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Christopher M. Dobson - Publications

Affiliations: 
University of Cambridge, Cambridge, England, United Kingdom 
Area:
structures and properties of biological molecules
Website:
http://www.ch.cam.ac.uk/staff/cmd.html

500 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2020 Arter WE, Xu CK, Castellana-Cruz M, Herling TW, Krainer G, Saar KL, Kumita JR, Dobson CM, Knowles TPJ. Rapid Structural, Kinetic, and Immunochemical Analysis of Alpha-Synuclein Oligomers in Solution. Nano Letters. PMID 33079553 DOI: 10.1021/acs.nanolett.0c03260  0.84
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  1
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  1
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  1
2020 Chrabąszczewska M, Sieradzan AK, Rodziewicz-Motowidło S, Grubb A, Dobson CM, Kumita JR, Kozak M. Structural Characterization of Covalently Stabilized Human Cystatin C Oligomers. International Journal of Molecular Sciences. 21. PMID 32824145 DOI: 10.3390/ijms21165860  0.4
2020 Du Z, Chakrabarti S, Kulaberoglu Y, Smith ESJ, Dobson CM, Itzhaki LS, Kumita JR. Probing the unfolded protein response in long-lived naked mole-rats. Biochemical and Biophysical Research Communications. 529: 1151-1157. PMID 32819579 DOI: 10.1016/j.bbrc.2020.06.118  0.4
2020 Yang J, Dear AJ, Yao QQ, Liu Z, Dobson CM, Knowles TPJ, Wu S, Perrett S. Amelioration of aggregate cytotoxicity by catalytic conversion of protein oligomers into amyloid fibrils. Nanoscale. PMID 32794533 DOI: 10.1039/d0nr01481h  0.84
2020 Limbocker R, Mannini B, Ruggeri FS, Cascella R, Xu CK, Perni M, Chia S, Chen SW, Habchi J, Bigi A, Kreiser RP, Wright AK, Albright JA, Kartanas T, Kumita JR, ... ... Dobson CM, et al. Trodusquemine displaces protein misfolded oligomers from cell membranes and abrogates their cytotoxicity through a generic mechanism. Communications Biology. 3: 435. PMID 32792544 DOI: 10.1038/s42003-020-01140-8  1
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  1
2020 Ke PC, Zhou R, Serpell LC, Riek R, Knowles TPJ, Lashuel HA, Gazit E, Hamley IW, Davis TP, Fändrich M, Otzen DE, Chapman MR, Dobson CM, Eisenberg DS, Mezzenga R. Half a century of amyloids: past, present and future. Chemical Society Reviews. PMID 32632432 DOI: 10.1039/c9cs00199a  0.84
2020 Limbocker R, Mannini B, Cataldi R, Chhangur S, Wright AK, Kreiser RP, Albright JA, Chia S, Habchi J, Sormanni P, Kumita JR, Ruggeri FS, Dobson CM, Chiti F, Aprile FA, et al. Rationally Designed Antibodies as Research Tools to Study the Structure-Toxicity Relationship of Amyloid-β Oligomers. International Journal of Molecular Sciences. 21. PMID 32630615 DOI: 10.3390/ijms21124542  1
2020 Aprile FA, Sormanni P, Podpolny M, Chhangur S, Needham LM, Ruggeri FS, Perni M, Limbocker R, Heller GT, Sneideris T, Scheidt T, Mannini B, Habchi J, Lee SF, Salinas PC, ... ... Dobson CM, et al. Rational design of a conformation-specific antibody for the quantification of Aβ oligomers. Proceedings of the National Academy of Sciences of the United States of America. PMID 32493749 DOI: 10.1073/pnas.1919464117  1
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  1
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  1
2020 Dear AJ, Michaels TCT, Meisl G, Klenerman D, Wu S, Perrett S, Linse S, Dobson CM, Knowles TPJ. Kinetic diversity of amyloid oligomers. Proceedings of the National Academy of Sciences of the United States of America. PMID 32414930 DOI: 10.1073/pnas.1922267117  0.84
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  1
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  1
2020 Ruggeri FS, Flagmeier P, Kumita JR, Meisl G, Chirgadze DY, Bongiovanni MN, Knowles TPJ, Dobson CM. The Influence of Pathogenic Mutations in α-Synuclein on Biophysical and Structural Characteristics of Amyloid Fibrils. Acs Nano. PMID 32159944 DOI: 10.1021/acsnano.9b09676  0.84
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  1
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  1
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  1
2020 Froula JM, Castellana-Cruz M, Anabtawi NM, Camino JD, Chen SW, Thrasher DR, Freire J, Yazdi AA, Fleming S, Dobson CM, Kumita JR, Cremades N, Volpicelli-Daley LA. Correction: Defining α-synuclein species responsible for Parkinson's disease phenotypes in mice. The Journal of Biological Chemistry. 295: 1142. PMID 31980482 DOI: 10.1074/jbc.AAC119.012485  0.48
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  1
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  1
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  1
2019 Galvagnion C, Topgaard D, Makasewicz K, Buell AK, Linse S, Sparr E, Dobson CM. Lipid Dynamics and Phase Transition within α-Synuclein Amyloid Fibrils. The Journal of Physical Chemistry Letters. 7872-7877. PMID 31790267 DOI: 10.1021/acs.jpclett.9b03005  1
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  1
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  1
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  1
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  1
2019 Ng JSW, Hanspal MA, Matharu NS, Barros TP, Esbjörner EK, Wilson MR, Yerbury JJ, Dobson CM, Kumita JR. Using Tetracysteine-Tagged TDP-43 with a Biarsenical Dye To Monitor Real-Time Trafficking in a Cell Model of Amyotrophic Lateral Sclerosis. Biochemistry. PMID 31529970 DOI: 10.1021/acs.biochem.9b00592  0.4
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  1
2019 Agerschou ED, Flagmeier P, Saridaki T, Galvagnion C, Komnig D, Heid L, Prasad V, Shaykhalishahi H, Willbold D, Dobson CM, Voigt A, Falkenbürger B, Hoyer W, Buell AK. An engineered monomer binding-protein for α-synuclein efficiently inhibits the proliferation of amyloid fibrils. Elife. 8. PMID 31389332 DOI: 10.7554/eLife.46112  1
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  1
2019 Waudby CA, Dobson CM, Christodoulou J. Nature and Regulation of Protein Folding on the Ribosome. Trends in Biochemical Sciences. PMID 31301980 DOI: 10.1016/j.tibs.2019.06.008  0.64
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  1
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  1
2019 Froula JM, Castellana-Cruz M, Anabtawi NM, Camino JD, Chen SW, Thrasher DR, Freire J, Yazdi AA, Fleming S, Dobson CM, Kumita JR, Cremades N, Volpicelli-Daley LA. Defining α-synuclein species responsible for Parkinson disease phenotypes in mice. The Journal of Biological Chemistry. PMID 31142553 DOI: 10.1074/jbc.RA119.007743  0.48
2019 Vivoli Vega M, Cascella R, Chen SW, Fusco G, De Simone A, Dobson CM, Cecchi C, Chiti F. The toxicity of misfolded protein oligomers is independent of their secondary structure. Acs Chemical Biology. PMID 31074957 DOI: 10.1021/acschembio.9b00324  0.72
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  1
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  1
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  1
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  1
2019 De S, Wirthensohn DC, Flagmeier P, Hughes C, Aprile FA, Ruggeri FS, Whiten DR, Emin D, Xia Z, Varela JA, Sormanni P, Kundel F, Knowles TPJ, Dobson CM, Bryant C, et al. Different soluble aggregates of Aβ42 can give rise to cellular toxicity through different mechanisms. Nature Communications. 10: 1541. PMID 30948723 DOI: 10.1038/s41467-019-09477-3  1
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  1
2019 Cater JH, Kumita JR, Zeineddine Abdallah R, Zhao G, Bernardo-Gancedo A, Henry A, Winata W, Chi M, Grenyer BSF, Townsend ML, Ranson M, Buhimschi CS, Charnock-Jones DS, Dobson CM, Wilson MR, et al. Human pregnancy zone protein stabilizes misfolded proteins including preeclampsia- and Alzheimer's-associated amyloid beta peptide. Proceedings of the National Academy of Sciences of the United States of America. PMID 30850528 DOI: 10.1073/pnas.1817298116  0.4
2019 Liu X, Toprakcioglu Z, Dear AJ, Levin A, Ruggeri FS, Taylor CG, Hu M, Kumita JR, Andreasen M, Dobson CM, Shimanovich U, Knowles TPJ. Fabrication and Characterization of Reconstituted Silk Microgels for the Storage and Release of Small Molecules. Macromolecular Rapid Communications. e1800898. PMID 30840348 DOI: 10.1002/marc.201800898  0.84
2019 Weiffert T, Meisl G, Flagmeier P, De S, Dunning CJR, Frohm B, Zetterberg H, Blennow K, Portelius E, Klenerman D, Dobson CM, Knowles TPJ, Linse S. Increased secondary nucleation underlies accelerated aggregation of the four-residue N-terminally truncated Aβ42 species Aβ5-42. Acs Chemical Neuroscience. PMID 30793584 DOI: 10.1021/acschemneuro.8b00676  0.84
2019 Limbocker R, Chia S, Ruggeri FS, Perni M, Cascella R, Heller GT, Meisl G, Mannini B, Habchi J, Michaels TCT, Challa PK, Ahn M, Casford ST, Fernando N, Xu CK, ... ... Dobson CM, et al. Trodusquemine enhances Aβ aggregation but suppresses its toxicity by displacing oligomers from cell membranes. Nature Communications. 10: 225. PMID 30644384 DOI: 10.1038/s41467-018-07699-5  1
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  1
2019 Andreasen M, Meisl G, Taylor JD, Michaels TCT, Levin A, Otzen DE, Chapman MR, Dobson CM, Matthews SJ, Knowles TPJ. Physical Determinants of Amyloid Assembly in Biofilm Formation. Mbio. 10. PMID 30622185 DOI: 10.1128/mBio.02279-18  0.84
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  1
2018 Lee JE, Sang JC, Rodrigues M, Carr AR, Horrocks MH, De S, Bongiovanni MN, Flagmeier P, Dobson CM, Wales DJ, Lee SF, Klenerman D. Mapping Surface Hydrophobicity of α-Synuclein Oligomers at the Nanoscale. Nano Letters. PMID 30380895 DOI: 10.1021/acs.nanolett.8b02916  0.6
2018 Iljina M, Dear AJ, Garcia GA, De S, Tosatto L, Flagmeier P, Whiten DR, Michaels TCT, Frenkel D, Dobson CM, Knowles TPJ, Klenerman D. Quantifying Co-Oligomer Formation by α-Synuclein. Acs Nano. PMID 30371053 DOI: 10.1021/acsnano.8b03575  0.84
2018 Dear AJ, Šarić A, Michaels TCT, Dobson CM, Knowles TPJ. Statistical Mechanics of Globular Oligomer Formation by Protein Molecules. The Journal of Physical Chemistry. B. PMID 30336667 DOI: 10.1021/acs.jpcb.8b07805  0.84
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  1
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  1
2018 Chatterjee D, Bhatt M, Butler D, De Genst E, Dobson CM, Messer A, Kordower JH. Proteasome-targeted nanobodies alleviate pathology and functional decline in an α-synuclein-based Parkinson's disease model. Npj Parkinson's Disease. 4: 25. PMID 30155513 DOI: 10.1038/s41531-018-0062-4  0.36
2018 van der Wateren IM, Knowles TPJ, Buell AK, Dobson CM, Galvagnion C. C-terminal truncation of α-synuclein promotes amyloid fibril amplification at physiological pH. Chemical Science. 9: 5506-5516. PMID 30061982 DOI: 10.1039/c8sc01109e  1
2018 Horrocks M, Whiten DR, Zuo Y, Calo L, Choi ML, De S, Flagmeier P, Wirthensohn DC, Kundel F, Lee SF, Dobson C, Gandhi S, Spillantini M, Klenerman D, Ranasinghe RT, et al. Nanoscopic characterization of individual endogenous protein aggregates in human neuronal cells. Chembiochem : a European Journal of Chemical Biology. PMID 30051958 DOI: 10.1002/cbic.201800209  0.6
2018 Månsson C, van Cruchten RTP, Weininger U, Yang X, Cukalevski R, Arosio P, Dobson CM, Knowles TPJ, Akke M, Linse S, Emanuelsson C. Conserved S/T-residues of the human chaperone DNAJB6 are required for effective inhibition of Aβ42 amyloid fibril formation. Biochemistry. PMID 30024736 DOI: 10.1021/acs.biochem.8b00353  0.84
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  1
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  1
2018 Perni M, Flagmeier P, Limbocker R, Cascella R, Aprile FA, Galvagnion C, Heller GT, Meisl G, Chen SW, Kumita JR, Challa PK, Kirkegaard JB, Cohen SIA, Mannini B, Barbut D, ... ... Dobson CM, et al. Multistep Inhibition of α-Synuclein Aggregation and Toxicity in Vitro and in Vivo by Trodusquemine. Acs Chemical Biology. PMID 29953201 DOI: 10.1021/acschembio.8b00466  1
2018 Brown JWP, Meisl G, Knowles TPJ, Buell AK, Dobson CM, Galvagnion C. Kinetic barriers to α-synuclein protofilament formation and conversion into mature fibrils. Chemical Communications (Cambridge, England). PMID 29951679 DOI: 10.1039/c8cc03002b  1
2018 Whiten DR, Cox D, Horrocks MH, Taylor CG, De S, Flagmeier P, Tosatto L, Kumita JR, Ecroyd H, Dobson CM, Klenerman D, Wilson MR. Single-Molecule Characterization of the Interactions between Extracellular Chaperones and Toxic α-Synuclein Oligomers. Cell Reports. 23: 3492-3500. PMID 29924993 DOI: 10.1016/j.celrep.2018.05.074  0.6
2018 Zhang Y, Yates EV, Hong L, Saar KL, Meisl G, Dobson CM, Knowles TPJ. On-chip measurements of protein unfolding from direct observations of micron-scale diffusion. Chemical Science. 9: 3503-3507. PMID 29780480 DOI: 10.1039/c7sc04331g  0.84
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  1
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  1
2018 Needham LM, Weber J, Fyfe JWB, Kabia OM, Do DT, Klimont E, Zhang Y, Rodrigues M, Dobson CM, Gandhi S, Bohndiek SE, Snaddon TN, Lee SF. Correction to 'Bifunctional fluorescent probes for detection of amyloid aggregates and reactive oxygen species'. Royal Society Open Science. 5: 180308. PMID 29658954 DOI: 10.1098/rsos.180308  0.36
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  1
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  1
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  1
2018 Herling TW, Levin A, Saar KL, Dobson CM, Knowles TPJ. Microfluidic approaches for probing amyloid assembly and behaviour. Lab On a Chip. PMID 29527600 DOI: 10.1039/c7lc01241a  0.84
2018 Needham LM, Weber J, Fyfe JWB, Kabia OM, Do DT, Klimont E, Zhang Y, Rodrigues M, Dobson CM, Ghandi S, Bohndiek SE, Snaddon TN, Lee SF. Bifunctional fluorescent probes for detection of amyloid aggregates and reactive oxygen species. Royal Society Open Science. 5: 171399. PMID 29515860 DOI: 10.1098/rsos.171399  0.36
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  1
2018 Perni M, Challa PK, Kirkegaard JB, Limbocker R, Koopman M, Hardenberg MC, Sormanni P, Müller T, Saar KL, Roode LWY, Habchi J, Vecchi G, Fernando NW, Casford S, Nollen EAA, ... ... Dobson CM, et al. Massively parallel C. elegans tracking provides multi-dimensional fingerprints for phenotypic discovery. Journal of Neuroscience Methods. PMID 29452179 DOI: 10.1016/j.jneumeth.2018.02.005  1
2018 Cox D, Whiten DR, Brown J, Horrocks MH, San Gil R, Dobson CM, Klenerman D, van Oijen AM, Ecroyd H. The small heat shock protein Hsp27 binds α-synuclein fibrils, preventing elongation and cytotoxicity. The Journal of Biological Chemistry. PMID 29382725 DOI: 10.1074/jbc.M117.813865  0.4
2018 Shimanovich U, Pinotsi D, Shimanovich K, Yu N, Bolisetty S, Adamcik J, Mezzenga R, Charmet J, Vollrath F, Gazit E, Dobson CM, Schierle GK, Holland C, Kaminski CF, Knowles TPJ. Biophotonics of Native Silk Fibrils. Macromolecular Bioscience. PMID 29377575 DOI: 10.1002/mabi.201700295  0.84
2018 Yang J, Dear AJ, Michaels TCT, Dobson CM, Knowles TPJ, Wu S, Perrett S. Direct observation of oligomerization by single molecule fluorescence reveals a multi-step aggregation mechanism for the yeast prion protein Ure2. Journal of the American Chemical Society. PMID 29357227 DOI: 10.1021/jacs.7b10439  0.84
2018 Varela JA, Rodrigues M, De S, Flagmeier P, Gandhi S, Dobson CM, Klenerman D, Lee S. Optical structural analysis of individual α-synuclein oligomers. Angewandte Chemie (International Ed. in English). PMID 29342318 DOI: 10.1002/anie.201710779  0.6
2018 Gang H, Galvagnion C, Meisl G, Müller T, Buell AK, Levin A, Dobson CM, Mu BZ, Knowles TPJ. A microfluidic diffusion platform for characterizing the size of lipid vesicles and the thermodynamics of protein-lipid interactions. Analytical Chemistry. PMID 29313342 DOI: 10.1021/acs.analchem.7b04820  1
2018 Kundel F, De S, Flagmeier P, Horrocks MH, Kjaergaard M, Shammas SL, Jackson SE, Dobson CM, Klenerman D. Hsp70 inhibits the nucleation and elongation of tau and sequesters tau aggregates with high affinity. Acs Chemical Biology. PMID 29300447 DOI: 10.1021/acschembio.7b01039  0.6
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  1
2017 Drews A, De S, Flagmeier P, Wirthensohn DC, Chen WH, Whiten DR, Rodrigues M, Vincke C, Muyldermans S, Paterson RW, Slattery CF, Fox NC, Schott JM, Zetterberg H, Dobson CM, et al. Inhibiting the Ca2+ Influx Induced by Human CSF. Cell Reports. 21: 3310-3316. PMID 29241555 DOI: 10.1016/j.celrep.2017.11.057  0.6
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  1
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  1
2017 Gregory JM, Whiten DR, Brown RA, Barros TP, Kumita JR, Yerbury JJ, Satapathy S, McDade K, Smith C, Luheshi LM, Dobson CM, Wilson MR. Clusterin protects neurons against intracellular proteotoxicity. Acta Neuropathologica Communications. 5: 81. PMID 29115989 DOI: 10.1186/s40478-017-0481-1  0.44
2017 Ahn M, Waudby CA, Bernardo-Gancedo A, De Genst E, Dhulesia A, Salvatella X, Christodoulou J, Dobson CM, Kumita JR. Application of Lysine-specific Labeling to Detect Transient Interactions Present During Human Lysozyme Amyloid Fibril Formation. Scientific Reports. 7: 15018. PMID 29101328 DOI: 10.1038/s41598-017-14739-5  0.72
2017 Villadiego J, Labrador-Garrido A, Franco JM, Leal-Lasarte M, De Genst EJ, Dobson CM, Pozo D, Toledo-Aral JJ, Roodveldt C. Immunization with α-synuclein/Grp94 reshapes peripheral immunity and suppresses microgliosis in a chronic Parkinsonism model. Glia. PMID 29024008 DOI: 10.1002/glia.23237  0.56
2017 Mason TO, Michaels TCT, Levin A, Dobson CM, Gazit E, Knowles TPJ, Buell AK. Thermodynamics of polypeptide supramolecular assembly in the short chain limit. Journal of the American Chemical Society. PMID 28994295 DOI: 10.1021/jacs.7b00229  1
2017 Meisl G, Yang X, Dobson CM, Linse S, Knowles TPJ. Modulation of electrostatic interactions to reveal a reaction network unifying the aggregation behaviour of the Aβ42 peptide and its variants. Chemical Science. 8: 4352-4362. PMID 28979758 DOI: 10.1039/c7sc00215g  0.84
2017 Pfammatter M, Andreasen M, Meisl G, Taylor CG, Adamcik J, Bolisetty S, Sanchez-Ferrer A, Klenerman D, Dobson CM, Mezzenga R, Knowles TPJ, Aguzzi AA, Hornemann S. Absolute Quantification of Amyloid Propagons by Digital Microfluidics. Analytical Chemistry. PMID 28972786 DOI: 10.1021/acs.analchem.7b03279  0.84
2017 Łapińska U, Saar KL, Yates EV, Herling TW, Müller T, Challa PK, Dobson CM, Knowles TPJ. Gradient-free determination of isoelectric points of proteins on chip. Physical Chemistry Chemical Physics : Pccp. PMID 28817152 DOI: 10.1039/c7cp01503h  0.84
2017 Shimanovich U, Michaels TCT, de Genst EJ, Matak-Vinkovic D, Dobson CM, Knowles TPJ. Sequential release of proteins from structured multishell microcapsules. Biomacromolecules. PMID 28792742 DOI: 10.1021/acs.biomac.7b00351  0.84
2017 Shimanovich U, Ruggeri FS, De Genst E, Adamcik J, Barros TP, Porter D, Müller T, Mezzenga R, Dobson CM, Vollrath F, Holland C, Knowles TPJ. Silk micrococoons for protein stabilisation and molecular encapsulation. Nature Communications. 8: 15902. PMID 28722016 DOI: 10.1038/ncomms15902  0.84
2017 Hanspal MA, Dobson CM, Yerbury JJ, Kumita JR. The relevance of contact-independent cell-to-cell transfer of TDP-43 and SOD1 in amyotrophic lateral sclerosis. Biochimica Et Biophysica Acta. PMID 28711596 DOI: 10.1016/j.bbadis.2017.07.007  0.4
2017 Cremades N, Dobson CM. The contribution of biophysical and structural studies of protein self-assembly to the design of therapeutic strategies for amyloid diseases. Neurobiology of Disease. PMID 28709995 DOI: 10.1016/j.nbd.2017.07.009  0.48
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  1
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  1
2017 Iljina M, Hong L, Horrocks MH, Ludtmann MH, Choi ML, Hughes CD, Ruggeri FS, Guilliams T, Buell AK, Lee JE, Gandhi S, Lee SF, Bryant CE, Vendruscolo M, Knowles TPJ, ... Dobson CM, et al. Nanobodies raised against monomeric ɑ-synuclein inhibit fibril formation and destabilize toxic oligomeric species. Bmc Biology. 15: 57. PMID 28673288 DOI: 10.1186/s12915-017-0390-6  1
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  1
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  1
2017 Chiti F, Dobson CM. Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade. Annual Review of Biochemistry. PMID 28498720 DOI: 10.1146/annurev-biochem-061516-045115  0.52
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  1
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  1
2017 Flagmeier P, De S, Wirthensohn DC, Lee SF, Vincke C, Muyldermans S, Knowles TPJ, Gandhi S, Dobson CM, Klenerman D. Ultrasensitive Measurement of Ca(2+) Influx into Lipid Vesicles Induced by Protein Aggregates. Angewandte Chemie (International Ed. in English). PMID 28474754 DOI: 10.1002/anie.201700966  0.84
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  1
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  1
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  1
2017 Perni M, Galvagnion C, Maltsev A, Meisl G, Müller MB, Challa PK, Kirkegaard JB, Flagmeier P, Cohen SI, Cascella R, Chen SW, Limboker R, Sormanni P, Heller GT, Aprile FA, ... ... Dobson CM, et al. A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity. Proceedings of the National Academy of Sciences of the United States of America. PMID 28096355 DOI: 10.1073/pnas.1610586114  1
2016 Šarić A, Buell AK, Meisl G, Michaels TCT, Dobson CM, Linse S, Knowles TPJ, Frenkel D. Physical determinants of the self-replication of protein fibrils. Nature Physics. 12: 874-880. PMID 31031819 DOI: 10.1038/nphys3828  1
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  1
2016 Ahn M, Hagan CL, Bernardo-Gancedo A, De Genst E, Newby FN, Christodoulou J, Dhulesia A, Dumoulin M, Robinson CV, Dobson CM, Kumita JR. The Significance of the Location of Mutations for the Native-State Dynamics of Human Lysozyme. Biophysical Journal. 111: 2358-2367. PMID 27926837 DOI: 10.1016/j.bpj.2016.10.028  0.72
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  1
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  1
2016 Evangelisti E, Cascella R, Becatti M, Marrazza G, Dobson CM, Chiti F, Stefani M, Cecchi C. Binding affinity of amyloid oligomers to cellular membranes is a generic indicator of cellular dysfunction in protein misfolding diseases. Scientific Reports. 6: 32721. PMID 27619987 DOI: 10.1038/srep32721  0.52
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  1
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  1
2016 Zhang Y, Buell AK, Müller T, De Genst E, Benesch J, Dobson CM, Knowles TP. Protein aggregate-ligand binding assays based on microfluidic diffusional separation. Chembiochem : a European Journal of Chemical Biology. PMID 27472818 DOI: 10.1002/cbic.201600384  1
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  1
2016 Cascella R, Capitini C, Fani G, Dobson CM, Cecchi C, Chiti F. Quantification of the relative contributions of loss-of-function and gain-of-function mechanisms in TDP-43 proteinopathies. The Journal of Biological Chemistry. PMID 27445339 DOI: 10.1074/jbc.M116.737726  0.52
2016 Mason TO, Michaels TC, Levin A, Gazit E, Dobson CM, Buell AK, Knowles TP. Synthesis of non-equilibrium supra-molecular peptide polymers on a microfluidic platform. Journal of the American Chemical Society. PMID 27387359 DOI: 10.1021/jacs.6b04136  1
2016 Iljina M, Garcia GA, Dear AJ, Flint J, Narayan P, Michaels TC, Dobson CM, Frenkel D, Knowles TP, Klenerman D. Quantitative analysis of co-oligomer formation by amyloid-beta peptide isoforms. Scientific Reports. 6: 28658. PMID 27346247 DOI: 10.1038/srep28658  0.6
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  1
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  1
2016 Angelova PR, Ludtmann MH, Horrocks MH, Negoda A, Cremades N, Klenerman D, Dobson CM, Wood NW, Pavlov EV, Gandhi S, Abramov AY. Ca2+ is a key factor in α-synuclein-induced neurotoxicity. Development (Cambridge, England). 143: e1.1. PMID 27190039 DOI: 10.1242/dev.139345  0.48
2016 Kakkar V, Månsson C, de Mattos EP, Bergink S, van der Zwaag M, van Waarde MA, Kloosterhuis NJ, Melki R, van Cruchten RT, Al-Karadaghi S, Arosio P, Dobson CM, Knowles TP, Bates GP, van Deursen JM, et al. The S/T-Rich Motif in the DNAJB6 Chaperone Delays Polyglutamine Aggregation and the Onset of Disease in a Mouse Model. Molecular Cell. PMID 27151442 DOI: 10.1016/j.molcel.2016.03.017  1
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  1
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  1
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  1
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  1
2016 Pinotsi D, Michel CH, Buell AK, Laine RF, Mahou P, Dobson CM, Kaminski CF, Kaminski Schierle GS. Nanoscopic insights into seeding mechanisms and toxicity of α-synuclein species in neurons. Proceedings of the National Academy of Sciences of the United States of America. PMID 26993805 DOI: 10.1073/pnas.1516546113  1
2016 Angelova PR, Ludtmann MH, Horrocks MH, Negoda A, Cremades N, Klenerman D, Dobson CM, Wood NW, Pavlov EV, Gandhi S, Abramov AY. Calcium is a key factor in α-synuclein induced neurotoxicity. Journal of Cell Science. PMID 26989132 DOI: 10.1242/jcs.180737  0.48
2016 Wolff M, Mittag JJ, Herling TW, Genst ED, Dobson CM, Knowles TP, Braun D, Buell AK. Quantitative thermophoretic study of disease-related protein aggregates. Scientific Reports. 6: 22829. PMID 26984748 DOI: 10.1038/srep22829  1
2016 Pedersen JT, Chen SW, Borg CB, Ness S, Bahl JM, Heegard NH, Dobson CM, Hemmingsen L, Cremades N, Teilum K. Amyloid-β and α-Synuclein Decrease the Level of Metal-Catalyzed Reactive Oxygen Species by Radical Scavenging and Redox Silencing. Journal of the American Chemical Society. PMID 26967463 DOI: 10.1021/jacs.5b13577  0.48
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  1
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  1
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  1
2016 Iljina M, Garcia GA, Horrocks MH, Tosatto L, Choi ML, Ganzinger KA, Abramov AY, Gandhi S, Wood NW, Cremades N, Dobson CM, Knowles TP, Klenerman D. Kinetic model of the aggregation of alpha-synuclein provides insights into prion-like spreading. Proceedings of the National Academy of Sciences of the United States of America. PMID 26884195 DOI: 10.1073/pnas.1524128113  1
2016 Yates EV, Meisl G, Knowles TP, Dobson CM. An Environmentally Sensitive Fluorescent Dye as a Multidimensional Probe of Amyloid Formation. The Journal of Physical Chemistry. B. PMID 26865546 DOI: 10.1021/acs.jpcb.5b09663  0.68
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  0.76
2016 Saar KL, Yates EV, Müller T, Saunier S, Dobson CM, Knowles TP. Automated Ex Situ Assays of Amyloid Formation on a Microfluidic Platform. Biophysical Journal. 110: 555-560. PMID 26840721 DOI: 10.1016/j.bpj.2015.11.3523  0.68
2016 Cappelli S, Penco A, Mannini B, Cascella R, Wilson M, Ecroyd H, Li X, Buxbaum J, Dobson CM, Cecchi C, Relini A, Chiti F. Effect of molecular chaperones on aberrant protein oligomers in vitro: super- versus sub-stoichiometric chaperone concentrations. Biological Chemistry. PMID 26812789 DOI: 10.1515/hsz-2015-0250  0.8
2016 Horrocks MH, Lee SF, Gandhi S, Magdalinou NK, Chen SW, Devine MJ, Tosatto L, Kjaergaard M, Beckwith JS, Zetterberg H, Iljina M, Cremades N, Dobson CM, Wood NW, Klenerman D. Single-molecule imaging of individual amyloid protein aggregates in human biofluids. Acs Chemical Neuroscience. PMID 26800462 DOI: 10.1021/acschemneuro.5b00324  1
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  1
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  1
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  1
2015 Tosatto L, Horrocks MH, Dear AJ, Knowles TP, Dalla Serra M, Cremades N, Dobson CM, Klenerman D. Single-molecule FRET studies on alpha-synuclein oligomerization of Parkinson's disease genetically related mutants. Scientific Reports. 5: 16696. PMID 26582456 DOI: 10.1038/srep16696  1
2015 Deas E, Cremades N, Angelova PR, Ludtmann M, Yao Z, Chen S, Horrocks M, Banushi B, Little D, Devine M, Gissen P, Klenerman D, Dobson C, Wood N, Gandhi S, et al. Alpha-synuclein oligomers interact with metal ions to induce oxidative stress and neuronal death in Parkinson's disease. Antioxidants & Redox Signaling. PMID 26564470 DOI: 10.1089/ars.2015.6343  0.76
2015 Terol PA, Kumita JR, Hook SC, Dobson CM, Esbjörner EK. Solvent exposure of Tyr10 as a probe of structural differences between monomeric and aggregated forms of the amyloid-β peptide. Biochemical and Biophysical Research Communications. PMID 26551456 DOI: 10.1016/j.bbrc.2015.11.018  1
2015 Michaels TC, Yde P, Willis JC, Jensen MH, Otzen D, Dobson CM, Buell AK, Knowles TP. The length distribution of frangible biofilaments. The Journal of Chemical Physics. 143: 164901. PMID 26520548 DOI: 10.1063/1.4933230  1
2015 Zeineddine R, Pundavela JF, Corcoran L, Stewart EM, Do-Ha D, Bax M, Guillemin G, Vine KL, Hatters DM, Ecroyd H, Dobson CM, Turner BJ, Ooi L, Wilson MR, Cashman NR, et al. SOD1 protein aggregates stimulate macropinocytosis in neurons to facilitate their propagation. Molecular Neurodegeneration. 10: 57. PMID 26520394 DOI: 10.1186/s13024-015-0053-4  1
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  1
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  1
2015 Labrador-Garrido A, Cejudo-Guillén M, Daturpalli S, Leal MM, Klippstein R, De Genst EJ, Villadiego J, Toledo-Aral JJ, Dobson CM, Jackson SE, Pozo D, Roodveldt C. Chaperome screening leads to identification of Grp94/Gp96 and FKBP4/52 as modulators of the α-synuclein-elicited immune response. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. PMID 26443817 DOI: 10.1096/fj.15-275131  0.76
2015 Yagi-Utsumi M, Dobson CM. Conformational Effects of the A21G Flemish Mutation on the Aggregation of Amyloid β Peptide. Biological & Pharmaceutical Bulletin. 38: 1668-72. PMID 26424029 DOI: 10.1248/bpb.b15-00466  1
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  1
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  1
2015 Horrocks MH, Tosatto L, Dear AJ, Garcia GA, Iljina M, Cremades N, Dalla Serra M, Knowles TP, Dobson CM, Klenerman D. Fast Flow Microfluidics and Single-Molecule Fluorescence for the Rapid Characterization of α-Synuclein Oligomers. Analytical Chemistry. 87: 8818-26. PMID 26258431 DOI: 10.1021/acs.analchem.5b01811  1
2015 Herling TW, Garcia GA, Michaels TC, Grentz W, Dean J, Shimanovich U, Gang H, Müller T, Kav B, Terentjev EM, Dobson CM, Knowles TP. Force generation by the growth of amyloid aggregates. Proceedings of the National Academy of Sciences of the United States of America. 112: 9524-9. PMID 26195762 DOI: 10.1073/pnas.1417326112  0.72
2015 Wyatt AR, Kumita JR, Farrawell NE, Dobson CM, Wilson MR. Alpha-2-Macroglobulin Is Acutely Sensitive to Freezing and Lyophilization: Implications for Structural and Functional Studies. Plos One. 10: e0130036. PMID 26103636 DOI: 10.1371/journal.pone.0130036  1
2015 Dworzak J, Renvoisé B, Habchi J, Yates EV, Combadière C, Knowles TP, Dobson CM, Blackstone C, Paulsen O, Murphy PM. Neuronal Cx3cr1 Deficiency Protects against Amyloid β-Induced Neurotoxicity. Plos One. 10: e0127730. PMID 26038823 DOI: 10.1371/journal.pone.0127730  0.68
2015 Zhou XM, Shimanovich U, Herling TW, Wu S, Dobson CM, Knowles TP, Perrett S. Enzymatically Active Microgels from Self-Assembling Protein Nanofibrils for Microflow Chemistry. Acs Nano. 9: 5772-81. PMID 26030507 DOI: 10.1021/acsnano.5b00061  0.6
2015 Pietralik Z, Kumita JR, Dobson CM, Kozak M. The influence of novel gemini surfactants containing cycloalkyl side-chains on the structural phases of DNA in solution. Colloids and Surfaces. B, Biointerfaces. 131: 83-92. PMID 25969417 DOI: 10.1016/j.colsurfb.2015.04.042  0.4
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  1
2015 De Genst E, Chirgadze DY, Klein FA, Butler DC, Matak-Vinković D, Trottier Y, Huston JS, Messer A, Dobson CM. Structure of a single-chain Fv bound to the 17 N-terminal residues of huntingtin provides insights into pathogenic amyloid formation and suppression. Journal of Molecular Biology. 427: 2166-78. PMID 25861763 DOI: 10.1016/j.jmb.2015.03.021  0.36
2015 Chen SW, Drakulic S, Deas E, Ouberai M, Aprile FA, Arranz R, Ness S, Roodveldt C, Guilliams T, De-Genst EJ, Klenerman D, Wood NW, Knowles TP, Alfonso C, Rivas G, ... ... Dobson CM, et al. Structural characterization of toxic oligomers that are kinetically trapped during α-synuclein fibril formation. Proceedings of the National Academy of Sciences of the United States of America. 112: E1994-2003. PMID 25855634 DOI: 10.1073/pnas.1421204112  1
2015 Baldwin AJ, Egan DL, Warren FJ, Barker PD, Dobson CM, Butterworth PJ, Ellis PR. Investigating the mechanisms of amylolysis of starch granules by solution-state NMR. Biomacromolecules. 16: 1614-21. PMID 25815624 DOI: 10.1021/acs.biomac.5b00190  1
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  1
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  1
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  1
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  1
2015 Shimanovich U, Efimov I, Mason TO, Flagmeier P, Buell AK, Gedanken A, Linse S, Åkerfeldt KS, Dobson CM, Weitz DA, Knowles TP. Protein microgels from amyloid fibril networks. Acs Nano. 9: 43-51. PMID 25469621 DOI: 10.1021/nn504869d  1
2015 Dworzak J, Renvoisé B, Habchi J, Yates EV, Combadière C, Knowles TP, Dobson CM, Blackstone C, Paulsen O, Murphy PM. Neuronal Cx3cr1 deficiency protects against amyloid β-induced neurotoxicity Plos One. 10. DOI: 10.1371/journal.pone.0127730  1
2015 Herling TW, Garcia GA, Michaels TCT, Grentz W, Dean J, Shimanovich U, Gang H, Müller T, Kav B, Terentjev EM, Dobson CM, Knowles TPJ. Force generation by the growth of amyloid aggregates Proceedings of the National Academy of Sciences of the United States of America. 112: 9524-9529. DOI: 10.1073/pnas.1417326112  1
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  1
2015 Zhou XM, Shimanovich U, Herling TW, Wu S, Dobson CM, Knowles TPJ, Perrett S. Enzymatically Active Microgels from Self-Assembling Protein Nanofibrils for Microflow Chemistry Acs Nano. 9: 5772-5781. DOI: 10.1021/acsnano.5b00061  1
2015 Pietralik Z, Kumita JR, Dobson CM, Kozak M. The influence of novel gemini surfactants containing cycloalkyl side-chains on the structural phases of DNA in solution Colloids and Surfaces B: Biointerfaces. 131: 83-92. DOI: 10.1016/j.colsurfb.2015.04.042  1
2015 Dobson CM. Alzheimer’s disease: addressing a twenty-first century plague Rendiconti Lincei. 26: 251-262. DOI: 10.1007/s12210-015-0453-y  1
2014 Labrador-Garrido A, Cejudo-Guillén M, Klippstein R, De Genst EJ, Tomas-Gallardo L, Leal MM, Villadiego J, Toledo-Aral JJ, Dobson CM, Pozo D, Roodveldt C. Chaperoned amyloid proteins for immune manipulation: α-Synuclein/Hsp70 shifts immunity toward a modulatory phenotype. Immunity, Inflammation and Disease. 2: 226-38. PMID 25866630 DOI: 10.1002/iid3.39  0.56
2014 Levin A, Mason TO, Adler-Abramovich L, Buell AK, Meisl G, Galvagnion C, Bram Y, Stratford SA, Dobson CM, Knowles TP, Gazit E. Ostwald's rule of stages governs structural transitions and morphology of dipeptide supramolecular polymers. Nature Communications. 5: 5219. PMID 25391268 DOI: 10.1038/ncomms6219  1
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  1
2014 Ganzinger KA, Narayan P, Qamar SS, Weimann L, Ranasinghe RT, Aguzzi A, Dobson CM, McColl J, St George-Hyslop P, Klenerman D. Single-molecule imaging reveals that small amyloid-β1-42 oligomers interact with the cellular prion protein (PrP(C)). Chembiochem : a European Journal of Chemical Biology. 15: 2515-21. PMID 25294384 DOI: 10.1002/cbic.201402377  0.76
2014 Ma?nsson C, Arosio P, Hussein R, Kampinga HH, Hashem RM, Boelens WC, Dobson CM, Knowles TPJ, Linse S, Emanuelsson C. Interaction of the molecular chaperone DNAJB6 with growing amyloid-beta 42 (Aβ42) aggregates leads to sub-stoichiometric inhibition of amyloid formation Journal of Biological Chemistry. 289: 31066-31076. PMID 25217638 DOI: 10.1074/jbc.M114.595124  0.76
2014 De Genst E, Messer A, Dobson CM. Antibodies and protein misfolding: From structural research tools to therapeutic strategies. Biochimica Et Biophysica Acta. 1844: 1907-1919. PMID 25194824 DOI: 10.1016/j.bbapap.2014.08.016  0.36
2014 Buell AK, Dobson CM, Knowles TPJ. The physical chemistry of the amyloid phenomenon: Thermodynamics and kinetics of fi lamentous protein aggregation Essays in Biochemistry. 56: 11-39. PMID 25131584 DOI: 10.1042/BSE0560011  1
2014 Mannini B, Mulvihill E, Sgromo C, Cascella R, Khodarahmi R, Ramazzotti M, Dobson CM, Cecchi C, Chiti F. Toxicity of protein oligomers is rationalized by a function combining size and surface hydrophobicity. Acs Chemical Biology. 9: 2309-17. PMID 25079908 DOI: 10.1021/cb500505m  0.8
2014 Meisl G, Yang X, Hellstrand E, Frohm B, Kirkegaard JB, Cohen SIA, Dobson CM, Linse S, Knowles TPJ. Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides Proceedings of the National Academy of Sciences of the United States of America. 111: 9384-9389. PMID 24938782 DOI: 10.1073/pnas.1401564111  1
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  1
2014 Esbjörner EK, Chan F, Rees E, Erdelyi M, Luheshi LM, Bertoncini CW, Kaminski CF, Dobson CM, Kaminski Schierle GS. Direct observations of amyloid β self-assembly in live cells provide insights into differences in the kinetics of Aβ(1-40) and Aβ(1-42) aggregation. Chemistry & Biology. 21: 732-42. PMID 24856820 DOI: 10.1016/j.chembiol.2014.03.014  0.44
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  1
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  1
2014 Wyatt AR, Kumita JR, Mifsud RW, Gooden CA, Wilson MR, Dobson CM. Hypochlorite-induced structural modifications enhance the chaperone activity of human ?2-macroglobulin Proceedings of the National Academy of Sciences of the United States of America. 111: E2081-E2090. PMID 24799681 DOI: 10.1073/pnas.1403379111  1
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  1
2014 Garcia GA, Cohen SIA, Dobson CM, Knowles TPJ. Nucleation-conversion-polymerization reactions of biological macromolecules with prenucleation clusters Physical Review E - Statistical, Nonlinear, and Soft Matter Physics. 89. PMID 24730879 DOI: 10.1103/PhysRevE.89.032712  0.76
2014 Wacker J, Rönicke R, Westermann M, Wulff M, Reymann KG, Dobson CM, Horn U, Crowther DC, Luheshi LM, Fändrich M. Oligomer-targeting with a conformational antibody fragment promotes toxicity in Aβ-expressing flies. Acta Neuropathologica Communications. 2: 43. PMID 24725347 DOI: 10.1186/2051-5960-2-43  0.76
2014 Narayan P, Holmström KM, Kim DH, Whitcomb DJ, Wilson MR, St George-Hyslop P, Wood NW, Dobson CM, Cho K, Abramov AY, Klenerman D. Rare individual amyloid-β oligomers act on astrocytes to initiate neuronal damage. Biochemistry. 53: 2442-53. PMID 24717093 DOI: 10.1021/bi401606f  1
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  1
2014 Dobson CM. Dynamics and timekeeping in biological systems Annual Review of Biochemistry. 83: 159-164. PMID 24606145 DOI: 10.1146/annurev-biochem-013014-102724  1
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  1
2014 Tóth G, Gardai SJ, Zago W, Bertoncini CW, Cremades N, Roy SL, Tambe MA, Rochet JC, Galvagnion C, Skibinski G, Finkbeiner S, Bova M, Regnstrom K, Chiou SS, Johnston J, ... ... Dobson CM, et al. Targeting the intrinsically disordered structural ensemble of α-synuclein by small molecules as a potential therapeutic strategy for Parkinson's disease. Plos One. 9: e87133. PMID 24551051 DOI: 10.1371/journal.pone.0087133  1
2014 Lorenzen N, Nielsen SB, Buell AK, Kaspersen JD, Arosio P, Vad BS, Paslawski W, Christiansen G, Valnickova-Hansen Z, Andreasen M, Enghild JJ, Pedersen JS, Dobson CM, Knowles TPJ, Otzen DE. The role of stable α-synuclein oligomers in the molecular events underlying amyloid formation Journal of the American Chemical Society. 136: 3859-3868. PMID 24527756 DOI: 10.1021/ja411577t  0.76
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  1
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  0.76
2014 Pinotsi D, Buell AK, Galvagnion C, Dobson CM, Kaminski Schierle GS, Kaminski CF. Direct observation of heterogeneous amyloid fibril growth kinetics via two-color super-resolution microscopy Nano Letters. 14: 339-345. PMID 24303845 DOI: 10.1021/nl4041093  0.76
2014 Bolognesi B, Cohen SIA, Aran Terol P, Esbjörner EK, Giorgetti S, Mossuto MF, Natalello A, Brorsson AC, Knowles TPJ, Dobson CM, Luheshi LM. Single point mutations induce a switch in the molecular mechanism of the aggregation of the Alzheimer's disease associated Aβ42 peptide Acs Chemical Biology. 9: 378-382. PMID 24199868 DOI: 10.1021/cb400616y  1
2014 Mannini B, Mulvihill E, Sgromo C, Cascella R, Khodarahmi R, Ramazzotti M, Dobson CM, Cecchi C, Chiti F. Toxicity of protein oligomers is rationalized by a function combining size and surface hydrophobicity Acs Chemical Biology. 9: 2309-2317. DOI: 10.1021/cb500505m  1
2014 De Genst E, Chirgadze DY, Klein FAC, Butler DC, Matak-Vinkovi? D, Trottier Y, Huston JS, Messer A, Dobson CM. Structure of a Single-Chain Fv Bound to the 17 N-Terminal Residues of Huntingtin Provides Insights into Pathogenic Amyloid Formation and Suppression Journal of Molecular Biology. DOI: 10.1016/j.jmb.2015.03.021  1
2014 Esbjörner EK, Chan F, Rees E, Erdelyi M, Luheshi LM, Bertoncini CW, Kaminski CF, Dobson CM, Kaminski Schierle GS. Direct observations of amyloid β Self-assembly in live cells provide insights into differences in the kinetics of Aβ(1-40) and Aβ(1-42) aggregation Chemistry and Biology. 21: 732-742. DOI: 10.1016/j.chembiol.2014.03.014  0.76
2014 De Genst E, Messer A, Dobson CM. Antibodies and protein misfolding: From structural research tools to therapeutic strategies Biochimica Et Biophysica Acta - Proteins and Proteomics. 1844: 1907-1919. DOI: 10.1016/j.bbapap.2014.08.016  0.76
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  1
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  0.76
2013 Roodveldt C, Labrador-Garrido A, Gonzalez-Rey E, Lachaud CC, Guilliams T, Fernandez-Montesinos R, Benitez-Rondan A, Robledo G, Hmadcha A, Delgado M, Dobson CM, Pozo D. Preconditioning of microglia by α-synuclein strongly affects the response induced by toll-like receptor (TLR) stimulation. Plos One. 8: e79160. PMID 24236103 DOI: 10.1371/journal.pone.0079160  0.76
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  1
2013 Mohr BG, Dobson CM, Garman SC, Muthukumar M. Electrostatic origin of in vitro aggregation of human γ-crystallin Journal of Chemical Physics. 139. PMID 24089726 DOI: 10.1063/1.4816367  0.72
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  0.76
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  0.76
2013 De Genst E, Chan PH, Pardon E, Hsu ST, Kumita JR, Christodoulou J, Menzer L, Chirgadze DY, Robinson CV, Muyldermans S, Matagne A, Wyns L, Dobson CM, Dumoulin M. A nanobody binding to non-amyloidogenic regions of the protein human lysozyme enhances partial unfolding but inhibits amyloid fibril formation. The Journal of Physical Chemistry. B. 117: 13245-58. PMID 23919586 DOI: 10.1021/jp403425z  1
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  1
2013 Aprile FA, Dhulesia A, Stengel F, Roodveldt C, Benesch JL, Tortora P, Robinson CV, Salvatella X, Dobson CM, Cremades N. Hsp70 oligomerization is mediated by an interaction between the interdomain linker and the substrate-binding domain. Plos One. 8: e67961. PMID 23840795 DOI: 10.1371/journal.pone.0067961  1
2013 Ouberai MM, Wang J, Swann MJ, Galvagnion C, Guilliams T, Dobson CM, Welland ME. α-Synuclein senses lipid packing defects and induces lateral expansion of lipids leading to membrane remodeling Journal of Biological Chemistry. 288: 20883-20895. PMID 23740253 DOI: 10.1074/jbc.M113.478297  0.76
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  1
2013 Pinotsi D, Buell AK, Dobson CM, Kaminski Schierle GS, Kaminski CF. A Label-Free, Quantitative Assay of Amyloid Fibril Growth Based on Intrinsic Fluorescence Chembiochem. 14: 846-850. PMID 23592254 DOI: 10.1002/cbic.201300103  0.76
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  1
2013 Xu LQ, Wu S, Buell AK, Cohen SI, Chen LJ, Hu WH, Cusack SA, Itzhaki LS, Zhang H, Knowles TP, Dobson CM, Welland ME, Jones GW, Perrett S. Influence of specific HSP70 domains on fibril formation of the yeast prion protein Ure2. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 368: 20110410. PMID 23530260 DOI: 10.1098/rstb.2011.0410  1
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, ... ... Dobson CM, et al. Atomic structure and hierarchical assembly of a cross-β amyloid fibril. Proceedings of the National Academy of Sciences of the United States of America. 110: 5468-73. PMID 23513222 DOI: 10.1073/pnas.1219476110  1
2013 Vendruscolo M, Dobson CM. Structural biology: Protein self-assembly intermediates. Nature Chemical Biology. 9: 216-7. PMID 23508184 DOI: 10.1038/nchembio.1210  1
2013 Buell AK, Hung P, Salvatella X, Welland ME, Dobson CM, Knowles TPJ. Electrostatic effects in filamentous protein aggregation Biophysical Journal. 104: 1116-1126. PMID 23473495 DOI: 10.1016/j.bpj.2013.01.031  1
2013 Chan FTS, Kaminski Schierle GS, Kumita JR, Bertoncini CW, Dobson CM, Kaminski CF. Protein amyloids develop an intrinsic fluorescence signature during aggregation Analyst. 138: 2156-2162. PMID 23420088 DOI: 10.1039/c3an36798c  1
2013 Wyatt AR, Const P, Ecroyd H, Dobson CM, Wilson MR, Kumita JR, Yerbury JJ. Protease-activated alpha-2-macroglobulin can inhibit amyloid formation via two distinct mechanisms Febs Letters. 587: 398-403. PMID 23353684 DOI: 10.1016/j.febslet.2013.01.020  1
2013 Narayan P, Ganzinger KA, McColl J, Weimann L, Meehan S, Qamar S, Carver JA, Wilson MR, St George-Hyslop P, Dobson CM, Klenerman D. Single molecule characterization of the interactions between amyloid-β peptides and the membranes of hippocampal cells. Journal of the American Chemical Society. 135: 1491-8. PMID 23339742 DOI: 10.1021/ja3103567  1
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  0.76
2013 Lancaster DL, Dobson CM, Rachubinski RA. Chaperone proteins select and maintain [PIN+] prion conformations in Saccharomyces cerevisiae. The Journal of Biological Chemistry. 288: 1266-76. PMID 23148221 DOI: 10.1074/jbc.M112.377564  0.72
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  0.76
2013 Dobson CM. The Amyloid Phenomenon and Its Significance Amyloid Fibrils and Prefibrillar Aggregates: Molecular and Biological Properties. 1-19. DOI: 10.1002/9783527654185.ch1  1
2012 Ahn M, de Genst E, Kaminski Schierle GS, Erdelyi M, Kaminski CF, Dobson CM, Kumita JR. Analysis of the Native Structure, Stability and Aggregation of Biotinylated Human Lysozyme Plos One. 7. PMID 23166837 DOI: 10.1371/journal.pone.0050192  1
2012 Narayan P, Meehan S, Carver JA, Wilson MR, Dobson CM, Klenerman D. Amyloid-β oligomers are sequestered by both intracellular and extracellular chaperones Biochemistry. 51: 9270-9276. PMID 23106396 DOI: 10.1021/bi301277k  1
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  1
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  1
2012 De Genst E, Dobson CM. Nanobodies as structural probes of protein misfolding and fibril formation. Methods in Molecular Biology (Clifton, N.J.). 911: 533-558. PMID 22886275 DOI: 10.1007/978-1-61779-968-6_34  1
2012 Lorenzen N, Cohen SIA, Nielsen SB, Herling TW, Christiansen G, Dobson CM, Knowles TPJ, Otzen D. Role of elongation and secondary pathways in S6 amyloid fibril growth Biophysical Journal. 102: 2167-2175. PMID 22824281 DOI: 10.1016/j.bpj.2012.03.047  0.76
2012 Mannini B, Cascella R, Zampagni M, Van Waarde-Verhagen M, Meehan S, Roodveldt C, Campioni S, Boninsegna M, Penco A, Relini A, Kampinga HH, Dobson CM, Wilson MR, Cecchi C, Chiti F. Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers Proceedings of the National Academy of Sciences of the United States of America. 109: 12479-12484. PMID 22802614 DOI: 10.1073/pnas.1117799109  0.76
2012 Bemporad F, De Simone A, Chiti F, Dobson CM. Characterizing intermolecular interactions that initiate native-like protein aggregation. Biophysical Journal. 102: 2595-604. PMID 22713575 DOI: 10.1016/j.bpj.2012.03.057  1
2012 Waudby CA, Mantle MD, Cabrita LD, Gladden LF, Dobson CM, Christodoulou J. Rapid distinction of intracellular and extracellular proteins using NMR diffusion measurements Journal of the American Chemical Society. 134: 11312-11315. PMID 22694283 DOI: 10.1021/ja304912c  0.76
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  1
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  1
2012 Cremades N, Cohen SI, Deas E, Abramov AY, Chen AY, Orte A, Sandal M, Clarke RW, Dunne P, Aprile FA, Bertoncini CW, Wood NW, Knowles TP, Dobson CM, Klenerman D. Direct observation of the interconversion of normal and toxic forms of α-synuclein. Cell. 149: 1048-59. PMID 22632969 DOI: 10.1016/j.cell.2012.03.037  1
2012 McGuire EK, Motskin M, Bolognesi B, Bergin SD, Knowles TPJ, Skepper J, Luheshi LM, McComb DW, Dobson CM, Porter AE. Selenium-enhanced electron microscopic imaging of different aggregate forms of a segment of the amyloid β peptide in cells Acs Nano. 6: 4740-4747. PMID 22631869 DOI: 10.1021/nn204859e  1
2012 Buell AK, Dobson CM, Welland ME. Measuring the kinetics of amyloid fibril elongation using quartz crystal microbalances Methods in Molecular Biology. 849: 101-119. PMID 22528086 DOI: 10.1007/978-1-61779-551-0_8  1
2012 De Simone A, Kitchen C, Kwan AH, Sunde M, Dobson CM, Frenkel D. Intrinsic disorder modulates protein self-assembly and aggregation. Proceedings of the National Academy of Sciences of the United States of America. 109: 6951-6. PMID 22509003 DOI: 10.1073/pnas.1118048109  0.76
2012 Buell AK, Dhulesia A, White DA, Knowles TP, Dobson CM, Welland ME. Detailed analysis of the energy barriers for amyloid fibril growth. Angewandte Chemie (International Ed. in English). 51: 5247-51. PMID 22489083 DOI: 10.1002/anie.201108040  1
2012 Speretta E, Jahn TR, Tartaglia GG, Favrin G, Barros TP, Imarisio S, Lomas DA, Luheshi LM, Crowther DC, Dobson CM. Expression in drosophila of tandem amyloid β peptides provides insights into links between aggregation and neurotoxicity. The Journal of Biological Chemistry. 287: 20748-54. PMID 22461632 DOI: 10.1074/jbc.M112.350124  1
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  0.76
2012 Gregory JM, Barros TP, Meehan S, Dobson CM, Luheshi LM. The aggregation and neurotoxicity of TDP-43 and its ALS-associated 25 kDa fragment are differentially affected by molecular chaperones in Drosophila. Plos One. 7: e31899. PMID 22384095 DOI: 10.1371/journal.pone.0031899  0.72
2012 Evangelisti E, Cecchi C, Cascella R, Sgromo C, Becatti M, Dobson CM, Chiti F, Stefani M. Membrane lipid composition and its physicochemical properties define cell vulnerability to aberrant protein oligomers Journal of Cell Science. 125: 2416-2427. PMID 22344258 DOI: 10.1242/jcs.098434  0.76
2012 Narayan P, Orte A, Clarke RW, Bolognesi B, Hook S, Ganzinger KA, Meehan S, Wilson MR, Dobson CM, Klenerman D. The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β 1-40 peptide Nature Structural and Molecular Biology. 19: 79-84. PMID 22179788 DOI: 10.1038/nsmb.2191  1
2012 Abelein A, Bolognesi B, Dobson CM, Gräslund A, Lendel C. Hydrophobicity and conformational change as mechanistic determinants for nonspecific modulators of amyloid β self-assembly Biochemistry. 51: 126-137. PMID 22133042 DOI: 10.1021/bi201745g  0.76
2012 Kumita JR, Helmfors L, Williams J, Luheshi LM, Menzer L, Dumoulin M, Lomas DA, Crowther DC, Dobson CM, Brorsson AC. Disease-related amyloidogenic variants of human lysozyme trigger the unfolded protein response and disturb eye development in Drosophila melanogaster. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 26: 192-202. PMID 21965601 DOI: 10.1096/fj.11-185983  1
2012 Fusco G, De Simone A, Hsu ST, Bemporad F, Vendruscolo M, Chiti F, Dobson CM. ¹H, ¹³C and ¹⁵N resonance assignments of human muscle acylphosphatase. Biomolecular Nmr Assignments. 6: 27-9. PMID 21643968 DOI: 10.1007/s12104-011-9318-1  1
2012 Gregory JM, Barros TP, Meehan S, Dobson CM, Luheshi LM. The aggregation and neurotoxicity of TDP-43 and its als-associated 25 kDa fragment are differentially affected by molecular chaperones in drosophila Plos One. 7. DOI: 10.1371/journal.pone.0031899  0.76
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  0.76
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  1
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  1
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  1
2011 Buell AK, Esbjörner EK, Riss PJ, White DA, Aigbirhio FI, Toth G, Welland ME, Dobson CM, Knowles TP. Probing small molecule binding to amyloid fibrils. Physical Chemistry Chemical Physics : Pccp. 13: 20044-52. PMID 22006124 DOI: 10.1039/c1cp22283j  0.76
2011 Shammas SL, Waudby CA, Wang S, Buell AK, Knowles TP, Ecroyd H, Welland ME, Carver JA, Dobson CM, Meehan S. Binding of the molecular chaperone αB-crystallin to Aβ amyloid fibrils inhibits fibril elongation. Biophysical Journal. 101: 1681-9. PMID 21961594 DOI: 10.1016/j.bpj.2011.07.056  0.76
2011 Knowles TP, White DA, Abate AR, Agresti JJ, Cohen SI, Sperling RA, De Genst EJ, Dobson CM, Weitz DA. Observation of spatial propagation of amyloid assembly from single nuclei. Proceedings of the National Academy of Sciences of the United States of America. 108: 14746-51. PMID 21876182 DOI: 10.1073/pnas.1105555108  1
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  0.76
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  1
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  1
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  1
2011 Whyteside G, Alcocer MJ, Kumita JR, Dobson CM, Lazarou M, Pleass RJ, Archer DB. Native-state stability determines the extent of degradation relative to secretion of protein variants from Pichia pastoris. Plos One. 6: e22692. PMID 21818368 DOI: 10.1371/journal.pone.0022692  1
2011 Kaminski Schierle GS, Van De Linde S, Erdelyi M, Esbjörner EK, Klein T, Rees E, Bertoncini CW, Dobson CM, Sauer M, Kaminski CF. In situ measurements of the formation and morphology of intracellular β-amyloid fibrils by super-resolution fluorescence imaging Journal of the American Chemical Society. 133: 12902-12905. PMID 21793568 DOI: 10.1021/ja201651w  0.76
2011 Bayro MJ, Debelouchina GT, Eddy MT, Birkett NR, MacPhee CE, Rosay M, Maas WE, Dobson CM, Griffin RG. Intermolecular structure determination of amyloid fibrils with magic-angle spinning and dynamic nuclear polarization NMR. Journal of the American Chemical Society. 133: 13967-74. PMID 21774549 DOI: 10.1021/ja203756x  1
2011 Knowles TPJ, Devlin GL, Dobson CM, Welland ME. Probing protein aggregation with quartz crystal microbalances Methods in Molecular Biology. 752: 137-145. PMID 21713635 DOI: 10.1007/978-1-60327-223-0_9  1
2011 Cabrita LD, Waudby CA, Dobson CM, Christodoulou J. Solution-state nuclear magnetic resonance spectroscopy and protein folding Methods in Molecular Biology. 752: 97-120. PMID 21713633 DOI: 10.1007/978-1-60327-223-0_7  1
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  0.76
2011 Levitan K, Chereau D, Cohen SIA, Knowles TPJ, Dobson CM, Fink AL, Anderson JP, Goldstein JM, Millhauser GL. Conserved C-terminal charge exerts a profound influence on the aggregation rate of α-synuclein Journal of Molecular Biology. 411: 329-333. PMID 21689664 DOI: 10.1016/j.jmb.2011.05.046  0.76
2011 Mossuto MF, Bolognesi B, Guixer B, Dhulesia A, Agostini F, Kumita JR, Tartaglia GG, Dumoulin M, Dobson CM, Salvatella X. Disulfide bonds reduce the toxicity of the amyloid fibrils formed by an extracellular protein. Angewandte Chemie (International Ed. in English). 50: 7048-51. PMID 21671315 DOI: 10.1002/anie.201100986  0.76
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  1
2011 Shammas SL, Knowles TPJ, Baldwin AJ, MacPhee CE, Welland ME, Dobson CM, Devlin GL. Perturbation of the stability of amyloid fibrils through alteration of electrostatic interactions Biophysical Journal. 100: 2783-2791. PMID 21641324 DOI: 10.1016/j.bpj.2011.04.039  1
2011 Buell AK, Dhulesia A, Mossuto MF, Cremades N, Kumita JR, Dumoulin M, Welland ME, Knowles TP, Salvatella X, Dobson CM. Population of nonnative states of lysozyme variants drives amyloid fibril formation. Journal of the American Chemical Society. 133: 7737-43. PMID 21528861 DOI: 10.1021/ja109620d  1
2011 Wyatt AR, Yerbury JJ, Berghofer P, Greguric I, Katsifis A, Dobson CM, Wilson MR. Clusterin facilitates in vivo clearance of extracellular misfolded proteins Cellular and Molecular Life Sciences. 68: 3919-3931. PMID 21505792 DOI: 10.1007/s00018-011-0684-8  0.76
2011 Kamatari YO, Smith LJ, Dobson CM, Akasaka K. Cavity hydration as a gateway to unfolding: An NMR study of hen lysozyme at high pressure and low temperature Biophysical Chemistry. 156: 24-30. PMID 21367514 DOI: 10.1016/j.bpc.2011.01.009  0.88
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  1
2011 Kaminski Schierle GS, Bertoncini CW, Chan FT, van der Goot AT, Schwedler S, Skepper J, Schlachter S, van Ham T, Esposito A, Kumita JR, Nollen EA, Dobson CM, Kaminski CF. A FRET sensor for non-invasive imaging of amyloid formation in vivo. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. 12: 673-80. PMID 21308945 DOI: 10.1002/cphc.201000996  1
2011 Raimondi S, Guglielmi F, Giorgetti S, Di Gaetano S, Arciello A, Monti DM, Relini A, Nichino D, Doglia SM, Natalello A, Pucci P, Mangione P, Obici L, Merlini G, Stoppini M, ... ... Dobson CM, et al. Effects of the known pathogenic mutations on the aggregation pathway of the amyloidogenic peptide of apolipoprotein A-I. Journal of Molecular Biology. 407: 465-76. PMID 21296086 DOI: 10.1016/j.jmb.2011.01.044  0.76
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  1
2011 Wang YQ, Buell AK, Wang XY, Welland ME, Dobson CM, Knowles TPJ, Perrett S. Relationship between prion propensity and the rates of individual molecular steps of fibril assembly Journal of Biological Chemistry. 286: 12101-12107. PMID 21233211 DOI: 10.1074/jbc.M110.208934  0.76
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  1
2010 Buell AK, Dobson CM, Knowles TPJ, Welland ME. Interactions between Amyloidophilic dyes and their relevance to studies of amyloid inhibitors Biophysical Journal. 99: 3492-3497. PMID 21081099 DOI: 10.1016/j.bpj.2010.08.074  0.76
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  1
2010 Roodveldt C, Labrador-Garrido A, Gonzalez-Rey E, Fernandez-Montesinos R, Caro M, Lachaud CC, Waudby CA, Delgado M, Dobson CM, Pozo D. Glial innate immunity generated by non-aggregated alpha-synuclein in mouse: Differences between wild-type and Parkinson's disease-linked mutants Plos One. 5. PMID 21048992 DOI: 10.1371/journal.pone.0013481  1
2010 Dhulesia A, Cremades N, Kumita JR, Hsu ST, Mossuto MF, Dumoulin M, Nietlispach D, Akke M, Salvatella X, Dobson CM. Local cooperativity in an amyloidogenic state of human lysozyme observed at atomic resolution. Journal of the American Chemical Society. 132: 15580-8. PMID 20958028 DOI: 10.1021/ja103524m  1
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  0.76
2010 Buell AK, Blundell JR, Dobson CM, Welland ME, Terentjev EM, Knowles TP. Frequency factors in a landscape model of filamentous protein aggregation. Physical Review Letters. 104: 228101. PMID 20873942 DOI: 10.1103/PhysRevLett.104.228101  0.76
2010 Sandberg A, Luheshi LM, Söllvander S, Pereira de Barros T, Macao B, Knowles TP, BiverstÃ¥l H, Lendel C, Ekholm-Petterson F, Dubnovitsky A, Lannfelt L, Dobson CM, Härd T. Stabilization of neurotoxic Alzheimer amyloid-beta oligomers by protein engineering. Proceedings of the National Academy of Sciences of the United States of America. 107: 15595-600. PMID 20713699 DOI: 10.1073/pnas.1001740107  0.76
2010 Bayro MJ, Maly T, Birkett NR, Macphee CE, Dobson CM, Griffin RG. High-resolution MAS NMR analysis of PI3-SH3 amyloid fibrils: backbone conformation and implications for protofilament assembly and structure . Biochemistry. 49: 7474-84. PMID 20707313 DOI: 10.1021/bi100864t  1
2010 Buell AK, White DA, Meier C, Welland ME, Knowles TP, Dobson CM. Surface attachment of protein fibrils via covalent modification strategies. The Journal of Physical Chemistry. B. 114: 10925-38. PMID 20695458 DOI: 10.1021/jp101579n  1
2010 Mossuto MF, Dhulesia A, Devlin G, Frare E, Kumita JR, de Laureto PP, Dumoulin M, Fontana A, Dobson CM, Salvatella X. The non-core regions of human lysozyme amyloid fibrils influence cytotoxicity. Journal of Molecular Biology. 402: 783-96. PMID 20624399 DOI: 10.1016/j.jmb.2010.07.005  1
2010 De Genst EJ, Guilliams T, Wellens J, O'Day EM, Waudby CA, Meehan S, Dumoulin M, Hsu ST, Cremades N, Verschueren KH, Pardon E, Wyns L, Steyaert J, Christodoulou J, Dobson CM. Structure and properties of a complex of α-synuclein and a single-domain camelid antibody. Journal of Molecular Biology. 402: 326-43. PMID 20620148 DOI: 10.1016/j.jmb.2010.07.001  1
2010 Carulla N, Zhou M, Giralt E, Robinson CV, Dobson CM. Structure and intermolecular dynamics of aggregates populated during amyloid fibril formation studied by hydrogen/deuterium exchange Accounts of Chemical Research. 43: 1072-1079. PMID 20557067 DOI: 10.1021/ar9002784  1
2010 Bolognesi B, Kumita JR, Barros TP, Esbjorner EK, Luheshi LM, Crowther DC, Wilson MR, Dobson CM, Favrin G, Yerbury JJ. ANS binding reveals common features of cytotoxic amyloid species. Acs Chemical Biology. 5: 735-40. PMID 20550130 DOI: 10.1021/cb1001203  1
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  1
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  1
2010 Hagan CL, Johnson RJ, Dhulesia A, Dumoulin M, Dumont J, De Genst E, Christodoulou J, Robinson CV, Dobson CM, Kumita JR. A non-natural variant of human lysozyme (I59T) mimics the in vitro behaviour of the I56T variant that is responsible for a form of familial amyloidosis. Protein Engineering, Design & Selection : Peds. 23: 499-506. PMID 20382744 DOI: 10.1093/protein/gzq023  1
2010 White DA, Buell AK, Knowles TP, Welland ME, Dobson CM. Protein aggregation in crowded environments. Journal of the American Chemical Society. 132: 5170-5. PMID 20334356 DOI: 10.1021/ja909997e  1
2010 Luheshi LM, Hoyer W, de Barros TP, van Dijk Härd I, Brorsson AC, Macao B, Persson C, Crowther DC, Lomas DA, Ståhl S, Dobson CM, Härd T. Sequestration of the Abeta peptide prevents toxicity and promotes degradation in vivo. Plos Biology. 8: e1000334. PMID 20305716 DOI: 10.1371/journal.pbio.1000334  1
2010 Waudby CA, Knowles TP, Devlin GL, Skepper JN, Ecroyd H, Carver JA, Welland ME, Christodoulou J, Dobson CM, Meehan S. The interaction of alphaB-crystallin with mature alpha-synuclein amyloid fibrils inhibits their elongation. Biophysical Journal. 98: 843-51. PMID 20197038 DOI: 10.1016/j.bpj.2009.10.056  1
2010 Cabrita LD, Dobson CM, Christodoulou J. Protein folding on the ribosome Current Opinion in Structural Biology. 20: 33-45. PMID 20149635 DOI: 10.1016/j.sbi.2010.01.005  1
2010 Campioni S, Mannini B, Zampagni M, Pensalfini A, Parrini C, Evangelisti E, Relini A, Stefani M, Dobson CM, Cecchi C, Chiti F. A causative link between the structure of aberrant protein oligomers and their toxicity Nature Chemical Biology. 6: 140-147. PMID 20081829 DOI: 10.1038/nchembio.283  0.88
2010 Lendel C, Bolognesi B, Wahlström A, Dobson CM, Gräslund A. Detergent-like interaction of congo red with the amyloid β peptide Biochemistry. 49: 1358-1360. PMID 20070125 DOI: 10.1021/bi902005t  1
2010 Brorsson AC, Kumita JR, MacLeod I, Bolognesi B, Speretta E, Luheshi LM, Knowles TP, Dobson CM, Crowther DC. Methods and models in neurodegenerative and systemic protein aggregation diseases. Frontiers in Bioscience (Landmark Edition). 15: 373-96. PMID 20036826 DOI: 10.2741/3626  0.76
2010 Hsu STD, Blaser G, Behrens C, Cabrita LD, Dobson CM, Jackson SE. Folding study of venus reveals a strong ion dependence of its yellow fluorescence under mildly acidic conditions Journal of Biological Chemistry. 285: 4859-4869. PMID 19901033 DOI: 10.1074/jbc.M109.000695  0.76
2010 van Ham TJ, Esposito A, Kumita JR, Hsu ST, Kaminski Schierle GS, Kaminski CF, Dobson CM, Nollen EA, Bertoncini CW. Towards multiparametric fluorescent imaging of amyloid formation: studies of a YFP model of alpha-synuclein aggregation. Journal of Molecular Biology. 395: 627-42. PMID 19891973 DOI: 10.1016/j.jmb.2009.10.066  0.76
2010 McGuire EK, Motskin M, Knowles TPJ, Dobson CM, McComb DW, Porter AE. Imaging Alzheimer's disease-related protein aggregates in human cells using a selenium label Journal of Physics: Conference Series. 241. DOI: 10.1088/1742-6596/241/1/012020  0.76
2010 Cabrita LD, Dobson CM, Christodoulou J. Early nascent chain folding events on the ribosome Israel Journal of Chemistry. 50: 99-108. DOI: 10.1002/ijch.201000015  1
2010 DOBSON CM, SALI A, KARPLUS M. ChemInform Abstract: Protein Folding: A Perspective from Theory and Experiment Cheminform. 29: no-no. DOI: 10.1002/chin.199826366  1
2010 White DA, Dobson CM, Welland ME, Knowles TPJ. Quantitative approaches for characterising fibrillar protein nanostructures Materials Research Society Symposium Proceedings. 1274: 33-39.  0.76
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  1
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  1
2009 Cabrita LD, Hsu STD, Launay H, Dobson CM, Christodoulou J. Probing ribosome-nascent chain complexes produced in vivo by NMR spectroscopy Proceedings of the National Academy of Sciences of the United States of America. 106: 22239-22244. PMID 20018739 DOI: 10.1073/pnas.0903750106  1
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  1
2009 Poon S, Birkett NR, Fowler SB, Luisi BF, Dobson CM, Zurdo J. Amyloidogenicity and aggregate cytotoxicity of human glucagon-like peptide-1 (hGLP-1) Protein and Peptide Letters. 16: 1548-1556. PMID 20001917 DOI: 10.2174/092986609789839232  0.64
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  1
2009 Roodveldt C, Bertoncini CW, Andersson A, Van Der Goot AT, Hsu ST, Fernández-Montesinos R, De Jong J, Van Ham TJ, Nollen EA, Pozo D, Christodoulou J, Dobson CM. Chaperone proteostasis in Parkinson's disease: Stabilization of the Hsp70/α-synuclein complex by Hip Embo Journal. 28: 3758-3770. PMID 19875982 DOI: 10.1038/emboj.2009.298  0.76
2009 Vuchelen A, O'Day E, De Genst E, Pardon E, Wyns L, Dumoulin M, Dobson CM, Christodoulou J, Hsu ST. (1)H, (13)C and (15)N assignments of a camelid nanobody directed against human alpha-synuclein. Biomolecular Nmr Assignments. 3: 231-3. PMID 19763886 DOI: 10.1007/s12104-009-9182-4  1
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  1
2009 Hsu STD, Behrens C, Cabrita LD, Dobson CM. 1H, 15N and 13C assignments of yellow fluorescent protein (YFP) Venus Biomolecular Nmr Assignments. 3: 67-72. PMID 19636949 DOI: 10.1007/s12104-009-9143-y  0.76
2009 Hsu STD, Cabrita LD, Christodoulou J, Dobson CM. 1H, 15N and 13C assignments of domain 5 of Dictyostelium discoideum gelation factor (ABP-120) in its native and 8M urea-denatured states Biomolecular Nmr Assignments. 3: 29-31. PMID 19636940 DOI: 10.1007/s12104-008-9134-4  0.76
2009 Hsu STD, Dobson CM. 1H, 15N and 13C assignments of the dimeric ribosome binding domain of trigger factor from Escherichia coli Biomolecular Nmr Assignments. 3: 17-20. PMID 19636937 DOI: 10.1007/s12104-008-9130-8  0.76
2009 Porter AE, Knowles TPJ, Muller K, Meehan S, McGuire E, Skepper J, Welland ME, Dobson CM. Imaging Amyloid Fibrils within Cells Using a Se-Labelling Strategy Journal of Molecular Biology. 392: 868-871. PMID 19635483 DOI: 10.1016/j.jmb.2009.07.061  1
2009 Bayro MJ, Maly T, Birkett NR, Dobson CM, Griffin RG. Long-range correlations between aliphatic 13C nuclei in protein MAS NMR spectroscopy. Angewandte Chemie (International Ed. in English). 48: 5708-10. PMID 19562810 DOI: 10.1002/anie.200901520  0.64
2009 Luheshi LM, Dobson CM. Bridging the gap: From protein misfolding to protein misfolding diseases Febs Letters. 583: 2581-2586. PMID 19545568 DOI: 10.1016/j.febslet.2009.06.030  1
2009 White DA, Buell AK, Dobson CM, Welland ME, Knowles TP. Biosensor-based label-free assays of amyloid growth. Febs Letters. 583: 2587-92. PMID 19523953 DOI: 10.1016/j.febslet.2009.06.008  1
2009 Hsu STD, Cabrita LD, Fucini P, Christodoulou J, Dobson CM. Probing side-chain dynamics of a ribosome-bound nascent chain using methyl NMR spectroscopy Journal of the American Chemical Society. 131: 8366-8367. PMID 19492839 DOI: 10.1021/ja902778n  0.76
2009 Yanamandra K, Alexeyev O, Zamotin V, Srivastava V, Shchukarev A, Brorsson AC, Tartaglia GG, Vogl T, Kayed R, Wingsle G, Olsson J, Dobson CM, Bergh A, Elgh F, Morozova-Roche LA. Amyloid formation by the pro-inflammatory S100A8/A9 proteins in the ageing prostate. Plos One. 4: e5562. PMID 19440546 DOI: 10.1371/journal.pone.0005562  0.56
2009 Hsu STD, Bertoncini CW, Dobson CM. Use of protonless NMR spectroscopy to alleviate the loss of information resulting from exchange-broadening Journal of the American Chemical Society. 131: 7222-7223. PMID 19432443 DOI: 10.1021/ja902307q  1
2009 Carulla N, Zhou M, Arimon M, Gairí M, Giralt E, Robinson CV, Dobson CM. Experimental characterization of disordered and ordered aggregates populated during the process of amyloid fibril formation. Proceedings of the National Academy of Sciences of the United States of America. 106: 7828-33. PMID 19416886 DOI: 10.1073/pnas.0812227106  1
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  1
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  0.68
2009 Hsu ST, Cabrita LD, Fucini P, Dobson CM, Christodoulou J. Structure, dynamics and folding of an immunoglobulin domain of the gelation factor (ABP-120) from Dictyostelium discoideum. Journal of Molecular Biology. 388: 865-79. PMID 19281823 DOI: 10.1016/j.jmb.2009.02.063  0.48
2009 Haakensen M, Dobson CM, Hill JE, Ziola B. Reclassification of Pediococcus dextrinicus (Coster and White 1964) back 1978 (Approved Lists 1980) as Lactobacillus dextrinicus comb. nov., and emended description of the genus Lactobacillus. International Journal of Systematic and Evolutionary Microbiology. 59: 615-21. PMID 19244449 DOI: 10.1099/ijs.0.65779-0  0.72
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  1
2009 Yerbury JJ, Kumita JR, Meehan S, Dobson CM, Wilson MR. alpha2-Macroglobulin and haptoglobin suppress amyloid formation by interacting with prefibrillar protein species. The Journal of Biological Chemistry. 284: 4246-54. PMID 19074141 DOI: 10.1074/jbc.M807242200  0.76
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  1
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  0.48
2008 Macao B, Hoyer W, Sandberg A, Brorsson AC, Dobson CM, Härd T. Recombinant amyloid beta-peptide production by coexpression with an affibody ligand. Bmc Biotechnology. 8: 82. PMID 18973685 DOI: 10.1186/1472-6750-8-82  0.44
2008 Chan PH, Pardon E, Menzer L, De Genst E, Kumita JR, Christodoulou J, Saerens D, Brans A, Bouillenne F, Archer DB, Robinson CV, Muyldermans S, Matagne A, Redfield C, Wyns L, ... Dobson CM, et al. Engineering a camelid antibody fragment that binds to the active site of human lysozyme and inhibits its conversion into amyloid fibrils. Biochemistry. 47: 11041-54. PMID 18816062 DOI: 10.1021/bi8005797  1
2008 Orte A, Birkett NR, Clarke RW, Devlin GL, Dobson CM, Klenerman D. Direct characterization of amyloidogenic oligomers by single-molecule fluorescence. Proceedings of the National Academy of Sciences of the United States of America. 105: 14424-9. PMID 18796612 DOI: 10.1073/pnas.0803086105  1
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  1
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  0.76
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  1
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  1
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  1
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  0.76
2008 Baldwin AJ, Anthony-Cahill SJ, Knowles TP, Lippens G, Christodoulou J, Barker PD, Dobson CM. Measurement of amyloid fibril length distributions by inclusion of rotational motion in solution NMR diffusion measurements. Angewandte Chemie (International Ed. in English). 47: 3385-7. PMID 18350531 DOI: 10.1002/anie.200703915  1
2008 Dalal S, Canet D, Kaiser SE, Dobson CM, Regan L. Conservation of mechanism, variation of rate: folding kinetics of three homologous four-helix bundle proteins. Protein Engineering, Design & Selection : Peds. 21: 197-206. PMID 18299293 DOI: 10.1093/protein/gzm088  1
2008 van Nuland NA, Dobson CM, Regan L. Characterization of folding the four-helix bundle protein Rop by real-time NMR. Protein Engineering, Design & Selection : Peds. 21: 165-70. PMID 18299292 DOI: 10.1093/protein/gzm081  0.76
2008 Luheshi LM, Crowther DC, Dobson CM. Protein misfolding and disease: from the test tube to the organism. Current Opinion in Chemical Biology. 12: 25-31. PMID 18295611 DOI: 10.1016/j.cbpa.2008.02.011  0.52
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  0.36
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  1
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  1
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  1
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  1
2007 Vendruscolo M, Dobson CM. Chemical biology: More charges against aggregation. Nature. 449: 555. PMID 17914388 DOI: 10.1038/449555a  0.44
2007 Baldwin AJ, Christodoulou J, Barker PD, Dobson CM, Lippens G. Contribution of rotational diffusion to pulsed field gradient diffusion measurements. The Journal of Chemical Physics. 127: 114505. PMID 17887855 DOI: 10.1063/1.2759211  0.44
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  1
2007 Knowles TP, Shu W, Devlin GL, Meehan S, Auer S, Dobson CM, Welland ME. Kinetics and thermodynamics of amyloid formation from direct measurements of fluctuations in fibril mass. Proceedings of the National Academy of Sciences of the United States of America. 104: 10016-21. PMID 17540728 DOI: 10.1073/pnas.0610659104  1
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  0.44
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  1
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  0.76
2007 Yerbury JJ, Poon S, Meehan S, Thompson B, Kumita JR, Dobson CM, Wilson MR. The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 21: 2312-22. PMID 17412999 DOI: 10.1096/fj.06-7986com  1
2007 Kumita JR, Poon S, Caddy GL, Hagan CL, Dumoulin M, Yerbury JJ, Stewart EM, Robinson CV, Wilson MR, Dobson CM. The extracellular chaperone clusterin potently inhibits human lysozyme amyloid formation by interacting with prefibrillar species. Journal of Molecular Biology. 369: 157-67. PMID 17407782 DOI: 10.1016/j.jmb.2007.02.095  1
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  0.52
2007 Dobson CM. Diseases of protein misfolding Genes and Common Diseases. 113-131. DOI: 10.1017/CBO9780511543555.008  1
2006 Calamai M, Kumita JR, Mifsud J, Parrini C, Ramazzotti M, Ramponi G, Taddei N, Chiti F, Dobson CM. Nature and significance of the interactions between amyloid fibrils and biological polyelectrolytes. Biochemistry. 45: 12806-15. PMID 17042499 DOI: 10.1021/bi0610653  1
2006 Smith JF, Knowles TP, Dobson CM, Macphee CE, Welland ME. Characterization of the nanoscale properties of individual amyloid fibrils. Proceedings of the National Academy of Sciences of the United States of America. 103: 15806-11. PMID 17038504 DOI: 10.1073/pnas.0604035103  1
2006 Dumoulin M, Kumita JR, Dobson CM. Normal and aberrant biological self-assembly: Insights from studies of human lysozyme and its amyloidogenic variants. Accounts of Chemical Research. 39: 603-10. PMID 16981676 DOI: 10.1021/ar050070g  1
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  0.68
2006 Knowles TP, Smith JF, Craig A, Dobson CM, Welland ME. Spatial persistence of angular correlations in amyloid fibrils. Physical Review Letters. 96: 238301. PMID 16803412 DOI: 10.1103/PhysRevLett.96.238301  1
2006 Devlin GL, Knowles TP, Squires A, McCammon MG, Gras SL, Nilsson MR, Robinson CV, Dobson CM, MacPhee CE. The component polypeptide chains of bovine insulin nucleate or inhibit aggregation of the parent protein in a conformation-dependent manner. Journal of Molecular Biology. 360: 497-509. PMID 16774767 DOI: 10.1016/j.jmb.2006.05.007  1
2006 Dobson CM. An accidental breach of a protein's natural defenses Nature Structural and Molecular Biology. 13: 295-297. PMID 16715043 DOI: 10.1038/nsmb0406-295  1
2006 Fändrich M, Zandomeneghi G, Krebs MR, Kittler M, Buder K, Rossner A, Heinemann SH, Dobson CM, Diekmann S. Apomyoglobin reveals a random-nucleation mechanism in amyloid protofibril formation. Acta Histochemica. 108: 215-9. PMID 16714052 DOI: 10.1016/j.acthis.2006.03.012  1
2006 Dobson CM. Protein aggregation and its consequences for human disease Protein and Peptide Letters. 13: 219-227. PMID 16515449 DOI: 10.2174/092986606775338362  1
2006 Kumita JR, Johnson RJ, Alcocer MJ, Dumoulin M, Holmqvist F, McCammon MG, Robinson CV, Archer DB, Dobson CM. Impact of the native-state stability of human lysozyme variants on protein secretion by Pichia pastoris. The Febs Journal. 273: 711-20. PMID 16441658 DOI: 10.1111/j.1742-4658.2005.05099.x  1
2006 Chandran V, Stollar EJ, Lindorff-Larsen K, Harper JF, Chazin WJ, Dobson CM, Luisi BF, Christodoulou J. Structure of the regulatory apparatus of a calcium-dependent protein kinase (CDPK): a novel mode of calmodulin-target recognition. Journal of Molecular Biology. 357: 400-10. PMID 16430916 DOI: 10.1016/j.jmb.2005.11.093  1
2006 Vaz DC, Rodrigues JR, Sebald W, Dobson CM, Brito RM. Enthalpic and entropic contributions mediate the role of disulfide bonds on the conformational stability of interleukin-4. Protein Science : a Publication of the Protein Society. 15: 33-44. PMID 16373475 DOI: 10.1110/ps.051593306  1
2005 Thorn DC, Meehan S, Sunde M, Rekas A, Gras SL, MacPhee CE, Dobson CM, Wilson MR, Carver JA. Amyloid fibril formation by bovine milk κ-casein and its inhibition by the molecular chaperones α3- and β-casein Biochemistry. 44: 17027-17036. PMID 16363816 DOI: 10.1021/bi051352r  0.72
2005 Wright CF, Teichmann SA, Clarke J, Dobson CM. The importance of sequence diversity in the aggregation and evolution of proteins. Nature. 438: 878-81. PMID 16341018 DOI: 10.1038/nature04195  1
2005 Johnson RJ, Christodoulou J, Dumoulin M, Caddy GL, Alcocer MJ, Murtagh GJ, Kumita JR, Larsson G, Robinson CV, Archer DB, Luisi B, Dobson CM. Rationalising lysozyme amyloidosis: insights from the structure and solution dynamics of T70N lysozyme. Journal of Molecular Biology. 352: 823-36. PMID 16126226 DOI: 10.1016/j.jmb.2005.07.040  1
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  1
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  1
2005 Parrini C, Taddei N, Ramazzotti M, Degl'Innocenti D, Ramponi G, Dobson CM, Chiti F. Glycine residues appear to be evolutionarily conserved for their ability to inhibit aggregation Structure. 13: 1143-1151. PMID 16084386 DOI: 10.1016/j.str.2005.04.022  1
2005 Carulla N, Caddy GL, Hall DR, Zurdo J, Gairí M, Feliz M, Giralt E, Robinson CV, Dobson CM. Molecular recycling within amyloid fibrils. Nature. 436: 554-8. PMID 16049488 DOI: 10.1038/nature03986  0.48
2005 Dobson CM. Structural biology: Prying into prions Nature. 435: 747-749. PMID 15944684 DOI: 10.1038/435747a  1
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  1
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  1
2005 Dumoulin M, Canet D, Last AM, Pardon E, Archer DB, Muyldermans S, Wyns L, Matagne A, Robinson CV, Redfield C, Dobson CM. Reduced global cooperativity is a common feature underlying the amyloidogenicity of pathogenic lysozyme mutations. Journal of Molecular Biology. 346: 773-88. PMID 15713462 DOI: 10.1016/j.jmb.2004.11.020  1
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  0.44
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  0.64
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  0.44
2004 Dobson CM. Chemical space and biology Nature. 432: 824-828. PMID 15602547 DOI: 10.1038/nature03192  1
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  1
2004 Dobson CM. Experimental investigation of protein folding and misfolding Methods. 34: 4-14. PMID 15283911 DOI: 10.1016/j.ymeth.2004.03.002  1
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  1
2004 Christodoulou J, Larsson G, Fucini P, Connell SR, Pertinhez TA, Hanson CL, Redfield C, Nierhaus KH, Robinson CV, Schleucher J, Dobson CM. Heteronuclear NMR investigations of dynamic regions of intact Escherichia coli ribosomes. Proceedings of the National Academy of Sciences of the United States of America. 101: 10949-54. PMID 15263071 DOI: 10.1073/pnas.0400928101  1
2004 Krebs MR, Morozova-Roche LA, Daniel K, Robinson CV, Dobson CM. Observation of sequence specificity in the seeding of protein amyloid fibrils. Protein Science : a Publication of the Protein Society. 13: 1933-8. PMID 15215533 DOI: 10.1110/ps.04707004  0.48
2004 De Felice FG, Vieira MN, Meirelles MN, Morozova-Roche LA, Dobson CM, Ferreira ST. Formation of amyloid aggregates from human lysozyme and its disease-associated variants using hydrostatic pressure. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 18: 1099-101. PMID 15155566 DOI: 10.1096/fj.03-1072fje  1
2004 Ventura S, Zurdo J, Narayanan S, Parreño M, Mangues R, Reif B, Chiti F, Giannoni E, Dobson CM, Aviles FX, Serrano L. Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case. Proceedings of the National Academy of Sciences of the United States of America. 101: 7258-63. PMID 15123800 DOI: 10.1073/pnas.0308249101  0.52
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  0.72
2004 Kammerer RA, Kostrewa D, Zurdo J, Detken A, García-Echeverría C, Green JD, Müller SA, Meier BH, Winkler FK, Dobson CM, Steinmetz MO. Exploring amyloid formation by a de novo design. Proceedings of the National Academy of Sciences of the United States of America. 101: 4435-40. PMID 15070736 DOI: 10.1073/pnas.0306786101  1
2004 Gilbert RJ, Fucini P, Connell S, Fuller SD, Nierhaus KH, Robinson CV, Dobson CM, Stuart DI. Three-dimensional structures of translating ribosomes by Cryo-EM. Molecular Cell. 14: 57-66. PMID 15068803 DOI: 10.1016/s1097-2765(04)00163-7  0.48
2004 Quezada CM, Schulman BA, Froggatt JJ, Dobson CM, Redfield C. Local and global cooperativity in the human alpha-lactalbumin molten globule. Journal of Molecular Biology. 338: 149-58. PMID 15050830 DOI: 10.1016/j.jmb.2004.02.045  1
2004 Dobson CM. Principles of protein folding, misfolding and aggregation Seminars in Cell and Developmental Biology. 15: 3-16. PMID 15036202 DOI: 10.1016/j.semcdb.2003.12.008  1
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  1
2004 Jaroniec CP, MacPhee CE, Bajaj VS, McMahon MT, Dobson CM, Griffin RG. High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy. Proceedings of the National Academy of Sciences of the United States of America. 101: 711-6. PMID 14715898 DOI: 10.1073/pnas.0304849101  1
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  0.4
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  0.76
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  1
2003 Nilsson MR, Dobson CM. Chemical modification of insulin in amyloid fibrils. Protein Science : a Publication of the Protein Society. 12: 2637-41. PMID 14573875 DOI: 10.1110/ps.0360403  1
2003 Laurine E, Grégoire C, Fändrich M, Engemann S, Marchal S, Thion L, Mohr M, Monsarrat B, Michel B, Dobson CM, Wanker E, Érard M, Verdier JM. Lithostathine Quadruple-helical Filaments Form Proteinase K-resistant Deposits in Creutzfeldt-Jakob Disease Journal of Biological Chemistry. 278: 51770-51778. PMID 13129929 DOI: 10.1074/jbc.M306767200  1
2003 Dumoulin M, Last AM, Desmyter A, Decanniere K, Canet D, Larsson G, Spencer A, Archer DB, Sasse J, Muyldermans S, Wyns L, Redfield C, Matagne A, Robinson CV, Dobson CM. A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme. Nature. 424: 783-8. PMID 12917687 DOI: 10.1038/nature01870  1
2003 Canet D, Lyon CE, Scheek RM, Robillard GT, Dobson CM, Hore PJ, van Nuland NA. Rapid formation of non-native contacts during the folding of HPr revealed by real-time photo-CIDNP NMR and stopped-flow fluorescence experiments. Journal of Molecular Biology. 330: 397-407. PMID 12823977 DOI: 10.1016/S0022-2836(03)00507-2  0.76
2003 Dobson CM. Protein folding and disease: A view from the first Horizon Symposium Nature Reviews Drug Discovery. 2: 154-160. PMID 12563307 DOI: 10.1038/nrd1013  1
2003 Nilsson MR, Dobson CM. In vitro characterization of lactoferrin aggregation and amyloid formation. Biochemistry. 42: 375-82. PMID 12525164 DOI: 10.1021/bi0204746  1
2002 Jaroniec CP, MacPhee CE, Astrof NS, Dobson CM, Griffin RG. Molecular conformation of a peptide fragment of transthyretin in an amyloid fibril. Proceedings of the National Academy of Sciences of the United States of America. 99: 16748-53. PMID 12481032 DOI: 10.1073/pnas.252625999  0.76
2002 López De La Paz M, Goldie K, Zurdo J, Lacroix E, Dobson CM, Hoenger A, Serrano L. De novo designed peptide-based amyloid fibrils. Proceedings of the National Academy of Sciences of the United States of America. 99: 16052-7. PMID 12456886 DOI: 10.1073/pnas.252340199  1
2002 Sandilands A, Hutcheson AM, Long HA, Prescott AR, Vrensen G, Löster J, Klopp N, Lutz RB, Graw J, Masaki S, Dobson CM, MacPhee CE, Quinlan RA. Altered aggregation properties of mutant gamma-crystallins cause inherited cataract. The Embo Journal. 21: 6005-14. PMID 12426373 DOI: 10.1093/emboj/cdf609  1
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  1
2002 Dobson CM. Getting out of shape Nature. 418: 729-730. PMID 12181546 DOI: 10.1038/418729a  1
2002 Jiménez JL, Nettleton EJ, Bouchard M, Robinson CV, Dobson CM, Saibil HR. The protofilament structure of insulin amyloid fibrils. Proceedings of the National Academy of Sciences of the United States of America. 99: 9196-201. PMID 12093917 DOI: 10.1073/pnas.142459399  0.48
2002 Canet D, Last AM, Tito P, Sunde M, Spencer A, Archer DB, Redfield C, Robinson CV, Dobson CM. Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme. Nature Structural Biology. 9: 308-15. PMID 11887182 DOI: 10.1038/nsb768  0.48
2001 Fändrich M, Fletcher MA, Dobson CM. Amyloid fibrils from muscle myoglobin. Nature. 410: 165-6. PMID 11242064 DOI: 10.1038/35065514  0.32
2001 Paci E, Smith LJ, Dobson CM, Karplus M. Exploration of partially unfolded states of human alpha-lactalbumin by molecular dynamics simulation. Journal of Molecular Biology. 306: 329-47. PMID 11237603 DOI: 10.1006/jmbi.2000.4337  1
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  1
2001 Bouchard M, Zurdo J, Nettleton EJ, Dobson CM, Robinson CV. Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy. Protein Science : a Publication of the Protein Society. 9: 1960-7. PMID 11106169 DOI: 10.1110/ps.9.10.1960  0.44
2000 Fändrich M, Tito MA, Leroux MR, Rostom AA, Hartl FU, Dobson CM, Robinson CV. Observation of the noncovalent assembly and disassembly pathways of the chaperone complex MtGimC by mass spectrometry Proceedings of the National Academy of Sciences of the United States of America. 97: 14151-14155. PMID 11087821 DOI: 10.1073/pnas.240326597  1
2000 Dobson CM, Ellison GB, Tuck AF, Vaida V. Atmospheric aerosols as prebiotic chemical reactors. Proceedings of the National Academy of Sciences of the United States of America. 97: 11864-8. PMID 11035775 DOI: 10.1073/pnas.200366897  0.76
2000 Nettleton EJ, Tito P, Sunde M, Bouchard M, Dobson CM, Robinson CV. Characterization of the oligomeric states of insulin in self-assembly and amyloid fibril formation by mass spectrometry. Biophysical Journal. 79: 1053-65. PMID 10920035 DOI: 10.1016/S0006-3495(00)76359-4  0.36
2000 Dinner AR, Sali A, Smith LJ, Dobson CM, Karplus M. Understanding protein folding via free-energy surfaces from theory and experiment. Trends in Biochemical Sciences. 25: 331-9. PMID 10871884 DOI: 10.1016/S0968-0004(00)01610-8  0.64
2000 Morgan CJ, Wilkins DK, Smith LJ, Kawata Y, Dobson CM. A compact monomeric intermediate identified by NMR in the denaturation of dimeric triose phosphate isomerase Journal of Molecular Biology. 300: 11-16. PMID 10864494 DOI: 10.1006/jmbi.2000.3834  1
2000 Rostom AA, Fucini P, Benjamin DR, Juenemann R, Nierhaus KH, Hartl FU, Dobson CM, Robinson CV. Detection and selective dissociation of intact ribosomes in a mass spectrometer Proceedings of the National Academy of Sciences of the United States of America. 97: 5185-5190. PMID 10805779 DOI: 10.1073/pnas.97.10.5185  1
2000 Penkett CJ, Dobson CM, Smith LJ, Bright JR, Pickford AR, Campbell ID, Potts JR. Identification of residues involved in the interaction of Staphylococcus aureus fibronectin-binding protein with the 4F15F1 module pair of human fibronectin using heteronuclear NMR spectroscopy Biochemistry. 39: 2887-2893. PMID 10715108 DOI: 10.1021/bi992267k  1
1999 Leroux MR, Fändrich M, Klunker D, Siegers K, Lupas AN, Brown JR, Schiebel E, Dobson CM, Hartl FU. MtGimC, a novel archaeal chaperone related to the eukaryotic chaperonin cofactor GimC/prefoldin. The Embo Journal. 18: 6730-43. PMID 10581246 DOI: 10.1093/emboj/18.23.6730  1
1999 Chiti F, Taddei N, White PM, Bucciantini M, Magherini F, Stefani M, Dobson CM. Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nature Structural Biology. 6: 1005-9. PMID 10542090 DOI: 10.1038/14890  0.88
1999 Redfield C, Schulman BA, Milhollen MA, Kim PS, Dobson CM. α-Lactalbumin forms a compact molten globule in the absence of disulfide bonds Nature Structural Biology. 6: 948-952. PMID 10504730 DOI: 10.1038/13318  0.72
1999 Dobson CM. Protein misfolding, evolution and disease Trends in Biochemical Sciences. 24: 329-332. PMID 10470028 DOI: 10.1016/S0968-0004(99)01445-0  1
1999 Vis H, Dobson CM, Robinson CV. Selective association of protein molecules followed by mass spectrometry. Protein Science : a Publication of the Protein Society. 8: 1368-70. PMID 10386888 DOI: 10.1110/ps.8.6.1368  0.32
1999 Forge V, Wijesinha RT, Balbach J, Brew K, Robinson CV, Redfield C, Dobson CM. Rapid collapse and slow structural reorganisation during the refolding of bovine α-lactalbumin Journal of Molecular Biology. 288: 673-688. PMID 10329172 DOI: 10.1006/jmbi.1999.2687  1
1999 Dobson CM, Karplus M. The fundamentals of protein folding: bringing together theory and experiment. Current Opinion in Structural Biology. 9: 92-101. PMID 10047588 DOI: 10.1016/S0959-440X(99)80012-8  1
1999 Boyd J, Dobson CM, Morar AS, Williams RJP, Pielak GJ. 1H and 15N hyperfine shifts of cytochrome c [15] Journal of the American Chemical Society. 121: 9247-9248. DOI: 10.1021/ja9920361  1
1998 Dobson CM, Šali A, Karplus M. Protein Folding: A Perspective from Theory and Experiment. Angewandte Chemie (International Ed. in English). 37: 868-893. PMID 29711488 DOI: 10.1002/(SICI)1521-3773(19980420)37:7<868::AID-ANIE868>3.0.CO;2-H  1
1998 Smith LJ, Mark AE, Dobson CM, Van Gunsteren WF. Molecular dynamics simulations of peptide fragments from hen lysozyme: Insight into non-native protein conformations Journal of Molecular Biology. 280: 703-719. PMID 9677298 DOI: 10.1006/jmbi.1998.1892  0.88
1998 Morgan CJ, Miranker A, Dobson CM. Characterization of collapsed states in the early stages of the refolding of hen lysozyme Biochemistry. 37: 8473-8480. PMID 9622499 DOI: 10.1021/bi9731504  1
1998 Guijarro JI, Morton CJ, Plaxco KW, Campbell ID, Dobson CM. Folding kinetics of the SH3 domain of PI3 kinase by real-time NMR combined with optical spectroscopy. Journal of Molecular Biology. 276: 657-67. PMID 9551103 DOI: 10.1006/jmbi.1997.1553  0.88
1998 Plaxco KW, Guijarro JI, Morton CJ, Pitkeathly M, Campbell ID, Dobson CM. The folding kinetics and thermodynamics of the Fyn-SH3 domain. Biochemistry. 37: 2529-37. PMID 9485402 DOI: 10.1021/bi972075u  1
1998 Van Nuland NA, Meijberg W, Warner J, Forge V, Scheek RM, Robillard GT, Dobson CM. Slow cooperative folding of a small globular protein HPr. Biochemistry. 37: 622-37. PMID 9425085 DOI: 10.1021/bi9717946  1
1997 Plaxco KW, Morton CJ, Grimshaw SB, Jones JA, Pitkeathly M, Campbell ID, Dobson CM. The effects of guanidine hydrochloride on the 'random coil' conformations and NMR chemical shifts of the peptide series GGXGG. Journal of Biomolecular Nmr. 10: 221-30. PMID 20700831 DOI: 10.1023/A:1018340217891  0.88
1997 Hubbard JAM, Raleigh DP, Bonnerjea JR, Dobson CM. Identification of the epitopes of calcitonin gene-related peptide (CGRP) for two anti-CGRP monoclonal antibodies by 2D NMR Protein Science. 6: 1945-1952. PMID 9300494 DOI: 10.1002/pro.5560060915  0.88
1997 Schulman BA, Kim PS, Dobson CM, Redfield C. A residue-specific NMR view of the non-cooperative unfolding of a molten globule Nature Structural Biology. 4: 630-634. PMID 9253412 DOI: 10.1038/nsb0897-630  0.88
1997 Plaxco KW, Spitzfaden C, Campbell ID, Dobson CM. A comparison of the folding kinetics and thermodynamics of two homologous fibronectin type III modules. Journal of Molecular Biology. 270: 763-70. PMID 9245603 DOI: 10.1006/jmbi.1997.1148  1
1997 Balbach J, Forge V, Lau WS, Jones JA, van Nuland NA, Dobson CM. Detection of residue contacts in a protein folding intermediate. Proceedings of the National Academy of Sciences of the United States of America. 94: 7182-5. PMID 9207065 DOI: 10.1073/pnas.94.14.7182  1
1997 Chung EW, Nettleton EJ, Morgan CJ, Gross M, Miranker A, Radford SE, Dobson CM, Robinson CV. Hydrogen exchange properties of proteins in native and denatured states monitored by mass spectrometry and NMR. Protein Science : a Publication of the Protein Society. 6: 1316-24. PMID 9194192 DOI: 10.1002/pro.5560060620  0.4
1997 Morozova-Roche LA, Arico-Muendel CC, Haynie DT, Emelyanenko VI, Van Dael H, Dobson CM. Structural characterisation and comparison of the native and A-states of equine lysozyme Journal of Molecular Biology. 268: 903-921. PMID 9180380 DOI: 10.1006/jmbi.1997.0996  1
1997 Booth DR, Sunde M, Bellotti V, Robinson CV, Hutchinson WL, Fraser PE, Hawkins PN, Dobson CM, Radford SE, Blake CC, Pepys MB. Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. Nature. 385: 787-93. PMID 9039909 DOI: 10.1038/385787a0  0.88
1996 Plaxco KW, Dobson CM. Time-resolved biophysical methods in the study of protein folding. Current Opinion in Structural Biology. 6: 630-6. PMID 8913685 DOI: 10.1016/S0959-440X(96)80029-7  1
1996 Balbach J, Forge V, Lau WS, van Nuland NA, Brew K, Dobson CM. Protein folding monitored at individual residues during a two-dimensional NMR experiment. Science (New York, N.Y.). 274: 1161-3. PMID 8895458 DOI: 10.1126/science.274.5290.1161  0.88
1996 Plaxco KW, Spitzfaden C, Campbell ID, Dobson CM. Rapid refolding of a proline-rich all-beta-sheet fibronectin type III module. Proceedings of the National Academy of Sciences of the United States of America. 93: 10703-6. PMID 8855243 DOI: 10.1073/pnas.93.20.10703  0.88
1996 Miranker AD, Dobson CM. Collapse and cooperativity in protein folding. Current Opinion in Structural Biology. 6: 31-42. PMID 8696971 DOI: 10.1016/S0959-440X(96)80092-3  1
1996 Smith LJ, Bolin KA, Schwalbe H, MacArthur MW, Thornton JM, Dobson CM. Analysis of main chain torsion angles in proteins: prediction of NMR coupling constants for native and random coil conformations. Journal of Molecular Biology. 255: 494-506. PMID 8568893 DOI: 10.1006/jmbi.1996.0041  0.88
1996 Miranker A, Robinson CV, Radford SE, Dobson CM. Investigation of protein folding by mass spectrometry. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 10: 93-101. PMID 8566553 DOI: 10.1096/fasebj.10.1.8566553  0.32
1996 Robinson CV, Chung EW, Kragelund BB, Knudsen J, Aplin RT, Poulsen FM, Dobson CM. Probing the nature of noncovalent interactions by mass spectrometry. A study of protein-CoA ligand binding and assembly Journal of the American Chemical Society. 118: 8646-8653. DOI: 10.1021/ja960211x  1
1995 Kragelund BB, Robinson CV, Knudsen J, Dobson CM, Poulsen FM. Folding of a four-helix bundle: Studies of acyl-coenzyme A binding protein Biochemistry. 34: 7217-7224. PMID 7766632 DOI: 10.1021/bi00021a037  1
1995 Dobson CM. Finding the right fold Nature Structural Biology. 2: 513-517. PMID 7664116 DOI: 10.1038/nsb0795-513  0.88
1995 Smith LJ, Mark AE, Dobson CM, Van Gunsteren WF. Comparison of MD simulations and NMR experiments for hen lysozyme. Analysis of local fluctuations, cooperative motions, and global changes Biochemistry. 34: 10918-10931. PMID 7662673 DOI: 10.1021/bi00034a026  1
1995 Yang JJ, Buck M, Pitkeathly M, Kotik M, Haynie DT, Dobson CM, Radford SE. Conformational properties of four peptides spanning the sequence of hen lysozyme Journal of Molecular Biology. 252: 483-491. PMID 7563067 DOI: 10.1006/jmbi.1995.0513  1
1995 Morozova LA, Haynie DT, Arico-Muendel C, Arico-Muendelu C, Van Dael H, Dobson CM. Structural basis of the stability of a lysozyme molten globule Nature Structural Biology. 2: 871-875. PMID 7552711 DOI: 10.1038/nsb1095-871  1
1995 Balbach J, Forge V, van Nuland NA, Winder SL, Hore PJ, Dobson CM. Following protein folding in real time using NMR spectroscopy. Nature Structural Biology. 2: 865-70. PMID 7552710 DOI: 10.1038/nsb1095-865  0.88
1995 Schulman BA, Redfield C, Peng Zy, Dobson CM, Kim PS. Different Subdomains are Most Protected From Hydrogen Exchange in the Molten Globule and Native States of Human α-Lactalbumin Journal of Molecular Biology. 253: 651-657. PMID 7473740 DOI: 10.1006/jmbi.1995.0579  1
1994 Lumb KJ, Cheetham JC, Dobson CM. 1H nuclear magnetic resonance studies of hen lysozyme-N-acetylglucosamine oligosaccharide complexes in solution. Application of chemical shifts for the comparison of conformational changes in solution and in the crystal. Journal of Molecular Biology. 235: 1072-87. PMID 8289309 DOI: 10.1006/jmbi.1994.1058  0.84
1994 Alexandrescu AT, Ng YL, Dobson CM. Characterization of a trifluoroethanol-induced partially folded state of alpha-lactalbumin. Journal of Molecular Biology. 235: 587-99. PMID 8289283 DOI: 10.1006/jmbi.1994.1015  1
1994 Itzhaki LS, Evans PA, Dobson CM, Radford SE. Tertiary interactions in the folding pathway of hen lysozyme: Kinetic studies using fluorescent probes Biochemistry. 33: 5212-5220. PMID 8172895 DOI: 10.1021/bi00183a026  0.88
1994 Dobson CM, Evans PA, Radford SE. Understanding how proteins fold: the lysozyme story so far Trends in Biochemical Sciences. 19: 31-37. PMID 8140619 DOI: 10.1016/0968-0004(94)90171-6  0.88
1994 Li X, Bokman AM, Llinás M, Smith RAG, Dobson CM. Solution structure of the kringle domain from urokinase-type plasminogen activator Journal of Molecular Biology. 235: 1548-1559. PMID 8107091 DOI: 10.1006/jmbi.1994.1106  1
1994 Smith LJ, Alexandrescu AT, Pitkeathly M, Dobson CM. Solution structure of a peptide fragment of human alpha-lactalbumin in trifluoroethanol: a model for local structure in the molten globule. Structure (London, England : 1993). 2: 703-12. PMID 7994570 DOI: 10.1016/S0969-2126(00)00071-X  1
1994 Hadfield AT, Harvey DJ, Archer DB, MacKenzie DA, Jeenes DJ, Radford SE, Lowe G, Dobson CM, Johnson LN. Crystal structure of the mutant D52S hen egg white lysozyme with an oligosaccharide product Journal of Molecular Biology. 243: 856-872. PMID 7966306 DOI: 10.1006/jmbi.1994.1688  1
1994 Dobson CM. Protein Folding: Solid evidence for molten globules Current Biology. 4: 636-640. PMID 7953543 DOI: 10.1016/S0960-9822(00)00141-X  0.76
1994 Smith LJ, Redfield C, Smith RA, Dobson CM, Clore GM, Gronenborn AM, Walter MR, Naganbushan TL, Wlodawer A. Comparison of four independently determined structures of human recombinant interleukin-4. Nature Structural Biology. 1: 301-10. PMID 7664036 DOI: 10.1038/nsb0594-301  0.36
1993 Alexandrescu AT, Evans PA, Pitkeathly M, Baum J, Dobson CM. Structure and dynamics of the acid-denatured molten globule state of alpha-lactalbumin: a two-dimensional NMR study. Biochemistry. 32: 1707-18. PMID 8439536 DOI: 10.1021/bi00058a003  1
1993 O'Connell JP, Kelly SM, Raleigh DP, Hubbard JA, Price NC, Dobson CM, Smith BJ. On the role of the C-terminus of alpha-calcitonin-gene-related peptide (alpha CGRP). The structure of des-phenylalaninamide37-alpha CGRP and its interaction with the CGRP receptor. The Biochemical Journal. 291: 205-10. PMID 8385932 DOI: 10.1042/bj2910205  0.72
1993 Dobson CM. Flexible friends Current Biology. 3: 530-532. DOI: 10.1016/0960-9822(93)90049-T  1
1993 Dobson CM. Folding and binding Current Opinion in Structural Biology. 3: 57-59. DOI: 10.1016/0959-440X(93)90202-V  1
1992 Lumb KJ, Aplin RT, Radford SE, Archer DB, Jeenes DJ, Lambert N, MacKenzie DA, Dobson CM, Lowe G. A study of D52S hen lysozyme-GlcNAc oligosaccharide complexes by NMR spectroscopy and electrospray mass spectrometry. Febs Letters. 296: 153-7. PMID 1733771 DOI: 10.1016/0014-5793(92)80368-Q  1
1992 Radford SE, Dobson CM, Evans PA. The folding of hen lysozyme involves partially structured intermediates and multiple pathways Nature. 358: 302-307. PMID 1641003 DOI: 10.1038/358302a0  0.76
1992 Cooper A, Eyles SJ, Radford SE, Dobson CM. Thermodynamic consequences of the removal of a disulphide bridge from hen lysozyme. Journal of Molecular Biology. 225: 939-43. PMID 1613799 DOI: 10.1016/0022-2836(92)90094-Z  0.32
1992 Sutcliffe MJ, Dobson CM, Oswald RE. Solution structure of neuronal bungarotoxin determined by two-dimensional NMR spectroscopy: Calculation of tertiary structure using systematic homologous model building, dynamical simulated annealing, and restrained molecular dynamics Biochemistry®. 31: 2962-2970. PMID 1550821 DOI: 10.1021/bi00126a017  1
1992 Lumb KJ, Dobson CM. 1H nuclear magnetic resonance studies of the interaction of urea with hen lysozyme. Origins of the conformational change induced in hen lysozyme by N-acetylglucosamine oligosaccharides Journal of Molecular Biology. 227: 9-14. PMID 1522604 DOI: 10.1016/0022-2836(92)90677-C  1
1992 Alexandrescu AT, Broadhurst RW, Wormald C, Chyan CL, Baum J, Dobson CM. 1H-NMR assignments and local environments of aromatic residues in bovine, human and guinea pig variants of alpha-lactalbumin. European Journal of Biochemistry / Febs. 210: 699-709. PMID 1483454 DOI: 10.1111/j.1432-1033.1992.tb17471.x  1
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