| Year |
Citation |
Score |
| 2024 |
Rinauro DJ, Chiti F, Vendruscolo M, Limbocker R. Misfolded protein oligomers: mechanisms of formation, cytotoxic effects, and pharmacological approaches against protein misfolding diseases. Molecular Neurodegeneration. 19: 20. PMID 38378578 DOI: 10.1186/s13024-023-00651-2 |
0.357 |
|
| 2023 |
Olivieri C, Wang Y, Walker C, Subrahmanian MV, Ha KN, Bernlohr DA, Gao J, Camilloni C, Vendruscolo M, Taylor SS, Veglia G. The αC-β4 loop controls the allosteric cooperativity between nucleotide and substrate in the catalytic subunit of protein kinase A. Biorxiv : the Preprint Server For Biology. PMID 37745542 DOI: 10.1101/2023.09.12.557419 |
0.68 |
|
| 2023 |
Vendruscolo M. Thermodynamic and kinetic approaches for drug discovery to target protein misfolding and aggregation. Expert Opinion On Drug Discovery. 18: 881-891. PMID 37276120 DOI: 10.1080/17460441.2023.2221024 |
0.306 |
|
| 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 |
0.47 |
|
| 2023 |
Limbocker R, Cremades N, Cascella R, Tessier PM, Vendruscolo M, Chiti F. Characterization of Pairs of Toxic and Nontoxic Misfolded Protein Oligomers Elucidates the Structural Determinants of Oligomer Toxicity in Protein Misfolding Diseases. Accounts of Chemical Research. PMID 37071750 DOI: 10.1021/acs.accounts.3c00045 |
0.394 |
|
| 2023 |
Bhardwaj T, Gadhave K, Kapuganti SK, Kumar P, Brotzakis ZF, Saumya KU, Nayak N, Kumar A, Joshi R, Mukherjee B, Bhardwaj A, Thakur KG, Garg N, Vendruscolo M, Giri R. Amyloidogenic proteins in the SARS-CoV and SARS-CoV-2 proteomes. Nature Communications. 14: 945. PMID 36806058 DOI: 10.1038/s41467-023-36234-4 |
0.349 |
|
| 2022 |
Baumann KN, Šneiderienė G, Sanguanini M, Schneider M, Rimon O, González Díaz A, Greer H, Thacker D, Linse S, Knowles TPJ, Vendruscolo M. A Kinetic Map of the Influence of Biomimetic Lipid Model Membranes on Aβ Aggregation. Acs Chemical Neuroscience. 14: 323-329. PMID 36574473 DOI: 10.1021/acschemneuro.2c00765 |
0.796 |
|
| 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 |
0.445 |
|
| 2022 |
Olivieri C, Li GC, Wang Y, V S M, Walker C, Kim J, Camilloni C, De Simone A, Vendruscolo M, Bernlohr DA, Taylor SS, Veglia G. ATP-competitive inhibitors modulate the substrate binding cooperativity of a kinase by altering its conformational entropy. Science Advances. 8: eabo0696. PMID 35905186 DOI: 10.1126/sciadv.abo0696 |
0.536 |
|
| 2022 |
Toprakcioglu Z, Kamada A, Michaels TCT, Xie M, Krausser J, Wei J, Saric A, Vendruscolo M, Knowles TPJ. Adsorption free energy predicts amyloid protein nucleation rates. Proceedings of the National Academy of Sciences of the United States of America. 119: e2109718119. PMID 35901206 DOI: 10.1073/pnas.2109718119 |
0.301 |
|
| 2022 |
Löhr T, Kohlhoff K, Heller GT, Camilloni C, Vendruscolo M. A Small Molecule Stabilizes the Disordered Native State of the Alzheimer's Aβ Peptide. Acs Chemical Neuroscience. 13: 1738-1745. PMID 35649268 DOI: 10.1021/acschemneuro.2c00116 |
0.813 |
|
| 2022 |
Michaels TCT, Dear AJ, Cohen SIA, Vendruscolo M, Knowles TPJ. Kinetic profiling of therapeutic strategies for inhibiting the formation of amyloid oligomers. The Journal of Chemical Physics. 156: 164904. PMID 35490011 DOI: 10.1063/5.0077609 |
0.303 |
|
| 2021 |
Löhr T, Kohlhoff K, Heller GT, Camilloni C, Vendruscolo M. A kinetic ensemble of the Alzheimer's Aβ peptide. Nature Computational Science. 1: 71-78. PMID 38217162 DOI: 10.1038/s43588-020-00003-w |
0.344 |
|
| 2021 |
Kulenkampff K, Wolf Perez AM, Sormanni P, Habchi J, Vendruscolo M. Quantifying misfolded protein oligomers as drug targets and biomarkers in Alzheimer and Parkinson diseases. Nature Reviews. Chemistry. 5: 277-294. PMID 37117282 DOI: 10.1038/s41570-021-00254-9 |
0.317 |
|
| 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 |
0.48 |
|
| 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 |
0.477 |
|
| 2021 |
Morgunov AS, Liis Saar K, Vendruscolo M, Knowles TPJ. New frontiers for machine learning in protein science. Journal of Molecular Biology. 167232. PMID 34499920 DOI: 10.1016/j.jmb.2021.167232 |
0.304 |
|
| 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 |
0.397 |
|
| 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 |
0.451 |
|
| 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 |
0.474 |
|
| 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 |
0.472 |
|
| 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, ... ... Vendruscolo M, 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 |
0.459 |
|
| 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 |
0.381 |
|
| 2021 |
Sinnige T, Meisl G, Michaels TCT, Vendruscolo M, Knowles TPJ, Morimoto RI. Kinetic analysis reveals that independent nucleation events determine the progression of polyglutamine aggregation in . Proceedings of the National Academy of Sciences of the United States of America. 118. PMID 33836595 DOI: 10.1073/pnas.2021888118 |
0.334 |
|
| 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, ... ... Vendruscolo M, 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 |
0.315 |
|
| 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 |
0.34 |
|
| 2021 |
Ruggeri FS, Habchi J, Chia S, Horne RI, Vendruscolo M, Knowles TPJ. Infrared nanospectroscopy reveals the molecular interaction fingerprint of an aggregation inhibitor with single Aβ42 oligomers. Nature Communications. 12: 688. PMID 33514697 DOI: 10.1038/s41467-020-20782-0 |
0.325 |
|
| 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, ... Vendruscolo M, 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 |
0.337 |
|
| 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, ... Vendruscolo M, et al. A dopamine metabolite stabilizes neurotoxic amyloid-β oligomers. Communications Biology. 4: 19. PMID 33398040 DOI: 10.1038/s42003-020-01490-3 |
0.416 |
|
| 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 |
0.397 |
|
| 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 |
0.412 |
|
| 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 |
0.374 |
|
| 2020 |
Kreiser RP, Wright AK, Block NR, Hollows JE, Nguyen LT, LeForte K, Mannini B, Vendruscolo M, Limbocker R. Therapeutic Strategies to Reduce the Toxicity of Misfolded Protein Oligomers. International Journal of Molecular Sciences. 21. PMID 33212787 DOI: 10.3390/ijms21228651 |
0.317 |
|
| 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 |
0.428 |
|
| 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, ... Vendruscolo M, 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 |
0.691 |
|
| 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 |
0.397 |
|
| 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 |
0.518 |
|
| 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 |
0.536 |
|
| 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, ... ... Vendruscolo M, 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 |
0.496 |
|
| 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 |
0.545 |
|
| 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, ... Vendruscolo M, 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 |
0.528 |
|
| 2020 |
Kelmer Sacramento E, Kirkpatrick JM, Mazzetto M, Baumgart M, Bartolome A, Di Sanzo S, Caterino C, Sanguanini M, Papaevgeniou N, Lefaki M, Childs D, Bagnoli S, Terzibasi Tozzini E, Di Fraia D, Romanov N, ... ... Vendruscolo M, et al. Reduced proteasome activity in the aging brain results in ribosome stoichiometry loss and aggregation. Molecular Systems Biology. 16: e9596. PMID 32558274 DOI: 10.15252/Msb.20209596 |
0.787 |
|
| 2020 |
Ruggeri FS, Mannini B, Schmid R, Vendruscolo M, Knowles TPJ. Single molecule secondary structure determination of proteins through infrared absorption nanospectroscopy. Nature Communications. 11: 2945. PMID 32522983 DOI: 10.1038/S41467-020-16728-1 |
0.355 |
|
| 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, ... ... Vendruscolo M, 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 |
0.508 |
|
| 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 |
0.547 |
|
| 2020 |
Horvath A, Miskei M, Ambrus V, Vendruscolo M, Fuxreiter M. Sequence-based prediction of protein binding mode landscapes. Plos Computational Biology. 16: e1007864. PMID 32453748 DOI: 10.1371/Journal.Pcbi.1007864 |
0.365 |
|
| 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 |
0.411 |
|
| 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 |
0.473 |
|
| 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 |
0.543 |
|
| 2020 |
Sanguanini M, Baumann KN, Preet S, Chia S, Habchi J, Knowles TPJ, Vendruscolo M. Complexity in lipid membrane composition induces resilience to Aβ42 aggregation. Acs Chemical Neuroscience. PMID 32212722 DOI: 10.1021/Acschemneuro.0C00101 |
0.803 |
|
| 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 |
0.516 |
|
| 2020 |
Miskei M, Horváth A, Vendruscolo M, Fuxreiter M. Sequence-based determinants and prediction of fuzzy interactions in protein complexes. Journal of Molecular Biology. PMID 32112804 DOI: 10.1016/J.Jmb.2020.02.017 |
0.35 |
|
| 2020 |
Metrick MA, Ferreira NDC, Saijo E, Kraus A, Newell K, Zanusso G, Vendruscolo M, Ghetti B, Caughey B. A single ultrasensitive assay for detection and discrimination of tau aggregates of Alzheimer and Pick diseases. Acta Neuropathologica Communications. 8: 22. PMID 32087764 DOI: 10.1186/S40478-020-0887-Z |
0.301 |
|
| 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 |
0.484 |
|
| 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 |
0.513 |
|
| 2020 |
Knowles TPJ, Vendruscolo M. Chris Dobson (1949-2019). Nature Chemical Biology. 16: 105. PMID 31974526 DOI: 10.1038/S41589-019-0456-6 |
0.365 |
|
| 2020 |
Sui X, Pires DEV, Ormsby AR, Cox D, Nie S, Vecchi G, Vendruscolo M, Ascher DB, Reid GE, Hatters DM. Widespread remodeling of proteome solubility in response to different protein homeostasis stresses. Proceedings of the National Academy of Sciences of the United States of America. PMID 31964829 DOI: 10.1073/Pnas.1912897117 |
0.376 |
|
| 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 |
0.498 |
|
| 2019 |
Baum J, Chiti F, De Simone A, Knowles TPJ, Kumita JR, Radford SE, Robinson CV, Salvatella X, Valelli K, Vendruscolo M, Pastore A, Tartaglia GG. Homage to Chris Dobson. Frontiers in Molecular Biosciences. 6: 137. PMID 31921887 DOI: 10.3389/Fmolb.2019.00137 |
0.524 |
|
| 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 |
0.526 |
|
| 2019 |
Maritan M, Romeo M, Oberti L, Sormanni P, Tasaki M, Russo R, Ambrosetti A, Motta P, Rognoni P, Mazzini G, Barbiroli A, Palladini G, Vendruscolo M, Diomede L, Bolognesi M, et al. Inherent biophysical properties modulate the toxicity of soluble amyloidogenic light chains. Journal of Molecular Biology. PMID 31874151 DOI: 10.1016/J.Jmb.2019.12.015 |
0.37 |
|
| 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 |
0.545 |
|
| 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 |
0.496 |
|
| 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 |
0.572 |
|
| 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 |
0.534 |
|
| 2019 |
Metrick MA, do Carmo Ferreira N, Saijo E, Hughson AG, Kraus A, Orrú C, Miller MW, Zanusso G, Ghetti B, Vendruscolo M, Caughey B. Million-fold sensitivity enhancement in proteopathic seed amplification assays for biospecimens by Hofmeister ion comparisons. Proceedings of the National Academy of Sciences of the United States of America. PMID 31641070 DOI: 10.1073/Pnas.1909322116 |
0.389 |
|
| 2019 |
Ruggeri FS, Šneideris T, Chia S, Vendruscolo M, Knowles TPJ. Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy. Journal of Visualized Experiments : Jove. PMID 31566623 DOI: 10.3791/60108 |
0.464 |
|
| 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 |
0.505 |
|
| 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 |
0.55 |
|
| 2019 |
Löhr T, Camilloni C, Bonomi M, Vendruscolo M. A Practical Guide to the Simultaneous Determination of Protein Structure and Dynamics Using Metainference. Methods in Molecular Biology (Clifton, N.J.). 2022: 313-340. PMID 31396909 DOI: 10.1007/978-1-4939-9608-7_13 |
0.665 |
|
| 2019 |
Zhao L, Vecchi G, Vendruscolo M, Körner R, Hayer-Hartl M, Hartl FU. The Hsp70 Chaperone System Stabilizes a Thermo-sensitive Subproteome in E. coli. Cell Reports. 28: 1335-1345.e6. PMID 31365874 DOI: 10.1016/J.Celrep.2019.06.081 |
0.398 |
|
| 2019 |
Bonomi M, Bussi G, Camilloni C, Tribello GA, Banáš P, Barducci A, Bernetti M, Bolhuis PG, Bottaro S, Branduardi D, Capelli R, Carloni P, Ceriotti M, Cesari A, Chen H, ... ... Vendruscolo M, et al. Promoting transparency and reproducibility in enhanced molecular simulations Nature Methods. 16: 670-673. PMID 31363226 DOI: 10.1038/S41592-019-0506-8 |
0.671 |
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| 2019 |
De S, Whiten DR, Ruggeri FS, Hughes C, Rodrigues M, Sideris DI, Taylor CG, Aprile FA, Muyldermans S, Knowles TPJ, Vendruscolo M, Bryant C, Blennow K, Skoog I, Kern S, et al. Soluble aggregates present in cerebrospinal fluid change in size and mechanism of toxicity during Alzheimer's disease progression. Acta Neuropathologica Communications. 7: 120. PMID 31349874 DOI: 10.1186/S40478-019-0777-4 |
0.371 |
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| 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 |
0.509 |
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| 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 |
0.557 |
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| 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 |
0.478 |
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| 2019 |
Eshun-Wilson L, Zhang R, Portran D, Nachury MV, Toso DB, Löhr T, Vendruscolo M, Bonomi M, Fraser JS, Nogales E. Effects of α-tubulin acetylation on microtubule structure and stability. Proceedings of the National Academy of Sciences of the United States of America. PMID 31072936 DOI: 10.1073/Pnas.1900441116 |
0.353 |
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| 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 |
0.505 |
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| 2019 |
Huang C, Wagner-Valladolid S, Stephens AD, Jung R, Poudel C, Sinnige T, Lechler MC, Schlörit N, Lu M, Laine RF, Michel CH, Vendruscolo M, Kaminski CF, Kaminski Schierle GS, David DC. Intrinsically aggregation-prone proteins form amyloid-like aggregates and contribute to tissue aging in . Elife. 8. PMID 31050339 DOI: 10.7554/Elife.43059 |
0.428 |
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| 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 |
0.536 |
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| 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 |
0.405 |
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| 2019 |
Kukic P, Lo Piccolo GM, Nogueira MO, Svergun DI, Vendruscolo M, Felli IC, Pierattelli R. The free energy landscape of the oncogene protein E7 of human papillomavirus type 16 reveals a complex interplay between ordered and disordered regions. Scientific Reports. 9: 5822. PMID 30967564 DOI: 10.1038/S41598-019-41925-4 |
0.439 |
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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 |
0.46 |
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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, ... Vendruscolo M, 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 |
0.525 |
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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 |
0.542 |
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| 2019 |
Sanagavarapu K, Nüske E, Nasir I, Meisl G, Immink JN, Sormanni P, Vendruscolo M, Knowles TPJ, Malmendal A, Cabaleiro-Lago C, Linse S. A method of predicting the in vitro fibril formation propensity of Aβ40 mutants based on their inclusion body levels in E. coli. Scientific Reports. 9: 3680. PMID 30842594 DOI: 10.1038/S41598-019-39216-Z |
0.401 |
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| 2019 |
Sormanni P, Vendruscolo M. Protein Solubility Predictions Using the CamSol Method in the Study of Protein Homeostasis. Cold Spring Harbor Perspectives in Biology. PMID 30833455 DOI: 10.1101/Cshperspect.A033845 |
0.434 |
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| 2019 |
Ruggeri FS, Šneideris T, Vendruscolo M, Knowles TPJ. Atomic force microscopy for single molecule characterisation of protein aggregation. Archives of Biochemistry and Biophysics. PMID 30742801 DOI: 10.1016/J.Abb.2019.02.001 |
0.43 |
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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, ... ... Vendruscolo M, 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 |
0.504 |
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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 |
0.505 |
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| 2019 |
Huang C, Wagner-Valladolid S, Stephens AD, Jung R, Poudel C, Sinnige T, Lechler MC, Schlörit N, Lu M, Laine RF, Michel CH, Vendruscolo M, Kaminski CF, Schierle GSK, David DC. Author response: Intrinsically aggregation-prone proteins form amyloid-like aggregates and contribute to tissue aging in Caenorhabditis elegans Elife. DOI: 10.7554/Elife.43059.020 |
0.383 |
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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 |
0.456 |
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| 2019 |
Heller GT, Aprile FA, Bonomi M, Camilloni C, De Simone A, Vendruscolo M. Probing Specificity in Disordered Protein Interactions with Small Molecules using Integrative Methods Biophysical Journal. 116: 180a. DOI: 10.1016/J.Bpj.2018.11.998 |
0.613 |
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| 2019 |
Löhr T, Kohlhoff K, Heller G, Vendruscolo M. Structure and Dynamics of Alzheimer's Associated Amyloid-Beta Peptide Biophysical Journal. 116: 437a. DOI: 10.1016/J.Bpj.2018.11.2352 |
0.771 |
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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 |
0.427 |
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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 |
0.424 |
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| 2018 |
Marinho da Silva Neto A, Silva SR, Vendruscolo M, Camilloni C, Montalvao RW. A superposition free method for protein conformational ensemble analyses and local clustering based on a differential geometry representation of backbone. Proteins. PMID 30582223 DOI: 10.1002/Prot.25652 |
0.656 |
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| 2018 |
Bonomi M, Vendruscolo M. Determination of protein structural ensembles using cryo-electron microscopy. Current Opinion in Structural Biology. 56: 37-45. PMID 30502729 DOI: 10.1016/J.Sbi.2018.10.006 |
0.394 |
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| 2018 |
Rangan R, Bonomi M, Heller GT, Cesari A, Bussi G, Vendruscolo M. Determination of Structural Ensembles of Proteins: Restraining vs Reweighting. Journal of Chemical Theory and Computation. PMID 30428663 DOI: 10.1021/Acs.Jctc.8B00738 |
0.375 |
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| 2018 |
Bonomi M, Hanot S, Greenberg CH, Sali A, Nilges M, Vendruscolo M, Pellarin R. Bayesian Weighing of Electron Cryo-Microscopy Data for Integrative Structural Modeling. Structure (London, England : 1993). PMID 30393052 DOI: 10.1016/J.Str.2018.09.011 |
0.496 |
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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 |
0.532 |
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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 |
0.52 |
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| 2018 |
Waudby CA, Wlodarski T, Karyadi ME, Cassaignau AME, Chan SHS, Wentink AS, Schmidt-Engler JM, Camilloni C, Vendruscolo M, Cabrita LD, Christodoulou J. Systematic mapping of free energy landscapes of a growing filamin domain during biosynthesis. Proceedings of the National Academy of Sciences of the United States of America. PMID 30201720 DOI: 10.1073/Pnas.1716252115 |
0.654 |
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| 2018 |
Tomba G, Camilloni C, Vendruscolo M. Determination of the conformational states of strychnine using NMR residual dipolar couplings in a tensor-free approach. Methods (San Diego, Calif.). PMID 30036639 DOI: 10.1016/J.Ymeth.2018.07.005 |
0.644 |
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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 |
0.503 |
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| 2018 |
Papaleo E, Camilloni C, Teilum K, Vendruscolo M, Lindorff-Larsen K. Molecular dynamics ensemble refinement of the heterogeneous native state of NCBD using chemical shifts and NOEs. Peerj. 6: e5125. PMID 30013831 DOI: 10.7717/Peerj.5125 |
0.69 |
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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 |
0.548 |
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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, ... ... Vendruscolo M, 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 |
0.5 |
|
| 2018 |
Vahidi S, Ripstein ZA, Bonomi M, Yuwen T, Mabanglo MF, Juravsky JB, Rizzolo K, Velyvis A, Houry WA, Vendruscolo M, Rubinstein JL, Kay LE. Reversible inhibition of the ClpP protease via an N-terminal conformational switch. Proceedings of the National Academy of Sciences of the United States of America. PMID 29941580 DOI: 10.1073/Pnas.1805125115 |
0.433 |
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| 2018 |
Possenti A, Vendruscolo M, Camilloni C, Tiana G. A method for partitioning the information contained in a protein sequence between its structure and function. Proteins. PMID 29790601 DOI: 10.1002/Prot.25527 |
0.637 |
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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 |
0.492 |
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| 2018 |
Bongiovanni MN, Aprile FA, Sormanni P, Vendruscolo M. A Rationally Designed Hsp70 Variant Rescues the Aggregation-Associated Toxicity of Human IAPP in Cultured Pancreatic Islet β-Cells. International Journal of Molecular Sciences. 19. PMID 29757200 DOI: 10.3390/Ijms19051443 |
0.401 |
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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 |
0.796 |
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| 2018 |
Qamar S, Wang G, Randle SJ, Ruggeri FS, Varela JA, Lin JQ, Phillips EC, Miyashita A, Williams D, Ströhl F, Meadows W, Ferry R, Dardov VJ, Tartaglia GG, Farrer LA, ... ... Vendruscolo M, et al. FUS Phase Separation Is Modulated by a Molecular Chaperone and Methylation of Arginine Cation-π Interactions. Cell. 173: 720-734.e15. PMID 29677515 DOI: 10.1016/J.Cell.2018.03.056 |
0.323 |
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| 2018 |
Bonomi M, Pellarin R, Vendruscolo M. Simultaneous Determination of Protein Structure and Dynamics Using Cryo-Electron Microscopy. Biophysical Journal. 114: 1604-1613. PMID 29642030 DOI: 10.1016/J.Bpj.2018.02.028 |
0.353 |
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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 |
0.469 |
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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 |
0.586 |
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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 |
0.718 |
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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 |
0.546 |
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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, ... Vendruscolo M, 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 |
0.401 |
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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 |
0.386 |
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| 2018 |
Staats R, Flagmeier P, Vendruscolo M. Systematic Development of Small Molecules to Inhibit Specific Steps of α-Synuclein Aggregation in Parkinson's Disease Biophysical Journal. 114: 77a. DOI: 10.1016/J.Bpj.2017.11.469 |
0.33 |
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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 |
0.467 |
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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 |
0.461 |
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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 |
0.473 |
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| 2018 |
Simone Ruggeri F, Habchi J, Chia S, Vendruscolo M, Knowles TP. Probing the Interaction of ABETA42 Amyloid Species with an Aggregation Suppressor Molecule by Infrared Nanospectroscopy Biophysical Journal. 114: 224a. DOI: 10.1016/J.Bpj.2017.11.1246 |
0.318 |
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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 |
0.488 |
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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 |
0.703 |
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| 2017 |
Piovesan D, Tabaro F, Paladin L, Necci M, Micetic I, Camilloni C, Davey N, Dosztányi Z, Mészáros B, Monzon AM, Parisi G, Schad E, Sormanni P, Tompa P, Vendruscolo M, et al. MobiDB 3.0: more annotations for intrinsic disorder, conformational diversity and interactions in proteins. Nucleic Acids Research. PMID 29136219 DOI: 10.1093/Nar/Gkx1071 |
0.65 |
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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 |
0.502 |
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| 2017 |
Martínez-Sáez N, Sun S, Oldrini D, Sormanni P, Boutureira O, Carboni F, Compañón I, Deery M, Vendruscolo M, Corzana F, Adamo R, Bernardes GJL. Oxetane grafts site-selectively installed on native disulfides enhance protein stability and activity in vivo. Angewandte Chemie (International Ed. in English). PMID 28968001 DOI: 10.1002/Anie.201708847 |
0.351 |
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| 2017 |
Aprile FA, Källstig E, Limorenko G, Vendruscolo M, Ron D, Hansen C. The molecular chaperones DNAJB6 and Hsp70 cooperate to suppress α-synuclein aggregation. Scientific Reports. 7: 9039. PMID 28831037 DOI: 10.1038/S41598-017-08324-Z |
0.379 |
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| 2017 |
Heller GT, Aprile FA, Bonomi M, Camilloni C, De Simone A, Vendruscolo M. Sequence Specificity in the Entropy-Driven Binding of a Small Molecule and a Disordered Peptide. Journal of Molecular Biology. PMID 28743590 DOI: 10.1016/J.Jmb.2017.07.016 |
0.652 |
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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 |
0.499 |
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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 |
0.453 |
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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, 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 |
0.711 |
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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 |
0.543 |
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| 2017 |
Heller GT, Aprile FA, Vendruscolo M. Methods of probing the interactions between small molecules and disordered proteins. Cellular and Molecular Life Sciences : Cmls. PMID 28631009 DOI: 10.1007/S00018-017-2563-4 |
0.402 |
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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 |
0.512 |
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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 |
0.582 |
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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 |
0.42 |
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| 2017 |
Kukic P, Pustovalova Y, Camilloni C, Gianni S, Korzhnev DM, Vendruscolo M. Structural characterization of the early events in the nucleation-condensation mechanism in a protein folding process. Journal of the American Chemical Society. PMID 28401755 DOI: 10.1021/Jacs.7B01540 |
0.684 |
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| 2017 |
Hultqvist G, Åberg E, Camilloni C, Sundell GN, Andersson E, Dogan J, Chi CN, Vendruscolo M, Jemth P. Emergence and evolution of an interaction between intrinsically disordered proteins. Elife. 6. PMID 28398197 DOI: 10.7554/Elife.16059 |
0.649 |
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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 |
0.507 |
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| 2017 |
Yoshimura Y, Holmberg MA, Kukic P, Andersen CB, Mata-Cabana A, Falsone SF, Vendruscolo M, Nollen EA, Mulder FA. MOAG-4 Promotes the Aggregation of α-Synuclein by Competing with Self-Protective Electrostatic Interactions. The Journal of Biological Chemistry. PMID 28336532 DOI: 10.1074/Jbc.M116.764886 |
0.447 |
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| 2017 |
Sormanni P, Piovesan D, Heller GT, Bonomi M, Kukic P, Camilloni C, Fuxreiter M, Dosztanyi Z, Pappu RV, Babu MM, Longhi S, Tompa P, Dunker AK, Uversky VN, Tosatto SC, ... Vendruscolo M, et al. Simultaneous quantification of protein order and disorder. Nature Chemical Biology. 13: 339-342. PMID 28328918 DOI: 10.1038/Nchembio.2331 |
0.658 |
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| 2017 |
Sin O, de Jong T, Mata-Cabana A, Kudron M, Zaini MA, Aprile FA, Seinstra RI, Stroo E, Prins RW, Martineau CN, Wang HH, Hogewerf W, Steinhof A, Wanker EE, Vendruscolo M, et al. Identification of an RNA Polymerase III Regulator Linked to Disease-Associated Protein Aggregation. Molecular Cell. 65: 1096-1108.e6. PMID 28306505 DOI: 10.1016/J.Molcel.2017.02.022 |
0.431 |
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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, ... ... Vendruscolo M, 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 |
0.404 |
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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 |
0.442 |
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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 |
0.531 |
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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, ... ... Vendruscolo M, 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 |
0.472 |
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| 2017 |
Borkar AN, Vallurupalli P, Camilloni C, Kay LE, Vendruscolo M. Simultaneous NMR characterisation of multiple minima in the free energy landscape of an RNA UUCG tetraloop. Physical Chemistry Chemical Physics : Pccp. PMID 28067358 DOI: 10.1039/C6Cp08313G |
0.605 |
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| 2017 |
Bonomi M, Heller GT, Camilloni C, Vendruscolo M. Principles of protein structural ensemble determination. Current Opinion in Structural Biology. 42: 106-116. PMID 28063280 DOI: 10.1016/J.Sbi.2016.12.004 |
0.687 |
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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 |
0.513 |
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| 2017 |
Wang Y, Camilloni C, Kim J, Vendruscolo M, Gao J, Veglia G. Characterization of Protein Kinase a Free Energy Landscape by NMR-Restrained Metadynamics Biophysical Journal. 112: 50a. DOI: 10.1016/J.Bpj.2016.11.310 |
0.722 |
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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 |
0.444 |
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| 2017 |
Cassaignau AM, Launay HM, Waudby CA, Wlodarski T, Karyadi M, Robertson AL, Wang X, Camilloni C, Vendruscolo M, Woolhead CA, Cabrita L, Christodoulou J. Structural Investigation of an Immunoglobulin Domain on the Ribosome using NMR Spectroscopy Biophysical Journal. 112: 41a. DOI: 10.1016/J.Bpj.2016.11.258 |
0.677 |
|
| 2016 |
Holliday MJ, Camilloni C, Armstrong GS, Vendruscolo M, Eisenmesser EZ. Networks of Dynamic Allostery Regulate Enzyme Function. Structure (London, England : 1993). PMID 28089447 DOI: 10.1016/J.Str.2016.12.003 |
0.591 |
|
| 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 |
0.504 |
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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 |
0.694 |
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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 |
0.479 |
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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 |
0.691 |
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| 2016 |
Bonomi M, Camilloni C, Vendruscolo M. Metadynamic metainference: Enhanced sampling of the metainference ensemble using metadynamics. Scientific Reports. 6: 31232. PMID 27561930 DOI: 10.1038/Srep31232 |
0.618 |
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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 |
0.486 |
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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 |
0.71 |
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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 |
0.697 |
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| 2016 |
Borkar AN, Bardaro MF, Camilloni C, Aprile FA, Varani G, Vendruscolo M. Structure of a low-population binding intermediate in protein-RNA recognition. Proceedings of the National Academy of Sciences of the United States of America. PMID 27286828 DOI: 10.1073/Pnas.1521349113 |
0.639 |
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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 |
0.537 |
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| 2016 |
Camilloni C, Sala BM, Sormanni P, Porcari R, Corazza A, De Rosa M, Zanini S, Barbiroli A, Esposito G, Bolognesi M, Bellotti V, Vendruscolo M, Ricagno S. Rational design of mutations that change the aggregation rate of a protein while maintaining its native structure and stability. Scientific Reports. 6: 25559. PMID 27150430 DOI: 10.1038/Srep25559 |
0.685 |
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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 |
0.523 |
|
| 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 |
0.712 |
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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 |
0.503 |
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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 |
0.559 |
|
| 2016 |
Bonetti D, Camilloni C, Visconti L, Longhi S, Brunori M, Vendruscolo M, Gianni S. Identification and Structural Characterization of an Intermediate in the Folding of the Measles Virus X domain. The Journal of Biological Chemistry. PMID 27002146 DOI: 10.1074/Jbc.M116.721126 |
0.65 |
|
| 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 |
0.506 |
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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 |
0.697 |
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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 |
0.511 |
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| 2016 |
Toto A, Camilloni C, Giri R, Brunori M, Vendruscolo M, Gianni S. Molecular Recognition by Templated Folding of an Intrinsically Disordered Protein. Scientific Reports. 6: 21994. PMID 26912067 DOI: 10.1038/Srep21994 |
0.664 |
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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 |
0.499 |
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| 2016 |
Bonomi M, Camilloni C, Cavalli A, Vendruscolo M. Metainference: A Bayesian inference method for heterogeneous systems. Science Advances. 2: e1501177. PMID 26844300 DOI: 10.1126/Sciadv.1501177 |
0.609 |
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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 |
0.54 |
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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 |
0.404 |
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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 |
0.445 |
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| 2015 |
Camilloni C, Vendruscolo M. Using pseudocontact shifts and residual dipolar couplings as exact NMR restraints for the determination of protein structural ensembles. Biochemistry. PMID 26624789 DOI: 10.1021/Acs.Biochem.5B01138 |
0.663 |
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| 2015 |
Kukic P, Lundström P, Camilloni C, Evenäs J, Akke M, Vendruscolo M. Structural insights into the calcium-mediated allosteric transition in the C-terminal domain of calmodulin from NMR measurements. Biochemistry. PMID 26618792 DOI: 10.1021/Acs.Biochem.5B00961 |
0.639 |
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| 2015 |
Murakami T, Qamar S, Lin JQ, Schierle GS, Rees E, Miyashita A, Costa AR, Dodd RB, Chan FT, Michel CH, Kronenberg-Versteeg D, Li Y, Yang SP, Wakutani Y, Meadows W, ... ... Vendruscolo M, et al. ALS/FTD Mutation-Induced Phase Transition of FUS Liquid Droplets and Reversible Hydrogels into Irreversible Hydrogels Impairs RNP Granule Function. Neuron. PMID 26526393 DOI: 10.1016/J.Neuron.2015.10.030 |
0.32 |
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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 |
0.523 |
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| 2015 |
Kukic P, Kannan A, Dijkstra MJ, Abeln S, Camilloni C, Vendruscolo M. Mapping the Protein Fold Universe Using the CamTube Force Field in Molecular Dynamics Simulations. Plos Computational Biology. 11: e1004435. PMID 26505754 DOI: 10.1371/Journal.Pcbi.1004435 |
0.665 |
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| 2015 |
Granata D, Baftizadeh F, Habchi J, Galvagnion C, De Simone A, Camilloni C, Laio A, Vendruscolo M. The inverted free energy landscape of an intrinsically disordered peptide by simulations and experiments. Scientific Reports. 5: 15449. PMID 26498066 DOI: 10.1038/Srep15449 |
0.654 |
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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 |
0.56 |
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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 |
0.434 |
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| 2015 |
Joshi P, Vendruscolo M. Druggability of Intrinsically Disordered Proteins. Advances in Experimental Medicine and Biology. 870: 383-400. PMID 26387110 DOI: 10.1007/978-3-319-20164-1_13 |
0.413 |
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| 2015 |
Fu B, Vendruscolo M. Structure and Dynamics of Intrinsically Disordered Proteins. Advances in Experimental Medicine and Biology. 870: 35-48. PMID 26387099 DOI: 10.1007/978-3-319-20164-1_2 |
0.46 |
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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 |
0.584 |
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| 2015 |
Heller GT, Sormanni P, Vendruscolo M. Targeting disordered proteins with small molecules using entropy. Trends in Biochemical Sciences. 40: 491-6. PMID 26275458 DOI: 10.1016/J.Tibs.2015.07.004 |
0.416 |
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| 2015 |
Sormanni P, Aprile FA, Vendruscolo M. Rational design of antibodies targeting specific epitopes within intrinsically disordered proteins. Proceedings of the National Academy of Sciences of the United States of America. 112: 9902-7. PMID 26216991 DOI: 10.1073/Pnas.1422401112 |
0.336 |
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| 2015 |
Collepardo-Guevara R, Portella G, Vendruscolo M, Frenkel D, Schlick T, Orozco M. Chromatin Unfolding by Epigenetic Modifications Explained by Dramatic Impairment of Internucleosome Interactions: A Multiscale Computational Study. Journal of the American Chemical Society. 137: 10205-15. PMID 26192632 DOI: 10.1021/Jacs.5B04086 |
0.312 |
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| 2015 |
Aprile FA, Sormanni P, Vendruscolo M. A Rational Design Strategy for the Selective Activity Enhancement of a Molecular Chaperone toward a Target Substrate. Biochemistry. 54: 5103-12. PMID 26192230 DOI: 10.1021/Acs.Biochem.5B00459 |
0.409 |
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| 2015 |
Pustovalova Y, Kukic P, Vendruscolo M, Korzhnev DM. Probing the Residual Structure of the Low Populated Denatured State of ADA2h under Folding Conditions by Relaxation Dispersion Nuclear Magnetic Resonance Spectroscopy. Biochemistry. 54: 4611-22. PMID 26115097 DOI: 10.1021/Acs.Biochem.5B00345 |
0.437 |
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| 2015 |
Borkar AN, Vallurupalli P, Camilloni C, Kay LE, Vendruscolo M. 89 Constructing free energy landscapes of RNAs at atomic resolution and characterisation of their excited states. Journal of Biomolecular Structure & Dynamics. 33: 58. PMID 26103301 DOI: 10.1080/07391102.2015.1032706 |
0.557 |
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| 2015 |
Brewer KD, Bacaj T, Cavalli A, Camilloni C, Swarbrick JD, Liu J, Zhou A, Zhou P, Barlow N, Xu J, Seven AB, Prinslow EA, Voleti R, Häussinger D, Bonvin AM, ... ... Vendruscolo M, et al. Dynamic binding mode of a Synaptotagmin-1-SNARE complex in solution. Nature Structural & Molecular Biology. 22: 555-64. PMID 26030874 DOI: 10.1038/Nsmb.3035 |
0.607 |
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| 2015 |
Camilloni C, Vendruscolo M. Reply to "Comment on 'A Tensor-Free Method for the Structural and Dynamic Refinement of Proteins using Residual Dipolar Couplings'". The Journal of Physical Chemistry. B. 119: 8225-6. PMID 26030476 DOI: 10.1021/Acs.Jpcb.5B04166 |
0.65 |
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| 2015 |
Cavalli A, Vendruscolo M. Analysis of the performance of the CHESHIRE and YAPP methods at CASD-NMR round 3. Journal of Biomolecular Nmr. PMID 25990018 DOI: 10.1007/S10858-015-9940-9 |
0.344 |
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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 |
0.54 |
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| 2015 |
Holliday MJ, Camilloni C, Armstrong GS, Isern NG, Zhang F, Vendruscolo M, Eisenmesser EZ. Structure and Dynamics of GeoCyp: A Thermophilic Cyclophilin with a Novel Substrate Binding Mechanism That Functions Efficiently at Low Temperatures. Biochemistry. 54: 3207-17. PMID 25923019 DOI: 10.1021/Acs.Biochem.5B00263 |
0.634 |
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| 2015 |
Kukic P, Alvin Leung HT, Bemporad F, Aprile FA, Kumita JR, De Simone A, Camilloni C, Vendruscolo M. Structure and dynamics of the integrin LFA-1 I-domain in the inactive state underlie its inside-out/outside-in signaling and allosteric mechanisms. Structure (London, England : 1993). 23: 745-53. PMID 25773142 DOI: 10.1016/J.Str.2014.12.020 |
0.624 |
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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 |
0.548 |
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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 |
0.709 |
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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 |
0.571 |
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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 |
0.44 |
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| 2015 |
Sormanni P, Camilloni C, Fariselli P, Vendruscolo M. The s2D method: simultaneous sequence-based prediction of the statistical populations of ordered and disordered regions in proteins. Journal of Molecular Biology. 427: 982-96. PMID 25534081 DOI: 10.1016/J.Jmb.2014.12.007 |
0.655 |
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| 2015 |
Porcari R, Proukakis C, Waudby CA, Bolognesi B, Mangione PP, Paton JF, Mullin S, Cabrita LD, Penco A, Relini A, Verona G, Vendruscolo M, Stoppini M, Tartaglia GG, Camilloni C, et al. The H50Q mutation induces a 10-fold decrease in the solubility of α-synuclein. The Journal of Biological Chemistry. 290: 2395-404. PMID 25505181 DOI: 10.1074/Jbc.M114.610527 |
0.642 |
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| 2015 |
Sormanni P, Aprile FA, Vendruscolo M. The CamSol method of rational design of protein mutants with enhanced solubility. Journal of Molecular Biology. 427: 478-90. PMID 25451785 DOI: 10.1016/J.Jmb.2014.09.026 |
0.407 |
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| 2015 |
Takahashi H, Adachi N, Shirafuji T, Danno S, Ueyama T, Vendruscolo M, Shuvaev AN, Sugimoto T, Seki T, Hamada D, Irie K, Hirai H, Sakai N, Saito N. Identification and characterization of PKCγ, a kinase associated with SCA14, as an amyloidogenic protein. Human Molecular Genetics. 24: 525-39. PMID 25217572 DOI: 10.1093/Hmg/Ddu472 |
0.413 |
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| 2015 |
Camilloni C, Vendruscolo M. A tensor-free method for the structural and dynamical refinement of proteins using residual dipolar couplings. The Journal of Physical Chemistry. B. 119: 653-61. PMID 24824082 DOI: 10.1021/Jp5021824 |
0.657 |
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| 2015 |
Waudby C, Proukakis C, Porcari R, Bellotti V, Shapira A, Christodoulou J, Camilloni C, Tartaglia GG, Stoppini M, Verona G, Vendruscolo M, Relini A, Penco A, Cabrita L, Mullin S, et al. 1H, 13C, and 15N chemical shift assignments for alpha-synuclein monomer (WT) Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr25227 |
0.558 |
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| 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 |
0.476 |
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| 2015 |
Wlodarski T, Waudby C, Sammy C, Vendruscolo M, Christodoulou J. The Computational Studies of Co-Translational Protein Folding Biophysical Journal. 108: 515a. DOI: 10.1016/J.Bpj.2014.11.2823 |
0.469 |
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| 2014 |
Sanfelice D, De Simone A, Cavalli A, Faggiano S, Vendruscolo M, Pastore A. Characterization of the conformational fluctuations in the Josephin domain of ataxin-3. Biophysical Journal. 107: 2932-40. PMID 25517158 DOI: 10.1016/J.Bpj.2014.10.008 |
0.336 |
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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 |
0.523 |
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| 2014 |
Gianni S, Camilloni C, Giri R, Toto A, Bonetti D, Morrone A, Sormanni P, Brunori M, Vendruscolo M. Understanding the frustration arising from the competition between function, misfolding, and aggregation in a globular protein. Proceedings of the National Academy of Sciences of the United States of America. 111: 14141-6. PMID 25228761 DOI: 10.1073/Pnas.1405233111 |
0.686 |
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| 2014 |
Boomsma W, Tian P, Frellsen J, Ferkinghoff-Borg J, Hamelryck T, Lindorff-Larsen K, Vendruscolo M. Equilibrium simulations of proteins using molecular fragment replacement and NMR chemical shifts. Proceedings of the National Academy of Sciences of the United States of America. 111: 13852-7. PMID 25192938 DOI: 10.1073/Pnas.1404948111 |
0.45 |
|
| 2014 |
Leung HT, Kukic P, Camilloni C, Bemporad F, De Simone A, Aprile FA, Kumita JR, Vendruscolo M. NMR characterization of the conformational fluctuations of the human lymphocyte function-associated antigen-1 I-domain. Protein Science : a Publication of the Protein Society. 23: 1596-606. PMID 25147050 DOI: 10.1002/Pro.2538 |
0.62 |
|
| 2014 |
Camilloni C, Sahakyan AB, Holliday MJ, Isern NG, Zhang F, Eisenmesser EZ, Vendruscolo M. Cyclophilin A catalyzes proline isomerization by an electrostatic handle mechanism. Proceedings of the National Academy of Sciences of the United States of America. 111: 10203-8. PMID 24982184 DOI: 10.1073/Pnas.1404220111 |
0.767 |
|
| 2014 |
Camilloni C, Vendruscolo M. Statistical mechanics of the denatured state of a protein using replica-averaged metadynamics. Journal of the American Chemical Society. 136: 8982-91. PMID 24884637 DOI: 10.1021/Ja5027584 |
0.678 |
|
| 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 |
0.489 |
|
| 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 |
0.561 |
|
| 2014 |
Blombach F, Launay H, Snijders AP, Zorraquino V, Wu H, de Koning B, Brouns SJ, Ettema TJ, Camilloni C, Cavalli A, Vendruscolo M, Dickman MJ, Cabrita LD, La Teana A, Benelli D, et al. Archaeal MBF1 binds to 30S and 70S ribosomes via its helix-turn-helix domain. The Biochemical Journal. 462: 373-84. PMID 24825021 DOI: 10.1042/Bj20131474 |
0.612 |
|
| 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 |
0.711 |
|
| 2014 |
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 |
0.543 |
|
| 2014 |
Fu B, Sahakyan AB, Camilloni C, Tartaglia GG, Paci E, Caflisch A, Vendruscolo M, Cavalli A. ALMOST: an all atom molecular simulation toolkit for protein structure determination. Journal of Computational Chemistry. 35: 1101-5. PMID 24676684 DOI: 10.1002/Jcc.23588 |
0.811 |
|
| 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 |
0.695 |
|
| 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 |
0.565 |
|
| 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, ... ... Vendruscolo M, 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 |
|
| 2014 |
Kukic P, Camilloni C, Cavalli A, Vendruscolo M. Determination of the individual roles of the linker residues in the interdomain motions of calmodulin using NMR chemical shifts. Journal of Molecular Biology. 426: 1826-38. PMID 24530797 DOI: 10.1016/J.Jmb.2014.02.002 |
0.664 |
|
| 2014 |
Kannan A, Camilloni C, Sahakyan AB, Cavalli A, Vendruscolo M. A conformational ensemble derived using NMR methyl chemical shifts reveals a mechanical clamping transition that gates the binding of the HU protein to DNA. Journal of the American Chemical Society. 136: 2204-7. PMID 24517490 DOI: 10.1021/Ja4105396 |
0.795 |
|
| 2014 |
Montalvao R, Camilloni C, De Simone A, Vendruscolo M. New opportunities for tensor-free calculations of residual dipolar couplings for the study of protein dynamics. Journal of Biomolecular Nmr. 58: 233-8. PMID 24477919 DOI: 10.1007/S10858-013-9801-3 |
0.672 |
|
| 2014 |
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 |
0.548 |
|
| 2014 |
Kendrick AA, Holliday MJ, Isern NG, Zhang F, Camilloni C, Huynh C, Vendruscolo M, Armstrong G, Eisenmesser EZ. The dynamics of interleukin-8 and its interaction with human CXC receptor I peptide. Protein Science : a Publication of the Protein Society. 23: 464-80. PMID 24442768 DOI: 10.1002/Pro.2430 |
0.611 |
|
| 2014 |
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 |
0.52 |
|
| 2014 |
Varadi M, Kosol S, Lebrun P, Valentini E, Blackledge M, Dunker AK, Felli IC, Forman-Kay JD, Kriwacki RW, Pierattelli R, Sussman J, Svergun DI, Uversky VN, Vendruscolo M, Wishart D, et al. pE-DB: a database of structural ensembles of intrinsically disordered and of unfolded proteins. Nucleic Acids Research. 42: D326-35. PMID 24174539 DOI: 10.1093/Nar/Gkt960 |
0.416 |
|
| 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 |
0.405 |
|
| 2014 |
Holliday M, Camilloni C, Armstrong G, Isern N, Zhang F, Vendruscolo M, Eisenmesser E. Backbone assignments for human Cyclophilin C Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr25341 |
0.547 |
|
| 2014 |
Holliday M, Camilloni C, Armstrong G, Isern N, Zhang F, Vendruscolo M, Eisenmesser E. Backbone amide assignments for human Cyclophilin C with saturating concentrations of the model peptide GSFGPDLRAGD Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr25339 |
0.571 |
|
| 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 |
0.498 |
|
| 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 |
0.564 |
|
| 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 |
0.561 |
|
| 2014 |
Fu B, Kukic P, Camilloni C, Vendruscolo M. MD Simulations of Intrinsically Disordered Proteins with Replica-Averaged Chemical Shift Restraints Biophysical Journal. 106: 481a. DOI: 10.1016/J.Bpj.2013.11.2714 |
0.671 |
|
| 2014 |
Camilloni C, Vendruscolo M. Conformational Equilibrium between the Sub States of the Acidic Denatured State of ACBP Determined by NMR Chemical Shifts and Metadynamics Biophysical Journal. 106: 459a-460a. DOI: 10.1016/J.Bpj.2013.11.2605 |
0.684 |
|
| 2014 |
Habchi J, Joshi P, Spilotros A, Svergun D, Vendruscolo M. Structural and Mechanistic Analyses of the Effects of Small Compounds on Amyloid Beta Self-Assembly Biophysical Journal. 106: 269a. DOI: 10.1016/J.Bpj.2013.11.1579 |
0.409 |
|
| 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 |
0.729 |
|
| 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 |
0.584 |
|
| 2013 |
Camilloni C, Cavalli A, Vendruscolo M. Replica-Averaged Metadynamics. Journal of Chemical Theory and Computation. 9: 5610-7. PMID 26592295 DOI: 10.1021/Ct4006272 |
0.64 |
|
| 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 |
0.517 |
|
| 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 |
0.556 |
|
| 2013 |
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 |
0.565 |
|
| 2013 |
Tsytlonok M, Sormanni P, Rowling PJ, Vendruscolo M, Itzhaki LS. Subdomain architecture and stability of a giant repeat protein. The Journal of Physical Chemistry. B. 117: 13029-37. PMID 24053231 DOI: 10.1021/Jp402360X |
0.308 |
|
| 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 |
0.704 |
|
| 2013 |
De Simone A, Gustavsson M, Montalvao RW, Shi L, Veglia G, Vendruscolo M. Structures of the excited states of phospholamban and shifts in their populations upon phosphorylation. Biochemistry. 52: 6684-94. PMID 23968132 DOI: 10.1021/Bi400517B |
0.385 |
|
| 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 |
0.532 |
|
| 2013 |
Camilloni C, Vendruscolo M. A relationship between the aggregation rates of α-synuclein variants and the β-sheet populations in their monomeric forms. The Journal of Physical Chemistry. B. 117: 10737-41. PMID 23941114 DOI: 10.1021/Jp405614J |
0.692 |
|
| 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 |
0.535 |
|
| 2013 |
Suardíaz R, Sahakyan AB, Vendruscolo M. A geometrical parametrization of C1'-C5' RNA ribose chemical shifts calculated by density functional theory. The Journal of Chemical Physics. 139: 034101. PMID 23883004 DOI: 10.1063/1.4811498 |
0.786 |
|
| 2013 |
Borkar AN, De Simone A, Montalvao RW, Vendruscolo M. A method of determining RNA conformational ensembles using structure-based calculations of residual dipolar couplings. The Journal of Chemical Physics. 138: 215103. PMID 23758399 DOI: 10.1063/1.4804301 |
0.344 |
|
| 2013 |
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 |
0.524 |
|
| 2013 |
Granata D, Camilloni C, Vendruscolo M, Laio A. Characterization of the free-energy landscapes of proteins by NMR-guided metadynamics. Proceedings of the National Academy of Sciences of the United States of America. 110: 6817-22. PMID 23572592 DOI: 10.1073/Pnas.1218350110 |
0.667 |
|
| 2013 |
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 |
0.721 |
|
| 2013 |
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, ... ... Vendruscolo M, 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 |
0.538 |
|
| 2013 |
Vendruscolo M, Dobson CM. Structural biology: Protein self-assembly intermediates. Nature Chemical Biology. 9: 216-7. PMID 23508184 DOI: 10.1038/Nchembio.1210 |
0.514 |
|
| 2013 |
Cavalli A, Camilloni C, Vendruscolo M. Molecular dynamics simulations with replica-averaged structural restraints generate structural ensembles according to the maximum entropy principle. The Journal of Chemical Physics. 138: 094112. PMID 23485282 DOI: 10.1063/1.4793625 |
0.645 |
|
| 2013 |
Sahakyan AB, Vendruscolo M. Analysis of the contributions of ring current and electric field effects to the chemical shifts of RNA bases. The Journal of Physical Chemistry. B. 117: 1989-98. PMID 23398371 DOI: 10.1021/Jp3057306 |
0.653 |
|
| 2013 |
Vendruscolo M. Assessment of the quality of energy functions for protein folding by using a criterion derived with the help of the noisy go model. Journal of Biological Physics. 27: 205-15. PMID 23345744 DOI: 10.1023/A:1013152026788 |
0.333 |
|
| 2013 |
Camilloni C, Cavalli A, Vendruscolo M. Assessment of the use of NMR chemical shifts as replica-averaged structural restraints in molecular dynamics simulations to characterize the dynamics of proteins. The Journal of Physical Chemistry. B. 117: 1838-43. PMID 23327201 DOI: 10.1021/Jp3106666 |
0.666 |
|
| 2013 |
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 |
0.53 |
|
| 2013 |
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, ... ... Vendruscolo M, 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 |
0.456 |
|
| 2013 |
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, ... ... Vendruscolo M, et al. Atomic-resolution structure of a doublet cross-beta amyloid fibril Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr19058 |
0.44 |
|
| 2013 |
Cavalli A, Camilloni C, Vendruscolo M. Erratum: “Molecular dynamics simulations with replica-averaged structural restraints generate structural ensembles according to the maximum entropy principle” [J. Chem. Phys. 138, 094112 (2013)] The Journal of Chemical Physics. 139: 169903. DOI: 10.1063/1.4828456 |
0.62 |
|
| 2013 |
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 |
0.467 |
|
| 2013 |
Granata D, Baftizadeh Baghal F, Camilloni C, Vendruscolo M, Laio A. Thermodynamics of an Intrinsically Disordered Protein by Atomistic Simulations Biophysical Journal. 104: 55a. DOI: 10.1016/J.Bpj.2012.11.344 |
0.691 |
|
| 2013 |
Vendruscolo M. Characterization of Free Energy Landscapes of Proteins using NMR Spectroscopy Biophysical Journal. 104: 45a. DOI: 10.1016/J.Bpj.2012.11.287 |
0.438 |
|
| 2013 |
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 |
0.398 |
|
| 2012 |
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 |
0.484 |
|
| 2012 |
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 |
0.693 |
|
| 2012 |
Markley JL, Akutsu H, Asakura T, Baldus M, Boelens R, Bonvin A, Kaptein R, Bax A, Bezsonova I, Gryk MR, Hoch JC, Korzhnev DM, Maciejewski MW, Case D, Chazin WJ, ... ... Vendruscolo M, et al. In support of the BMRB. Nature Structural & Molecular Biology. 19: 854-60. PMID 22955930 DOI: 10.1038/Nsmb.2371 |
0.608 |
|
| 2012 |
Chambers JE, Petrova K, Tomba G, Vendruscolo M, Ron D. ADP ribosylation adapts an ER chaperone response to short-term fluctuations in unfolded protein load. The Journal of Cell Biology. 198: 371-85. PMID 22869598 DOI: 10.1083/Jcb.20120200511112014C |
0.382 |
|
| 2012 |
Montalvao RW, De Simone A, Vendruscolo M. Determination of structural fluctuations of proteins from structure-based calculations of residual dipolar couplings. Journal of Biomolecular Nmr. 53: 281-92. PMID 22729708 DOI: 10.1007/S10858-012-9644-3 |
0.446 |
|
| 2012 |
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 |
0.537 |
|
| 2012 |
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 |
0.496 |
|
| 2012 |
Chen J, Yagi H, Sormanni P, Vendruscolo M, Makabe K, Nakamura T, Goto Y, Kuwajima K. Fibrillogenic propensity of the GroEL apical domain: a Janus-faced minichaperone. Febs Letters. 586: 1120-7. PMID 22575645 DOI: 10.1016/J.Febslet.2012.03.019 |
0.359 |
|
| 2012 |
Neudecker P, Robustelli P, Cavalli A, Walsh P, Lundström P, Zarrine-Afsar A, Sharpe S, Vendruscolo M, Kay LE. Structure of an intermediate state in protein folding and aggregation. Science (New York, N.Y.). 336: 362-6. PMID 22517863 DOI: 10.1126/Science.1214203 |
0.466 |
|
| 2012 |
Sahakyan AB, Cavalli A, Vranken WF, Vendruscolo M. Protein structure validation using side-chain chemical shifts. The Journal of Physical Chemistry. B. 116: 4754-9. PMID 22455760 DOI: 10.1021/Jp2122054 |
0.712 |
|
| 2012 |
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 |
0.515 |
|
| 2012 |
Camilloni C, De Simone A, Vranken WF, Vendruscolo M. Determination of secondary structure populations in disordered states of proteins using nuclear magnetic resonance chemical shifts. Biochemistry. 51: 2224-31. PMID 22360139 DOI: 10.1021/Bi3001825 |
0.677 |
|
| 2012 |
Rosato A, Aramini JM, Arrowsmith C, Bagaria A, Baker D, Cavalli A, Doreleijers JF, Eletsky A, Giachetti A, Guerry P, Gutmanas A, Güntert P, He Y, Herrmann T, Huang YJ, ... ... Vendruscolo M, et al. Blind testing of routine, fully automated determination of protein structures from NMR data. Structure (London, England : 1993). 20: 227-36. PMID 22325772 DOI: 10.1016/J.Str.2012.01.002 |
0.556 |
|
| 2012 |
Camilloni C, Robustelli P, De Simone A, Cavalli A, Vendruscolo M. Characterization of the conformational equilibrium between the two major substates of RNase A using NMR chemical shifts. Journal of the American Chemical Society. 134: 3968-71. PMID 22320129 DOI: 10.1021/Ja210951Z |
0.682 |
|
| 2012 |
Vendruscolo M. Proteome folding and aggregation. Current Opinion in Structural Biology. 22: 138-43. PMID 22317916 DOI: 10.1016/J.Sbi.2012.01.005 |
0.442 |
|
| 2012 |
Agostini F, Vendruscolo M, Tartaglia GG. Sequence-based prediction of protein solubility. Journal of Molecular Biology. 421: 237-41. PMID 22172487 DOI: 10.1016/J.Jmb.2011.12.005 |
0.446 |
|
| 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 |
0.533 |
|
| 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 |
0.354 |
|
| 2011 |
Wolff K, Vendruscolo M, Porto M. Coarse-grained model for protein folding based on structural profiles. Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics. 84: 041934. PMID 22181202 DOI: 10.1103/Physreve.84.041934 |
0.407 |
|
| 2011 |
De Simone A, Montalvao RW, Vendruscolo M. Determination of Conformational Equilibria in Proteins Using Residual Dipolar Couplings. Journal of Chemical Theory and Computation. 7: 4189-4195. PMID 22180735 DOI: 10.1021/Ct200361B |
0.411 |
|
| 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 |
0.577 |
|
| 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 |
0.548 |
|
| 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 |
0.399 |
|
| 2011 |
Sahakyan AB, Vranken WF, Cavalli A, Vendruscolo M. Using side-chain aromatic proton chemical shifts for a quantitative analysis of protein structures. Angewandte Chemie (International Ed. in English). 50: 9620-3. PMID 21887824 DOI: 10.1002/Anie.201101641 |
0.713 |
|
| 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 |
0.471 |
|
| 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 |
0.417 |
|
| 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 |
0.469 |
|
| 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 |
0.579 |
|
| 2011 |
Vendruscolo M. Excited-state control of protein activity. Journal of Molecular Biology. 412: 153-4. PMID 21806994 DOI: 10.1016/J.Jmb.2011.07.047 |
0.309 |
|
| 2011 |
Sahakyan AB, Vranken WF, Cavalli A, Vendruscolo M. Structure-based prediction of methyl chemical shifts in proteins. Journal of Biomolecular Nmr. 50: 331-46. PMID 21748266 DOI: 10.1007/S10858-011-9524-2 |
0.722 |
|
| 2011 |
Kang L, Wu KP, Vendruscolo M, Baum J. The A53T mutation is key in defining the differences in the aggregation kinetics of human and mouse α-synuclein. Journal of the American Chemical Society. 133: 13465-70. PMID 21721555 DOI: 10.1021/Ja203979J |
0.565 |
|
| 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 |
0.77 |
|
| 2011 |
Vendruscolo M. Protein regulation: the statistical theory of allostery. Nature Chemical Biology. 7: 411-2. PMID 21685884 DOI: 10.1038/Nchembio.603 |
0.36 |
|
| 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 |
0.575 |
|
| 2011 |
Cavalli A, Montalvao RW, Vendruscolo M. Using chemical shifts to determine structural changes in proteins upon complex formation. The Journal of Physical Chemistry. B. 115: 9491-4. PMID 21639128 DOI: 10.1021/Jp202647Q |
0.383 |
|
| 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 |
0.773 |
|
| 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, ... ... Vendruscolo M, 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 |
0.535 |
|
| 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 |
0.503 |
|
| 2011 |
Olzscha H, Schermann SM, Woerner AC, Pinkert S, Hecht MH, Tartaglia GG, Vendruscolo M, Hayer-Hartl M, Hartl FU, Vabulas RM. Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions. Cell. 144: 67-78. PMID 21215370 DOI: 10.1016/J.Cell.2010.11.050 |
0.452 |
|
| 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 |
0.531 |
|
| 2011 |
Wolff K, Vendruscolo M, Porto M. Asymmetric folding pathways and transient misfolding in a coarse-grained model of proteins Epl (Europhysics Letters). 94: 48005. DOI: 10.1209/0295-5075/94/48005 |
0.417 |
|
| 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 |
0.536 |
|
| 2010 |
Szczepankiewicz O, Cabaleiro-Lago C, Tartaglia GG, Vendruscolo M, Hunter T, Hunter GJ, Nilsson H, Thulin E, Linse S. Interactions in the native state of monellin, which play a protective role against aggregation. Molecular Biosystems. 7: 521-32. PMID 21076757 DOI: 10.1039/C0Mb00155D |
0.447 |
|
| 2010 |
Gianni S, Ivarsson Y, De Simone A, Travaglini-Allocatelli C, Brunori M, Vendruscolo M. Structural characterization of a misfolded intermediate populated during the folding process of a PDZ domain. Nature Structural & Molecular Biology. 17: 1431-7. PMID 21076399 DOI: 10.1038/Nsmb.1956 |
0.458 |
|
| 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 |
0.522 |
|
| 2010 |
Lee Y, Zhou T, Tartaglia GG, Vendruscolo M, Wilke CO. Translationally optimal codons associate with aggregation-prone sites in proteins. Proteomics. 10: 4163-71. PMID 21046618 DOI: 10.1002/Pmic.201000229 |
0.359 |
|
| 2010 |
Pechmann S, Vendruscolo M. Derivation of a solubility condition for proteins from an analysis of the competition between folding and aggregation. Molecular Biosystems. 6: 2490-7. PMID 20957252 DOI: 10.1039/C005160H |
0.457 |
|
| 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 |
0.533 |
|
| 2010 |
Vendruscolo M. Enzymatic activity in disordered states of proteins. Current Opinion in Chemical Biology. 14: 671-5. PMID 20832351 DOI: 10.1016/J.Cbpa.2010.08.022 |
0.392 |
|
| 2010 |
Masino L, Nicastro G, Calder L, Vendruscolo M, Pastore A. Functional interactions as a survival strategy against abnormal aggregation. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 25: 45-54. PMID 20810784 DOI: 10.1096/Fj.10-161208 |
0.461 |
|
| 2010 |
Tartaglia GG, Vendruscolo M. Proteome-level interplay between folding and aggregation propensities of proteins. Journal of Molecular Biology. 402: 919-28. PMID 20709078 DOI: 10.1016/J.Jmb.2010.08.013 |
0.457 |
|
| 2010 |
Robustelli P, Kohlhoff K, Cavalli A, Vendruscolo M. Using NMR chemical shifts as structural restraints in molecular dynamics simulations of proteins. Structure (London, England : 1993). 18: 923-33. PMID 20696393 DOI: 10.1016/J.Str.2010.04.016 |
0.802 |
|
| 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 |
0.485 |
|
| 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 |
0.506 |
|
| 2010 |
De Gortari I, Portella G, Salvatella X, Bajaj VS, van der Wel PC, Yates JR, Segall MD, Pickard CJ, Payne MC, Vendruscolo M. Time averaging of NMR chemical shifts in the MLF peptide in the solid state. Journal of the American Chemical Society. 132: 5993-6000. PMID 20387894 DOI: 10.1021/Ja9062629 |
0.359 |
|
| 2010 |
Wolff K, Vendruscolo M, Porto M. Efficient identification of near-native conformations in ab initio protein structure prediction using structural profiles. Proteins. 78: 249-58. PMID 19701942 DOI: 10.1002/Prot.22533 |
0.371 |
|
| 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 |
0.527 |
|
| 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 |
0.505 |
|
| 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 |
0.515 |
|
| 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 |
0.516 |
|
| 2009 |
De Simone A, Cavalli A, Hsu ST, Vranken W, Vendruscolo M. Accurate random coil chemical shifts from an analysis of loop regions in native states of proteins. Journal of the American Chemical Society. 131: 16332-3. PMID 19852475 DOI: 10.1021/Ja904937A |
0.339 |
|
| 2009 |
Tartaglia GG, Vendruscolo M. Correlation between mRNA expression levels and protein aggregation propensities in subcellular localisations. Molecular Biosystems. 5: 1873-6. PMID 19763336 DOI: 10.1039/B913099N |
0.373 |
|
| 2009 |
Kohlhoff KJ, Robustelli P, Cavalli A, Salvatella X, Vendruscolo M. Fast and accurate predictions of protein NMR chemical shifts from interatomic distances. Journal of the American Chemical Society. 131: 13894-5. PMID 19739624 DOI: 10.1021/Ja903772T |
0.789 |
|
| 2009 |
Auer S, Trovato A, Vendruscolo M. A condensation-ordering mechanism in nanoparticle-catalyzed peptide aggregation. Plos Computational Biology. 5: e1000458. PMID 19680431 DOI: 10.1371/Journal.Pcbi.1000458 |
0.347 |
|
| 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 |
0.557 |
|
| 2009 |
Pechmann S, Levy ED, Tartaglia GG, Vendruscolo M. Physicochemical principles that regulate the competition between functional and dysfunctional association of proteins. Proceedings of the National Academy of Sciences of the United States of America. 106: 10159-64. PMID 19502422 DOI: 10.1073/Pnas.0812414106 |
0.437 |
|
| 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 |
0.507 |
|
| 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 |
0.722 |
|
| 2009 |
Routledge KE, Tartaglia GG, Platt GW, Vendruscolo M, Radford SE. Competition between intramolecular and intermolecular interactions in an amyloid-forming protein. Journal of Molecular Biology. 389: 776-86. PMID 19393661 DOI: 10.1016/J.Jmb.2009.04.042 |
0.459 |
|
| 2009 |
De Simone A, Richter B, Salvatella X, Vendruscolo M. Toward an accurate determination of free energy landscapes in solution states of proteins. Journal of the American Chemical Society. 131: 3810-1. PMID 19292482 DOI: 10.1021/Ja8087295 |
0.441 |
|
| 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 |
0.47 |
|
| 2009 |
Friel CT, Smith DA, Vendruscolo M, Gsponer J, Radford SE. The mechanism of folding of Im7 reveals competition between functional and kinetic evolutionary constraints. Nature Structural & Molecular Biology. 16: 318-24. PMID 19252485 DOI: 10.1038/Nsmb.1562 |
0.43 |
|
| 2009 |
Periole X, Rampioni A, Vendruscolo M, Mark AE. Factors that affect the degree of twist in beta-sheet structures: a molecular dynamics simulation study of a cross-beta filament of the GNNQQNY peptide. The Journal of Physical Chemistry. B. 113: 1728-37. PMID 19154133 DOI: 10.1021/Jp8078259 |
0.328 |
|
| 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 |
0.506 |
|
| 2009 |
Robustelli P, Cavalli A, Vendruscolo M. Determination of protein structures in the solid state from NMR chemical shifts. Structure (London, England : 1993). 16: 1764-9. PMID 19081052 DOI: 10.1016/J.Str.2008.10.016 |
0.425 |
|
| 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 |
0.57 |
|
| 2008 |
Vendruscolo M, Tartaglia GG. Towards quantitative predictions in cell biology using chemical properties of proteins. Molecular Biosystems. 4: 1170-5. PMID 19396379 DOI: 10.1039/B805710A |
0.362 |
|
| 2008 |
Wolff K, Vendruscolo M, Porto M. Stochastic reconstruction of protein structures from effective connectivity profiles. Pmc Biophysics. 1: 5. PMID 19351427 DOI: 10.1186/1757-5036-1-5 |
0.395 |
|
| 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 |
0.523 |
|
| 2008 |
Calosci N, Chi CN, Richter B, Camilloni C, Engström A, Eklund L, Travaglini-Allocatelli C, Gianni S, Vendruscolo M, Jemth P. Comparison of successive transition states for folding reveals alternative early folding pathways of two homologous proteins. Proceedings of the National Academy of Sciences of the United States of America. 105: 19241-6. PMID 19033470 DOI: 10.1073/Pnas.0804774105 |
0.653 |
|
| 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 |
0.532 |
|
| 2008 |
Montalvao RW, Cavalli A, Salvatella X, Blundell TL, Vendruscolo M. Structure determination of protein-protein complexes using NMR chemical shifts: case of an endonuclease colicin-immunity protein complex. Journal of the American Chemical Society. 130: 15990-6. PMID 18980319 DOI: 10.1021/Ja805258Z |
0.431 |
|
| 2008 |
Herrera FE, Chesi A, Paleologou KE, Schmid A, Munoz A, Vendruscolo M, Gustincich S, Lashuel HA, Carloni P. Inhibition of alpha-synuclein fibrillization by dopamine is mediated by interactions with five C-terminal residues and with E83 in the NAC region. Plos One. 3: e3394. PMID 18852892 DOI: 10.1371/Journal.Pone.0003394 |
0.537 |
|
| 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 |
0.504 |
|
| 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 |
0.593 |
|
| 2008 |
Cheng TM, Lu YE, Vendruscolo M, Lio' P, Blundell TL. Prediction by graph theoretic measures of structural effects in proteins arising from non-synonymous single nucleotide polymorphisms. Plos Computational Biology. 4: e1000135. PMID 18654622 DOI: 10.1371/Journal.Pcbi.1000135 |
0.368 |
|
| 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 |
0.451 |
|
| 2008 |
Vendruscolo M. Protein dynamics under light control. Nature Chemical Biology. 4: 449-50. PMID 18641621 DOI: 10.1038/Nchembio0808-449 |
0.346 |
|
| 2008 |
Wolff K, Vendruscolo M, Porto M. A stochastic method for the reconstruction of protein structures from one-dimensional structural profiles. Gene. 422: 47-51. PMID 18577428 DOI: 10.1016/J.Gene.2008.06.004 |
0.394 |
|
| 2008 |
Tartaglia GG, Vendruscolo M. The Zyggregator method for predicting protein aggregation propensities. Chemical Society Reviews. 37: 1395-401. PMID 18568165 DOI: 10.1039/B706784B |
0.421 |
|
| 2008 |
Dhulesia A, Gsponer J, Vendruscolo M. Mapping of two networks of residues that exhibit structural and dynamical changes upon binding in a PDZ domain protein. Journal of the American Chemical Society. 130: 8931-9. PMID 18558679 DOI: 10.1021/Ja0752080 |
0.369 |
|
| 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 |
0.574 |
|
| 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 |
0.52 |
|
| 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 |
0.475 |
|
| 2008 |
Bemporad F, Gsponer J, Hopearuoho HI, Plakoutsi G, Stati G, Stefani M, Taddei N, Vendruscolo M, Chiti F. Biological function in a non-native partially folded state of a protein. The Embo Journal. 27: 1525-35. PMID 18451804 DOI: 10.1038/Emboj.2008.82 |
0.397 |
|
| 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 |
0.506 |
|
| 2008 |
Geierhaas CD, Salvatella X, Clarke J, Vendruscolo M. Characterisation of transition state structures for protein folding using 'high', 'medium' and 'low' {Phi}-values. Protein Engineering, Design & Selection : Peds. 21: 215-22. PMID 18299294 DOI: 10.1093/Protein/Gzm092 |
0.579 |
|
| 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 |
|
| 2008 |
Pechmann S, Levy ED, Tartaglia GG, Vendruscolo M. Competition between protein aggregation and protein complex formation Bmc Bioinformatics. 9. DOI: 10.1186/1471-2105-9-S10-O2 |
0.419 |
|
| 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 |
0.556 |
|
| 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 |
0.495 |
|
| 2007 |
Salvatella X, Richter B, Vendruscolo M. Influence of the fluctuations of the alignment tensor on the analysis of the structure and dynamics of proteins using residual dipolar couplings. Journal of Biomolecular Nmr. 40: 71-81. PMID 18030429 DOI: 10.1007/S10858-007-9210-6 |
0.403 |
|
| 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 |
0.607 |
|
| 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 |
0.53 |
|
| 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 |
0.52 |
|
| 2007 |
Vendruscolo M, Dobson CM. Chemical biology: More charges against aggregation. Nature. 449: 555. PMID 17914388 DOI: 10.1038/449555A |
0.501 |
|
| 2007 |
Monsellier E, Ramazzotti M, de Laureto PP, Tartaglia GG, Taddei N, Fontana A, Vendruscolo M, Chiti F. The distribution of residues in a polypeptide sequence is a determinant of aggregation optimized by evolution. Biophysical Journal. 93: 4382-91. PMID 17766358 DOI: 10.1529/Biophysj.107.111336 |
0.32 |
|
| 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 |
0.569 |
|
| 2007 |
Periole X, Vendruscolo M, Mark AE. Molecular dynamics simulations from putative transition states of α-spectrin SH3 domain Proteins: Structure, Function and Genetics. 69: 536-550. PMID 17623848 DOI: 10.1002/Prot.21491 |
0.356 |
|
| 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 |
|
| 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 |
0.495 |
|
| 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 |
0.515 |
|
| 2007 |
Tartaglia GG, Cavalli A, Vendruscolo M. Prediction of local structural stabilities of proteins from their amino acid sequences. Structure (London, England : 1993). 15: 139-43. PMID 17292832 DOI: 10.1016/J.Str.2006.12.007 |
0.39 |
|
| 2007 |
Vendruscolo M. Determination of conformationally heterogeneous states of proteins. Current Opinion in Structural Biology. 17: 15-20. PMID 17239581 DOI: 10.1016/J.Sbi.2007.01.002 |
0.451 |
|
| 2007 |
Richter B, Gsponer J, Várnai P, Salvatella X, Vendruscolo M. The MUMO (minimal under-restraining minimal over-restraining) method for the determination of native state ensembles of proteins. Journal of Biomolecular Nmr. 37: 117-35. PMID 17225069 DOI: 10.1007/S10858-006-9117-7 |
0.445 |
|
| 2007 |
Gianni S, Geierhaas CD, Calosci N, Jemth P, Vuister GW, Travaglini-Allocatelli C, Vendruscolo M, Brunori M. A PDZ domain recapitulates a unifying mechanism for protein folding. Proceedings of the National Academy of Sciences of the United States of America. 104: 128-33. PMID 17179214 DOI: 10.1073/Pnas.0602770104 |
0.443 |
|
| 2007 |
Geierhaas CD, Nickson AA, Lindorff-Larsen K, Clarke J, Vendruscolo M. BPPred: a Web-based computational tool for predicting biophysical parameters of proteins. Protein Science : a Publication of the Protein Society. 16: 125-34. PMID 17123959 DOI: 10.1110/Ps.062383807 |
0.543 |
|
| 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 |
0.481 |
|
| 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 |
0.484 |
|
| 2006 |
Francis CJ, Lindorff-Larsen K, Best RB, Vendruscolo M. Characterization of the residual structure in the unfolded state of the Delta131Delta fragment of staphylococcal nuclease. Proteins. 65: 145-52. PMID 16862593 DOI: 10.1002/Prot.21077 |
0.645 |
|
| 2006 |
Best RB, Lindorff-Larsen K, DePristo MA, Vendruscolo M. Relation between native ensembles and experimental structures of proteins. Proceedings of the National Academy of Sciences of the United States of America. 103: 10901-6. PMID 16829580 DOI: 10.1073/Pnas.0511156103 |
0.66 |
|
| 2006 |
Bastolla U, Porto M, Roman HE, Vendruscolo M. A protein evolution model with independent sites that reproduces site-specific amino acid distributions from the Protein Data Bank. Bmc Evolutionary Biology. 6: 43-43. PMID 16737532 DOI: 10.1186/1471-2148-6-43 |
0.326 |
|
| 2006 |
Geierhaas CD, Best RB, Paci E, Vendruscolo M, Clarke J. Structural comparison of the two alternative transition states for folding of TI I27. Biophysical Journal. 91: 263-75. PMID 16603501 DOI: 10.1529/Biophysj.105.077057 |
0.698 |
|
| 2006 |
Gsponer J, Vendruscolo M. Theoretical approaches to protein aggregation. Protein and Peptide Letters. 13: 287-93. PMID 16515457 DOI: 10.2174/092986606775338407 |
0.458 |
|
| 2006 |
Best RB, Vendruscolo M. Structural interpretation of hydrogen exchange protection factors in proteins: characterization of the native state fluctuations of CI2. Structure (London, England : 1993). 14: 97-106. PMID 16407069 DOI: 10.1016/J.Str.2005.09.012 |
0.632 |
|
| 2006 |
Gsponer J, Hopearuoho H, Whittaker SB, Spence GR, Moore GR, Paci E, Radford SE, Vendruscolo M. Determination of an ensemble of structures representing the intermediate state of the bacterial immunity protein Im7. Proceedings of the National Academy of Sciences of the United States of America. 103: 99-104. PMID 16371468 DOI: 10.1073/Pnas.0508667102 |
0.432 |
|
| 2006 |
Lindorff-Larsen K, Best RB, Vendruscolo M. Interpreting dynamically-averaged scalar couplings in proteins. Journal of Biomolecular Nmr. 32: 273-80. PMID 16211481 DOI: 10.1007/S10858-005-8873-0 |
0.625 |
|
| 2006 |
Salvi G, De Los Rios P, Vendruscolo M. Effective interactions between chaotropic agents and proteins. Proteins. 61: 492-9. PMID 16152629 DOI: 10.1002/Prot.20626 |
0.363 |
|
| 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 |
0.405 |
|
| 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 |
0.599 |
|
| 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 |
0.553 |
|
| 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 |
0.567 |
|
| 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 |
0.548 |
|
| 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 |
0.528 |
|
| 2005 |
Bastolla U, Porto M, Roman HE, Vendruscolo M. Looking at structure, stability, and evolution of proteins through the principal eigenvector of contact matrices and hydrophobicity profiles. Gene. 347: 219-230. PMID 15777696 DOI: 10.1016/J.Gene.2004.12.015 |
0.396 |
|
| 2005 |
Cavalli A, Vendruscolo M, Paci E. Comparison of sequence-based and structure-based energy functions for the reversible folding of a peptide. Biophysical Journal. 88: 3158-66. PMID 15749768 DOI: 10.1529/Biophysj.104.055335 |
0.362 |
|
| 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 |
0.661 |
|
| 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 |
0.56 |
|
| 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 |
0.711 |
|
| 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 |
0.499 |
|
| 2005 |
Porto M, Roman HE, Vendruscolo M, Bastolla U. Prediction of Site-Specific Amino Acid Distributions and Limits of Divergent Evolutionary Changes in Protein Sequences Molecular Biology and Evolution. 22: 630-638. PMID 15537801 DOI: 10.1093/Molbev/Msi048 |
0.372 |
|
| 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 |
0.439 |
|
| 2005 |
Paci E, Vendruscolo M. Detection of non-native hydrophobic interactions in the denatured state of lysozyme by molecular dynamics simulations Journal of Physics: Condensed Matter. 17: S1617-S1626. DOI: 10.1088/0953-8984/17/18/017 |
0.417 |
|
| 2004 |
Bastolla U, Porto M, Roman HE, Vendruscolo M. Principal eigenvector of contact matrices and hydrophobicity profiles in proteins. Proteins. 58: 22-30. PMID 15523667 DOI: 10.1002/Prot.20240 |
0.342 |
|
| 2004 |
Geierhaas CD, Paci E, Vendruscolo M, Clarke J. Comparison of the transition states for folding of two Ig-like proteins from different superfamilies. Journal of Molecular Biology. 343: 1111-23. PMID 15476825 DOI: 10.1016/J.Jmb.2004.08.100 |
0.591 |
|
| 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 |
0.576 |
|
| 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 |
0.551 |
|
| 2004 |
Porto M, Bastolla U, Roman HE, Vendruscolo M. Reconstruction of protein structures from a vectorial representation. Physical Review Letters. 92: 218101. PMID 15245321 DOI: 10.1103/Physrevlett.92.218101 |
0.358 |
|
| 2004 |
Best RB, Vendruscolo M. Determination of protein structures consistent with NMR order parameters. Journal of the American Chemical Society. 126: 8090-1. PMID 15225030 DOI: 10.1021/Ja0396955 |
0.588 |
|
| 2004 |
Paci E, Gsponer J, Salvatella X, Vendruscolo M. Molecular dynamics studies of the process of amyloid aggregation of peptide fragments of transthyretin. Journal of Molecular Biology. 340: 555-69. PMID 15210354 DOI: 10.1016/J.Jmb.2004.05.009 |
0.41 |
|
| 2004 |
Lindorff-Larsen K, Vendruscolo M, Paci E, Dobson CM. Transition states for protein folding have native topologies despite high structural variability. Nature Structural & Molecular Biology. 11: 443-9. PMID 15098020 DOI: 10.1038/Nsmb765 |
0.53 |
|
| 2004 |
Lindorff-Larsen K, Kristjansdottir S, Teilum K, Fieber W, Dobson CM, Poulsen FM, Vendruscolo M. Determination of an ensemble of structures representing the denatured state of the bovine acyl-coenzyme a binding protein. Journal of the American Chemical Society. 126: 3291-9. PMID 15012160 DOI: 10.1021/Ja039250G |
0.554 |
|
| 2004 |
Paci E, Friel CT, Lindorff-Larsen K, Radford SE, Karplus M, Vendruscolo M. Comparison of the transition state ensembles for folding of Im7 and Im9 determined using all-atom molecular dynamics simulations with phi value restraints. Proteins. 54: 513-25. PMID 14747999 DOI: 10.1002/Prot.10595 |
0.53 |
|
| 2004 |
Lindorff-Larsen K, Paci E, Serrano L, Dobson CM, Vendruscolo M. Calculation of mutational free energy changes in transition states for protein folding. Biophysical Journal. 85: 1207-14. PMID 12885664 DOI: 10.1016/S0006-3495(03)74556-1 |
0.528 |
|
| 2003 |
Bastolla U, Porto M, Roman HE, Vendruscolo M. Statistical properties of neutral evolution. Journal of Molecular Evolution. 57. PMID 15008407 DOI: 10.1007/S00239-003-0013-4 |
0.361 |
|
| 2003 |
Vendruscolo M, Paci E, Dobson CM, Karplus M. Rare fluctuations of native proteins sampled by equilibrium hydrogen exchange. Journal of the American Chemical Society. 125: 15686-7. PMID 14677926 DOI: 10.1021/Ja036523Z |
0.59 |
|
| 2003 |
Vendruscolo M, Paci E, Karplus M, Dobson CM. Structures and relative free energies of partially folded states of proteins. Proceedings of the National Academy of Sciences of the United States of America. 100: 14817-21. PMID 14657374 DOI: 10.1073/Pnas.2036516100 |
0.646 |
|
| 2003 |
Vendruscolo M, Zurdo J, MacPhee CE, Dobson CM. Protein folding and misfolding: a paradigm of self-assembly and regulation in complex biological systems. Philosophical Transactions. Series a, Mathematical, Physical, and Engineering Sciences. 361: 1205-22. PMID 12816607 DOI: 10.1098/Rsta.2003.1194 |
0.512 |
|
| 2003 |
Paci E, Cavalli A, Vendruscolo M, Caflisch A. Analysis of the distributed computing approach applied to the folding of a small beta peptide. Proceedings of the National Academy of Sciences of the United States of America. 100: 8217-22. PMID 12815104 DOI: 10.1073/Pnas.1331838100 |
0.583 |
|
| 2003 |
Bastolla U, Porto M, Roman HE, Vendruscolo M. Connectivity of neutral networks, overdispersion, and structural conservation in protein evolution. Journal of Molecular Evolution. 56: 243-254. PMID 12612828 DOI: 10.1007/S00239-002-2350-0 |
0.381 |
|
| 2003 |
Vendruscolo M, Paci E. Protein folding: bringing theory and experiment closer together. Current Opinion in Structural Biology. 13: 82-7. PMID 12581664 DOI: 10.1016/S0959-440X(03)00007-1 |
0.375 |
|
| 2003 |
Paci E, Clarke J, Steward A, Vendruscolo M, Karplus M. Self-consistent determination of the transition state for protein folding: application to a fibronectin type III domain. Proceedings of the National Academy of Sciences of the United States of America. 100: 394-9. PMID 12515856 DOI: 10.1073/Pnas.232704999 |
0.645 |
|
| 2002 |
Paci E, Vendruscolo M, Karplus M. Validity of Gō models: comparison with a solvent-shielded empirical energy decomposition. Biophysical Journal. 83: 3032-8. PMID 12496075 DOI: 10.1016/S0006-3495(02)75308-3 |
0.479 |
|
| 2002 |
Bastolla U, Porto M, Roman HE, Vendruscolo M. Lack of self-averaging in neutral evolution of proteins. Physical Review Letters. 89: 208101. PMID 12443510 DOI: 10.1103/Physrevlett.89.208101 |
0.355 |
|
| 2002 |
Paci E, Vendruscolo M, Dobson CM, Karplus M. Determination of a transition state at atomic resolution from protein engineering data. Journal of Molecular Biology. 324: 151-63. PMID 12421565 DOI: 10.1016/S0022-2836(02)00944-0 |
0.62 |
|
| 2002 |
Vendruscolo M, Dokholyan NV, Paci E, Karplus M. Small-world view of the amino acids that play a key role in protein folding. Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics. 65: 061910. PMID 12188762 DOI: 10.1103/Physreve.65.061910 |
0.519 |
|
| 2002 |
Kabakçioglu A, Kanter I, Vendruscolo M, Domany E. Statistical properties of contact vectors. Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics. 65: 041904. PMID 12005870 DOI: 10.1103/Physreve.65.041904 |
0.326 |
|
| 2002 |
Paci E, Vendruscolo M, Karplus M. Native and non-native interactions along protein folding and unfolding pathways Proteins: Structure, Function and Genetics. 47: 379-392. PMID 11948791 DOI: 10.1002/Prot.10089 |
0.516 |
|
| 2002 |
Getz G, Vendruscolo M, Sachs D, Domany E. Automated assignment of SCOP and CATH protein structure classifications from FSSP scores. Proteins. 46: 405-15. PMID 11835515 DOI: 10.1002/Prot.1176 |
0.344 |
|
| 2002 |
Davis R, Dobson CM, Vendruscolo M. Determination of the structures of distinct transition state ensembles for a β-sheet peptide with parallel folding pathways The Journal of Chemical Physics. 117: 9510-9517. DOI: 10.1063/1.1516784 |
0.533 |
|
| 2001 |
Bastolla U, Farwer J, Knapp EW, Vendruscolo M. How to guarantee optimal stability for most representative structures in the Protein Data Bank. Proteins. 44: 79-96. PMID 11391771 DOI: 10.1002/Prot.1075 |
0.423 |
|
| 2001 |
Vendruscolo M, Paci E, Dobson CM, Karplus M. Three key residues form a critical contact network in a protein folding transition state. Nature. 409: 641-5. PMID 11214326 DOI: 10.1038/35054591 |
0.628 |
|
| 2000 |
Park K, Vendruscolo M, Domany E. Toward an energy function for the contact map representation of proteins. Proteins. 40: 237-48. PMID 10842339 DOI: 10.1002/(Sici)1097-0134(20000801)40:2<237::Aid-Prot60>3.0.Co;2-P |
0.342 |
|
| 2000 |
Bastolla U, Vendruscolo M, Knapp EW. A statistical mechanical method to optimize energy functions for protein folding. Proceedings of the National Academy of Sciences of the United States of America. 97: 3977-81. PMID 10760269 DOI: 10.1073/Pnas.97.8.3977 |
0.376 |
|
| 2000 |
Vendruscolo M, Domany E. Protein folding using contact maps. Vitamins and Hormones. 58: 171-212. PMID 10668399 DOI: 10.1016/S0083-6729(00)58025-X |
0.312 |
|
| 2000 |
Vendruscolo M, Najmanovich R, Domany E. Can a pairwise contact potential stabilize native protein folds against decoys obtained by threading? Proteins: Structure, Function and Genetics. 38: 134-148. PMID 10656261 DOI: 10.1002/(Sici)1097-0134(20000201)38:2<134::Aid-Prot3>3.0.Co;2-A |
0.362 |
|
| 2000 |
Clementi C, Vendruscolo M, Maritan A, Domany E. Folding Lennard-Jones proteins by a contact potential. Proteins. 37: 544-53. PMID 10651270 DOI: 10.1002/(Sici)1097-0134(19991201)37:4<544::Aid-Prot5>3.0.Co;2-7 |
0.362 |
|
| 2000 |
Bastolla U, Vendruscolo M, Roman HE. Structurally constrained protein evolution: results from a lattice simulation European Physical Journal B. 15: 385-397. DOI: 10.1007/S100510051140 |
0.341 |
|
| 1999 |
Bastolla U, Roman HE, Vendruscolo M. Neutral Evolution Of Model Proteins : Diffusion In Sequence Space And Overdispersion Journal of Theoretical Biology. 200: 49-64. PMID 10479539 DOI: 10.1006/Jtbi.1999.0975 |
0.315 |
|
| 1999 |
Vendruscolo M, Najmanovich R, Domany E. Protein Folding in Contact Map Space Physical Review Letters. 82: 656-659. DOI: 10.1103/Physrevlett.82.656 |
0.312 |
|
| 1999 |
Vendruscolo M. An optimal derivation of a potential for protein folding Physica a: Statistical Mechanics and Its Applications. 262: 35-39. DOI: 10.1016/S0378-4371(98)00358-6 |
0.345 |
|
| 1999 |
Vendruscolo M. Hydrophobicity and unique folding of selected polymers The European Physical Journal B. 8: 323-326. DOI: 10.1007/S100510050695 |
0.302 |
|
| 1998 |
Vendruscolo M, Domany E. Efficient dynamics in the space of contact maps. Folding & Design. 3: 329-36. PMID 9806935 DOI: 10.1016/S1359-0278(98)00045-5 |
0.373 |
|
| 1998 |
Vendruscolo M, Domany E. Pairwise contact potentials are unsuitable for protein folding The Journal of Chemical Physics. 109: 11101-11108. DOI: 10.1063/1.477748 |
0.348 |
|
| 1998 |
Vendruscolo M. Protein stability and foldability–designability complementarity Physica a: Statistical Mechanics and Its Applications. 249: 576-580. DOI: 10.1016/S0378-4371(97)00518-9 |
0.358 |
|
| 1997 |
Vendruscolo M, Kussell E, Domany E. Recovery of protein structure from contact maps. Folding & Design. 2: 295-306. PMID 9377713 DOI: 10.1016/S1359-0278(97)00041-2 |
0.342 |
|
| 1997 |
Vendruscolo M, Maritan A, Banavar JR. Stability Threshold as a Selection Principle for Protein Design Physical Review Letters. 78: 3967-3970. DOI: 10.1103/Physrevlett.78.3967 |
0.341 |
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