Conformational and Functional Differences between Recombinant Human Lens αA- and αB-Crystallin

This publication has 34 references indexed in Scilit:

• Cloning, Expression, and Chaperone-like Activity of Human αA-Crystallin
  Published by Elsevier ,1996
• Immobilization of the C-terminal Extension of Bovine αA-Crystallin Reduces Chaperone-like Activity
  Journal of Biological Chemistry, 1996
• Conformational Properties of Substrate Proteins Bound to a Molecular Chaperone α-Crystallin
  Published by Elsevier ,1996
• The Mutation Asp69→Ser Affects the Chaperone‐Like Activity of αA‐Crystallin
  European Journal of Biochemistry, 1995
• αA‐crystallin confers cellular thermoresistance
  FEBS Letters, 1994
• Expression of the α‐Crystallin/Small Heat‐Shock Protein/Molecular Chaperone Genes in the Lens and other Tissues
  Published by Wiley ,1994
• Two-dimensional gel electrophoretic analysis of human lens proteins
  Current Eye Research, 1992
• On the structure of α-crystallin: Construction of hybrid molecules and homopolymers
  Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1989
• Spectroscopic investigations of bovine lens crystallins. 1. Circular dichroism and intrinsic fluorescence
  Biochemistry, 1982
• Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
  Nature, 1970