Intermolecular exchange and stabilization of recombinant human alphaA- and alphaB-crystallin.
about
Detection of protein-protein interactions among lens crystallins in a mammalian two-hybrid system assayBinding determinants of the small heat shock protein, αB-crystallin: recognition of the 'IxI' motifMultiple molecular architectures of the eye lens chaperone B-crystallin elucidated by a triple hybrid approachConformational change and destabilization of cataract gammaC-crystallin T5P mutantHeat shock proteins and heat shock factor 1 in carcinogenesis and tumor development: an updateThe cardiomyopathy and lens cataract mutation in alphaB-crystallin alters its protein structure, chaperone activity, and interaction with intermediate filaments in vitro.The R116C mutation in alpha A-crystallin diminishes its protective ability against stress-induced lens epithelial cell apoptosis.Deamidation affects structural and functional properties of human alphaA-crystallin and its oligomerization with alphaB-crystallin.Human embryonic, fetal, and adult hemoglobins have different subunit interface strengths. Correlation with lifespan in the red cell.Role of alphaBI5 and alphaBT162 residues in subunit interaction during oligomerization of alphaB-crystallin.AlphaA-crystallin R49Cneo mutation influences the architecture of lens fiber cell membranes and causes posterior and nuclear cataracts in mice.Alpha-crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network.Structural and functional changes in the alpha A-crystallin R116C mutant in hereditary cataracts.Monitoring the prevention of amyloid fibril formation by alpha-crystallin. Temperature dependence and the nature of the aggregating species.Analysis of the dominant effects mediated by wild type or R120G mutant of αB-crystallin (HspB5) towards Hsp27 (HspB1)The quaternary organization and dynamics of the molecular chaperone HSP26 are thermally regulated.Confocal fluorescence resonance energy transfer microscopy study of protein-protein interactions of lens crystallins in living cells.Degradation of C-terminal truncated alpha A-crystallins by the ubiquitin-proteasome pathway.Spectral contribution of the individual tryptophan of alphaB-crystallin: a study by site-directed mutagenesisAlpha-crystallin-derived peptides as therapeutic chaperones.Importance of eye lens α-crystallin heteropolymer with 3:1 αA to αB ratio: stability, aggregation, and modifications.Monitoring the interaction between β2-microglobulin and the molecular chaperone αB-crystallin by NMR and mass spectrometry: αB-crystallin dissociates β2-microglobulin oligomers.Protein-protein interactions involving congenital cataract T5P gammaC-crystallin mutant: a confocal fluorescence microscopy study.A novel mutation (F71L) in alphaA-crystallin with defective chaperone-like function associated with age-related cataract.Lens aging: effects of crystallins.Small heat-shock proteins: important players in regulating cellular proteostasis.Lens Biology and BiochemistryDifferential protective activity of alpha A- and alphaB-crystallin in lens epithelial cells.The lack of chaperonelike activity of Caenorhabditis elegans Hsp12.2 cannot be restored by domain swapping with human alphaB-crystallin.The molecular chaperone alpha-crystallin as an excipient in an insulin formulation.Lens alpha-crystallin: function and structure.Cell penetration peptides for enhanced entry of αB-crystallin into lens cellsMammalian Hsp22 is a heat-inducible small heat-shock protein with chaperone-like activity.Cholesterol-derived bile acids enhance the chaperone activity of α-crystallins.Fluorescence resonance energy transfer study of subunit exchange in human lens crystallins and congenital cataract crystallin mutants.Interactions and chaperone function of alphaA-crystallin with T5P gammaC-crystallin mutant.Subunit exchange, conformational stability, and chaperone-like function of the small heat shock protein 16.5 from Methanococcus jannaschii.Two basic residues of the h-VPAC1 receptor second transmembrane helix are essential for ligand binding and signal transduction.Role of the conserved SRLFDQFFG region of alpha-crystallin, a small heat shock protein. Effect on oligomeric size, subunit exchange, and chaperone-like activity.Thermal and acid denaturation of bovine lens α-crystallin.
P2860
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P2860
Intermolecular exchange and stabilization of recombinant human alphaA- and alphaB-crystallin.
description
1998 nî lūn-bûn
@nan
1998 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Intermolecular exchange and st ...... alphaA- and alphaB-crystallin.
@ast
Intermolecular exchange and st ...... alphaA- and alphaB-crystallin.
@en
type
label
Intermolecular exchange and st ...... alphaA- and alphaB-crystallin.
@ast
Intermolecular exchange and st ...... alphaA- and alphaB-crystallin.
@en
prefLabel
Intermolecular exchange and st ...... alphaA- and alphaB-crystallin.
@ast
Intermolecular exchange and st ...... alphaA- and alphaB-crystallin.
@en
P356
P1476
Intermolecular exchange and st ...... alphaA- and alphaB-crystallin.
@en
P304
P356
10.1074/JBC.273.1.286
P407
P577
1998-01-01T00:00:00Z