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

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

TM Treweek

A Rekas

RA Lindner

MJ Walker

JA Aquilina

CV Robinson

J Horwitz

MD Perng

Professor 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

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