Mark Wilson
Mark Wilson
Senior Professor of Molecular Bioscience
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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
Clusterin is a secreted mammalian chaperone
MR Wilson, SB Easterbrook-Smith
Trends in biochemical sciences 25 (3), 95-98, 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
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
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
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
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
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
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
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
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
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
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
Quality control of protein folding in extracellular space
JJ Yerbury, EM Stewart, AR Wyatt, MR Wilson
EMBO reports 6 (12), 1131-1136, 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
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
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
Apolipoprotein J (clusterin) induces cholesterol export from macrophage-foam cells: a potential anti-atherogenic function?
IC Gelissen, T Hochgrebe, MR Wilson, SB Easterbrook-Smith, W Jessup, ...
Biochemical Journal 331 (1), 231-237, 1998
Extracellular chaperones and proteostasis
AR Wyatt, JJ Yerbury, H Ecroyd, MR Wilson
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 (23), 3919-3931, 2011
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