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The binding of the small heat-shock protein αB-crystallin to fibrils of α-synuclein is driven by ent...

The binding of the small heat-shock protein αB-crystallin to fibrils of α-synuclein is driven by ent...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_8463877

The binding of the small heat-shock protein αB-crystallin to fibrils of α-synuclein is driven by entropic forces

About this item

Full title

The binding of the small heat-shock protein αB-crystallin to fibrils of α-synuclein is driven by entropic forces

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2021-09, Vol.118 (38), p.1-8

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

Molecular chaperones are key components of the cellular proteostasis network whose role includes the suppression of the formation and proliferation of pathogenic aggregates associated with neurodegenerative diseases. The molecular principles that allow chaperones to recognize misfolded and aggregated proteins remain, however, incompletely understoo...

Alternative Titles

Full title

The binding of the small heat-shock protein αB-crystallin to fibrils of α-synuclein is driven by entropic forces

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_8463877

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_8463877

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.2108790118

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