Multiple conformations of E. coli Hsp90 in solution: insights into the conformational dynamics of Hsp90.
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Putting the pieces together: integrative modeling platform software for structure determination of macromolecular assembliesGlucocorticoid receptor function regulated by coordinated action of the Hsp90 and Hsp70 chaperone cyclesA proteomic investigation of ligand-dependent HSP90 complexes reveals CHORDC1 as a novel ADP-dependent HSP90-interacting proteinHsp90-Tau complex reveals molecular basis for specificity in chaperone actionReview: The HSP90 molecular chaperone-an enigmatic ATPaseMolecular chaperones: guardians of the proteome in normal and disease statesCorresponding functional dynamics across the Hsp90 Chaperone family: insights from a multiscale analysis of MD simulationsModeling signal propagation mechanisms and ligand-based conformational dynamics of the Hsp90 molecular chaperone full-length dimerInsights into Mechanism of Glucokinase ActivationStructural Asymmetry in the Closed State of Mitochondrial Hsp90 (TRAP1) Supports a Two-Step ATP Hydrolysis MechanismElucidation of the Hsp90 C-terminal inhibitor binding siteConformational transitions upon ligand binding: holo-structure prediction from apo conformationsCharacterization of multi-functional properties and conformational analysis of MutS2 from Thermotoga maritima MSB8Exploring the Functional Complementation between Grp94 and Hsp90Robust, high-throughput solution structural analyses by small angle X-ray scattering (SAXS)Substrate-specific reorganization of the conformational ensemble of CSK implicates novel modes of kinase functionDifferential 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.A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering.Dynamic Interaction of Hsp90 with Its Client Protein p53.Dynamics of heat shock protein 90 C-terminal dimerization is an important part of its conformational cycle.Integration of small-angle X-ray scattering data into structural modeling of proteins and their assembliesModular control of cross-oligomerization: analysis of superstabilized Hsp90 homodimers in vivo.Integrative structure modeling of macromolecular assemblies from proteomics dataBiological and structural basis for Aha1 regulation of Hsp90 ATPase activity in maintaining proteostasis in the human disease cystic fibrosis.Probing molecular mechanisms of the Hsp90 chaperone: biophysical modeling identifies key regulators of functional dynamics.Heat shock protein 90 as a drug target against protozoan infections: biochemical characterization of HSP90 from Plasmodium falciparum and Trypanosoma evansi and evaluation of its inhibitor as a candidate drug.Conformational selection underlies recognition of a molybdoenzyme by its dedicated chaperoneN-terminal domain of human Hsp90 triggers binding to the cochaperone p23.Enforced N-domain proximity stimulates Hsp90 ATPase activity and is compatible with function in vivo.Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in client protein remodeling.Substrate binding drives large-scale conformational changes in the Hsp90 molecular chaperone.Client-loading conformation of the Hsp90 molecular chaperone revealed in the cryo-EM structure of the human Hsp90:Hop complex.Molecular chaperones and regulation of tau quality control: strategies for drug discovery in tauopathies.A dynamic view of ATP-coupled functioning cycle of Hsp90 N-terminal domain.MESMER: minimal ensemble solutions to multiple experimental restraints.Cross-monomer substrate contacts reposition the Hsp90 N-terminal domain and prime the chaperone activityAdvances in the discovery and development of heat-shock protein 90 inhibitors for cancer treatment.Molecular and thermodynamic insights into the conformational transitions of Hsp90.Solubility-promoting function of Hsp90 contributes to client maturation and robust cell growth.
P2860
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P2860
Multiple conformations of E. coli Hsp90 in solution: insights into the conformational dynamics of Hsp90.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Multiple conformations of E. c ...... formational dynamics of Hsp90.
@en
type
label
Multiple conformations of E. c ...... formational dynamics of Hsp90.
@en
prefLabel
Multiple conformations of E. c ...... formational dynamics of Hsp90.
@en
P2093
P2860
P1433
P1476
Multiple conformations of E. c ...... formational dynamics of Hsp90.
@en
P2093
David A Agard
Friedrich Förster
Kristin A Krukenberg
Luke M Rice
P2860
P304
P356
10.1016/J.STR.2008.01.021
P50
P577
2008-05-01T00:00:00Z