Species-dependent ensembles of conserved conformational states define the Hsp90 chaperone ATPase cycle.
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Heterozygous yeast deletion collection screens reveal essential targets of Hsp90Molecular 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 dimerSymmetry-free cryo-EM structures of the chaperonin TRiC along its ATPase-driven conformational cycle.Structural 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 kinaseSystematic Mutant Analyses Elucidate General and Client-Specific Aspects of Hsp90 FunctionMechanistic Asymmetry in Hsp90 DimersElucidation of the Hsp90 C-terminal inhibitor binding sitePannexin1 and Pannexin2 channels show quaternary similarities to connexons and different oligomerization numbers from each otherThreonine 22 phosphorylation attenuates Hsp90 interaction with cochaperones and affects its chaperone activityClient Proteins and Small Molecule Inhibitors Display Distinct Binding Preferences for Constitutive and Stress-Induced HSP90 Isoforms and Their Conformationally Restricted MutantsComputational 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.Architecture of the nitric-oxide synthase holoenzyme reveals large conformational changes and a calmodulin-driven release of the FMN domainHsp90 and co-chaperones twist the functions of diverse client proteins.Swe1Wee1-dependent tyrosine phosphorylation of Hsp90 regulates distinct facets of chaperone function.Drosophila glycoprotein 93 Is an ortholog of mammalian heat shock protein gp96 (grp94, HSP90b1, HSPC4) and retains disulfide bond-independent chaperone function for TLRs and integrins.Identification of residues on Hsp70 and Hsp90 ubiquitinated by the cochaperone CHIPProbing 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.A highly charged region in the middle domain of plant endoplasmic reticulum (ER)-localized heat-shock protein 90 is required for resistance to tunicamycin or high calcium-induced ER stresses.Enforced N-domain proximity stimulates Hsp90 ATPase activity and is compatible with function in vivo.Genome-scale co-evolutionary inference identifies functions and clients of bacterial Hsp90Targeting 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.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.Heterogeneity and dynamics in the assembly of the heat shock protein 90 chaperone complexes.Post-translational modifications of Hsp90 and their contributions to chaperone regulationCross-monomer substrate contacts reposition the Hsp90 N-terminal domain and prime the chaperone activityThe Hsp90 mosaic: a picture emergesMolecular and thermodynamic insights into the conformational transitions of Hsp90.Solubility-promoting function of Hsp90 contributes to client maturation and robust cell growth.Hsp70 and Hsp90 of E. coli Directly Interact for Collaboration in Protein Remodeling.Analysis of the tau-associated proteome reveals that exchange of Hsp70 for Hsp90 is involved in tau degradationTumor-intrinsic and tumor-extrinsic factors impacting hsp90- targeted therapy.
P2860
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P2860
Species-dependent ensembles of conserved conformational states define the Hsp90 chaperone ATPase cycle.
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
Species-dependent ensembles of ...... Hsp90 chaperone ATPase cycle.
@en
Species-dependent ensembles of ...... Hsp90 chaperone ATPase cycle.
@nl
type
label
Species-dependent ensembles of ...... Hsp90 chaperone ATPase cycle.
@en
Species-dependent ensembles of ...... Hsp90 chaperone ATPase cycle.
@nl
prefLabel
Species-dependent ensembles of ...... Hsp90 chaperone ATPase cycle.
@en
Species-dependent ensembles of ...... Hsp90 chaperone ATPase cycle.
@nl
P2860
P1433
P1476
Species-dependent ensembles of ...... Hsp90 chaperone ATPase cycle.
@en
P2093
Daniel R Southworth
David A Agard
P2860
P304
P356
10.1016/J.MOLCEL.2008.10.024
P577
2008-12-01T00:00:00Z