Recognition sequence 2 (residues 60-71) plays a role in oligomerization and exchange dynamics of alphaB-crystallin.
about
Solid-state NMR and SAXS studies provide a structural basis for the activation of αB-crystallin oligomersHydroimidazolone modification of the conserved Arg12 in small heat shock proteins: studies on the structure and chaperone function using mutant mimicsAnalysis of the dominant effects mediated by wild type or R120G mutant of αB-crystallin (HspB5) towards Hsp27 (HspB1)Novel roles for α-crystallins in retinal function and disease.Chemical modulation of the chaperone function of human alphaA-crystallin.High-resolution mass spectrometry analysis of protein oxidations and resultant loss of functionLens aging: effects of crystallins.Methionine sulfoxide reductase A (MsrA) restores alpha-crystallin chaperone activity lost upon methionine oxidationDeletion of (54)FLRAPSWF(61) residues decreases the oligomeric size and enhances the chaperone function of alphaB-crystallinEffect of site-directed mutagenesis of methylglyoxal-modifiable arginine residues on the structure and chaperone function of human alphaA-crystallin.Acetylation of lysine 92 improves the chaperone and anti-apoptotic activities of human αB-crystallin.
P2860
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P2860
Recognition sequence 2 (residues 60-71) plays a role in oligomerization and exchange dynamics of alphaB-crystallin.
description
2005 nî lūn-bûn
@nan
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
2005年學術文章
@zh
2005年學術文章
@zh-hant
name
Recognition sequence 2 (residu ...... dynamics of alphaB-crystallin.
@en
Recognition sequence 2
@nl
type
label
Recognition sequence 2 (residu ...... dynamics of alphaB-crystallin.
@en
Recognition sequence 2
@nl
prefLabel
Recognition sequence 2 (residu ...... dynamics of alphaB-crystallin.
@en
Recognition sequence 2
@nl
P356
P1433
P1476
Recognition sequence 2 (residu ...... dynamics of alphaB-crystallin.
@en
P2093
K Krishna Sharma
Yellamaraju Sreelakshmi
P304
12245-12252
P356
10.1021/BI051005H
P407
P577
2005-09-01T00:00:00Z