Conformational dynamics of the molecular chaperone Hsp90
about
Quantitative analysis of HSP90-client interactions reveals principles of substrate recognitionGlucocorticoid receptor function regulated by coordinated action of the Hsp90 and Hsp70 chaperone cyclesBacterial Heat Shock Protein ActivityMolecular chaperones: guardians of the proteome in normal and disease statesGRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulumThe delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiologyChaperone machines for protein folding, unfolding and disaggregationStructural Asymmetry in the Closed State of Mitochondrial Hsp90 (TRAP1) Supports a Two-Step ATP Hydrolysis MechanismAtomic structure of Hsp90-Cdc37-Cdk4 reveals that Hsp90 traps and stabilizes an unfolded kinaseThe heat shock protein/chaperone network and multiple stress resistanceThe activity of protein phosphatase 5 towards native clients is modulated by the middle- and C-terminal domains of Hsp90Approaches for defining the Hsp90-dependent proteome.Selective targeting of the stress chaperome as a therapeutic strategyC-terminal phosphorylation of Hsp70 and Hsp90 regulates alternate binding to co-chaperones CHIP and HOP to determine cellular protein folding/degradation balancesThe co-chaperone Hch1 regulates Hsp90 function differently than its homologue Aha1 and confers sensitivity to yeast to the Hsp90 inhibitor NVP-AUY922Exploring the Trypanosoma brucei Hsp83 potential as a target for structure guided drug designGambogic acid identifies an isoform-specific druggable pocket in the middle domain of Hsp90βKinetic analysis of ribosome-bound fluorescent proteins reveals an early, stable, cotranslational folding intermediate.Differential modulation of functional dynamics and allosteric interactions in the Hsp90-cochaperone complexes with p23 and Aha1: a computational study.Allosteric regulation of the Hsp90 dynamics and stability by client recruiter cochaperones: protein structure network modelingComputational modeling of allosteric regulation in the hsp90 chaperones: a statistical ensemble analysis of protein structure networks and allosteric communications.Comparing pharmacophore models derived from crystal structures and from molecular dynamics simulationsA review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering.Harmine is a potent antimalarial targeting Hsp90 and synergizes with chloroquine and artemisininProbing molecular mechanisms of the Hsp90 chaperone: biophysical modeling identifies key regulators of functional dynamics.Heat shock protein 90 in Alzheimer's diseaseCrystallization and preliminary X-ray diffraction analysis of Trap1 complexed with Hsp90 inhibitorsLow resolution structural studies indicate that the activator of Hsp90 ATPase 1 (Aha1) of Leishmania braziliensis has an elongated shape which allows its interaction with both N- and M-domains of Hsp90.Targeting heat-shock-protein 90 (Hsp90) by natural products: geldanamycin, a show case in cancer therapy.Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in client protein remodeling.Heterogeneity and dynamics in the assembly of the heat shock protein 90 chaperone complexes.Functional characterization of heat-shock protein 90 from Oryza sativa and crystal structure of its N-terminal domainMolecular and thermodynamic insights into the conformational transitions of Hsp90.Soluble guanylyl cyclase requires heat shock protein 90 for heme insertion during maturation of the NO-active enzyme.Hsp70 and Hsp90 of E. coli Directly Interact for Collaboration in Protein Remodeling.A Scaffold Merging Approach to Hsp90 C-terminal Inhibition: Synthesis and Evaluation of a Chimeric Library.Heat shock protein 90 in plants: molecular mechanisms and roles in stress responses.Recent advances in nanoparticle-based Förster resonance energy transfer for biosensing, molecular imaging and drug release profilingUncovering a region of heat shock protein 90 important for client binding in E. coli and chaperone function in yeast.Chemical Tools to Investigate Mechanisms Associated with HSP90 and HSP70 in Disease.
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Conformational dynamics of the molecular chaperone Hsp90
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
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scientific article published on 18 March 2011
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
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vědecký článek
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name
Conformational dynamics of the molecular chaperone Hsp90
@en
Conformational dynamics of the molecular chaperone Hsp90.
@nl
type
label
Conformational dynamics of the molecular chaperone Hsp90
@en
Conformational dynamics of the molecular chaperone Hsp90.
@nl
prefLabel
Conformational dynamics of the molecular chaperone Hsp90
@en
Conformational dynamics of the molecular chaperone Hsp90.
@nl
P2093
P2860
P1476
Conformational dynamics of the molecular chaperone Hsp90
@en
P2093
David A Agard
Kristin A Krukenberg
Timothy O Street
P2860
P304
P356
10.1017/S0033583510000314
P577
2011-03-18T00:00:00Z