Deamidation and Disulfide Bonding in Human Lens γ-Crystallins
- 1 September 1998
- journal article
- Published by Elsevier in Experimental Eye Research
- Vol. 67 (3) , 301-312
- https://doi.org/10.1006/exer.1998.0530
Abstract
No abstract availableKeywords
This publication has 58 references indexed in Scilit:
- Size of Human Lens β-Crystallin Aggregates Are Distinguished by N-terminal Truncation of βB1Published by Elsevier ,1997
- Cloning, Expression, and Chaperone-like Activity of Human αA-CrystallinPublished by Elsevier ,1996
- The Sequence of Human βB1-Crystallin cDNA Allows Mass Spectrometric Detection of βB1 Protein Missing Portions of Its N-terminal ExtensionPublished by Elsevier ,1996
- Nuclear light scattering, disulfide formation and membrane damage in lenses of older guinea pigs treated with hyperbaric oxygenExperimental Eye Research, 1995
- The Effect and Recovery of Long-term H2O2 Exposure on Lens Morphology and BiochemistryExperimental Eye Research, 1993
- Two-dimensional gel electrophoretic analysis of human lens proteinsCurrent Eye Research, 1992
- The effect of phosphorylation on the structure of α-crystallinBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1989
- THE EFFECTS OF NEAR‐UV RADIATION ON HUMAN LENS β‐CRYSTALLINS: PROTEIN STRUCTURAL CHANGES and THE PRODUCTION OF O2_ and H2O2Photochemistry and Photobiology, 1989
- Definition and comparison of the phosphorylation sites of the A and B chains of bovine α-crystallinExperimental Eye Research, 1988
- Two human γ-crystallin genes are linked and riddled with Alu-repeatsGene, 1985