Molecular chaperone ability to inhibit amyloid-derived neurotoxicity, but not amorphous protein aggr...
Molecular chaperone ability to inhibit amyloid-derived neurotoxicity, but not amorphous protein aggregation, depends on a conserved pH-sensitive Asp residue
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Publisher
Cold Spring Harbor: Cold Spring Harbor Laboratory Press
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Language
English
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Cold Spring Harbor: Cold Spring Harbor Laboratory Press
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Contents
Proteins can self-assemble into amyloid fibrils or amorphous aggregates and thereby cause disease. Molecular chaperones can prevent both these types of protein aggregation, but the respective mechanisms are not fully understood. The BRICHOS domain constitutes a disease-associated small heat shock protein-like chaperone family, with activities again...
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Full title
Molecular chaperone ability to inhibit amyloid-derived neurotoxicity, but not amorphous protein aggregation, depends on a conserved pH-sensitive Asp residue
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TN_cdi_proquest_journals_2605427464
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_2605427464
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E-ISSN
2692-8205
DOI
10.1101/2021.12.01.470723
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https://www.proquest.com/docview/2605427464?pq-origsite=primo&accountid=13902
