Insights into hydrophobicity and the chaperone-like function of alphaA- and alphaB-crystallins: an isothermal titration calorimetric study.
about
Temperature-dependent structural and functional properties of a mutant (F71L) αA-crystallin: molecular basis for early onset of age-related cataractHydroimidazolone modification of the conserved Arg12 in small heat shock proteins: studies on the structure and chaperone function using mutant mimicsStructural and functional roles of deamidation of N146 and/or truncation of NH2- or COOH-termini in human αB-crystallin.Functional validation of hydrophobic adaptation to physiological temperature in the small heat shock protein αA-crystallinProtein polymer nanoparticles engineered as chaperones protect against apoptosis in human retinal pigment epithelial cellsConserved F84 and P86 residues in alphaB-crystallin are essential to effectively prevent the aggregation of substrate proteins.Importance of eye lens α-crystallin heteropolymer with 3:1 αA to αB ratio: stability, aggregation, and modifications.Mini-alphaB-crystallin: a functional element of alphaB-crystallin with chaperone-like activityA novel mutation (F71L) in alphaA-crystallin with defective chaperone-like function associated with age-related cataract.Mechanism of suppression of protein aggregation by α-crystallin.An examination of alpha B-crystallin as a modifier of SOD1 aggregate pathology and toxicity in models of familial amyotrophic lateral sclerosis.Structural and functional properties of NH(2)-terminal domain, core domain, and COOH-terminal extension of αA- and αB-crystallins.Therapeutic potential of α-crystallin.Deletion of (54)FLRAPSWF(61) residues decreases the oligomeric size and enhances the chaperone function of alphaB-crystallinParadoxical acceleration of dithiothreitol-induced aggregation of insulin in the presence of a chaperone.Effect of site-directed mutagenesis of methylglyoxal-modifiable arginine residues on the structure and chaperone function of human alphaA-crystallin.Functional Amyloid Protection in the Eye Lens: Retention of α-Crystallin Molecular Chaperone Activity after Modification into Amyloid Fibrils.A S52P mutation in the 'α-crystallin domain' of Mycobacterium leprae HSP18 reduces its oligomeric size and chaperone function.Arginine controls heat-induced cluster-cluster aggregation of lysozyme at around the isoelectric point.Glutamic acid residues in the C-terminal extension of small heat shock protein 25 are critical for structural and functional integrity.Hyperglycemia induced expression, phosphorylation, and translocation of αB-crystallin in rat skeletal muscle.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
Insights into hydrophobicity and the chaperone-like function of alphaA- and alphaB-crystallins: an isothermal titration calorimetric study.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
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2005年学术文章
@zh
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
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name
Insights into hydrophobicity a ...... titration calorimetric study.
@en
Insights into hydrophobicity a ...... titration calorimetric study.
@nl
type
label
Insights into hydrophobicity a ...... titration calorimetric study.
@en
Insights into hydrophobicity a ...... titration calorimetric study.
@nl
prefLabel
Insights into hydrophobicity a ...... titration calorimetric study.
@en
Insights into hydrophobicity a ...... titration calorimetric study.
@nl
P2860
P356
P1476
Insights into hydrophobicity a ...... l titration calorimetric study
@en
P2093
M Satish Kumar
Mili Kapoor
P2860
P304
21726-21730
P356
10.1074/JBC.M500405200
P407
P577
2005-04-06T00:00:00Z