TM Treweek
R120G alpha B-crystallin promotes the unfolding of reducedalpha-lactalbumin and is inherently unstable
Treweek, TM; Rekas, A; Lindner, RA; Walker, MJ; Aquilina, JA; Robinson, CV; Horwitz, J; Perng, MD; Quinlan, RA; Carver, JA
Authors
A Rekas
RA Lindner
MJ Walker
JA Aquilina
CV Robinson
J Horwitz
MD Perng
Roy Quinlan r.a.quinlan@durham.ac.uk
Emeritus Professor
JA Carver
Citation
Treweek, T., Rekas, A., Lindner, R., Walker, M., Aquilina, J., Robinson, C., …Carver, J. (2005). R120G alpha B-crystallin promotes the unfolding of reducedalpha-lactalbumin and is inherently unstable. The FEBS Journal, 272(3), 711-724
| Journal Article Type | Article |
|---|---|
| Publication Date | 2005-02 |
| Journal | FEBS Journal |
| Print ISSN | 1742-464X |
| Publisher | Wiley |
| Volume | 272 |
| Issue | 3 |
| Pages | 711-724 |
| Keywords | cataract; lens proteins; molecular chaparone; protein aggregation;protein unfoldingHEAT-SHOCK PROTEINS; CHAPERONE-LIKE FUNCTION; DESMIN-RELATED MYOPATHY;C-TERMINAL EXTENSIONS; A-CRYSTALLIN; MOLECULAR CHAPERONE;NMR-SPECTROSCOPY; MISSENSE MUTATION; SUBUNIT |
| Public URL | https://durham-repository.worktribe.com/output/1573985 |