NH2-terminal stabilization of small heat shock protein structure: a comparison of two NH2-terminal deletion mutants of alphaA-crystallin.
about
Investigation of the chaperone function of the small heat shock protein-AgsA.Conserved F84 and P86 residues in alphaB-crystallin are essential to effectively prevent the aggregation of substrate proteins.A novel mutation in CRYAA is associated with autosomal dominant suture cataracts in a Chinese family
P2860
NH2-terminal stabilization of small heat shock protein structure: a comparison of two NH2-terminal deletion mutants of alphaA-crystallin.
description
2005 nî lūn-bûn
@nan
2005 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
name
NH2-terminal stabilization of ...... mutants of alphaA-crystallin.
@ast
NH2-terminal stabilization of ...... mutants of alphaA-crystallin.
@en
type
label
NH2-terminal stabilization of ...... mutants of alphaA-crystallin.
@ast
NH2-terminal stabilization of ...... mutants of alphaA-crystallin.
@en
prefLabel
NH2-terminal stabilization of ...... mutants of alphaA-crystallin.
@ast
NH2-terminal stabilization of ...... mutants of alphaA-crystallin.
@en
P2093
P1433
P1476
NH2-terminal stabilization of ...... mutants of alphaA-crystallin.
@en
P2093
Chaoxing Yang
Jane F Koretz
John C Salerno
P304
P577
2005-08-29T00:00:00Z