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Subunit exchange of polydisperse proteins: mass spectrometry reveals consequences of alphaA-crystallin truncation

Abstract:

The small heat shock protein, alpha-crystallin, plays a key role in maintaining lens transparency by chaperoning structurally compromised proteins. This is of particular importance in the human lens, where proteins are exposed to post-translational modifications over the life-time of an individual. Here, we examine the structural and functional consequences of one particular modification of alphaA-crystallin involving the truncation of 5 C-terminal residues (alphaA(1-168)). Using novel mass s...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1074/jbc.M500135200

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Institution:
University of Oxford
Oxford college:
University College
Role:
Author
More by this author
Institution:
University of Oxford
Oxford college:
Exeter College
Role:
Author
Publisher:
American Society for Biochemistry and Molecular Biology
Journal:
Journal of biological chemistry More from this journal
Volume:
280
Issue:
15
Pages:
14485-14491
Publication date:
2005-04-01
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
Pmid:
15701626
Language:
English
Keywords:
Pubs id:
pubs:59270
UUID:
uuid:a7d3cf68-ed97-4ecb-b46c-fbc91d6258ec
Local pid:
pubs:59270
Source identifiers:
59270
Deposit date:
2017-01-25

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