about
Clusterin is an ATP-independent chaperone with very broad substrate specificity that stabilizes stressed proteins in a folding-competent stateProtease-activated alpha-2-macroglobulin can inhibit amyloid formation via two distinct mechanismsThe extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptideSingle molecule characterization of the interactions between amyloid-β peptides and the membranes of hippocampal cells.Hypochlorite-induced structural modifications enhance the chaperone activity of human α2-macroglobulin.Spinal motor neuron protein supersaturation patterns are associated with inclusion body formation in ALS.Quality control of protein folding in extracellular space.Comparison of virulence gene profiles of Escherichia coli strains isolated from healthy and diarrheic swine.Basal superoxide as a sex-specific immune constraint.Oxidant trade-offs in immunity: an experimental test in a lizardSmall heat-shock proteins and clusterin: intra- and extracellular molecular chaperones with a common mechanism of action and function?SerpinB2 (PAI-2) Modulates Proteostasis via Binding Misfolded Proteins and Promotion of Cytoprotective Inclusion Formation.Alpha-2-Macroglobulin Is Acutely Sensitive to Freezing and Lyophilization: Implications for Structural and Functional Studies.Clusterin Seals the Ocular Surface Barrier in Mouse Dry Eye.Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers.SOD1 protein aggregates stimulate macropinocytosis in neurons to facilitate their propagation.Acute phase proteins are major clients for the chaperone action of α₂-macroglobulin in human plasmaClusterin interacts with Paclitaxel and confer Paclitaxel resistance in ovarian cancerPotential roles of abundant extracellular chaperones in the control of amyloid formation and toxicity.Chapter 6: The chaperone action of Clusterin and its putative role in quality control of extracellular protein folding.Rare individual amyloid-β oligomers act on astrocytes to initiate neuronal damage.Extracellular chaperones and proteostasis.Evidence that clusterin has discrete chaperone and ligand binding sites.A significant component of ageing (DNA damage) is reflected in fading breeding colors: an experimental test using innate antioxidant mimetics in painted dragon lizards.Sex-specific SOD levels and DNA damage in painted dragon lizards (Ctenophorus pictus).Net superoxide levels: steeper increase with activity in cooler female and hotter male lizards.Carotenoid intake does not mediate a relationship between reactive oxygen species and bright colouration: experimental test in a lizard.Walking the tightrope: proteostasis and neurodegenerative disease.Effect of molecular chaperones on aberrant protein oligomers in vitro: super-versus sub-stoichiometric chaperone concentrations.Expression and purification of chaperone-active recombinant clusterin.Transcriptome profiling of a TGF-beta-induced epithelial-to-mesenchymal transition reveals extracellular clusterin as a target for therapeutic antibodies.Opacity factor activity and epithelial cell binding by the serum opacity factor protein of Streptococcus pyogenes are functionally discrete.Stress-induced retrotranslocation of clusterin/ApoJ into the cytosol.Effects of glycosylation on the structure and function of the extracellular chaperone clusterin.Poly(2-alkylacrylic acid) polymers deliver molecules to the cytosol by pH-sensitive disruption of endosomal vesicles.Modes of L929 cell death induced by TNF-alpha and other cytotoxic agents.A reexamination of the role of clusterin as a complement regulator.The heat shock response is modulated by and interferes with toxic effects of scrapie prion protein and amyloid β.Structural characterization of clusterin-chaperone client protein complexes.ANS binding reveals common features of cytotoxic amyloid species.
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P50
description
Australian biologist
@en
Australian biologist
@en-ca
Australian biologist
@en-gb
biólogo australiano
@es
wetenschapper
@nl
عالم أحياء أسترالي
@ar
name
Mark R. Wilson
@ast
Mark R. Wilson
@en
Mark R. Wilson
@es
Mark R. Wilson
@nl
Mark R. Wilson
@sl
type
label
Mark R. Wilson
@ast
Mark R. Wilson
@en
Mark R. Wilson
@es
Mark R. Wilson
@nl
Mark R. Wilson
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altLabel
Mark R Wilson
@en
Mark Wilson
@en
prefLabel
Mark R. Wilson
@ast
Mark R. Wilson
@en
Mark R. Wilson
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Mark R. Wilson
@nl
Mark R. Wilson
@sl
P1053
B-3254-2018
P106
P1153
55547134962
P21
P2798
P31
P496
0000-0002-9551-7445