Dynamics of heat shock protein 90 C-terminal dimerization is an important part of its conformational cycle.
about
The 'active life' of Hsp90 complexesGRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulumTargeting Hsp90 in urothelial carcinomaCorresponding functional dynamics across the Hsp90 Chaperone family: insights from a multiscale analysis of MD simulationsStructure insights into mechanisms of ATP hydrolysis and the activation of human heat-shock protein 90Structural Asymmetry in the Closed State of Mitochondrial Hsp90 (TRAP1) Supports a Two-Step ATP Hydrolysis MechanismElucidation of the Hsp90 C-terminal inhibitor binding siteThreonine 22 phosphorylation attenuates Hsp90 interaction with cochaperones and affects its chaperone activityDifferential modulation of functional dynamics and allosteric interactions in the Hsp90-cochaperone complexes with p23 and Aha1: a computational study.Computational modeling of allosteric regulation in the hsp90 chaperones: a statistical ensemble analysis of protein structure networks and allosteric communications.An Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humansProbing molecular mechanisms of the Hsp90 chaperone: biophysical modeling identifies key regulators of functional dynamics.Gyrase B inhibitor impairs HIV-1 replication by targeting Hsp90 and the capsid protein.Mechanisms of cellular proteostasis: insights from single-molecule approachesTargeting heat-shock-protein 90 (Hsp90) by natural products: geldanamycin, a show case in cancer therapy.Resolving hot spots in the C-terminal dimerization domain that determine the stability of the molecular chaperone Hsp90Molecular chaperones and regulation of tau quality control: strategies for drug discovery in tauopathies.Post-translational modifications of Hsp90 and their contributions to chaperone regulationHeat shock protein 90's mechanochemical cycle is dominated by thermal fluctuations.Hsp70 and Hsp90 of E. coli Directly Interact for Collaboration in Protein Remodeling.Tumor-intrinsic and tumor-extrinsic factors impacting hsp90- targeted therapy.Uncovering a region of heat shock protein 90 important for client binding in E. coli and chaperone function in yeast.Potential C-terminal-domain inhibitors of heat shock protein 90 derived from a C-terminal peptide helix.HSP90 protects the human T-cell leukemia virus type 1 (HTLV-1) tax oncoprotein from proteasomal degradation to support NF-κB activation and HTLV-1 replicationProtein Quality Control by Molecular Chaperones in Neurodegeneration.Molecular basis for the actions of Hsp90 inhibitors and cancer therapy.Single vesicle biochips for ultra-miniaturized nanoscale fluidics and single molecule bioscience.A co-expression strategy to achieve labeling of individual subunits within a dimeric protein for single molecule analysis.Targeting the Diabetic Chaperome to Improve Peripheral Neuropathy.Single-molecule fluorescence spectroscopy maps the folding landscape of a large protein.Alternative approaches to Hsp90 modulation for the treatment of cancer.Molecular Dynamics Simulations Reveal the Mechanisms of Allosteric Activation of Hsp90 by Designed Ligands.Differences in conformational dynamics within the Hsp90 chaperone family reveal mechanistic insightsDynamics of the regulation of Hsp90 by the co-chaperone Sti1.Structural bioinformatics and protein docking analysis of the molecular chaperone-kinase interactions: towards allosteric inhibition of protein kinases by targeting the hsp90-cdc37 chaperone machinery.Slow domain reconfiguration causes power-law kinetics in a two-state enzyme.Atomistic simulations and network-based modeling of the Hsp90-Cdc37 chaperone binding with Cdk4 client protein: A mechanism of chaperoning kinase clients by exploiting weak spots of intrinsically dynamic kinase domains.Interaction of E. coli Hsp90 with DnaK Involves the DnaJ Binding Region of DnaK.Chaperones: Speedy motion for function.Two states or not two states: Single-molecule folding studies of protein L.
P2860
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P2860
Dynamics of heat shock protein 90 C-terminal dimerization is an important part of its conformational cycle.
description
2010 nî lūn-bûn
@nan
2010 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Dynamics of heat shock protein ...... t of its conformational cycle.
@ast
Dynamics of heat shock protein ...... t of its conformational cycle.
@en
type
label
Dynamics of heat shock protein ...... t of its conformational cycle.
@ast
Dynamics of heat shock protein ...... t of its conformational cycle.
@en
prefLabel
Dynamics of heat shock protein ...... t of its conformational cycle.
@ast
Dynamics of heat shock protein ...... t of its conformational cycle.
@en
P2093
P2860
P356
P1476
Dynamics of heat shock protein ...... t of its conformational cycle.
@en
P2093
P2860
P304
16101-16106
P356
10.1073/PNAS.1000916107
P407
P577
2010-08-24T00:00:00Z