Intracellular carboxy-terminal degradation of the alpha A chain of alpha-crystallin
- PMID: 4448172
- DOI: 10.1111/j.1432-1033.1974.tb03765.x
Intracellular carboxy-terminal degradation of the alpha A chain of alpha-crystallin
Similar articles
-
Intracellular degradation of alpha-crystallin. Fractionation and characterization of degraded alpha A-chains.Eur J Biochem. 1974 Oct 2;48(2):563-70. doi: 10.1111/j.1432-1033.1974.tb03798.x. Eur J Biochem. 1974. PMID: 4448184 No abstract available.
-
Lens crystallin changes associated with amphibian metamorphosis: involvement of a beta-crystallin polypeptide.Biochem Biophys Res Commun. 1989 Nov 15;164(3):1423-30. doi: 10.1016/0006-291x(89)91829-9. Biochem Biophys Res Commun. 1989. PMID: 2590209
-
The degradation of alpha-crystallin at its carboxyl-terminal portion by calpain in bovine lens.Invest Ophthalmol Vis Sci. 1986 Aug;27(8):1269-73. Invest Ophthalmol Vis Sci. 1986. PMID: 3015824
-
Proteolysis of lens proteins (autolysis).Exp Eye Res. 1976 Jun;22(6):625-37. doi: 10.1016/0014-4835(76)90007-5. Exp Eye Res. 1976. PMID: 776642 Review. No abstract available.
-
Lens research: from protein to gene.Exp Eye Res. 1985 Oct;41(4):429-48. doi: 10.1016/s0014-4835(85)80002-6. Exp Eye Res. 1985. PMID: 3910446 Review. No abstract available.
Cited by
-
Alpha-crystallin can function as a molecular chaperone.Proc Natl Acad Sci U S A. 1992 Nov 1;89(21):10449-53. doi: 10.1073/pnas.89.21.10449. Proc Natl Acad Sci U S A. 1992. PMID: 1438232 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources