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Structure of Hsp90–Hsp70–Hop–GR reveals the Hsp90 client-loading mechanism

Structure of Hsp90–Hsp70–Hop–GR reveals the Hsp90 client-loading mechanism

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_9179170

Structure of Hsp90–Hsp70–Hop–GR reveals the Hsp90 client-loading mechanism

About this item

Full title

Structure of Hsp90–Hsp70–Hop–GR reveals the Hsp90 client-loading mechanism

Publisher

London: Nature Publishing Group UK

Journal title

Nature (London), 2022-01, Vol.601 (7893), p.460-464

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Maintaining a healthy proteome is fundamental for the survival of all organisms
1
. Integral to this are Hsp90 and Hsp70, molecular chaperones that together facilitate the folding, remodelling and maturation of the many ‘client proteins’ of Hsp90
2
. The glucocorticoid receptor (GR) is a model client protein that is strictly dependent o...

Alternative Titles

Full title

Structure of Hsp90–Hsp70–Hop–GR reveals the Hsp90 client-loading mechanism

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_9179170

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_9179170

Other Identifiers

ISSN

0028-0836

E-ISSN

1476-4687

DOI

10.1038/s41586-021-04252-1

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