Subunit exchange demonstrates a differential chaperone activity of calf alpha-crystallin toward beta LOW- and individual gamma-crystallins.
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The thermal structural transition of α-crystallin inhibits the heat induced self-aggregationA protein aggregation based test for screening of the agents affecting thermostability of proteinsThe thermal structural transition of alpha-crystallin modulates subunit interactions and increases protein solubilityQuantification of anti-aggregation activity of chaperones: a test-system based on dithiothreitol-induced aggregation of bovine serum albuminIn vivo substrates of the lens molecular chaperones αA-crystallin and αB-crystallinDeamidation affects structural and functional properties of human alphaA-crystallin and its oligomerization with alphaB-crystallin.Aggregation of deamidated human betaB2-crystallin and incomplete rescue by alpha-crystallin chaperone.Confocal fluorescence resonance energy transfer microscopy study of protein-protein interactions of lens crystallins in living cells.Alpha-crystallin-derived peptides as therapeutic chaperones.Lens aging: effects of crystallins.Mechanism of suppression of protein aggregation by 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.Changes in solvent accessibility of wild-type and deamidated βB2-crystallin following complex formation with αA-crystallin.Effect of dicarbonyl-induced browning on alpha-crystallin chaperone-like activity: physiological significance and caveats of in vitro aggregation assaysInsights into the domains required for dimerization and assembly of human alphaB crystallin.Partially folded aggregation intermediates of human gammaD-, gammaC-, and gammaS-crystallin are recognized and bound by human alphaB-crystallin chaperone.Fluorescence resonance energy transfer study of subunit exchange in human lens crystallins and congenital cataract crystallin mutants.α-crystallin modulates its chaperone activity by varying the exposed surface.Thermal denaturation and aggregation of apoform of glycogen phosphorylase b. Effect of crowding agents and chaperones
P2860
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P2860
Subunit exchange demonstrates a differential chaperone activity of calf alpha-crystallin toward beta LOW- and individual gamma-crystallins.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
2003年學術文章
@zh
2003年學術文章
@zh-hant
name
Subunit exchange demonstrates ...... individual gamma-crystallins.
@en
Subunit exchange demonstrates ...... individual gamma-crystallins.
@nl
type
label
Subunit exchange demonstrates ...... individual gamma-crystallins.
@en
Subunit exchange demonstrates ...... individual gamma-crystallins.
@nl
prefLabel
Subunit exchange demonstrates ...... individual gamma-crystallins.
@en
Subunit exchange demonstrates ...... individual gamma-crystallins.
@nl
P2093
P2860
P356
P1476
Subunit exchange demonstrates ...... d individual gamma-crystallins
@en
P2093
Annette Tardieu
Karine Prat
Nicolette H Lubsen
Tatiana Putilina
P2860
P304
13747-13756
P356
10.1074/JBC.M208157200
P407
P577
2003-01-31T00:00:00Z