Size of Human Lens β-Crystallin Aggregates Are Distinguished by N-terminal Truncation of βB1
Open Access
- 1 April 1997
- journal article
- research article
- Published by Elsevier
- Vol. 272 (17) , 11250-11255
- https://doi.org/10.1074/jbc.272.17.11250
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- The role of the sequence extensions in β-crystallin assemblyProtein Engineering, Design and Selection, 1994
- High resolution structure of an oligomeric eye lens β-crystallinJournal of Molecular Biology, 1991
- X-ray analysis of βB2-crystallin and evolution of oligomeric lens proteinsNature, 1990
- Rapid separation of bovine β-crystallin subunits βB1, βB2, βB3, βA3 and βA4Experimental Eye Research, 1990
- Age-dependent changes in the heat-stable crystallin, βBp, of the human lensCurrent Eye Research, 1986
- Proline‐ and alanine‐rich N‐terminal extension of the basic bovine β‐crystallin B1 chainsFEBS Letters, 1983
- Primary Gene Products of Bovine β‐Crystallin and Reassociation Behavior of Its AggregatesEuropean Journal of Biochemistry, 1982
- Human β-crystallinExperimental Eye Research, 1980
- The primary structure of the B2 chain of human α‐crystallinFEBS Letters, 1977
- The amino acid sequence of the A chain of human α‐crystallinFEBS Letters, 1975