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

Molecular chaperones in protein folding and proteostasis

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The Interaction of αB-Crystallin with Mature α-Synuclein Amyloid Fibrils Inhibits Their Elongation

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Identification of theDrosophilaOrtholog of HSPB8

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A comparison of the biochemical modifications caused by toxic and non-toxic protein oligomers in cells

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A causative link between the structure of aberrant protein oligomers and their toxicity

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Biological and Chemical Approaches to Diseases of Proteostasis Deficiency

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Chaperone proteostasis in Parkinson's disease: stabilization of the Hsp70/α-synuclein complex by Hip

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The role of molecular chaperones in human misfolding diseases

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Protease Activation of α2-Macroglobulin Modulates a Chaperone-like Action with Broad Specificity

(2008) Katie French et al.   BIOCHEMISTRY

Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging

(2008) R. I. Morimoto   GENES & DEVELOPMENT

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

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Vaccination with soluble Aβ oligomers generates toxicity-neutralizing antibodies

(2003) Mary P. Lambert et al.   JOURNAL OF NEUROCHEMISTRY