Definition and comparison of the phosphorylation sites of the A and B chains of bovine α-crystallin
- 1 February 1988
- journal article
- research article
- Published by Elsevier in Experimental Eye Research
- Vol. 46 (2) , 199-208
- https://doi.org/10.1016/s0014-4835(88)80077-0
Abstract
No abstract availableThis publication has 15 references indexed in Scilit:
- The phosphorylation sites of the B2 chain of bovine α-crystallinBiochemical and Biophysical Research Communications, 1987
- Identification of the specific phosphorylated serine in the bovine alpha crystallin A1chainCurrent Eye Research, 1987
- cAMP-dependent phosphorylation of bovine lens alpha-crystallin.Proceedings of the National Academy of Sciences, 1985
- Synthetic peptides reproducing the site phosphorylated by cAMP‐dependent protein kinase in protein phosphatase inhibitor‐1European Journal of Biochemistry, 1983
- Protein Phosphorylation Catalyzed by Cyclic AMP-Dependent and Cyclic GMP-Dependent Protein KinasesAnnual Review of Pharmacology and Toxicology, 1980
- Effects of sucrose on interactions of calf lens soluble proteinsExperimental Eye Research, 1978
- Evidence for a post-translational origin of subunit αB1 in the bovine lens α-crystallinExperimental Eye Research, 1978
- The hormonal control of glycogen metabolism: The amino acid sequence at the phosphorylation site of protein phosphatase inhibitor‐1FEBS Letters, 1977
- Stepwise degradations and deamidation of the eye lens protein α-crystallin in ageingNature, 1975
- Evidence for a “non-genetic” origin of the A1 chains of α-crystallinExperimental Eye Research, 1972