aging C. elegans. Cell. 161: 919-32. PMID 25957690 DOI: 10.1016/J.Cell.2015.03.032 |
0.565 |
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2015 |
De Genst E, Chirgadze DY, Klein FA, Butler DC, Matak-Vinković D, Trottier Y, Huston JS, Messer A, Dobson CM. Structure of a single-chain Fv bound to the 17 N-terminal residues of huntingtin provides insights into pathogenic amyloid formation and suppression. Journal of Molecular Biology. 427: 2166-78. PMID 25861763 DOI: 10.1016/J.Jmb.2015.03.021 |
0.432 |
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2015 |
Chen SW, Drakulic S, Deas E, Ouberai M, Aprile FA, Arranz R, Ness S, Roodveldt C, Guilliams T, De-Genst EJ, Klenerman D, Wood NW, Knowles TP, Alfonso C, Rivas G, ... ... Dobson CM, et al. Structural characterization of toxic oligomers that are kinetically trapped during α-synuclein fibril formation. Proceedings of the National Academy of Sciences of the United States of America. 112: E1994-2003. PMID 25855634 DOI: 10.1073/Pnas.1421204112 |
0.421 |
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2015 |
Baldwin AJ, Egan DL, Warren FJ, Barker PD, Dobson CM, Butterworth PJ, Ellis PR. Investigating the mechanisms of amylolysis of starch granules by solution-state NMR. Biomacromolecules. 16: 1614-21. PMID 25815624 DOI: 10.1021/Acs.Biomac.5B00190 |
0.32 |
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2015 |
Cohen SI, Arosio P, Presto J, Kurudenkandy FR, Biverstål H, Dolfe L, Dunning C, Yang X, Frohm B, Vendruscolo M, Johansson J, Dobson CM, Fisahn A, Knowles TP, Linse S. A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers. Nature Structural & Molecular Biology. 22: 207-13. PMID 25686087 DOI: 10.1038/Nsmb.2971 |
0.581 |
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2015 |
Galvagnion C, Buell AK, Meisl G, Michaels TC, Vendruscolo M, Knowles TP, Dobson CM. Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation. Nature Chemical Biology. 11: 229-34. PMID 25643172 DOI: 10.1038/Nchembio.1750 |
0.718 |
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2015 |
Ciryam P, Kundra R, Morimoto RI, Dobson CM, Vendruscolo M. Supersaturation is a major driving force for protein aggregation in neurodegenerative diseases. Trends in Pharmacological Sciences. 36: 72-7. PMID 25636813 DOI: 10.1016/J.Tips.2014.12.004 |
0.589 |
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2015 |
De Simone A, Aprile FA, Dhulesia A, Dobson CM, Vendruscolo M. Structure of a low-population intermediate state in the release of an enzyme product. Elife. 4. PMID 25575179 DOI: 10.7554/Elife.02777 |
0.457 |
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2015 |
Shimanovich U, Efimov I, Mason TO, Flagmeier P, Buell AK, Gedanken A, Linse S, Åkerfeldt KS, Dobson CM, Weitz DA, Knowles TP. Protein microgels from amyloid fibril networks. Acs Nano. 9: 43-51. PMID 25469621 DOI: 10.1021/Nn504869D |
0.66 |
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2015 |
Kent L, Dobson C, de-Genst E, Laman H. Abstract B35: Targeting the N-myc oncoprotein using nanobody technology Molecular Cancer Research. 13. DOI: 10.1158/1557-3125.Myc15-B35 |
0.3 |
|
2015 |
Knowles TPJ, Vendruscolo M, Dobson CM. The physical basis of protein misfolding disorders Physics Today. 68: 36-41. DOI: 10.1063/Pt.3.2719 |
0.49 |
|
2014 |
Labrador-Garrido A, Cejudo-Guillén M, Klippstein R, De Genst EJ, Tomas-Gallardo L, Leal MM, Villadiego J, Toledo-Aral JJ, Dobson CM, Pozo D, Roodveldt C. Chaperoned amyloid proteins for immune manipulation: α-Synuclein/Hsp70 shifts immunity toward a modulatory phenotype. Immunity, Inflammation and Disease. 2: 226-38. PMID 25866630 DOI: 10.1002/Iid3.39 |
0.318 |
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2014 |
Levin A, Mason TO, Adler-Abramovich L, Buell AK, Meisl G, Galvagnion C, Bram Y, Stratford SA, Dobson CM, Knowles TP, Gazit E. Ostwald's rule of stages governs structural transitions and morphology of dipeptide supramolecular polymers. Nature Communications. 5: 5219. PMID 25391268 DOI: 10.1038/Ncomms6219 |
0.639 |
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2014 |
Allison JR, Rivers RC, Christodoulou JC, Vendruscolo M, Dobson CM. A relationship between the transient structure in the monomeric state and the aggregation propensities of α-synuclein and β-synuclein. Biochemistry. 53: 7170-83. PMID 25389903 DOI: 10.1021/Bi5009326 |
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Ganzinger KA, Narayan P, Qamar SS, Weimann L, Ranasinghe RT, Aguzzi A, Dobson CM, McColl J, St George-Hyslop P, Klenerman D. Single-molecule imaging reveals that small amyloid-β1-42 oligomers interact with the cellular prion protein (PrP(C)). Chembiochem : a European Journal of Chemical Biology. 15: 2515-21. PMID 25294384 DOI: 10.1002/Cbic.201402377 |
0.39 |
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2014 |
Ma?nsson C, Arosio P, Hussein R, Kampinga HH, Hashem RM, Boelens WC, Dobson CM, Knowles TPJ, Linse S, Emanuelsson C. Interaction of the molecular chaperone DNAJB6 with growing amyloid-beta 42 (Aβ42) aggregates leads to sub-stoichiometric inhibition of amyloid formation Journal of Biological Chemistry. 289: 31066-31076. PMID 25217638 DOI: 10.1074/Jbc.M114.595124 |
0.438 |
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2014 |
De Genst E, Messer A, Dobson CM. Antibodies and protein misfolding: From structural research tools to therapeutic strategies. Biochimica Et Biophysica Acta. 1844: 1907-1919. PMID 25194824 DOI: 10.1016/J.Bbapap.2014.08.016 |
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2014 |
Buell AK, Dobson CM, Knowles TPJ. The physical chemistry of the amyloid phenomenon: Thermodynamics and kinetics of fi lamentous protein aggregation Essays in Biochemistry. 56: 11-39. PMID 25131584 DOI: 10.1042/Bse0560011 |
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Mannini B, Mulvihill E, Sgromo C, Cascella R, Khodarahmi R, Ramazzotti M, Dobson CM, Cecchi C, Chiti F. Toxicity of protein oligomers is rationalized by a function combining size and surface hydrophobicity. Acs Chemical Biology. 9: 2309-17. PMID 25079908 DOI: 10.1021/Cb500505M |
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2014 |
Meisl G, Yang X, Hellstrand E, Frohm B, Kirkegaard JB, Cohen SIA, Dobson CM, Linse S, Knowles TPJ. Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides Proceedings of the National Academy of Sciences of the United States of America. 111: 9384-9389. PMID 24938782 DOI: 10.1073/Pnas.1401564111 |
0.415 |
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2014 |
Fusco G, De Simone A, Gopinath T, Vostrikov V, Vendruscolo M, Dobson CM, Veglia G. Direct observation of the three regions in α-synuclein that determine its membrane-bound behaviour. Nature Communications. 5: 3827. PMID 24871041 DOI: 10.1038/Ncomms4827 |
0.508 |
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2014 |
Esbjörner EK, Chan F, Rees E, Erdelyi M, Luheshi LM, Bertoncini CW, Kaminski CF, Dobson CM, Kaminski Schierle GS. Direct observations of amyloid β self-assembly in live cells provide insights into differences in the kinetics of Aβ(1-40) and Aβ(1-42) aggregation. Chemistry & Biology. 21: 732-42. PMID 24856820 DOI: 10.1016/J.Chembiol.2014.03.014 |
0.407 |
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2014 |
Knowles TP, Vendruscolo M, Dobson CM. The amyloid state and its association with protein misfolding diseases. Nature Reviews. Molecular Cell Biology. 15: 384-96. PMID 24854788 DOI: 10.1038/Nrm3810 |
0.586 |
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2014 |
Buell AK, Galvagnion C, Gaspar R, Sparr E, Vendruscolo M, Knowles TP, Linse S, Dobson CM. Solution conditions determine the relative importance of nucleation and growth processes in α-synuclein aggregation. Proceedings of the National Academy of Sciences of the United States of America. 111: 7671-6. PMID 24817693 DOI: 10.1073/Pnas.1315346111 |
0.729 |
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2014 |
Wyatt AR, Kumita JR, Mifsud RW, Gooden CA, Wilson MR, Dobson CM. Hypochlorite-induced structural modifications enhance the chaperone activity of human ?2-macroglobulin Proceedings of the National Academy of Sciences of the United States of America. 111: E2081-E2090. PMID 24799681 DOI: 10.1073/Pnas.1403379111 |
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O'Brien EP, Ciryam P, Vendruscolo M, Dobson CM. Understanding the influence of codon translation rates on cotranslational protein folding. Accounts of Chemical Research. 47: 1536-44. PMID 24784899 DOI: 10.1021/Ar5000117 |
0.551 |
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2014 |
Garcia GA, Cohen SIA, Dobson CM, Knowles TPJ. Nucleation-conversion-polymerization reactions of biological macromolecules with prenucleation clusters Physical Review E - Statistical, Nonlinear, and Soft Matter Physics. 89. PMID 24730879 DOI: 10.1103/Physreve.89.032712 |
0.306 |
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2014 |
Wacker J, Rönicke R, Westermann M, Wulff M, Reymann KG, Dobson CM, Horn U, Crowther DC, Luheshi LM, Fändrich M. Oligomer-targeting with a conformational antibody fragment promotes toxicity in Aβ-expressing flies. Acta Neuropathologica Communications. 2: 43. PMID 24725347 DOI: 10.1186/2051-5960-2-43 |
0.391 |
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2014 |
Narayan P, Holmström KM, Kim DH, Whitcomb DJ, Wilson MR, St George-Hyslop P, Wood NW, Dobson CM, Cho K, Abramov AY, Klenerman D. Rare individual amyloid-β oligomers act on astrocytes to initiate neuronal damage. Biochemistry. 53: 2442-53. PMID 24717093 DOI: 10.1021/Bi401606F |
0.349 |
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2014 |
Cohen SI, Rajah L, Yoon CH, Buell AK, White DA, Sperling RA, Vendruscolo M, Terentjev EM, Dobson CM, Weitz DA, Knowles TP. Spatial propagation of protein polymerization. Physical Review Letters. 112: 098101. PMID 24655282 DOI: 10.1103/Physrevlett.112.098101 |
0.701 |
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2014 |
Arosio P, Vendruscolo M, Dobson CM, Knowles TP. Chemical kinetics for drug discovery to combat protein aggregation diseases. Trends in Pharmacological Sciences. 35: 127-35. PMID 24560688 DOI: 10.1016/J.Tips.2013.12.005 |
0.591 |
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2014 |
Tóth G, Gardai SJ, Zago W, Bertoncini CW, Cremades N, Roy SL, Tambe MA, Rochet JC, Galvagnion C, Skibinski G, Finkbeiner S, Bova M, Regnstrom K, Chiou SS, Johnston J, ... ... Dobson CM, et al. Targeting the intrinsically disordered structural ensemble of α-synuclein by small molecules as a potential therapeutic strategy for Parkinson's disease. Plos One. 9: e87133. PMID 24551051 DOI: 10.1371/Journal.Pone.0087133 |
0.703 |
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2014 |
Lorenzen N, Nielsen SB, Buell AK, Kaspersen JD, Arosio P, Vad BS, Paslawski W, Christiansen G, Valnickova-Hansen Z, Andreasen M, Enghild JJ, Pedersen JS, Dobson CM, Knowles TPJ, Otzen DE. The role of stable α-synuclein oligomers in the molecular events underlying amyloid formation Journal of the American Chemical Society. 136: 3859-3868. PMID 24527756 DOI: 10.1021/Ja411577T |
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Abeln S, Vendruscolo M, Dobson CM, Frenkel D. A simple lattice model that captures protein folding, aggregation and amyloid formation. Plos One. 9: e85185. PMID 24454816 DOI: 10.1371/Journal.Pone.0085185 |
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O'Brien EP, Vendruscolo M, Dobson CM. Kinetic modelling indicates that fast-translating codons can coordinate cotranslational protein folding by avoiding misfolded intermediates. Nature Communications. 5: 2988. PMID 24394622 DOI: 10.1038/Ncomms3988 |
0.538 |
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2014 |
Pinotsi D, Buell AK, Galvagnion C, Dobson CM, Kaminski Schierle GS, Kaminski CF. Direct observation of heterogeneous amyloid fibril growth kinetics via two-color super-resolution microscopy Nano Letters. 14: 339-345. PMID 24303845 DOI: 10.1021/Nl4041093 |
0.686 |
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2014 |
Bolognesi B, Cohen SIA, Aran Terol P, Esbjörner EK, Giorgetti S, Mossuto MF, Natalello A, Brorsson AC, Knowles TPJ, Dobson CM, Luheshi LM. Single point mutations induce a switch in the molecular mechanism of the aggregation of the Alzheimer's disease associated Aβ42 peptide Acs Chemical Biology. 9: 378-382. PMID 24199868 DOI: 10.1021/Cb400616Y |
0.39 |
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2014 |
Simone AD, Aprile FA, Dhulesia A, Dobson CM, Vendruscolo M. Author response: Structure of a low-population intermediate state in the release of an enzyme product Elife. DOI: 10.7554/Elife.02777.016 |
0.428 |
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2014 |
Knowles TPJ, Vendruscolo M, Dobson CM. Erratum: The amyloid state and its association with protein misfolding diseases Nature Reviews Molecular Cell Biology. 15: 496-496. DOI: 10.1038/Nrm3826 |
0.53 |
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2014 |
Ciryam P, Tartaglia GG, Morimoto RI, Dobson CM, O'Brien EP, Vendruscolo M. Proteome Metastability in Health, Aging, and Disease Biophysical Journal. 106: 59a. DOI: 10.1016/J.Bpj.2013.11.405 |
0.583 |
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2014 |
Arosio P, Vendruscolo M, Dobson CM, Knowles TP. Insights into the Inhibition Mechanism of Biomolecular Self-Assembly from Chemical Kinetics Biophysical Journal. 106: 682a. DOI: 10.1016/J.Bpj.2013.11.3776 |
0.583 |
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2014 |
Ng JS, Barros TP, Esbjörner EK, Luheshi LM, Kumita JR, Dobson CM. Studying Distribution and Aggregation of TDP-43 in Mammalian Cells: A Comparison between Fluorescent Protein and Tetracysteine Labelling Strategies Biophysical Journal. 106: 458a. DOI: 10.1016/J.Bpj.2013.11.2599 |
0.429 |
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2014 |
Horrocks MH, Lee SF, Gandhi S, Iljina M, Tosatto L, Dobson CM, Klenerman D. Single-Molecule Characterisation of Alpha-Synuclein Oligomers Biophysical Journal. 106: 268a. DOI: 10.1016/J.Bpj.2013.11.1573 |
0.398 |
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2014 |
Aprile FA, Meisl G, Buell AK, Flagmeier P, Dobson CM, Vendruscolo M, Knowles TP. Determination of Primary Nucleation Mechanisms of α-Synuclein Amyloid Aggregation Biophysical Journal. 106: 268a. DOI: 10.1016/J.Bpj.2013.11.1570 |
0.74 |
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2014 |
Fusco G, Dobson CM. Probing the Interaction Between α-Synuclein and Lipid Membranes by NMR Spectroscopy Biophysical Journal. 106. DOI: 10.1016/J.Bpj.2013.11.1567 |
0.355 |
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2014 |
El Turk F, Tomba G, De Genst E, Guillams T, Kukic P, Vendruscolo M, Dobson C. Elucidating the Structural Basis of α-Synuclein Fibrillation using Small Camelid Nanobodies Biophysical Journal. 106: 257a. DOI: 10.1016/J.Bpj.2013.11.1512 |
0.6 |
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2013 |
Volpatti LR, Vendruscolo M, Dobson CM, Knowles TP. A clear view of polymorphism, twist, and chirality in amyloid fibril formation. Acs Nano. 7: 10443-8. PMID 24359171 DOI: 10.1021/Nn406121W |
0.549 |
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2013 |
Debelouchina GT, Bayro MJ, Fitzpatrick AW, Ladizhansky V, Colvin MT, Caporini MA, Jaroniec CP, Bajaj VS, Rosay M, Macphee CE, Vendruscolo M, Maas WE, Dobson CM, Griffin RG. Higher order amyloid fibril structure by MAS NMR and DNP spectroscopy. Journal of the American Chemical Society. 135: 19237-47. PMID 24304221 DOI: 10.1021/Ja409050A |
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Ciryam P, Tartaglia GG, Morimoto RI, Dobson CM, Vendruscolo M. Widespread aggregation and neurodegenerative diseases are associated with supersaturated proteins. Cell Reports. 5: 781-90. PMID 24183671 DOI: 10.1016/J.Celrep.2013.09.043 |
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2013 |
Waudby CA, Camilloni C, Fitzpatrick AW, Cabrita LD, Dobson CM, Vendruscolo M, Christodoulou J. In-cell NMR characterization of the secondary structure populations of a disordered conformation of α-synuclein within E. coli cells. Plos One. 8: e72286. PMID 23991082 DOI: 10.1371/Journal.Pone.0072286 |
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2013 |
De Simone A, Montalvao RW, Dobson CM, Vendruscolo M. Characterization of the interdomain motions in hen lysozyme using residual dipolar couplings as replica-averaged structural restraints in molecular dynamics simulations. Biochemistry. 52: 6480-6. PMID 23941501 DOI: 10.1021/Bi4007513 |
0.528 |
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2013 |
De Genst E, Chan PH, Pardon E, Hsu ST, Kumita JR, Christodoulou J, Menzer L, Chirgadze DY, Robinson CV, Muyldermans S, Matagne A, Wyns L, Dobson CM, Dumoulin M. A nanobody binding to non-amyloidogenic regions of the protein human lysozyme enhances partial unfolding but inhibits amyloid fibril formation. The Journal of Physical Chemistry. B. 117: 13245-58. PMID 23919586 DOI: 10.1021/Jp403425Z |
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2013 |
Zhu M, De Simone A, Schenk D, Toth G, Dobson CM, Vendruscolo M. Identification of small-molecule binding pockets in the soluble monomeric form of the Aβ42 peptide. The Journal of Chemical Physics. 139: 035101. PMID 23883055 DOI: 10.1063/1.4811831 |
0.55 |
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2013 |
Aprile FA, Dhulesia A, Stengel F, Roodveldt C, Benesch JL, Tortora P, Robinson CV, Salvatella X, Dobson CM, Cremades N. Hsp70 oligomerization is mediated by an interaction between the interdomain linker and the substrate-binding domain. Plos One. 8: e67961. PMID 23840795 DOI: 10.1371/Journal.Pone.0067961 |
0.503 |
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2013 |
Ouberai MM, Wang J, Swann MJ, Galvagnion C, Guilliams T, Dobson CM, Welland ME. α-Synuclein senses lipid packing defects and induces lateral expansion of lipids leading to membrane remodeling Journal of Biological Chemistry. 288: 20883-20895. PMID 23740253 DOI: 10.1074/Jbc.M113.478297 |
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Cohen SI, Linse S, Luheshi LM, Hellstrand E, White DA, Rajah L, Otzen DE, Vendruscolo M, Dobson CM, Knowles TP. Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism. Proceedings of the National Academy of Sciences of the United States of America. 110: 9758-63. PMID 23703910 DOI: 10.1073/Pnas.1218402110 |
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Pinotsi D, Buell AK, Dobson CM, Kaminski Schierle GS, Kaminski CF. A Label-Free, Quantitative Assay of Amyloid Fibril Growth Based on Intrinsic Fluorescence Chembiochem. 14: 846-850. PMID 23592254 DOI: 10.1002/Cbic.201300103 |
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Guilliams T, El-Turk F, Buell AK, O'Day EM, Aprile FA, Esbjörner EK, Vendruscolo M, Cremades N, Pardon E, Wyns L, Welland ME, Steyaert J, Christodoulou J, Dobson CM, De Genst E. Nanobodies raised against monomeric α-synuclein distinguish between fibrils at different maturation stages. Journal of Molecular Biology. 425: 2397-411. PMID 23557833 DOI: 10.1016/J.Jmb.2013.01.040 |
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Xu LQ, Wu S, Buell AK, Cohen SI, Chen LJ, Hu WH, Cusack SA, Itzhaki LS, Zhang H, Knowles TP, Dobson CM, Welland ME, Jones GW, Perrett S. Influence of specific HSP70 domains on fibril formation of the yeast prion protein Ure2. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 368: 20110410. PMID 23530260 DOI: 10.1098/Rstb.2011.0410 |
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Fitzpatrick AW, Debelouchina GT, Bayro MJ, Clare DK, Caporini MA, Bajaj VS, Jaroniec CP, Wang L, Ladizhansky V, Müller SA, MacPhee CE, Waudby CA, Mott HR, De Simone A, Knowles TP, ... ... Dobson CM, et al. Atomic structure and hierarchical assembly of a cross-β amyloid fibril. Proceedings of the National Academy of Sciences of the United States of America. 110: 5468-73. PMID 23513222 DOI: 10.1073/Pnas.1219476110 |
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Vendruscolo M, Dobson CM. Structural biology: Protein self-assembly intermediates. Nature Chemical Biology. 9: 216-7. PMID 23508184 DOI: 10.1038/Nchembio.1210 |
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Buell AK, Hung P, Salvatella X, Welland ME, Dobson CM, Knowles TPJ. Electrostatic effects in filamentous protein aggregation Biophysical Journal. 104: 1116-1126. PMID 23473495 DOI: 10.1016/J.Bpj.2013.01.031 |
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Chan FTS, Kaminski Schierle GS, Kumita JR, Bertoncini CW, Dobson CM, Kaminski CF. Protein amyloids develop an intrinsic fluorescence signature during aggregation Analyst. 138: 2156-2162. PMID 23420088 DOI: 10.1039/C3An36798C |
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Wyatt AR, Const P, Ecroyd H, Dobson CM, Wilson MR, Kumita JR, Yerbury JJ. Protease-activated alpha-2-macroglobulin can inhibit amyloid formation via two distinct mechanisms Febs Letters. 587: 398-403. PMID 23353684 DOI: 10.1016/J.Febslet.2013.01.020 |
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Narayan P, Ganzinger KA, McColl J, Weimann L, Meehan S, Qamar S, Carver JA, Wilson MR, St George-Hyslop P, Dobson CM, Klenerman D. Single molecule characterization of the interactions between amyloid-β peptides and the membranes of hippocampal cells. Journal of the American Chemical Society. 135: 1491-8. PMID 23339742 DOI: 10.1021/Ja3103567 |
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Ciryam P, Morimoto RI, Vendruscolo M, Dobson CM, O'Brien EP. In vivo translation rates can substantially delay the cotranslational folding of the Escherichia coli cytosolic proteome. Proceedings of the National Academy of Sciences of the United States of America. 110: E132-40. PMID 23256155 DOI: 10.1073/Pnas.1213624110 |
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Fitzpatrick A, Debelouchina G, Bayro M, Clare D, Caporini M, Bajaj V, Jaroniec C, Wang L, Ladizhansky V, Muller S, Macphee C, Waudby C, Mott H, simone AD, Knowles T, ... ... Dobson C, et al. Atomic-Resolution Structure Of A Cross-Beta Quadruplet Amyloid Fibril Determined By Solid-State Magic Angle Spinning Nmr And Cryo-Em Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr19157 |
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Fitzpatrick A, Debelouchina G, Bayro M, Clare D, Caporini M, Bajaj V, Jaroniec C, Wang L, Ladizhansky V, Muller S, MacPhee C, Waudby C, Mott H, Simone Ad, Knowles T, ... ... Dobson C, et al. Atomic-resolution structure of a doublet cross-beta amyloid fibril Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr19058 |
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O'Brien EP, Vendruscolo M, Dobson CM. Erratum: Prediction of variable translation rate effects on cotranslational protein folding Nature Communications. 4. DOI: 10.1038/Ncomms2559 |
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Cohen SIA, Vendruscolo M, Dobson CM, Knowles TPJ. The Kinetics and Mechanisms of Amyloid Formation Amyloid Fibrils and Prefibrillar Aggregates: Molecular and Biological Properties. 183-209. DOI: 10.1002/9783527654185.ch10 |
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2012 |
Ahn M, de Genst E, Kaminski Schierle GS, Erdelyi M, Kaminski CF, Dobson CM, Kumita JR. Analysis of the Native Structure, Stability and Aggregation of Biotinylated Human Lysozyme Plos One. 7. PMID 23166837 DOI: 10.1371/Journal.Pone.0050192 |
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Narayan P, Meehan S, Carver JA, Wilson MR, Dobson CM, Klenerman D. Amyloid-β oligomers are sequestered by both intracellular and extracellular chaperones Biochemistry. 51: 9270-9276. PMID 23106396 DOI: 10.1021/Bi301277K |
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Knowles TP, De Simone A, Fitzpatrick AW, Baldwin A, Meehan S, Rajah L, Vendruscolo M, Welland ME, Dobson CM, Terentjev EM. Twisting transition between crystalline and fibrillar phases of aggregated peptides. Physical Review Letters. 109: 158101. PMID 23102370 DOI: 10.1103/Physrevlett.109.158101 |
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Roodveldt C, Andersson A, De Genst EJ, Labrador-Garrido A, Buell AK, Dobson CM, Tartaglia GG, Vendruscolo M. A rationally designed six-residue swap generates comparability in the aggregation behavior of α-synuclein and β-synuclein. Biochemistry. 51: 8771-8. PMID 23003198 DOI: 10.1021/Bi300558Q |
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De Genst E, Dobson CM. Nanobodies as structural probes of protein misfolding and fibril formation. Methods in Molecular Biology (Clifton, N.J.). 911: 533-558. PMID 22886275 DOI: 10.1007/978-1-61779-968-6_34 |
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2012 |
Lorenzen N, Cohen SIA, Nielsen SB, Herling TW, Christiansen G, Dobson CM, Knowles TPJ, Otzen D. Role of elongation and secondary pathways in S6 amyloid fibril growth Biophysical Journal. 102: 2167-2175. PMID 22824281 DOI: 10.1016/J.Bpj.2012.03.047 |
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2012 |
Mannini B, Cascella R, Zampagni M, Van Waarde-Verhagen M, Meehan S, Roodveldt C, Campioni S, Boninsegna M, Penco A, Relini A, Kampinga HH, Dobson CM, Wilson MR, Cecchi C, Chiti F. Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers Proceedings of the National Academy of Sciences of the United States of America. 109: 12479-12484. PMID 22802614 DOI: 10.1073/Pnas.1117799109 |
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Bemporad F, De Simone A, Chiti F, Dobson CM. Characterizing intermolecular interactions that initiate native-like protein aggregation. Biophysical Journal. 102: 2595-604. PMID 22713575 DOI: 10.1016/J.Bpj.2012.03.057 |
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Waudby CA, Mantle MD, Cabrita LD, Gladden LF, Dobson CM, Christodoulou J. Rapid distinction of intracellular and extracellular proteins using NMR diffusion measurements Journal of the American Chemical Society. 134: 11312-11315. PMID 22694283 DOI: 10.1021/Ja304912C |
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O'Brien EP, Christodoulou J, Vendruscolo M, Dobson CM. Trigger factor slows co-translational folding through kinetic trapping while sterically protecting the nascent chain from aberrant cytosolic interactions. Journal of the American Chemical Society. 134: 10920-32. PMID 22680285 DOI: 10.1021/Ja302305U |
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O'Brien EP, Vendruscolo M, Dobson CM. Prediction of variable translation rate effects on cotranslational protein folding. Nature Communications. 3: 868. PMID 22643895 DOI: 10.1038/Ncomms1850 |
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Cremades N, Cohen SI, Deas E, Abramov AY, Chen AY, Orte A, Sandal M, Clarke RW, Dunne P, Aprile FA, Bertoncini CW, Wood NW, Knowles TP, Dobson CM, Klenerman D. Direct observation of the interconversion of normal and toxic forms of α-synuclein. Cell. 149: 1048-59. PMID 22632969 DOI: 10.1016/J.Cell.2012.03.037 |
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McGuire EK, Motskin M, Bolognesi B, Bergin SD, Knowles TPJ, Skepper J, Luheshi LM, McComb DW, Dobson CM, Porter AE. Selenium-enhanced electron microscopic imaging of different aggregate forms of a segment of the amyloid β peptide in cells Acs Nano. 6: 4740-4747. PMID 22631869 DOI: 10.1021/Nn204859E |
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Buell AK, Dobson CM, Welland ME. Measuring the kinetics of amyloid fibril elongation using quartz crystal microbalances Methods in Molecular Biology. 849: 101-119. PMID 22528086 DOI: 10.1007/978-1-61779-551-0_8 |
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De Simone A, Kitchen C, Kwan AH, Sunde M, Dobson CM, Frenkel D. Intrinsic disorder modulates protein self-assembly and aggregation. Proceedings of the National Academy of Sciences of the United States of America. 109: 6951-6. PMID 22509003 DOI: 10.1073/Pnas.1118048109 |
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Buell AK, Dhulesia A, White DA, Knowles TP, Dobson CM, Welland ME. Detailed analysis of the energy barriers for amyloid fibril growth. Angewandte Chemie (International Ed. in English). 51: 5247-51. PMID 22489083 DOI: 10.1002/Anie.201108040 |
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Speretta E, Jahn TR, Tartaglia GG, Favrin G, Barros TP, Imarisio S, Lomas DA, Luheshi LM, Crowther DC, Dobson CM. Expression in drosophila of tandem amyloid β peptides provides insights into links between aggregation and neurotoxicity. The Journal of Biological Chemistry. 287: 20748-54. PMID 22461632 DOI: 10.1074/Jbc.M112.350124 |
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Cohen SI, Vendruscolo M, Dobson CM, Knowles TP. From macroscopic measurements to microscopic mechanisms of protein aggregation. Journal of Molecular Biology. 421: 160-71. PMID 22406275 DOI: 10.1016/J.Jmb.2012.02.031 |
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2012 |
Gregory JM, Barros TP, Meehan S, Dobson CM, Luheshi LM. The aggregation and neurotoxicity of TDP-43 and its ALS-associated 25 kDa fragment are differentially affected by molecular chaperones in Drosophila. Plos One. 7: e31899. PMID 22384095 DOI: 10.1371/Journal.Pone.0031899 |
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Evangelisti E, Cecchi C, Cascella R, Sgromo C, Becatti M, Dobson CM, Chiti F, Stefani M. Membrane lipid composition and its physicochemical properties define cell vulnerability to aberrant protein oligomers Journal of Cell Science. 125: 2416-2427. PMID 22344258 DOI: 10.1242/Jcs.098434 |
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Narayan P, Orte A, Clarke RW, Bolognesi B, Hook S, Ganzinger KA, Meehan S, Wilson MR, Dobson CM, Klenerman D. The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β 1-40 peptide Nature Structural and Molecular Biology. 19: 79-84. PMID 22179788 DOI: 10.1038/Nsmb.2191 |
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Abelein A, Bolognesi B, Dobson CM, Gräslund A, Lendel C. Hydrophobicity and conformational change as mechanistic determinants for nonspecific modulators of amyloid β self-assembly Biochemistry. 51: 126-137. PMID 22133042 DOI: 10.1021/Bi201745G |
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2012 |
Kumita JR, Helmfors L, Williams J, Luheshi LM, Menzer L, Dumoulin M, Lomas DA, Crowther DC, Dobson CM, Brorsson AC. Disease-related amyloidogenic variants of human lysozyme trigger the unfolded protein response and disturb eye development in Drosophila melanogaster. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 26: 192-202. PMID 21965601 DOI: 10.1096/Fj.11-185983 |
0.358 |
|
2012 |
Fusco G, De Simone A, Hsu ST, Bemporad F, Vendruscolo M, Chiti F, Dobson CM. ¹H, ¹³C and ¹âµN resonance assignments of human muscle acylphosphatase. Biomolecular Nmr Assignments. 6: 27-9. PMID 21643968 DOI: 10.1007/S12104-011-9318-1 |
0.555 |
|
2012 |
Mannini B, Campioni S, Boninsegna M, Penco A, Cascella R, Zampagni M, Wilson MR, Meehan S, Roodveldt C, Dobson CM, Relini A, Cecchi C, Chiti F. Chaperones suppress the toxicity of aberrant protein aggregates. Molecular insight into the mechanism of action Febs Journal. 279: 224. DOI: 10.1111/J.1742-4658.2010.08705.X |
0.399 |
|
2012 |
Knowles TPJ, De Simone A, Fitzpatrick AW, Baldwin A, Meehan S, Rajah L, Vendruscolo M, Welland ME, Dobson CM, Terentjev EM. Twisting transition between crystalline and fibrillar phases of aggregated peptides Physical Review Letters. 109. DOI: 10.1103/PhysRevLett.109.158101 |
0.584 |
|
2012 |
Abelein A, Bolognesi B, Dobson CM, Gräslund A, Lendel C. Mechanism of Non-Specific Inhibitors of Amyloid Assembly: Interactions of Lacmoid with the Amyloid Beta Peptide Biophysical Journal. 102: 441a. DOI: 10.1016/J.Bpj.2011.11.2417 |
0.426 |
|
2012 |
Horrocks MH, Cremades N, Tosatto L, Guilliams T, De Genst E, Shim J, Dobson CM, Klenerman D. Investigating the Factors Affecting the Aggregation of Alpha-Synuclein using Single Molecule Fluorescence and Fast Flow Microfluidics Biophysical Journal. 102: 255a. DOI: 10.1016/J.Bpj.2011.11.1407 |
0.348 |
|
2012 |
Buell AK, Dhulesia A, White DA, Knowles TPJ, Dobson CM, Welland ME. Analyse der Energiebarrieren für das Wachstum von Amyloidfibrillen Angewandte Chemie. 124: 5339-5344. DOI: 10.1002/Ange.201108040 |
0.65 |
|
2011 |
De Simone A, Dhulesia A, Soldi G, Vendruscolo M, Hsu ST, Chiti F, Dobson CM. Experimental free energy surfaces reveal the mechanisms of maintenance of protein solubility. Proceedings of the National Academy of Sciences of the United States of America. 108: 21057-62. PMID 22160682 DOI: 10.1073/Pnas.1112197108 |
0.58 |
|
2011 |
Fitzpatrick AW, Knowles TP, Waudby CA, Vendruscolo M, Dobson CM. Inversion of the balance between hydrophobic and hydrogen bonding interactions in protein folding and aggregation. Plos Computational Biology. 7: e1002169. PMID 22022239 DOI: 10.1371/Journal.Pcbi.1002169 |
0.573 |
|
2011 |
Cohen SI, Vendruscolo M, Dobson CM, Knowles TP. Nucleated polymerisation in the presence of pre-formed seed filaments. International Journal of Molecular Sciences. 12: 5844-52. PMID 22016630 DOI: 10.3390/Ijms12095844 |
0.448 |
|
2011 |
Buell AK, Esbjörner EK, Riss PJ, White DA, Aigbirhio FI, Toth G, Welland ME, Dobson CM, Knowles TP. Probing small molecule binding to amyloid fibrils. Physical Chemistry Chemical Physics : Pccp. 13: 20044-52. PMID 22006124 DOI: 10.1039/C1Cp22283J |
0.742 |
|
2011 |
Shammas SL, Waudby CA, Wang S, Buell AK, Knowles TP, Ecroyd H, Welland ME, Carver JA, Dobson CM, Meehan S. Binding of the molecular chaperone αB-crystallin to Aβ amyloid fibrils inhibits fibril elongation. Biophysical Journal. 101: 1681-9. PMID 21961594 DOI: 10.1016/J.Bpj.2011.07.056 |
0.749 |
|
2011 |
Knowles TP, White DA, Abate AR, Agresti JJ, Cohen SI, Sperling RA, De Genst EJ, Dobson CM, Weitz DA. Observation of spatial propagation of amyloid assembly from single nuclei. Proceedings of the National Academy of Sciences of the United States of America. 108: 14746-51. PMID 21876182 DOI: 10.1073/Pnas.1105555108 |
0.405 |
|
2011 |
Cohen SI, Vendruscolo M, Dobson CM, Knowles TP. Nucleated polymerization with secondary pathways. III. Equilibrium behavior and oligomer populations. The Journal of Chemical Physics. 135: 065107. PMID 21842956 DOI: 10.1063/1.3608918 |
0.506 |
|
2011 |
Cohen SI, Vendruscolo M, Dobson CM, Knowles TP. Nucleated polymerization with secondary pathways. II. Determination of self-consistent solutions to growth processes described by non-linear master equations. The Journal of Chemical Physics. 135: 065106. PMID 21842955 DOI: 10.1063/1.3608917 |
0.461 |
|
2011 |
Cohen SI, Vendruscolo M, Welland ME, Dobson CM, Terentjev EM, Knowles TP. Nucleated polymerization with secondary pathways. I. Time evolution of the principal moments. The Journal of Chemical Physics. 135: 065105. PMID 21842954 DOI: 10.1063/1.3608916 |
0.642 |
|
2011 |
Vendruscolo M, Knowles TP, Dobson CM. Protein solubility and protein homeostasis: a generic view of protein misfolding disorders. Cold Spring Harbor Perspectives in Biology. 3. PMID 21825020 DOI: 10.1101/Cshperspect.A010454 |
0.59 |
|
2011 |
Whyteside G, Alcocer MJ, Kumita JR, Dobson CM, Lazarou M, Pleass RJ, Archer DB. Native-state stability determines the extent of degradation relative to secretion of protein variants from Pichia pastoris. Plos One. 6: e22692. PMID 21818368 DOI: 10.1371/Journal.Pone.0022692 |
0.368 |
|
2011 |
Kaminski Schierle GS, Van De Linde S, Erdelyi M, Esbjörner EK, Klein T, Rees E, Bertoncini CW, Dobson CM, Sauer M, Kaminski CF. In situ measurements of the formation and morphology of intracellular β-amyloid fibrils by super-resolution fluorescence imaging Journal of the American Chemical Society. 133: 12902-12905. PMID 21793568 DOI: 10.1021/Ja201651W |
0.427 |
|
2011 |
Bayro MJ, Debelouchina GT, Eddy MT, Birkett NR, MacPhee CE, Rosay M, Maas WE, Dobson CM, Griffin RG. Intermolecular structure determination of amyloid fibrils with magic-angle spinning and dynamic nuclear polarization NMR. Journal of the American Chemical Society. 133: 13967-74. PMID 21774549 DOI: 10.1021/Ja203756X |
0.51 |
|
2011 |
Knowles TPJ, Devlin GL, Dobson CM, Welland ME. Probing protein aggregation with quartz crystal microbalances Methods in Molecular Biology. 752: 137-145. PMID 21713635 DOI: 10.1007/978-1-60327-223-0_9 |
0.609 |
|
2011 |
Cabrita LD, Waudby CA, Dobson CM, Christodoulou J. Solution-state nuclear magnetic resonance spectroscopy and protein folding Methods in Molecular Biology. 752: 97-120. PMID 21713633 DOI: 10.1007/978-1-60327-223-0_7 |
0.425 |
|
2011 |
Kohlhoff KJ, Jahn TR, Lomas DA, Dobson CM, Crowther DC, Vendruscolo M. The iFly tracking system for an automated locomotor and behavioural analysis of Drosophila melanogaster. Integrative Biology : Quantitative Biosciences From Nano to Macro. 3: 755-60. PMID 21698336 DOI: 10.1039/C0Ib00149J |
0.766 |
|
2011 |
Levitan K, Chereau D, Cohen SIA, Knowles TPJ, Dobson CM, Fink AL, Anderson JP, Goldstein JM, Millhauser GL. Conserved C-terminal charge exerts a profound influence on the aggregation rate of α-synuclein Journal of Molecular Biology. 411: 329-333. PMID 21689664 DOI: 10.1016/J.Jmb.2011.05.046 |
0.362 |
|
2011 |
Mossuto MF, Bolognesi B, Guixer B, Dhulesia A, Agostini F, Kumita JR, Tartaglia GG, Dumoulin M, Dobson CM, Salvatella X. Disulfide bonds reduce the toxicity of the amyloid fibrils formed by an extracellular protein. Angewandte Chemie (International Ed. in English). 50: 7048-51. PMID 21671315 DOI: 10.1002/Anie.201100986 |
0.475 |
|
2011 |
Baldwin AJ, Knowles TP, Tartaglia GG, Fitzpatrick AW, Devlin GL, Shammas SL, Waudby CA, Mossuto MF, Meehan S, Gras SL, Christodoulou J, Anthony-Cahill SJ, Barker PD, Vendruscolo M, Dobson CM. Metastability of native proteins and the phenomenon of amyloid formation. Journal of the American Chemical Society. 133: 14160-3. PMID 21650202 DOI: 10.1021/Ja2017703 |
0.597 |
|
2011 |
Shammas SL, Knowles TPJ, Baldwin AJ, MacPhee CE, Welland ME, Dobson CM, Devlin GL. Perturbation of the stability of amyloid fibrils through alteration of electrostatic interactions Biophysical Journal. 100: 2783-2791. PMID 21641324 DOI: 10.1016/J.Bpj.2011.04.039 |
0.613 |
|
2011 |
Buell AK, Dhulesia A, Mossuto MF, Cremades N, Kumita JR, Dumoulin M, Welland ME, Knowles TP, Salvatella X, Dobson CM. Population of nonnative states of lysozyme variants drives amyloid fibril formation. Journal of the American Chemical Society. 133: 7737-43. PMID 21528861 DOI: 10.1021/Ja109620D |
0.753 |
|
2011 |
Wyatt AR, Yerbury JJ, Berghofer P, Greguric I, Katsifis A, Dobson CM, Wilson MR. Clusterin facilitates in vivo clearance of extracellular misfolded proteins Cellular and Molecular Life Sciences. 68: 3919-3931. PMID 21505792 DOI: 10.1007/s00018-011-0684-8) |
0.374 |
|
2011 |
Kamatari YO, Smith LJ, Dobson CM, Akasaka K. Cavity hydration as a gateway to unfolding: An NMR study of hen lysozyme at high pressure and low temperature Biophysical Chemistry. 156: 24-30. PMID 21367514 DOI: 10.1016/J.Bpc.2011.01.009 |
0.34 |
|
2011 |
Jahn TR, Kohlhoff KJ, Scott M, Tartaglia GG, Lomas DA, Dobson CM, Vendruscolo M, Crowther DC. Detection of early locomotor abnormalities in a Drosophila model of Alzheimer's disease. Journal of Neuroscience Methods. 197: 186-9. PMID 21315762 DOI: 10.1016/J.Jneumeth.2011.01.026 |
0.77 |
|
2011 |
Kaminski Schierle GS, Bertoncini CW, Chan FT, van der Goot AT, Schwedler S, Skepper J, Schlachter S, van Ham T, Esposito A, Kumita JR, Nollen EA, Dobson CM, Kaminski CF. A FRET sensor for non-invasive imaging of amyloid formation in vivo. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. 12: 673-80. PMID 21308945 DOI: 10.1002/Cphc.201000996 |
0.43 |
|
2011 |
Raimondi S, Guglielmi F, Giorgetti S, Di Gaetano S, Arciello A, Monti DM, Relini A, Nichino D, Doglia SM, Natalello A, Pucci P, Mangione P, Obici L, Merlini G, Stoppini M, ... Dobson CM, et al. Effects of the known pathogenic mutations on the aggregation pathway of the amyloidogenic peptide of apolipoprotein A-I. Journal of Molecular Biology. 407: 465-76. PMID 21296086 DOI: 10.1016/J.Jmb.2011.01.044 |
0.568 |
|
2011 |
Vendruscolo M, Dobson CM. Protein dynamics: Moore's law in molecular biology. Current Biology : Cb. 21: R68-70. PMID 21256436 DOI: 10.1016/J.Cub.2010.11.062 |
0.495 |
|
2011 |
Wang YQ, Buell AK, Wang XY, Welland ME, Dobson CM, Knowles TPJ, Perrett S. Relationship between prion propensity and the rates of individual molecular steps of fibril assembly Journal of Biological Chemistry. 286: 12101-12107. PMID 21233211 DOI: 10.1074/Jbc.M110.208934 |
0.764 |
|
2011 |
O'Brien EP, Christodoulou J, Vendruscolo M, Dobson CM. New scenarios of protein folding can occur on the ribosome Journal of the American Chemical Society. 133: 513-526. PMID 21204555 DOI: 10.1021/Ja107863Z |
0.55 |
|
2011 |
O'Brien EP, Christodoulou J, Dobson C, Vendruscolo M. On the Effect of the Ribosome and Trigger Factor on Nascent Chain Protein Folding Biophysical Journal. 100: 17a. DOI: 10.1016/J.Bpj.2010.12.304 |
0.548 |
|
2010 |
Buell AK, Dobson CM, Knowles TPJ, Welland ME. Interactions between Amyloidophilic dyes and their relevance to studies of amyloid inhibitors Biophysical Journal. 99: 3492-3497. PMID 21081099 DOI: 10.1016/J.Bpj.2010.08.074 |
0.745 |
|
2010 |
O'Brien EP, Hsu STD, Christodoulou J, Vendruscolo M, Dobson CM. Transient tertiary structure formation within the ribosome exit port Journal of the American Chemical Society. 132: 16928-16937. PMID 21062068 DOI: 10.1021/Ja106530Y |
0.532 |
|
2010 |
Roodveldt C, Labrador-Garrido A, Gonzalez-Rey E, Fernandez-Montesinos R, Caro M, Lachaud CC, Waudby CA, Delgado M, Dobson CM, Pozo D. Glial innate immunity generated by non-aggregated alpha-synuclein in mouse: Differences between wild-type and Parkinson's disease-linked mutants Plos One. 5. PMID 21048992 DOI: 10.1371/Journal.Pone.0013481 |
0.343 |
|
2010 |
Dhulesia A, Cremades N, Kumita JR, Hsu ST, Mossuto MF, Dumoulin M, Nietlispach D, Akke M, Salvatella X, Dobson CM. Local cooperativity in an amyloidogenic state of human lysozyme observed at atomic resolution. Journal of the American Chemical Society. 132: 15580-8. PMID 20958028 DOI: 10.1021/Ja103524M |
0.464 |
|
2010 |
Caporini MA, Bajaj VS, Veshtort M, Fitzpatrick A, MacPhee CE, Vendruscolo M, Dobson CM, Griffin RG. Accurate determination of interstrand distances and alignment in amyloid fibrils by magic angle spinning NMR. The Journal of Physical Chemistry. B. 114: 13555-61. PMID 20925357 DOI: 10.1021/Jp106675H |
0.652 |
|
2010 |
Buell AK, Blundell JR, Dobson CM, Welland ME, Terentjev EM, Knowles TP. Frequency factors in a landscape model of filamentous protein aggregation. Physical Review Letters. 104: 228101. PMID 20873942 DOI: 10.1103/Physrevlett.104.228101 |
0.759 |
|
2010 |
Sandberg A, Luheshi LM, Söllvander S, Pereira de Barros T, Macao B, Knowles TP, Biverstål H, Lendel C, Ekholm-Petterson F, Dubnovitsky A, Lannfelt L, Dobson CM, Härd T. Stabilization of neurotoxic Alzheimer amyloid-beta oligomers by protein engineering. Proceedings of the National Academy of Sciences of the United States of America. 107: 15595-600. PMID 20713699 DOI: 10.1073/Pnas.1001740107 |
0.387 |
|
2010 |
Bayro MJ, Maly T, Birkett NR, Macphee CE, Dobson CM, Griffin RG. High-resolution MAS NMR analysis of PI3-SH3 amyloid fibrils: backbone conformation and implications for protofilament assembly and structure . Biochemistry. 49: 7474-84. PMID 20707313 DOI: 10.1021/Bi100864T |
0.607 |
|
2010 |
Buell AK, White DA, Meier C, Welland ME, Knowles TP, Dobson CM. Surface attachment of protein fibrils via covalent modification strategies. The Journal of Physical Chemistry. B. 114: 10925-38. PMID 20695458 DOI: 10.1021/Jp101579N |
0.752 |
|
2010 |
Mossuto MF, Dhulesia A, Devlin G, Frare E, Kumita JR, de Laureto PP, Dumoulin M, Fontana A, Dobson CM, Salvatella X. The non-core regions of human lysozyme amyloid fibrils influence cytotoxicity. Journal of Molecular Biology. 402: 783-96. PMID 20624399 DOI: 10.1016/J.Jmb.2010.07.005 |
0.451 |
|
2010 |
De Genst EJ, Guilliams T, Wellens J, O'Day EM, Waudby CA, Meehan S, Dumoulin M, Hsu ST, Cremades N, Verschueren KH, Pardon E, Wyns L, Steyaert J, Christodoulou J, Dobson CM. Structure and properties of a complex of α-synuclein and a single-domain camelid antibody. Journal of Molecular Biology. 402: 326-43. PMID 20620148 DOI: 10.1016/J.Jmb.2010.07.001 |
0.473 |
|
2010 |
Carulla N, Zhou M, Giralt E, Robinson CV, Dobson CM. Structure and intermolecular dynamics of aggregates populated during amyloid fibril formation studied by hydrogen/deuterium exchange Accounts of Chemical Research. 43: 1072-1079. PMID 20557067 DOI: 10.1021/Ar9002784 |
0.585 |
|
2010 |
Bolognesi B, Kumita JR, Barros TP, Esbjorner EK, Luheshi LM, Crowther DC, Wilson MR, Dobson CM, Favrin G, Yerbury JJ. ANS binding reveals common features of cytotoxic amyloid species. Acs Chemical Biology. 5: 735-40. PMID 20550130 DOI: 10.1021/Cb1001203 |
0.403 |
|
2010 |
Tartaglia GG, Dobson CM, Hartl FU, Vendruscolo M. Physicochemical determinants of chaperone requirements. Journal of Molecular Biology. 400: 579-88. PMID 20416322 DOI: 10.1016/J.Jmb.2010.03.066 |
0.499 |
|
2010 |
Brorsson AC, Bolognesi B, Tartaglia GG, Shammas SL, Favrin G, Watson I, Lomas DA, Chiti F, Vendruscolo M, Dobson CM, Crowther DC, Luheshi LM. Intrinsic determinants of neurotoxic aggregate formation by the amyloid beta peptide. Biophysical Journal. 98: 1677-84. PMID 20409489 DOI: 10.1016/J.Bpj.2009.12.4320 |
0.554 |
|
2010 |
Hagan CL, Johnson RJ, Dhulesia A, Dumoulin M, Dumont J, De Genst E, Christodoulou J, Robinson CV, Dobson CM, Kumita JR. A non-natural variant of human lysozyme (I59T) mimics the in vitro behaviour of the I56T variant that is responsible for a form of familial amyloidosis. Protein Engineering, Design & Selection : Peds. 23: 499-506. PMID 20382744 DOI: 10.1093/Protein/Gzq023 |
0.541 |
|
2010 |
White DA, Buell AK, Knowles TP, Welland ME, Dobson CM. Protein aggregation in crowded environments. Journal of the American Chemical Society. 132: 5170-5. PMID 20334356 DOI: 10.1021/Ja909997E |
0.757 |
|
2010 |
Luheshi LM, Hoyer W, de Barros TP, van Dijk Härd I, Brorsson AC, Macao B, Persson C, Crowther DC, Lomas DA, Ståhl S, Dobson CM, Härd T. Sequestration of the Abeta peptide prevents toxicity and promotes degradation in vivo. Plos Biology. 8: e1000334. PMID 20305716 DOI: 10.1371/Journal.Pbio.1000334 |
0.413 |
|
2010 |
Waudby CA, Knowles TP, Devlin GL, Skepper JN, Ecroyd H, Carver JA, Welland ME, Christodoulou J, Dobson CM, Meehan S. The interaction of alphaB-crystallin with mature alpha-synuclein amyloid fibrils inhibits their elongation. Biophysical Journal. 98: 843-51. PMID 20197038 DOI: 10.1016/J.Bpj.2009.10.056 |
0.622 |
|
2010 |
Cabrita LD, Dobson CM, Christodoulou J. Protein folding on the ribosome Current Opinion in Structural Biology. 20: 33-45. PMID 20149635 DOI: 10.1016/J.Sbi.2010.01.005 |
0.37 |
|
2010 |
Campioni S, Mannini B, Zampagni M, Pensalfini A, Parrini C, Evangelisti E, Relini A, Stefani M, Dobson CM, Cecchi C, Chiti F. A causative link between the structure of aberrant protein oligomers and their toxicity Nature Chemical Biology. 6: 140-147. PMID 20081829 DOI: 10.1038/Nchembio.283 |
0.454 |
|
2010 |
Lendel C, Bolognesi B, Wahlström A, Dobson CM, Gräslund A. Detergent-like interaction of congo red with the amyloid β peptide Biochemistry. 49: 1358-1360. PMID 20070125 DOI: 10.1021/Bi902005T |
0.396 |
|
2010 |
Bodner CR, Maltsev AS, Dobson CM, Bax A. Differential phospholipid binding of alpha-synuclein variants implicated in Parkinson's disease revealed by solution NMR spectroscopy. Biochemistry. 49: 862-71. PMID 20041693 DOI: 10.1021/Bi901723P |
0.304 |
|
2010 |
Brorsson AC, Kumita JR, MacLeod I, Bolognesi B, Speretta E, Luheshi LM, Knowles TP, Dobson CM, Crowther DC. Methods and models in neurodegenerative and systemic protein aggregation diseases. Frontiers in Bioscience (Landmark Edition). 15: 373-96. PMID 20036826 DOI: 10.2741/3626 |
0.303 |
|
2010 |
Hsu STD, Blaser G, Behrens C, Cabrita LD, Dobson CM, Jackson SE. Folding study of venus reveals a strong ion dependence of its yellow fluorescence under mildly acidic conditions Journal of Biological Chemistry. 285: 4859-4869. PMID 19901033 DOI: 10.1074/Jbc.M109.000695 |
0.345 |
|
2010 |
van Ham TJ, Esposito A, Kumita JR, Hsu ST, Kaminski Schierle GS, Kaminski CF, Dobson CM, Nollen EA, Bertoncini CW. Towards multiparametric fluorescent imaging of amyloid formation: studies of a YFP model of alpha-synuclein aggregation. Journal of Molecular Biology. 395: 627-42. PMID 19891973 DOI: 10.1016/J.Jmb.2009.10.066 |
0.434 |
|
2010 |
Dobson CM, Hoch JC, Olejniczak ET, Poulsen FM. Conformations and conformational dynamics of proteins in solution studied by nuclear magnetic double resonance. Biophysical Journal. 32: 625-8. PMID 19431399 DOI: 10.1016/S0006-3495(80)84997-6 |
0.627 |
|
2010 |
White DA, Dobson CM, Welland ME, Knowles TPJ. Quantitative approaches for characterising fibrillar protein nanostructures Materials Research Society Symposium Proceedings. 1274: 33-39. DOI: 10.1557/Proc-1274-Qq04-05 |
0.611 |
|
2010 |
Narayan P, Orte A, Dobson CM, Klenerman D. Detecting and Characterizing Amyloid-β1-40 Oligomers using Single Molecule Fluorescence Biophysical Journal. 98: 651a. DOI: 10.1016/J.Bpj.2009.12.3571 |
0.406 |
|
2010 |
Cabrita LD, Dobson CM, Christodoulou J. Early nascent chain folding events on the ribosome Israel Journal of Chemistry. 50: 99-108. DOI: 10.1002/Ijch.201000015 |
0.332 |
|
2010 |
DOBSON CM, SALI A, KARPLUS M. ChemInform Abstract: Protein Folding: A Perspective from Theory and Experiment Cheminform. 29: no-no. DOI: 10.1002/chin.199826366 |
0.387 |
|
2009 |
Vendruscolo M, Dobson CM. Quantitative approaches to defining normal and aberrant protein homeostasis Faraday Discussions. 143: 277-291. PMID 20334107 DOI: 10.1039/B905825G |
0.533 |
|
2009 |
Allison JR, Varnai P, Dobson CM, Vendruscolo M. Determination of the free energy landscape of alpha-synuclein using spin label nuclear magnetic resonance measurements. Journal of the American Chemical Society. 131: 18314-26. PMID 20028147 DOI: 10.1021/Ja904716H |
0.524 |
|
2009 |
Cabrita LD, Hsu STD, Launay H, Dobson CM, Christodoulou J. Probing ribosome-nascent chain complexes produced in vivo by NMR spectroscopy Proceedings of the National Academy of Sciences of the United States of America. 106: 22239-22244. PMID 20018739 DOI: 10.1073/Pnas.0903750106 |
0.396 |
|
2009 |
Knowles TPJ, Waudby CA, Devlin GL, Cohen SIA, Aguzzi A, Vendruscolo M, Terentjev EM, Welland ME, Dobson CM. An analytical solution to the kinetics of breakable filament assembly Science. 326: 1533-1537. PMID 20007899 DOI: 10.1126/Science.1178250 |
0.671 |
|
2009 |
Poon S, Birkett NR, Fowler SB, Luisi BF, Dobson CM, Zurdo J. Amyloidogenicity and aggregate cytotoxicity of human glucagon-like peptide-1 (hGLP-1) Protein and Peptide Letters. 16: 1548-1556. PMID 20001917 DOI: 10.2174/092986609789839232 |
0.363 |
|
2009 |
Bui JM, Gsponer J, Vendruscolo M, Dobson CM. Analysis of sub-tauc and supra-tauc motions in protein Gbeta1 using molecular dynamics simulations. Biophysical Journal. 97: 2513-20. PMID 19883594 DOI: 10.1016/J.Bpj.2009.07.061 |
0.526 |
|
2009 |
Roodveldt C, Bertoncini CW, Andersson A, Van Der Goot AT, Hsu ST, Fernández-Montesinos R, De Jong J, Van Ham TJ, Nollen EA, Pozo D, Christodoulou J, Dobson CM. Chaperone proteostasis in Parkinson's disease: Stabilization of the Hsp70/α-synuclein complex by Hip Embo Journal. 28: 3758-3770. PMID 19875982 DOI: 10.1038/Emboj.2009.298 |
0.386 |
|
2009 |
Vuchelen A, O'Day E, De Genst E, Pardon E, Wyns L, Dumoulin M, Dobson CM, Christodoulou J, Hsu ST. (1)H, (13)C and (15)N assignments of a camelid nanobody directed against human alpha-synuclein. Biomolecular Nmr Assignments. 3: 231-3. PMID 19763886 DOI: 10.1007/S12104-009-9182-4 |
0.375 |
|
2009 |
Lendel C, Bertoncini CW, Cremades N, Waudby CA, Vendruscolo M, Dobson CM, Schenk D, Christodoulou J, Toth G. On the mechanism of nonspecific inhibitors of protein aggregation: Dissecting the interactions of α-synuclein with congo red and lacmoid Biochemistry. 48: 8322-8334. PMID 19645507 DOI: 10.1021/Bi901285X |
0.586 |
|
2009 |
Hsu STD, Behrens C, Cabrita LD, Dobson CM. 1H, 15N and 13C assignments of yellow fluorescent protein (YFP) Venus Biomolecular Nmr Assignments. 3: 67-72. PMID 19636949 DOI: 10.1007/S12104-009-9143-Y |
0.345 |
|
2009 |
Hsu STD, Cabrita LD, Christodoulou J, Dobson CM. 1H, 15N and 13C assignments of domain 5 of Dictyostelium discoideum gelation factor (ABP-120) in its native and 8M urea-denatured states Biomolecular Nmr Assignments. 3: 29-31. PMID 19636940 DOI: 10.1007/S12104-008-9134-4 |
0.301 |
|
2009 |
Porter AE, Knowles TPJ, Muller K, Meehan S, McGuire E, Skepper J, Welland ME, Dobson CM. Imaging Amyloid Fibrils within Cells Using a Se-Labelling Strategy Journal of Molecular Biology. 392: 868-871. PMID 19635483 DOI: 10.1016/J.Jmb.2009.07.061 |
0.618 |
|
2009 |
Bayro MJ, Maly T, Birkett NR, Dobson CM, Griffin RG. Long-range correlations between aliphatic 13C nuclei in protein MAS NMR spectroscopy. Angewandte Chemie (International Ed. in English). 48: 5708-10. PMID 19562810 DOI: 10.1002/anie.200901520 |
0.502 |
|
2009 |
Luheshi LM, Dobson CM. Bridging the gap: From protein misfolding to protein misfolding diseases Febs Letters. 583: 2581-2586. PMID 19545568 DOI: 10.1016/J.Febslet.2009.06.030 |
0.415 |
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2009 |
White DA, Buell AK, Dobson CM, Welland ME, Knowles TP. Biosensor-based label-free assays of amyloid growth. Febs Letters. 583: 2587-92. PMID 19523953 DOI: 10.1016/J.Febslet.2009.06.008 |
0.727 |
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2009 |
Hsu STD, Cabrita LD, Fucini P, Christodoulou J, Dobson CM. Probing side-chain dynamics of a ribosome-bound nascent chain using methyl NMR spectroscopy Journal of the American Chemical Society. 131: 8366-8367. PMID 19492839 DOI: 10.1021/Ja902778N |
0.325 |
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2009 |
Bodner CR, Dobson CM, Bax A. Multiple tight phospholipid-binding modes of alpha-synuclein revealed by solution NMR spectroscopy. Journal of Molecular Biology. 390: 775-90. PMID 19481095 DOI: 10.1016/J.Jmb.2009.05.066 |
0.304 |
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2009 |
Yanamandra K, Alexeyev O, Zamotin V, Srivastava V, Shchukarev A, Brorsson AC, Tartaglia GG, Vogl T, Kayed R, Wingsle G, Olsson J, Dobson CM, Bergh A, Elgh F, Morozova-Roche LA. Amyloid formation by the pro-inflammatory S100A8/A9 proteins in the ageing prostate. Plos One. 4: e5562. PMID 19440546 DOI: 10.1371/Journal.Pone.0005562 |
0.33 |
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2009 |
Hsu STD, Bertoncini CW, Dobson CM. Use of protonless NMR spectroscopy to alleviate the loss of information resulting from exchange-broadening Journal of the American Chemical Society. 131: 7222-7223. PMID 19432443 DOI: 10.1021/Ja902307Q |
0.345 |
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2009 |
Robustelli P, Cavalli A, Dobson CM, Vendruscolo M, Salvatella X. Folding of small proteins by Monte Carlo simulations with chemical shift restraints without the use of molecular fragment replacement or structural homology. The Journal of Physical Chemistry. B. 113: 7890-6. PMID 19425536 DOI: 10.1021/jp900780b |
0.511 |
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2009 |
Carulla N, Zhou M, Arimon M, Gairà M, Giralt E, Robinson CV, Dobson CM. Experimental characterization of disordered and ordered aggregates populated during the process of amyloid fibril formation. Proceedings of the National Academy of Sciences of the United States of America. 106: 7828-33. PMID 19416886 DOI: 10.1073/Pnas.0812227106 |
0.554 |
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2009 |
Buell AK, Tartaglia GG, Birkett NR, Waudby CA, Vendruscolo M, Salvatella X, Welland ME, Dobson CM, Knowles TP. Position-dependent electrostatic protection against protein aggregation. Chembiochem : a European Journal of Chemical Biology. 10: 1309-12. PMID 19415709 DOI: 10.1002/Cbic.200900144 |
0.782 |
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2009 |
Frare E, Mossuto MF, de Laureto PP, Tolin S, Menzer L, Dumoulin M, Dobson CM, Fontana A. Characterization of oligomeric species on the aggregation pathway of human lysozyme. Journal of Molecular Biology. 387: 17-27. PMID 19361437 DOI: 10.1016/J.Jmb.2009.01.049 |
0.466 |
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2009 |
Tartaglia GG, Pechmann S, Dobson CM, Vendruscolo M. A relationship between mRNA expression levels and protein solubility in E. coli. Journal of Molecular Biology. 388: 381-9. PMID 19281824 DOI: 10.1016/J.Jmb.2009.03.002 |
0.488 |
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2009 |
Hsu ST, Cabrita LD, Fucini P, Dobson CM, Christodoulou J. Structure, dynamics and folding of an immunoglobulin domain of the gelation factor (ABP-120) from Dictyostelium discoideum. Journal of Molecular Biology. 388: 865-79. PMID 19281823 DOI: 10.1016/J.Jmb.2009.02.063 |
0.378 |
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2009 |
Hamada D, Tanaka T, Tartaglia GG, Pawar A, Vendruscolo M, Kawamura M, Tamura A, Tanaka N, Dobson CM. Competition between folding, native-state dimerisation and amyloid aggregation in beta-lactoglobulin. Journal of Molecular Biology. 386: 878-90. PMID 19133274 DOI: 10.1016/J.Jmb.2008.12.038 |
0.552 |
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2009 |
Chiti F, Dobson CM. Amyloid formation by globular proteins under native conditions Nature Chemical Biology. 5: 15-22. PMID 19088715 DOI: 10.1038/Nchembio.131 |
0.455 |
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2009 |
Yerbury JJ, Kumita JR, Meehan S, Dobson CM, Wilson MR. alpha2-Macroglobulin and haptoglobin suppress amyloid formation by interacting with prefibrillar protein species. The Journal of Biological Chemistry. 284: 4246-54. PMID 19074141 DOI: 10.1074/Jbc.M807242200 |
0.369 |
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2009 |
Bayro M, Maly T, Birkett N, Dobson C, Griffin R. Resonance assignments of the SH3 domain of phosphatidylinositol-3-kinase (PI3-SH3) in amyloid fibril form determined by MAS NMR spectroscopy Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr16448 |
0.498 |
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2009 |
Robustelli P, Cavalli A, Dobson CM, Vendruscolo M, Salvatella X. Folding of small proteins by monte carlo simulations with chemical shift restraints without the use of molecular fragment replacement or structural homology Journal of Physical Chemistry B. 113: 7890-7896. DOI: 10.1021/Jp900780B |
0.567 |
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2009 |
Bayro MJ, Maly T, Birkett NR, Dobson CM, Griffin RG. Structural Investigation of an SH3 Amyloid Protein Fibril Biophysical Journal. 96: 86a. DOI: 10.1016/J.Bpj.2008.12.351 |
0.596 |
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2008 |
Knowles TP, Shu W, Huber F, Lang HP, Gerber C, Dobson CM, Welland ME. Label-free detection of amyloid growth with microcantilever sensors. Nanotechnology. 19: 384007. PMID 21832567 DOI: 10.1088/0957-4484/19/38/384007 |
0.56 |
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2008 |
Auer S, Dobson CM, Vendruscolo M, Maritan A. Self-templated nucleation in peptide and protein aggregation. Physical Review Letters. 101: 258101. PMID 19113754 DOI: 10.1103/Physrevlett.101.258101 |
0.552 |
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2008 |
Auer S, Meersman F, Dobson CM, Vendruscolo M. A generic mechanism of emergence of amyloid protofilaments from disordered oligomeric aggregates. Plos Computational Biology. 4: e1000222. PMID 19008938 DOI: 10.1371/Journal.Pcbi.1000222 |
0.567 |
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2008 |
Macao B, Hoyer W, Sandberg A, Brorsson AC, Dobson CM, Härd T. Recombinant amyloid beta-peptide production by coexpression with an affibody ligand. Bmc Biotechnology. 8: 82. PMID 18973685 DOI: 10.1186/1472-6750-8-82 |
0.369 |
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2008 |
Chan PH, Pardon E, Menzer L, De Genst E, Kumita JR, Christodoulou J, Saerens D, Brans A, Bouillenne F, Archer DB, Robinson CV, Muyldermans S, Matagne A, Redfield C, Wyns L, ... Dobson CM, et al. Engineering a camelid antibody fragment that binds to the active site of human lysozyme and inhibits its conversion into amyloid fibrils. Biochemistry. 47: 11041-54. PMID 18816062 DOI: 10.1021/Bi8005797 |
0.535 |
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2008 |
Calamai M, Tartaglia GG, Vendruscolo M, Chiti F, Dobson CM. Mutational analysis of the aggregation-prone and disaggregation-prone regions of acylphosphatase. Journal of Molecular Biology. 387: 965-74. PMID 18809411 DOI: 10.1016/J.Jmb.2008.09.003 |
0.532 |
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2008 |
Orte A, Birkett NR, Clarke RW, Devlin GL, Dobson CM, Klenerman D. Direct characterization of amyloidogenic oligomers by single-molecule fluorescence. Proceedings of the National Academy of Sciences of the United States of America. 105: 14424-9. PMID 18796612 DOI: 10.1073/Pnas.0803086105 |
0.406 |
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2008 |
Calloni G, Lendel C, Campioni S, Giannini S, Gliozzi A, Relini A, Vendruscolo M, Dobson CM, Salvatella X, Chiti F. Structure and dynamics of a partially folded protein are decoupled from its mechanism of aggregation. Journal of the American Chemical Society. 130: 13040-50. PMID 18767849 DOI: 10.1021/Ja8029224 |
0.611 |
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2008 |
Strodel B, Fitzpatrick AW, Vendruscolo M, Dobson CM, Wales DJ. Characterizing the first steps of amyloid formation for the ccbeta peptide. The Journal of Physical Chemistry. B. 112: 9998-10004. PMID 18646795 DOI: 10.1021/Jp801222X |
0.486 |
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2008 |
Tartaglia GG, Pawar AP, Campioni S, Dobson CM, Chiti F, Vendruscolo M. Prediction of aggregation-prone regions in structured proteins. Journal of Molecular Biology. 380: 425-36. PMID 18514226 DOI: 10.1016/J.Jmb.2008.05.013 |
0.589 |
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2008 |
Cheon M, Favrin G, Chang I, Dobson CM, Vendruscolo M. Calculation of the free energy barriers in the oligomerisation of Aβ peptide fragments Frontiers in Bioscience. 13: 5614-5622. PMID 18508610 DOI: 10.2741/3104 |
0.555 |
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2008 |
Gsponer J, Christodoulou J, Cavalli A, Bui JM, Richter B, Dobson CM, Vendruscolo M. A coupled equilibrium shift mechanism in calmodulin-mediated signal transduction. Structure (London, England : 1993). 16: 736-46. PMID 18462678 DOI: 10.1016/J.Str.2008.02.017 |
0.495 |
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2008 |
Rivers RC, Kumita JR, Tartaglia GG, Dedmon MM, Pawar A, Vendruscolo M, Dobson CM, Christodoulou J. Molecular determinants of the aggregation behavior of alpha- and beta-synuclein. Protein Science : a Publication of the Protein Society. 17: 887-98. PMID 18436957 DOI: 10.1110/Ps.073181508 |
0.547 |
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2008 |
Baldwin AJ, Anthony-Cahill SJ, Knowles TP, Lippens G, Christodoulou J, Barker PD, Dobson CM. Measurement of amyloid fibril length distributions by inclusion of rotational motion in solution NMR diffusion measurements. Angewandte Chemie (International Ed. in English). 47: 3385-7. PMID 18350531 DOI: 10.1002/Anie.200703915 |
0.329 |
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2008 |
Dalal S, Canet D, Kaiser SE, Dobson CM, Regan L. Conservation of mechanism, variation of rate: folding kinetics of three homologous four-helix bundle proteins. Protein Engineering, Design & Selection : Peds. 21: 197-206. PMID 18299293 DOI: 10.1093/Protein/Gzm088 |
0.417 |
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2008 |
van Nuland NA, Dobson CM, Regan L. Characterization of folding the four-helix bundle protein Rop by real-time NMR. Protein Engineering, Design & Selection : Peds. 21: 165-70. PMID 18299292 DOI: 10.1093/Protein/Gzm081 |
0.398 |
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2008 |
Luheshi LM, Crowther DC, Dobson CM. Protein misfolding and disease: from the test tube to the organism. Current Opinion in Chemical Biology. 12: 25-31. PMID 18295611 DOI: 10.1016/J.Cbpa.2008.02.011 |
0.399 |
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2008 |
Várnai P, Dobson CM, Vendruscolo M. Determination of the transition state ensemble for the folding of ubiquitin from a combination of Phi and Psi analyses. Journal of Molecular Biology. 377: 575-88. PMID 18262544 DOI: 10.1016/J.Jmb.2008.01.012 |
0.569 |
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2007 |
Auer S, Dobson CM, Vendruscolo M. Characterization of the nucleation barriers for protein aggregation and amyloid formation. Hfsp Journal. 1: 137-46. PMID 19404419 DOI: 10.2976/1.2760023 |
0.597 |
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2007 |
Gras SL, Tickler AK, Squires AM, Devlin GL, Horton MA, Dobson CM, MacPhee CE. Functionalised amyloid fibrils for roles in cell adhesion. Biomaterials. 29: 1553-62. PMID 18164758 DOI: 10.1016/J.Biomaterials.2007.11.028 |
0.386 |
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2007 |
Knowles TP, Fitzpatrick AW, Meehan S, Mott HR, Vendruscolo M, Dobson CM, Welland ME. Role of intermolecular forces in defining material properties of protein nanofibrils. Science (New York, N.Y.). 318: 1900-3. PMID 18096801 DOI: 10.1126/Science.1150057 |
0.657 |
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2007 |
Auer S, Miller MA, Krivov SV, Dobson CM, Karplus M, Vendruscolo M. Importance of metastable states in the free energy landscapes of polypeptide chains. Physical Review Letters. 99: 178104. PMID 17995375 DOI: 10.1103/Physrevlett.99.178104 |
0.618 |
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2007 |
Luheshi LM, Tartaglia GG, Brorsson AC, Pawar AP, Watson IE, Chiti F, Vendruscolo M, Lomas DA, Dobson CM, Crowther DC. Systematic in vivo analysis of the intrinsic determinants of amyloid Beta pathogenicity. Plos Biology. 5: e290. PMID 17973577 DOI: 10.1371/Journal.Pbio.0050290 |
0.563 |
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2007 |
Cheon M, Chang I, Mohanty S, Luheshi LM, Dobson CM, Vendruscolo M, Favrin G. Structural reorganisation and potential toxicity of oligomeric species formed during the assembly of amyloid fibrils Plos Computational Biology. 3: 1727-1738. PMID 17941703 DOI: 10.1371/Journal.Pcbi.0030173 |
0.565 |
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2007 |
Hsu ST, Fucini P, Cabrita LD, Launay H, Dobson CM, Christodoulou J. Structure and dynamics of a ribosome-bound nascent chain by NMR spectroscopy. Proceedings of the National Academy of Sciences of the United States of America. 104: 16516-21. PMID 17940046 DOI: 10.1073/Pnas.0704664104 |
0.385 |
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2007 |
Vendruscolo M, Dobson CM. Chemical biology: More charges against aggregation. Nature. 449: 555. PMID 17914388 DOI: 10.1038/449555A |
0.53 |
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2007 |
Meehan S, Knowles TP, Baldwin AJ, Smith JF, Squires AM, Clements P, Treweek TM, Ecroyd H, Tartaglia GG, Vendruscolo M, Macphee CE, Dobson CM, Carver JA. Characterisation of amyloid fibril formation by small heat-shock chaperone proteins human alphaA-, alphaB- and R120G alphaB-crystallins. Journal of Molecular Biology. 372: 470-84. PMID 17662998 DOI: 10.1016/J.Jmb.2007.06.060 |
0.607 |
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2007 |
Knowles TP, Shu W, Devlin GL, Meehan S, Auer S, Dobson CM, Welland ME. Kinetics and thermodynamics of amyloid formation from direct measurements of fluctuations in fibril mass. Proceedings of the National Academy of Sciences of the United States of America. 104: 10016-21. PMID 17540728 DOI: 10.1073/Pnas.0610659104 |
0.645 |
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2007 |
Cavalli A, Salvatella X, Dobson CM, Vendruscolo M. Protein structure determination from NMR chemical shifts. Proceedings of the National Academy of Sciences of the United States of America. 104: 9615-20. PMID 17535901 DOI: 10.1073/Pnas.0610313104 |
0.568 |
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2007 |
Meinhardt J, Tartaglia GG, Pawar A, Christopeit T, Hortschansky P, Schroeckh V, Dobson CM, Vendruscolo M, Fändrich M. Similarities in the thermodynamics and kinetics of aggregation of disease-related Abeta(1-40) peptides. Protein Science : a Publication of the Protein Society. 16: 1214-22. PMID 17525469 DOI: 10.1110/Ps.062734207 |
0.534 |
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2007 |
Tartaglia GG, Pechmann S, Dobson CM, Vendruscolo M. Life on the edge: a link between gene expression levels and aggregation rates of human proteins. Trends in Biochemical Sciences. 32: 204-6. PMID 17419062 DOI: 10.1016/J.Tibs.2007.03.005 |
0.543 |
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2007 |
Yerbury JJ, Poon S, Meehan S, Thompson B, Kumita JR, Dobson CM, Wilson MR. The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 21: 2312-22. PMID 17412999 DOI: 10.1096/Fj.06-7986Com |
0.446 |
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2007 |
Kumita JR, Poon S, Caddy GL, Hagan CL, Dumoulin M, Yerbury JJ, Stewart EM, Robinson CV, Wilson MR, Dobson CM. The extracellular chaperone clusterin potently inhibits human lysozyme amyloid formation by interacting with prefibrillar species. Journal of Molecular Biology. 369: 157-67. PMID 17407782 DOI: 10.1016/J.Jmb.2007.02.095 |
0.55 |
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2007 |
Gsponer J, Hopearuoho H, Cavalli A, Dobson CM, Vendruscolo M. Geometry, energetics, and dynamics of hydrogen bonds in proteins: structural information derived from NMR scalar couplings. Journal of the American Chemical Society. 128: 15127-35. PMID 17117864 DOI: 10.1021/Ja0614722 |
0.497 |
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2007 |
Squires AM, Devlin GL, Gras SL, Tickler AK, MacPhee CE, Dobson CM. X-ray scattering study of the effect of hydration on the cross-beta structure of amyloid fibrils. Journal of the American Chemical Society. 128: 11738-9. PMID 16953596 DOI: 10.1021/Ja063751V |
0.339 |
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2007 |
Dobson CM. Diseases of protein misfolding Genes and Common Diseases. 113-131. DOI: 10.1017/CBO9780511543555.008 |
0.312 |
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2006 |
Di Gaetano S, Guglielmi F, Arciello A, Mangione P, Monti M, Pagnozzi D, Raimondi S, Giorgetti S, Orrù S, Canale C, Pucci P, Dobson CM, Bellotti V, Piccoli R. Recombinant amyloidogenic domain of ApoA-I: analysis of its fibrillogenic potential. Biochemical and Biophysical Research Communications. 351: 223-8. PMID 17056013 DOI: 10.1016/J.Bbrc.2006.10.026 |
0.42 |
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2006 |
Calamai M, Kumita JR, Mifsud J, Parrini C, Ramazzotti M, Ramponi G, Taddei N, Chiti F, Dobson CM. Nature and significance of the interactions between amyloid fibrils and biological polyelectrolytes. Biochemistry. 45: 12806-15. PMID 17042499 DOI: 10.1021/Bi0610653 |
0.404 |
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2006 |
Smith JF, Knowles TP, Dobson CM, Macphee CE, Welland ME. Characterization of the nanoscale properties of individual amyloid fibrils. Proceedings of the National Academy of Sciences of the United States of America. 103: 15806-11. PMID 17038504 DOI: 10.1073/Pnas.0604035103 |
0.603 |
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2006 |
Meersman F, Dobson CM, Heremans K. Protein unfolding, amyloid fibril formation and configurational energy landscapes under high pressure conditions. Chemical Society Reviews. 35: 908-17. PMID 17003897 DOI: 10.1039/B517761H |
0.365 |
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2006 |
Dumoulin M, Kumita JR, Dobson CM. Normal and aberrant biological self-assembly: Insights from studies of human lysozyme and its amyloidogenic variants. Accounts of Chemical Research. 39: 603-10. PMID 16981676 DOI: 10.1021/Ar050070G |
0.426 |
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2006 |
Vendruscolo M, Dobson CM. Structural biology. Dynamic visions of enzymatic reactions. Science (New York, N.Y.). 313: 1586-7. PMID 16973868 DOI: 10.1126/Science.1132851 |
0.489 |
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2006 |
Baglioni S, Casamenti F, Bucciantini M, Luheshi LM, Taddei N, Chiti F, Dobson CM, Stefani M. Prefibrillar amyloid aggregates could be generic toxins in higher organisms. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 26: 8160-7. PMID 16885229 DOI: 10.1523/Jneurosci.4809-05.2006 |
0.425 |
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2006 |
Frare E, Mossuto MF, Polverino de Laureto P, Dumoulin M, Dobson CM, Fontana A. Identification of the core structure of lysozyme amyloid fibrils by proteolysis. Journal of Molecular Biology. 361: 551-61. PMID 16859705 DOI: 10.1016/J.Jmb.2006.06.055 |
0.456 |
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2006 |
Knowles TP, Smith JF, Craig A, Dobson CM, Welland ME. Spatial persistence of angular correlations in amyloid fibrils. Physical Review Letters. 96: 238301. PMID 16803412 DOI: 10.1103/Physrevlett.96.238301 |
0.589 |
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2006 |
Devlin GL, Knowles TP, Squires A, McCammon MG, Gras SL, Nilsson MR, Robinson CV, Dobson CM, MacPhee CE. The component polypeptide chains of bovine insulin nucleate or inhibit aggregation of the parent protein in a conformation-dependent manner. Journal of Molecular Biology. 360: 497-509. PMID 16774767 DOI: 10.1016/J.Jmb.2006.05.007 |
0.772 |
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2006 |
Chiti F, Dobson CM. Protein Misfolding, Functional Amyloid, and Human Disease Annual Review of Biochemistry. 75: 333-366. PMID 16756495 DOI: 10.1146/Annurev.Biochem.75.101304.123901 |
0.484 |
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2006 |
Dobson CM. An accidental breach of a protein's natural defenses Nature Structural and Molecular Biology. 13: 295-297. PMID 16715043 DOI: 10.1038/Nsmb0406-295 |
0.388 |
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2006 |
Fändrich M, Zandomeneghi G, Krebs MR, Kittler M, Buder K, Rossner A, Heinemann SH, Dobson CM, Diekmann S. Apomyoglobin reveals a random-nucleation mechanism in amyloid protofibril formation. Acta Histochemica. 108: 215-9. PMID 16714052 DOI: 10.1016/J.Acthis.2006.03.012 |
0.419 |
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2006 |
Bader R, Seeliger MA, Kelly SE, Ilag LL, Meersman F, Limones A, Luisi BF, Dobson CM, Itzhaki LS. Folding and fibril formation of the cell cycle protein Cks1. The Journal of Biological Chemistry. 281: 18816-24. PMID 16675442 DOI: 10.1074/Jbc.M603628200 |
0.715 |
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2006 |
Hall D, Dobson CM. Expanding to fill the gap: a possible role for inert biopolymers in regulating the extent of the 'macromolecular crowding' effect. Febs Letters. 580: 2584-90. PMID 16647066 DOI: 10.1016/J.Febslet.2006.04.005 |
0.319 |
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2006 |
Dobson CM. Protein aggregation and its consequences for human disease Protein and Peptide Letters. 13: 219-227. PMID 16515449 DOI: 10.2174/092986606775338362 |
0.44 |
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2006 |
Baldwin AJ, Bader R, Christodoulou J, MacPhee CE, Dobson CM, Barker PD. Cytochrome display on amyloid fibrils. Journal of the American Chemical Society. 128: 2162-3. PMID 16478140 DOI: 10.1021/Ja0565673 |
0.445 |
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2006 |
Kumita JR, Johnson RJ, Alcocer MJ, Dumoulin M, Holmqvist F, McCammon MG, Robinson CV, Archer DB, Dobson CM. Impact of the native-state stability of human lysozyme variants on protein secretion by Pichia pastoris. The Febs Journal. 273: 711-20. PMID 16441658 DOI: 10.1111/J.1742-4658.2005.05099.X |
0.532 |
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2006 |
Chandran V, Stollar EJ, Lindorff-Larsen K, Harper JF, Chazin WJ, Dobson CM, Luisi BF, Christodoulou J. Structure of the regulatory apparatus of a calcium-dependent protein kinase (CDPK): a novel mode of calmodulin-target recognition. Journal of Molecular Biology. 357: 400-10. PMID 16430916 DOI: 10.1016/J.Jmb.2005.11.093 |
0.3 |
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2006 |
Bader R, Bamford R, Zurdo J, Luisi BF, Dobson CM. Probing the mechanism of amyloidogenesis through a tandem repeat of the PI3-SH3 domain suggests a generic model for protein aggregation and fibril formation. Journal of Molecular Biology. 356: 189-208. PMID 16364365 DOI: 10.1016/J.Jmb.2005.11.034 |
0.435 |
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2006 |
Knowles TPJ, Smith JF, Devlin GL, Dobson CM, Welland ME. Analysis of structural order in amyloid fibrils Nanotechnology. 18: 044031. DOI: 10.1088/0957-4484/18/4/044031 |
0.626 |
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2006 |
Aprile FA, Sormanni P, Perni M, Arosio P, Limbocker R, Chhangur S, Mannini B, Linse S, Knowles T, Dobson CM, Vendruscolo M. O2-02-02: TARGETING AMYLOID FORMATION USING RATIONALLY DESIGNED ANTIBODIES Alzheimer's & Dementia. 14: P611-P611. DOI: 10.1016/J.Jalz.2018.06.2646 |
0.443 |
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2005 |
Thorn DC, Meehan S, Sunde M, Rekas A, Gras SL, MacPhee CE, Dobson CM, Wilson MR, Carver JA. Amyloid fibril formation by bovine milk κ-casein and its inhibition by the molecular chaperones α3- and β-casein Biochemistry. 44: 17027-17036. PMID 16363816 DOI: 10.1021/Bi051352R |
0.446 |
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2005 |
Wright CF, Teichmann SA, Clarke J, Dobson CM. The importance of sequence diversity in the aggregation and evolution of proteins. Nature. 438: 878-81. PMID 16341018 DOI: 10.1038/Nature04195 |
0.417 |
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2005 |
Meersman F, Dobson CM. Probing the pressure-temperature stability of amyloid fibrils provides new insights into their molecular properties. Biochimica Et Biophysica Acta. 1764: 452-60. PMID 16337233 DOI: 10.1016/J.Bbapap.2005.10.021 |
0.417 |
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2005 |
Calamai M, Chiti F, Dobson CM. Amyloid Fibril Formation Can Proceed from Different Conformations of a Partially Unfolded Protein Biophysical Journal. 89: 4201-4210. PMID 16169975 DOI: 10.1529/Biophysj.105.068726 |
0.481 |
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2005 |
Collins ES, Wirmer J, Hirai K, Tachibana H, Segawa S, Dobson CM, Schwalbe H. Characterisation of disulfide-bond dynamics in non-native states of lysozyme and its disulfide deletion mutants by NMR. Chembiochem : a European Journal of Chemical Biology. 6: 1619-27. PMID 16138305 DOI: 10.1002/Cbic.200500196 |
0.478 |
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2005 |
Johnson RJ, Christodoulou J, Dumoulin M, Caddy GL, Alcocer MJ, Murtagh GJ, Kumita JR, Larsson G, Robinson CV, Archer DB, Luisi B, Dobson CM. Rationalising lysozyme amyloidosis: insights from the structure and solution dynamics of T70N lysozyme. Journal of Molecular Biology. 352: 823-36. PMID 16126226 DOI: 10.1016/J.Jmb.2005.07.040 |
0.55 |
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2005 |
Paci E, Lindorff-Larsen K, Dobson CM, Karplus M, Vendruscolo M. Transition state contact orders correlate with protein folding rates. Journal of Molecular Biology. 352: 495-500. PMID 16120445 DOI: 10.1016/J.Jmb.2005.06.081 |
0.602 |
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2005 |
Salvatella X, Dobson CM, Fersht AR, Vendruscolo M. Determination of the folding transition states of barnase by using ΦI-value-restrained simulations validated by double mutant ΦIJ-values Proceedings of the National Academy of Sciences of the United States of America. 102: 12389-12394. PMID 16116084 DOI: 10.1073/Pnas.0408226102 |
0.551 |
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2005 |
Parrini C, Taddei N, Ramazzotti M, Degl'Innocenti D, Ramponi G, Dobson CM, Chiti F. Glycine residues appear to be evolutionarily conserved for their ability to inhibit aggregation Structure. 13: 1143-1151. PMID 16084386 DOI: 10.1016/J.Str.2005.04.022 |
0.308 |
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2005 |
Carulla N, Caddy GL, Hall DR, Zurdo J, Gairí M, Feliz M, Giralt E, Robinson CV, Dobson CM. Molecular recycling within amyloid fibrils. Nature. 436: 554-8. PMID 16049488 DOI: 10.1038/Nature03986 |
0.587 |
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2005 |
Plakoutsi G, Bemporad F, Calamai M, Taddei N, Dobson CM, Chiti F. Evidence for a mechanism of amyloid formation involving molecular reorganisation within native-like precursor aggregates. Journal of Molecular Biology. 351: 910-22. PMID 16024042 DOI: 10.1016/J.Jmb.2005.06.043 |
0.457 |
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2005 |
Wain R, Smith LJ, Dobson CM. Oxidative refolding of amyloidogenic variants of human lysozyme. Journal of Molecular Biology. 351: 662-71. PMID 16023673 DOI: 10.1016/J.Jmb.2005.06.035 |
0.411 |
|
2005 |
Fowler SB, Poon S, Muff R, Chiti F, Dobson CM, Zurdo J. Rational design of aggregation-resistant bioactive peptides: reengineering human calcitonin. Proceedings of the National Academy of Sciences of the United States of America. 102: 10105-10. PMID 16006528 DOI: 10.1073/Pnas.0501215102 |
0.414 |
|
2005 |
Hall D, Hirota N, Dobson CM. A toy model for predicting the rate of amyloid formation from unfolded protein. Journal of Molecular Biology. 351: 195-205. PMID 15993421 DOI: 10.1016/J.Jmb.2005.05.013 |
0.41 |
|
2005 |
Mok KH, Nagashima T, Day IJ, Hore PJ, Dobson CM. Multiple subsets of side-chain packing in partially folded states of alpha-lactalbumins. Proceedings of the National Academy of Sciences of the United States of America. 102: 8899-904. PMID 15956205 DOI: 10.1073/Pnas.0500661102 |
0.382 |
|
2005 |
Dobson CM. Structural biology: Prying into prions Nature. 435: 747-749. PMID 15944684 DOI: 10.1038/435747A |
0.334 |
|
2005 |
Pawar AP, Dubay KF, Zurdo J, Chiti F, Vendruscolo M, Dobson CM. Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases. Journal of Molecular Biology. 350: 379-92. PMID 15925383 DOI: 10.1016/J.Jmb.2005.04.016 |
0.594 |
|
2005 |
Vendruscolo M, Dobson CM. A glimpse at the organization of the protein universe. Proceedings of the National Academy of Sciences of the United States of America. 102: 5641-2. PMID 15827120 DOI: 10.1073/Pnas.0500274102 |
0.552 |
|
2005 |
Kristjansdottir S, Lindorff-Larsen K, Fieber W, Dobson CM, Vendruscolo M, Poulsen FM. Formation of native and non-native interactions in ensembles of denatured ACBP molecules from paramagnetic relaxation enhancement studies. Journal of Molecular Biology. 347: 1053-62. PMID 15784263 DOI: 10.1016/J.Jmb.2005.01.009 |
0.542 |
|
2005 |
Dirix C, Meersman F, MacPhee CE, Dobson CM, Heremans K. High hydrostatic pressure dissociates early aggregates of TTR105-115, but not the mature amyloid fibrils. Journal of Molecular Biology. 347: 903-9. PMID 15784251 DOI: 10.1016/J.Jmb.2005.01.073 |
0.4 |
|
2005 |
Marcon G, Plakoutsi G, Canale C, Relini A, Taddei N, Dobson CM, Ramponi G, Chiti F. Amyloid formation from HypF-N under conditions in which the protein is initially in its native state. Journal of Molecular Biology. 347: 323-35. PMID 15740744 DOI: 10.1016/J.Jmb.2005.01.034 |
0.471 |
|
2005 |
Dumoulin M, Canet D, Last AM, Pardon E, Archer DB, Muyldermans S, Wyns L, Matagne A, Robinson CV, Redfield C, Dobson CM. Reduced global cooperativity is a common feature underlying the amyloidogenicity of pathogenic lysozyme mutations. Journal of Molecular Biology. 346: 773-88. PMID 15713462 DOI: 10.1016/J.Jmb.2004.11.020 |
0.568 |
|
2005 |
Dedmon MM, Christodoulou J, Wilson MR, Dobson CM. Heat shock protein 70 inhibits alpha-synuclein fibril formation via preferential binding to prefibrillar species. The Journal of Biological Chemistry. 280: 14733-40. PMID 15671022 DOI: 10.1074/Jbc.M413024200 |
0.371 |
|
2005 |
Vendruscolo M, Dobson CM, Zewail AH, Mcmillan PF, Davies JF, Karplus M, Simons JP. Towards complete descriptions of the free-energy landscapes of proteins Philosophical Transactions of the Royal Society a: Mathematical, Physical and Engineering Sciences. 363: 433-452. PMID 15664892 DOI: 10.1098/Rsta.2004.1501 |
0.653 |
|
2005 |
Lindorff-Larsen K, Røgen P, Paci E, Vendruscolo M, Dobson CM. Protein folding and the organization of the protein topology universe. Trends in Biochemical Sciences. 30: 13-9. PMID 15653321 DOI: 10.1016/J.Tibs.2004.11.008 |
0.564 |
|
2005 |
Lindorff-Larsen K, Best RB, Depristo MA, Dobson CM, Vendruscolo M. Simultaneous determination of protein structure and dynamics. Nature. 433: 128-32. PMID 15650731 DOI: 10.1038/Nature03199 |
0.703 |
|
2005 |
Dedmon MM, Lindorff-Larsen K, Christodoulou J, Vendruscolo M, Dobson CM. Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble molecular dynamics simulations. Journal of the American Chemical Society. 127: 476-7. PMID 15643843 DOI: 10.1021/Ja044834J |
0.525 |
|
2005 |
Dumoulin M, Dobson CM. Probing the origins, diagnosis and treatment of amyloid diseases using antibodies. Biochimie. 86: 589-600. PMID 15556268 DOI: 10.1016/J.Biochi.2004.09.012 |
0.384 |
|
2005 |
Hamada D, Tanaka N, Tanaka T, Yanagihara I, Pawar A, Vendruscolo M, Dobson C. 1P079 Mechanism of amyloid formation by beta-lactoglobulin and its relationship with its folding process Seibutsu Butsuri. 45: S51. DOI: 10.2142/Biophys.45.S51_3 |
0.482 |
|
2004 |
Calamai M, Canale C, Relini A, Stefani M, Chiti F, Dobson CM. Reversal of protein aggregation provides evidence for multiple aggregated States. Journal of Molecular Biology. 346: 603-16. PMID 15670608 DOI: 10.1016/J.Jmb.2004.11.067 |
0.452 |
|
2004 |
Calloni G, Zoffoli S, Stefani M, Dobson CM, Chiti F. Investigating the effects of mutations on protein aggregation in the cell. The Journal of Biological Chemistry. 280: 10607-13. PMID 15611128 DOI: 10.1074/Jbc.M412951200 |
0.451 |
|
2004 |
Krebs MR, Macphee CE, Miller AF, Dunlop IE, Dobson CM, Donald AM. The formation of spherulites by amyloid fibrils of bovine insulin. Proceedings of the National Academy of Sciences of the United States of America. 101: 14420-4. PMID 15381766 DOI: 10.1073/Pnas.0405933101 |
0.4 |
|
2004 |
DuBay KF, Pawar AP, Chiti F, Zurdo J, Dobson CM, Vendruscolo M. Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains. Journal of Molecular Biology. 341: 1317-26. PMID 15302561 DOI: 10.1016/J.Jmb.2004.06.043 |
0.606 |
|
2004 |
Dobson CM. Experimental investigation of protein folding and misfolding Methods. 34: 4-14. PMID 15283911 DOI: 10.1016/J.Ymeth.2004.03.002 |
0.439 |
|
2004 |
Korzhnev DM, Salvatella X, Vendruscolo M, Di Nardo AA, Davidson AR, Dobson CM, Kay LE. Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR. Nature. 430: 586-90. PMID 15282609 DOI: 10.1038/Nature02655 |
0.569 |
|
2004 |
Christodoulou J, Larsson G, Fucini P, Connell SR, Pertinhez TA, Hanson CL, Redfield C, Nierhaus KH, Robinson CV, Schleucher J, Dobson CM. Heteronuclear NMR investigations of dynamic regions of intact Escherichia coli ribosomes. Proceedings of the National Academy of Sciences of the United States of America. 101: 10949-54. PMID 15263071 DOI: 10.1073/Pnas.0400928101 |
0.475 |
|
2004 |
Frare E, Polverino De Laureto P, Zurdo J, Dobson CM, Fontana A. A highly amyloidogenic region of hen lysozyme. Journal of Molecular Biology. 340: 1153-65. PMID 15236974 DOI: 10.1016/J.Jmb.2004.05.056 |
0.47 |
|
2004 |
Krebs MR, Morozova-Roche LA, Daniel K, Robinson CV, Dobson CM. Observation of sequence specificity in the seeding of protein amyloid fibrils. Protein Science : a Publication of the Protein Society. 13: 1933-8. PMID 15215533 DOI: 10.1110/Ps.04707004 |
0.575 |
|
2004 |
Wright CF, Christodoulou J, Dobson CM, Clarke J. The importance of loop length in the folding of an immunoglobulin domain. Protein Engineering, Design & Selection : Peds. 17: 443-53. PMID 15208402 DOI: 10.1093/Protein/Gzh052 |
0.365 |
|
2004 |
Dobson CM. In the footsteps of alchemists Science. 304: 1259-1262. PMID 15166354 DOI: 10.1126/Science.1093078 |
0.402 |
|
2004 |
De Felice FG, Vieira MN, Meirelles MN, Morozova-Roche LA, Dobson CM, Ferreira ST. Formation of amyloid aggregates from human lysozyme and its disease-associated variants using hydrostatic pressure. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 18: 1099-101. PMID 15155566 DOI: 10.1096/Fj.03-1072Fje |
0.433 |
|
2004 |
Bucciantini M, Calloni G, Chiti F, Formigli L, Nosi D, Dobson CM, Stefani M. Prefibrillar amyloid protein aggregates share common features of cytotoxicity. The Journal of Biological Chemistry. 279: 31374-82. PMID 15133040 DOI: 10.1074/Jbc.M400348200 |
0.431 |
|
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