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Molecular chaperones: guardians of the proteome in normal and disease states [version 1; peer review...

Molecular chaperones: guardians of the proteome in normal and disease states [version 1; peer review...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_ed0c75ccb25842e9a5dd573b16da20b8

Molecular chaperones: guardians of the proteome in normal and disease states [version 1; peer review: 2 approved]

About this item

Full title

Molecular chaperones: guardians of the proteome in normal and disease states [version 1; peer review: 2 approved]

Publisher

England: Faculty of 1000 Ltd

Journal title

F1000 research, 2015, Vol.4, p.1448

Language

English

Formats

Publication information

Publisher

England: Faculty of 1000 Ltd

More information

Scope and Contents

Contents

Proteins must adopt a defined three-dimensional structure in order to gain functional activity, or must they? An ever-increasing number of intrinsically disordered proteins and amyloid-forming polypeptides challenge this dogma. While molecular chaperones and proteases are traditionally associated with protein quality control inside the cell, it is...

Alternative Titles

Full title

Molecular chaperones: guardians of the proteome in normal and disease states [version 1; peer review: 2 approved]

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_ed0c75ccb25842e9a5dd573b16da20b8

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_ed0c75ccb25842e9a5dd573b16da20b8

Other Identifiers

ISSN

2046-1402

E-ISSN

2046-1402

DOI

10.12688/f1000research.7214.1

How to access this item