βB2-crystallin undergoes extensive truncation during aging in human lenses
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference36 articles.
1. Modification of water-insoluble human lens α-crystallin;Lund;Exp. Eye Res.,1996
2. The major in vivo modifications of human water insoluble lens crystallins are disulfide bonds, deamidation, meoxidation oxidation and backbone cleavage;Hanson;Exp. Eye Res.,2000
3. Age-dependent loss of the C-terminal amino acid from α crystallin;Emmons;Exp. Eye Res.,1992
4. Truncation of αA-crystallin from the human lens;Takemoto;Exp. Eye Res.,1991
5. Cleavage from the N-terminal region of βBp-crystallin during aging of normal human lens;Takemoto;Exp. Eye Res.,1987
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