| Clusterin has chaperone-like activity similar to that of small heat shock proteins DT Humphreys, JA Carver, SB Easterbrook-Smith, MR Wilson Journal of Biological Chemistry 274 (11), 6875-6881, 1999 | 555 | 1999 |
| Clusterin is a secreted mammalian chaperone MR Wilson, SB Easterbrook-Smith Trends in biochemical sciences 25 (3), 95-98, 2000 | 459 | 2000 |
| ANS binding reveals common features of cytotoxic amyloid species B Bolognesi, JR Kumita, TP Barros, EK Esbjorner, LM Luheshi, ... ACS chemical biology 5 (8), 735-740, 2010 | 431 | 2010 |
| The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures JJ Yerbury, S Poon, S Meehan, B Thompson, JR Kumita, CM Dobson, ... The FASEB Journal 21 (10), 2312-2322, 2007 | 383 | 2007 |
| Comparison of Virulence Gene Profiles of Escherichia coli Strains Isolated from Healthy and Diarrheic Swine TA Chapman, XY Wu, I Barchia, KA Bettelheim, S Driesen, D Trott, ... Applied and Environmental Microbiology 72 (7), 4782-4795, 2006 | 342 | 2006 |
| The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β1−40 peptide P Narayan, A Orte, RW Clarke, B Bolognesi, S Hook, KA Ganzinger, ... Nature structural & molecular biology 19 (1), 79-83, 2012 | 323 | 2012 |
| Clusterin is an ATP− independent chaperone with very broad substrate specificity that stabilizes stressed proteins in a folding-competent state S Poon, SB Easterbrook-Smith, MS Rybchyn, JA Carver, MR Wilson Biochemistry 39 (51), 15953-15960, 2000 | 318 | 2000 |
| Heat shock protein 70 inhibits α-synuclein fibril formation via preferential binding to prefibrillar species MM Dedmon, J Christodoulou, MR Wilson, CM Dobson Journal of Biological Chemistry 280 (15), 14733-14740, 2005 | 310 | 2005 |
| Poly (2-alkylacrylic acid) polymers deliver molecules to the cytosol by pH-sensitive disruption of endosomal vesicles RA Jones, CY Cheung, FE Black, JK Zia, PS Stayton, AS Hoffman, ... Biochemical Journal 372 (1), 65-75, 2003 | 258 | 2003 |
| Walking the tightrope: proteostasis and neurodegenerative disease JJ Yerbury, L Ooi, A Dillin, DN Saunders, DM Hatters, PM Beart, ... Journal of neurochemistry 137 (4), 489-505, 2016 | 241 | 2016 |
| Amyloid fibril formation by bovine milk κ-casein and its inhibition by the molecular chaperones αS-and β-casein DC Thorn, S Meehan, M Sunde, A Rekas, SL Gras, CE MacPhee, ... Biochemistry 44 (51), 17027-17036, 2005 | 238 | 2005 |
| Small heat‐shock proteins and clusterin: intra‐and extracellular molecular chaperones with a common mechanism of action and function? JA Carver, A Rekas, DC Thorn, MR Wilson IUBMB life 55 (12), 661-668, 2003 | 233 | 2003 |
| Extracellular chaperones and proteostasis AR Wyatt, JJ Yerbury, H Ecroyd, MR Wilson Annual review of biochemistry 82 (1), 295-322, 2013 | 197 | 2013 |
| Potential roles of abundant extracellular chaperones in the control of amyloid formation and toxicity MR Wilson, JJ Yerbury, S Poon Molecular BioSystems 4 (1), 42-52, 2008 | 189 | 2008 |
| Quality control of protein folding in extracellular space JJ Yerbury, EM Stewart, AR Wyatt, MR Wilson EMBO reports 6 (12), 1131-1136, 2005 | 169 | 2005 |
| Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers B Mannini, R Cascella, M Zampagni, M van Waarde-Verhagen, S Meehan, ... Proceedings of the National Academy of Sciences 109 (31), 12479-12484, 2012 | 168 | 2012 |
| Clusterin facilitates in vivo clearance of extracellular misfolded proteins AR Wyatt, JJ Yerbury, P Berghofer, I Greguric, A Katsifis, CM Dobson, ... Cellular and Molecular Life Sciences 68, 3919-3931, 2011 | 168 | 2011 |
| Stress‐induced retrotranslocation of clusterin/ApoJ into the cytosol P Nizard, S Tetley, Y Le Dréan, T Watrin, P Le Goff, MR Wilson, D Michel Traffic 8 (5), 554-565, 2007 | 167 | 2007 |
| Clusterin is an extracellular chaperone that specifically interacts with slowly aggregating proteins on their off-folding pathway S Poon, TM Treweek, MR Wilson, SB Easterbrook-Smith, JA Carver FEBS letters 513 (2-3), 259-266, 2002 | 158 | 2002 |
| Secondary nucleation and elongation occur at different sites on Alzheimer’s amyloid-β aggregates T Scheidt, U Łapińska, JR Kumita, DR Whiten, D Klenerman, MR Wilson, ... Science advances 5 (4), eaau3112, 2019 | 156 | 2019 |