| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10871869 | FEBS Letters | 2011 | 6 Pages |
Abstract
⺠We investigated the effect of F71L mutation in αA-crystallin. ⺠Thermal stability of the protein was compromised due to F71L substitution. ⺠The F71L-mutant has defective chaperone-like activity upon heat treatment. ⺠F71L-mutant failed to protect the αB-subunit from heat-induced aggregation. ⺠The F71L-mutation may cause cataract in synergy with other factors during aging.
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Authors
Vakdevi Validandi, V. Sudhakar Reddy, P.N.B.S. Srinivas, Niklaus H. Mueller, S.G. Bhagyalaxmi, T. Padma, J. Mark Petrash, G. Bhanuprakash Reddy,