A P39R mutation at the N-terminal domain of human αB-crystallin regulates its oligomeric state and chaperone-like activity
Author:
Funder
Japan Science and Technology Agency
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference23 articles.
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3. A novel mutation (F71L) in alphaA-crystallin with defective chaperone-like function associated with age-related cataract;Bhagyalaxmi;Biochim. Biophys. Acta,2009
4. Simultaneous racemization and isomerization at specific aspartic acid residues in alpha B-crystallin from the aged human lens;Fujii;Biochim. Biophys. Acta,1994
5. Simultaneous stereoinversion and isomerization at specific aspartic acid residues in alpha A-crystallin from human lens;Fujii;J. Biochem.,1994
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