M R Wilson

Summary

Affiliation: University of Wollongong
Country: Australia

Publications

  1. ncbi request reprint Potential roles of abundant extracellular chaperones in the control of amyloid formation and toxicity
    Mark R Wilson
    School of Biological Sciences, University of Wollongong, Wollongong, NSW, Australia
    Mol Biosyst 4:42-52. 2008
  2. doi request reprint Extracellular chaperones and proteostasis
    Amy R Wyatt
    School of Biological Sciences, University of Wollongong, Wollongong, New South Wales 2522, Australia
    Annu Rev Biochem 82:295-322. 2013
  3. ncbi request reprint Clusterin is a secreted mammalian chaperone
    M R Wilson
    Dept of Biological Sciences, University of Wollongong, Northfields Avenue, Wollongong, NSW Australia 2522
    Trends Biochem Sci 25:95-8. 2000
  4. ncbi request reprint Clusterin has chaperone-like activity similar to that of small heat shock proteins
    D T Humphreys
    Department of Biological Sciences, The University of Wollongong, Northfields Avenue, Wollongong, New South Wales 2522, Australia
    J Biol Chem 274:6875-81. 1999
  5. ncbi request reprint Clusterin is an ATP-independent chaperone with very broad substrate specificity that stabilizes stressed proteins in a folding-competent state
    S Poon
    Department of Biological Sciences, University of Wollongong, Northfields Avenue, Wollongong, NSW 2522, Australia
    Biochemistry 39:15953-60. 2000
  6. ncbi request reprint Therapeutic targets in extracellular protein deposition diseases
    A R Wyatt
    University of Wollongong, NSW, Australia
    Curr Med Chem 16:2855-66. 2009
  7. pmc Extracellular chaperones modulate the effects of Alzheimer's patient cerebrospinal fluid on Abeta(1-42) toxicity and uptake
    Justin J Yerbury
    University of Wollongong, NSW, Australia
    Cell Stress Chaperones 15:115-21. 2010
  8. doi request reprint alpha2-Macroglobulin and haptoglobin suppress amyloid formation by interacting with prefibrillar protein species
    Justin J Yerbury
    School of Biological Sciences, University of Wollongong, Northfields Avenue, Wollongong, New South Wales 2522, Australia
    J Biol Chem 284:4246-54. 2009
  9. pmc Quality control of protein folding in extracellular space
    Justin J Yerbury
    School of Biological Sciences, University of Wollongong, Wollongong, NSW 2522, Australia
    EMBO Rep 6:1131-6. 2005
  10. ncbi request reprint Small heat-shock proteins and clusterin: intra- and extracellular molecular chaperones with a common mechanism of action and function?
    John A Carver
    Department of Chemistry, University of Wollongong, Northfields Avenue, Wollongong, NSW 2522, Australia
    IUBMB Life 55:661-8. 2003

Collaborators

  • Carol V Robinson
  • Justin J Yerbury
  • J A Carver
  • C M Dobson
  • Heath Ecroyd
  • S R Partridge
  • Harry S Courtney
  • Mark J Walker
  • J Andrew Aquilina
  • Teresa M Treweek
  • Adriano Aguzzi
  • Amy R Wyatt
  • Stephen Poon
  • Simon B Easterbrook-Smith
  • Elise M Stewart
  • S Poon
  • A R Wyatt
  • Christine M Gillen
  • Katie French
  • Janet R Kumita
  • Matthew M Dedmon
  • Christoph Huber
  • David C Thorn
  • Rachel A Jones
  • Danny M Hatters
  • Johnathon N Lakins
  • S B Easterbrook-Smith
  • K J Gilmore
  • Manfred Rohde
  • G S Chhatwal
  • Anjuli M Timmer
  • Victor Nizet
  • D T Humphreys
  • Kai Schulze
  • Carlos A Guzman
  • Christine L Hagan
  • Soren Moestrup
  • Christian Jacobsen
  • Danielle Murphy-Durland
  • Mireille Dumoulin
  • Gemma L Caddy
  • Sally L Gras
  • Cait E MacPhee
  • Sarah Meehan
  • Fabio Montrasio
  • Petra Schwarz
  • John Christodoulou
  • Ernst Heinen
  • Harald Seeger
  • Agata Rekas
  • Margaret Sunde
  • Caroline Thielen
  • Yang Xin Fu
  • Gino Miele
  • Maree H Poniris
  • Geoffrey J Howlett
  • Greg J Pankhurst
  • Mark S Rybchyn
  • Martin P R Tenniswood
  • H E Quinn
  • M S Rybchyn
  • B D Wines

Detail Information

Publications31

  1. ncbi request reprint Potential roles of abundant extracellular chaperones in the control of amyloid formation and toxicity
    Mark R Wilson
    School of Biological Sciences, University of Wollongong, Wollongong, NSW, Australia
    Mol Biosyst 4:42-52. 2008
    ..Further advances in understanding of the mechanisms that control extracellular protein folding are likely to identify new strategies for effective disease therapies...
  2. doi request reprint Extracellular chaperones and proteostasis
    Amy R Wyatt
    School of Biological Sciences, University of Wollongong, Wollongong, New South Wales 2522, Australia
    Annu Rev Biochem 82:295-322. 2013
    ....
  3. ncbi request reprint Clusterin is a secreted mammalian chaperone
    M R Wilson
    Dept of Biological Sciences, University of Wollongong, Northfields Avenue, Wollongong, NSW Australia 2522
    Trends Biochem Sci 25:95-8. 2000
  4. ncbi request reprint Clusterin has chaperone-like activity similar to that of small heat shock proteins
    D T Humphreys
    Department of Biological Sciences, The University of Wollongong, Northfields Avenue, Wollongong, New South Wales 2522, Australia
    J Biol Chem 274:6875-81. 1999
    ..0:1.0 or greater), indicating that clusterin is a very efficient chaperone. Our results suggest that clusterin may play a sHSP-like role in cytoprotection...
  5. ncbi request reprint Clusterin is an ATP-independent chaperone with very broad substrate specificity that stabilizes stressed proteins in a folding-competent state
    S Poon
    Department of Biological Sciences, University of Wollongong, Northfields Avenue, Wollongong, NSW 2522, Australia
    Biochemistry 39:15953-60. 2000
    ....
  6. ncbi request reprint Therapeutic targets in extracellular protein deposition diseases
    A R Wyatt
    University of Wollongong, NSW, Australia
    Curr Med Chem 16:2855-66. 2009
    ..Newly identified potential drug targets include direct inhibition of protein aggregation, and manipulation of the expression levels of ECs and their receptors...
  7. pmc Extracellular chaperones modulate the effects of Alzheimer's patient cerebrospinal fluid on Abeta(1-42) toxicity and uptake
    Justin J Yerbury
    University of Wollongong, NSW, Australia
    Cell Stress Chaperones 15:115-21. 2010
    ..These results suggest that extracellular chaperones are an important element of a system of extracellular protein folding quality control that protects against Abeta toxicity and accumulation...
  8. doi request reprint alpha2-Macroglobulin and haptoglobin suppress amyloid formation by interacting with prefibrillar protein species
    Justin J Yerbury
    School of Biological Sciences, University of Wollongong, Northfields Avenue, Wollongong, New South Wales 2522, Australia
    J Biol Chem 284:4246-54. 2009
    ..These findings suggest that both alpha(2)M and Hp are likely to play an important role in controlling the inappropriate aggregation of proteins in the extracellular environment...
  9. pmc Quality control of protein folding in extracellular space
    Justin J Yerbury
    School of Biological Sciences, University of Wollongong, Wollongong, NSW 2522, Australia
    EMBO Rep 6:1131-6. 2005
    ....
  10. ncbi request reprint Small heat-shock proteins and clusterin: intra- and extracellular molecular chaperones with a common mechanism of action and function?
    John A Carver
    Department of Chemistry, University of Wollongong, Northfields Avenue, Wollongong, NSW 2522, Australia
    IUBMB Life 55:661-8. 2003
    ..g., Alzheimer's, Creutzfeldt-Jakob and Parkinson's diseases. The interaction of sHsps and clusterin with fibril-forming species is discussed along with their ability to prevent fibril formation...
  11. ncbi request reprint RHP is antigenically related to factor H and binds to the globular heads of C1q
    S B Easterbrook-Smith
    Department of Biochemistry, University of Sydney, NSW, Australia
    Mol Immunol 29:1203-7. 1992
    ..C1q-specific monoclonal antibody BUS-1, which blocks the binding of C1q to immune complexes, did not block the binding of RHP to C1q. This implies that the binding sites on C1q for IgG and RHP do not overlap...
  12. ncbi request reprint Apoptotic signal transduction: emerging pathways
    M R Wilson
    Department of Biological Sciences, University of Wollongong, NSW, Australia
    Biochem Cell Biol 76:573-82. 1998
    ..g., cytochrome c) from the intermembrane space to the cytosol. This review focuses on recent progress in these areas and discusses integration of this knowledge in our overall understanding of the processes that control apoptosis...
  13. pmc Identification of human plasma proteins as major clients for the extracellular chaperone clusterin
    Amy R Wyatt
    School of Biological Sciences, University of Wollongong, Wollongong, New South Wales 2522, Australia
    J Biol Chem 285:3532-9. 2010
    ..A better understanding of these mechanisms is likely to ultimately lead to the identification of new therapies for extracellular protein deposition disorders...
  14. doi request reprint Protease activation of alpha2-macroglobulin modulates a chaperone-like action with broad specificity
    Katie French
    School of Biological Sciences, University of Wollongong, Northfields Avenue, Wollongong, NSW 2522, Australia
    Biochemistry 47:1176-85. 2008
    ..We propose that alpha2M is a newly discovered and unique member of a small group of abundant extracellular proteins with chaperone properties that patrol extracellular spaces for unfolded/misfolded proteins and facilitate their disposal...
  15. ncbi request reprint The acute phase protein haptoglobin is a mammalian extracellular chaperone with an action similar to clusterin
    Justin J Yerbury
    School of Biological Sciences and the Institute for Biomolecular Science, University of Wollongong, Northfields Avenue, Wollongong, New South Wales 2522, Australia
    Biochemistry 44:10914-25. 2005
    ..Our results raise the possibility that Hp may exert an anti-inflammatory action in vivo by inhibiting the inappropriate self-association of "damaged" (misfolded) extracellular proteins...
  16. pmc Clusterin, a putative complement regulator, binds to the cell surface of Staphylococcus aureus clinical isolates
    S R Partridge
    Institute for Molecular Recognition, University of Wollongong, New South Wales, Australia
    Infect Immun 64:4324-9. 1996
    ..Such receptors may be an important new bacterial virulence determinant for S. aureus, as clusterin has been proposed to have a role in the regulation of complement activity...
  17. ncbi request reprint Mildly acidic pH activates the extracellular molecular chaperone clusterin
    Stephen Poon
    Department of Biological Sciences, University of Wollongong, Northfields Ave, Wollongong, New South Wales 2522, Australia
    J Biol Chem 277:39532-40. 2002
    ..We propose a model in which low pH-induced dissociation of clusterin aggregates increases the abundance of the heterodimeric chaperone-active species, which has greater hydrophobicity exposed to solution...
  18. ncbi request reprint The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures
    Justin J Yerbury
    School of Biological Sciences, University of Wollongong, Wollongong, Australia
    FASEB J 21:2312-22. 2007
    ..These findings suggest that clusterin is an important element in the control of extracellular protein misfolding...
  19. ncbi request reprint Clusterin is an extracellular chaperone that specifically interacts with slowly aggregating proteins on their off-folding pathway
    Stephen Poon
    Department of Chemistry, University of Wollongong, Northfields Avenue, 2522, Wollongong, NSW, Australia
    FEBS Lett 513:259-66. 2002
    ....
  20. ncbi request reprint Apoptosis: unmasking the executioner
    M R Wilson
    Department of Biological Sciences, University of Wollongong, Northfields Avenue, Wollongong, NSW 2522 Australia
    Cell Death Differ 5:646-52. 1998
    ..It is important to note that some critical features of these models are largely based on data acquired from cell-free studies. Further studies with intact cells are urgently needed to test the physiological validity of these models...
  21. ncbi request reprint Pinocytic loading of cytochrome c into intact cells specifically induces caspase-dependent permeabilization of mitochondria: evidence for a cytochrome c feedback loop
    K J Gilmore
    Department of Biological Sciences, University of Wollongong, Northfields Avenue, Wollongong. NWS. 2522. Australia
    Cell Death Differ 8:631-9. 2001
    ....
  22. ncbi request reprint Effects of glycosylation on the structure and function of the extracellular chaperone clusterin
    Elise M Stewart
    School of Biological Sciences and the Institute for Biomolecular Sciences, University of Wollongong, Northfields Avenue, Wollongong 2522, NSW, Australia
    Biochemistry 46:1412-22. 2007
    ..The current results suggest that it may be possible in the future to study the structure and chaperone function of clusterin using recombinant protein (lacking sugars) conveniently bulk-expressed in bacteria...
  23. pmc Structural characterization of clusterin-chaperone client protein complexes
    Amy R Wyatt
    School of Biological Sciences, University of Wollongong, Wollongong, New South Wales 2522, Australia
    J Biol Chem 284:21920-7. 2009
    ..In vivo, soluble complexes like those studied here are likely to serve as vehicles to dispose of otherwise dangerous aggregation-prone misfolded extracellular proteins...
  24. doi request reprint Opacity factor activity and epithelial cell binding by the serum opacity factor protein of Streptococcus pyogenes are functionally discrete
    Christine M Gillen
    School of Biological Sciences, University of Wollongong, New South Wales 2522, Australia
    J Biol Chem 283:6359-66. 2008
    ..We demonstrate that while the N terminus of SOF does not directly mediate intracellular uptake by epithelial cells, this domain enhances epithelial cell uptake mediated by full-length SOF, in comparison to the FnBD alone...
  25. ncbi request reprint pDMAEMA is internalised by endocytosis but does not physically disrupt endosomes
    Rachel A Jones
    Department of Biological Sciences, University of Wollongong, Northfields Avenue, Wollongong, NSW 2522, Australia
    J Control Release 96:379-91. 2004
    ..Further work will be required to establish the molecular mechanism(s) by which pDMAEMA facilitates transfection...
  26. ncbi request reprint Suppression of apolipoprotein C-II amyloid formation by the extracellular chaperone, clusterin
    Danny M Hatters
    Department of Biochemistry and Molecular Biology, The University of Melbourne, Victoria, Australia
    Eur J Biochem 269:2789-94. 2002
    ..We propose a general role for clusterin in suppressing the growth of extracellular amyloid...
  27. ncbi request reprint Evidence that clusterin has discrete chaperone and ligand binding sites
    Johnathon N Lakins
    Institute for Medicine and Engineering, University of Pennsylvania, 1170 Vagelos Research Labs, 3340 Smith Walk, Philadelphia, Pennsylvania 19104 6383, USA
    Biochemistry 41:282-91. 2002
    ..This hypothesis is supported by our demonstration that clusterin has discrete binding sites for LRP-2 and other (potentially toxic) molecules...
  28. ncbi request reprint Heat shock protein 70 inhibits alpha-synuclein fibril formation via preferential binding to prefibrillar species
    Matthew M Dedmon
    Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, United Kingdom
    J Biol Chem 280:14733-40. 2005
    ..This work therefore elucidates a specific role of Hsp70 in the pathogenesis of PD and supports the general concept that chaperone action is a crucial aspect in protecting against the otherwise damaging consequences of protein misfolding...
  29. ncbi request reprint The extracellular chaperone clusterin potently inhibits human lysozyme amyloid formation by interacting with prefibrillar species
    Janet R Kumita
    Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK
    J Mol Biol 369:157-67. 2007
    ....
  30. ncbi request reprint Amyloid fibril formation by bovine milk kappa-casein and its inhibition by the molecular chaperones alphaS- and beta-casein
    David C Thorn
    School of Chemistry and Physics, The University of Adelaide, Adelaide, South Australia 5005, Australia
    Biochemistry 44:17027-36. 2005
    ..Casein proteins may therefore play a preventative role in the development of corpora amylacea, a disorder associated with the accumulation of amyloid deposits in mammary tissue...
  31. ncbi request reprint Lymphotoxin-beta receptor-dependent genes in lymph node and follicular dendritic cell transcriptomes
    Christoph Huber
    Institute of Neuropathology, University Hospital of Zurich, Zurich, Switzerland
    J Immunol 174:5526-36. 2005
    ..Hence, the set of genes presented in this study includes markers emanating from LTbetaR signaling and transcripts relevant to GC and FDC function...