Mark R. Wilson

Research.com Recognitions

• 2019 - E. F. Lindquist Award, American Educational Research Association
• 2008 - Fellow of the American Educational Research Association

Overview

Best Publications

• Clusterin Has Chaperone-like Activity Similar to That of Small Heat Shock Proteins

  David T. Humphreys;John A. Carver;Simon B. Easterbrook-Smith;Mark R. Wilson

  557
  Citations

• Clusterin is a secreted mammalian chaperone.

  Mark R Wilson;Simon B Easterbrook-Smith

  466
  Citations

• ANS Binding Reveals Common Features of Cytotoxic Amyloid Species

  Benedetta Bolognesi;Janet R. Kumita;Teresa P. Barros;Elin K. Esbjorner

  426
  Citations

• The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures

  Justin J Yerbury;Stephen Poon;Sarah Meehan;Brianna Thompson

  350
  Citations

• Clusterin is an ATP-independent chaperone with very broad substrate specificity that stabilizes stressed proteins in a folding-competent state.

  Stephen Poon;Simon B. Easterbrook-Smith;Mark S. Rybchyn;John A. Carver

  323
  Citations

• The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β 1−40 peptide

  Priyanka Narayan;Angel Orte;Angel Orte;Richard W Clarke;Benedetta Bolognesi

  320
  Citations

• Comparison of virulence gene profiles of Escherichia coli strains isolated from healthy and diarrheic swine.

  Toni A. Chapman;Xi-Yang Wu;Xi-Yang Wu;Idris Barchia;Karl A. Bettelheim

  318
  Citations

• Amyloid fibril formation by bovine milk kappa-casein and its inhibition by the molecular chaperones alpha(s-) and beta-casein

  David C Thorn;Sarah Meehan;Margaret Sunde;Agata Rekas

  286
  Citations

• Heat Shock Protein 70 Inhibits α-Synuclein Fibril Formation via Preferential Binding to Prefibrillar Species

  Matthew M. Dedmon;John Christodoulou;Mark R. Wilson;Christopher M. Dobson

  279
  Citations

• Poly(2-alkylacrylic acid) polymers deliver molecules to the cytosol by pH-sensitive disruption of endosomal vesicles.

  Rachel A Jones;Charles Y Cheung;Fiona E Black;Jasmine K Zia

  242
  Citations

• Small heat-shock proteins and clusterin: intra- and extracellular molecular chaperones with a common mechanism of action and function?

  John A. Carver;Agata Rekas;David C. Thorn;Mark R. Wilson

  235
  Citations

• Walking the tightrope: proteostasis and neurodegenerative disease.

  Justin J. Yerbury;Justin J. Yerbury;Lezanne Ooi;Lezanne Ooi;Andrew Dillin;Andrew Dillin;Darren N. Saunders;Darren N. Saunders

  227
  Citations

• Potential roles of abundant extracellular chaperones in the control of amyloid formation and toxicity

  Mark R. Wilson;Justin J. Yerbury;Stephen Poon

  186
  Citations

• Extracellular chaperones and proteostasis

  Amy R. Wyatt;Justin J. Yerbury;Heath Ecroyd;Mark R. Wilson

  175
  Citations

• Quality control of protein folding in extracellular space.

  Justin J Yerbury;Elise M Stewart;Amy R Wyatt;Mark R Wilson

  168
  Citations

• Stress-induced retrotranslocation of clusterin/ApoJ into the cytosol.

  Philippe Nizard;Susanne Tetley;Yves Le Dréan;Tanguy Watrin

  166
  Citations

• Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers

  Benedetta Mannini;Roberta Cascella;Mariagioia Zampagni;Maria van Waarde-Verhagen

  163
  Citations

• Clusterin is an extracellular chaperone that specifically interacts with slowly aggregating proteins on their off-folding pathway

  Stephen Poon;Teresa M Treweek;Mark R Wilson;Simon B Easterbrook-Smith

  161
  Citations

• are the major source of host-protective regulatory IL-10 during intracellular protozoan infection

  Dragana Jankovic;Marika C. Kullberg;Carl G. Feng;Romina S. Goldszmid

  51
  Citations

• The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-beta 1-40 peptide

  Priyanka Narayan;Angel Orte;Richard W Clarke;Benedetta Bolognesi

  2
  Citations