Conformational dynamics of the molecular chaperone Hsp90 in complexes with a co-chaperone and anticancer drugs.
about
Modeling signal propagation mechanisms and ligand-based conformational dynamics of the Hsp90 molecular chaperone full-length dimerMixed Hsp90-cochaperone complexes are important for the progression of the reaction cycle.Posttranslational modification and conformational state of heat shock protein 90 differentially affect binding of chemically diverse small molecule inhibitorsThe 90-kDa heat shock protein Hsp90 protects tubulin against thermal denaturationBiochemical and biophysical characterization of the Mg2+-induced 90-kDa heat shock protein oligomers.Dynamics of heat shock protein 90 C-terminal dimerization is an important part of its conformational cycle.Probing molecular mechanisms of the Hsp90 chaperone: biophysical modeling identifies key regulators of functional dynamics.N-terminal domain of human Hsp90 triggers binding to the cochaperone p23.Heat shock protein 90's mechanochemical cycle is dominated by thermal fluctuations.Heat Shock Protein 90 Associates with the Per-Arnt-Sim Domain of Heme-free Soluble Guanylate Cyclase: IMplications for Enzyme Maturation.Oxidative stress plays a critical role in inactivating mutant BRAF by geldanamycin derivativesIn Vivo Conformational Dynamics of Hsp90 and Its Interactors.Conformational dynamics of the molecular chaperone Hsp90Engineering the surface properties of a human monoclonal antibody prevents self-association and rapid clearance in vivo.Differences in conformational dynamics within the Hsp90 chaperone family reveal mechanistic insightsApo-Hsp90 coexists in two open conformational states in solution.Spatially and kinetically resolved changes in the conformational dynamics of the Hsp90 chaperone machine.Analysis of protein conformation and dynamics by hydrogen/deuterium exchange MS.Hsp90·Cdc37 Complexes with Protein Kinases Form Cooperatively with Multiple Distinct Interaction Sites.Structural and dynamic insights into the energetics of activation loop rearrangement in FGFR1 kinase.Hsp90 charged-linker truncation reverses the functional consequences of weakened hydrophobic contacts in the N domain
P2860
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P2860
Conformational dynamics of the molecular chaperone Hsp90 in complexes with a co-chaperone and anticancer drugs.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年学术文章
@wuu
2007年学术文章
@zh-cn
2007年学术文章
@zh-hans
2007年学术文章
@zh-my
2007年学术文章
@zh-sg
2007年學術文章
@yue
2007年學術文章
@zh
2007年學術文章
@zh-hant
name
Conformational dynamics of the ...... haperone and anticancer drugs.
@en
Conformational dynamics of the ...... haperone and anticancer drugs.
@nl
type
label
Conformational dynamics of the ...... haperone and anticancer drugs.
@en
Conformational dynamics of the ...... haperone and anticancer drugs.
@nl
prefLabel
Conformational dynamics of the ...... haperone and anticancer drugs.
@en
Conformational dynamics of the ...... haperone and anticancer drugs.
@nl
P50
P1476
Conformational dynamics of the ...... haperone and anticancer drugs.
@en
P2093
Sophie E Jackson
P304
P356
10.1016/J.JMB.2007.04.059
P407
P577
2007-04-27T00:00:00Z