A positive charge preservation at position 116 of alpha A-crystallin is critical for its structural and functional integrity.
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Temperature-dependent structural and functional properties of a mutant (F71L) αA-crystallin: molecular basis for early onset of age-related cataractConcurrence of Danish dementia and cataract: insights from the interactions of dementia associated peptides with eye lens alpha-crystallinHydroimidazolone modification of the conserved Arg12 in small heat shock proteins: studies on the structure and chaperone function using mutant mimicsMechanism of small heat shock protein function in vivo: a knock-in mouse model demonstrates that the R49C mutation in alpha A-crystallin enhances protein insolubility and cell death2-ammonio-6-(3-oxidopyridinium-1-yl)hexanoate (OP-lysine) is a newly identified advanced glycation end product in cataractous and aged human lenses.Deamidation affects structural and functional properties of human alphaA-crystallin and its oligomerization with alphaB-crystallin.Detection and architecture of small heat shock protein monomers.Different experimental approaches in modelling cataractogenesis: An overview of selenite-induced nuclear cataract in rats.Small heat shock proteins in inherited peripheral neuropathies.Conserved F84 and P86 residues in alphaB-crystallin are essential to effectively prevent the aggregation of substrate proteins.Chemical modulation of the chaperone function of human alphaA-crystallin.Phenotype of cardiomyopathy in cardiac-specific heat shock protein B8 K141N transgenic mouse.Differential role of arginine mutations on the structure and functions of α-crystallin.Quaternary structural parameters of the congenital cataract causing mutants of αA-crystallin.Differential binding of mutant (R116C) and wildtype alphaA crystallin to actin.Effect of site-directed mutagenesis of methylglyoxal-modifiable arginine residues on the structure and chaperone function of human alphaA-crystallin.Hydroimidazolone modification of human alphaA-crystallin: Effect on the chaperone function and protein refolding ability.Structural properties of silkworm small heat-shock proteins: sHSP19.9 and sHSP20.8.A S52P mutation in the 'α-crystallin domain' of Mycobacterium leprae HSP18 reduces its oligomeric size and chaperone function.Importance of the positively charged residue at position 54 to the chaperoning function, conformational stability and amyloidogenic nature of human αA-crystallin.Oligomerization and chaperone-like activity of Drosophila melanogaster small heat shock protein DmHsp27 and three arginine mutants in the alpha-crystallin domain.Real-time heterogeneous protein-protein interaction between αA-crystallin N-terminal mutants and αB-crystallin using quartz crystal microbalance (QCM).
P2860
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P2860
A positive charge preservation at position 116 of alpha A-crystallin is critical for its structural and functional integrity.
description
2002 nî lūn-bûn
@nan
2002 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
A positive charge preservation ...... ural and functional integrity.
@ast
A positive charge preservation ...... ural and functional integrity.
@en
type
label
A positive charge preservation ...... ural and functional integrity.
@ast
A positive charge preservation ...... ural and functional integrity.
@en
prefLabel
A positive charge preservation ...... ural and functional integrity.
@ast
A positive charge preservation ...... ural and functional integrity.
@en
P2093
P356
P1433
P1476
A positive charge preservation ...... ural and functional integrity.
@en
P2093
Edathara C Abraham
Prajitha Thampi
Sibes Bera
Wha Ja Cho
P304
12421-12426
P356
10.1021/BI0204140
P407
P577
2002-10-01T00:00:00Z