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Small heat shock protein activity is regulated by variable oligomeric substructure

Abstract:

The alpha-crystallins are members of the small heat shock protein family of molecular chaperones that have evolved to minimize intracellular protein aggregation; however, they are also implicated in a number of protein deposition diseases. In this study, we employed novel mass spectrometry techniques to investigate the changes in quaternary structure associated with this switch from chaperone to adjuvant of aggregation. We replicated the oligomeric rearrangements observed for post-translation...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's Version

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Publisher copy:
10.1074/jbc.M804729200

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Department:
University College
More by this author
Department:
Exeter College
Publisher:
American Society for Biochemistry and Molecular Biology Publisher's website
Journal:
The Journal of Biological Chemistry Journal website
Volume:
283
Issue:
42
Pages:
28513-28517
Publication date:
2008-10-01
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
Pubs id:
pubs:59317
URN:
uri:8465f1b3-9ee6-4a36-b533-1fa506869364
UUID:
uuid:8465f1b3-9ee6-4a36-b533-1fa506869364
Local pid:
pubs:59317
Language:
English
Keywords:

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