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Protein rescue from aggregates by powerful molecular chaperone machines

Protein rescue from aggregates by powerful molecular chaperone machines

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_1436566479

Protein rescue from aggregates by powerful molecular chaperone machines

About this item

Full title

Protein rescue from aggregates by powerful molecular chaperone machines

Publisher

London: Nature Publishing Group UK

Journal title

Nature reviews. Molecular cell biology, 2013-10, Vol.14 (10), p.617-629

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Key Points
When cells are exposed to stresses, proteins may misfold and aggregate. Molecular chaperones function in a myriad of cellular activities, including protein folding, remodelling and, in the case of yeast heat shock protein 104 (Hsp104) and bacterial ClpB, in the disaggregation of aggregated proteins.
The oligomeric architecture of H...

Alternative Titles

Full title

Protein rescue from aggregates by powerful molecular chaperone machines

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_miscellaneous_1436566479

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_1436566479

Other Identifiers

ISSN

1471-0072

E-ISSN

1471-0080

DOI

10.1038/nrm3660

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