Formation of Four Isomers at the Asp-151 Residue of Aged Human αA-Crystallin by Natural Aging
- 1 November 1999
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 265 (3) , 746-751
- https://doi.org/10.1006/bbrc.1999.1748
Abstract
No abstract availableKeywords
This publication has 29 references indexed in Scilit:
- Human αB-crystallin gene and preferential promoter function in lensPublished by Elsevier ,2004
- The Conformation Formed by the Domain after Alanine-155 Induces Inversion of Aspartic Acid-151 in αA-Crystallin from Aged Human LensesBiochemical and Biophysical Research Communications, 1997
- Simultaneous Stereoinversion and Isomerization at Specific Aspartic Acid Residues in αA-Crystallin from Human LensThe Journal of Biochemistry, 1994
- Simultaneous racemization and isomerization at specific aspartic acid residues in αB-crystallin from the aged human lensBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1994
- Alpha-crystallin can function as a molecular chaperone.Proceedings of the National Academy of Sciences, 1992
- Alpha B-crystallin is a small heat shock protein.Proceedings of the National Academy of Sciences, 1991
- Site‐specific racemization in aging α‐crystallinFEBS Letters, 1990
- Aspartic acid racemization in heavy molecular weight crystallins and water insoluble protein from normal human lenses and cataracts.Proceedings of the National Academy of Sciences, 1978
- Aspartic acid racemisation in the human lens during ageing and in cataract formationNature, 1977
- The amino acid sequence of the A chain of human α‐crystallinFEBS Letters, 1975