[30] Lens α-crystallin: Chaperone-like properties
- 1 January 1998
- book chapter
- Published by Elsevier
- Vol. 290, 365-383
- https://doi.org/10.1016/s0076-6879(98)90032-5
Abstract
No abstract availableKeywords
This publication has 27 references indexed in Scilit:
- Immobilization of the C-terminal Extension of Bovine αA-Crystallin Reduces Chaperone-like ActivityJournal of Biological Chemistry, 1996
- The Mutation Asp69→Ser Affects the Chaperone‐Like Activity of αA‐CrystallinEuropean Journal of Biochemistry, 1995
- Temperature‐induced exposure of hydrophobic surfaces and its effect on the chaperone activity of α‐crystallinFEBS Letters, 1995
- On the thermal stability of .alpha.-crystallin: z new insight from infrared spectroscopyBiochemistry, 1995
- Temperature dependent chaperone‐like activity of alpha‐crystallinFEBS Letters, 1995
- α-Crystallin, a Molecular Chaperone, Forms a Stable Complex with Carbonic Anhydrase upon Heat DenaturationBiochemical and Biophysical Research Communications, 1993
- αB subunit of lens-specific protein α-crystallin is present in other ocular and non-ocular tissuesBiochemical and Biophysical Research Communications, 1989
- Calf lens α-crystallin quaternary structureJournal of Molecular Biology, 1986
- Intracellular Degradation of alpha-Crystallin. Fractionation and Characterization of Degraded alphaA-ChainsEuropean Journal of Biochemistry, 1974
- Intracellular Carboxy‐Terminal Degradation of the αA Chain of α‐CrystallinEuropean Journal of Biochemistry, 1974