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Journal article

R120G alphaB-crystallin promotes the unfolding of reduced alpha-lactalbumin and is inherently unstable.

Abstract:

alpha-Crystallin is the principal lens protein which, in addition to its structural role, also acts as a molecular chaperone, to prevent aggregation and precipitation of other lens proteins. One of its two subunits, alphaB-crystallin, is also expressed in many nonlenticular tissues, and a natural missense mutation, R120G, has been associated with cataract and desmin-related myopathy, a disorder of skeletal muscles [Vicart P, Caron A, Guicheney P, Li Z, Prevost MC, Faure A, Chateau D, Chapon F...

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Publication status:
Published

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Authors


Treweek, TM More by this author
Lindner, RA More by this author
Walker, MJ More by this author
Aquilina, JA More by this author
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Journal:
The FEBS journal
Volume:
272
Issue:
3
Pages:
711-724
Publication date:
2005-02-05
DOI:
EISSN:
1742-4658
ISSN:
1742-464X
URN:
uuid:df815a85-96f4-4a11-8032-7c32bb60088a
Source identifiers:
59361
Local pid:
pubs:59361

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