Atomic structure of Hsp90-Cdc37-Cdk4 reveals that Hsp90 traps and stabilizes an unfolded kinase
about
Exploring the Functional Complementation between Grp94 and Hsp90An Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humansProduction and purification of human Hsp90β in Escherichia coli.Structural and functional basis of protein phosphatase 5 substrate specificity.Unravelling biological macromolecules with cryo-electron microscopy.NMR characterization of HtpG, the E. coli Hsp90, using sparse labeling with 13C-methyl alanine.Involvement of cell surface 90 kDa heat shock protein (HSP90) in pattern recognition by human monocyte-derived macrophages.Modulation of Molecular Chaperones in Huntington's Disease and Other Polyglutamine Disorders.Mechanistic basis for the recognition of a misfolded protein by the molecular chaperone Hsp90.While the revolution will not be crystallized, biochemistry reigns supreme.DYRK1B mutations associated with metabolic syndrome impair the chaperone-dependent maturation of the kinase domain.Symmetry broken and rebroken during the ATP hydrolysis cycle of the mitochondrial Hsp90 TRAP1.Regulation of Rvb1/Rvb2 by a Domain within the INO80 Chromatin Remodeling Complex Implicates the Yeast Rvbs as Protein Assembly Chaperones.How Hsp90 and Cdc37 Lubricate Kinase Molecular Switches.Structural and Functional Analysis of GRP94 in the Closed State Reveals an Essential Role for the Pre-N Domain and a Potential Client-Binding Site.Heat Tolerance Induction of the Indian Meal Moth (Lepidoptera: Pyralidae) Is Accompanied by Upregulation of Heat Shock Proteins and Polyols.Hsp90 dependence of a kinase is determined by its conformational landscapeControl of Hsp90 chaperone and its clients by N-terminal acetylation and the N-end rule pathway.Ensemble-based modeling and rigidity decomposition of allosteric interaction networks and communication pathways in cyclin-dependent kinases: Differentiating kinase clients of the Hsp90-Cdc37 chaperone.Differential Regulation of G1 CDK Complexes by the Hsp90-Cdc37 Chaperone System.Protein Expression and Purification of the Hsp90-Cdc37-Cdk4 Kinase Complex from Saccharomyces cerevisiae.HSP90 recognizes the N-terminus of huntingtin involved in regulation of huntingtin aggregation by USP19.Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facilitates folding of kinase and non-kinase clients.Methylation-regulated decommissioning of multimeric PP2A complexes.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.Evidence for Hsp90 Co-chaperones in Regulating Hsp90 Function and Promoting Client Protein Folding.Detecting Posttranslational Modifications of Hsp90.Network-based modelling and percolation analysis of conformational dynamics and activation in the CDK2 and CDK4 proteins: dynamic and energetic polarization of the kinase lobes may determine divergence of the regulatory mechanisms.Methods to validate Hsp90 inhibitor specificity, to identify off-target effects, and to rethink approaches for further clinical development.Inhibition of HSP90α protects cultured neurons from oxygen-glucose deprivation induced necroptosis by decreasing RIP3 expression.Identifying the substrate proteins of U-box E3s E4B and CHIP by orthogonal ubiquitin transfer.Non-canonical roles of PFKFB3 in regulation of cell cycle through binding to CDK4.A Mitochondrial-targeted purine-based HSP90 antagonist for leukemia therapy.Functional and physical interaction between yeast Hsp90 and Hsp70.Genetic Identification of Separase Regulators in Caenorhabditis elegans.Phosphorylation induced cochaperone unfolding promotes kinase recruitment and client class-specific Hsp90 phosphorylation.Disease Variants of FGFR3 Reveal Molecular Basis for the Recognition and Additional Roles for Cdc37 in Hsp90 Chaperone System.The HSP90 chaperone machinery.The diverse roles of Hsp90 and where to find them.A switch point in the molecular chaperone Hsp90 responding to client interaction.
P2860
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P2860
Atomic structure of Hsp90-Cdc37-Cdk4 reveals that Hsp90 traps and stabilizes an unfolded kinase
description
2016 nî lūn-bûn
@nan
2016 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2016 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2016年の論文
@ja
2016年論文
@yue
2016年論文
@zh-hant
2016年論文
@zh-hk
2016年論文
@zh-mo
2016年論文
@zh-tw
2016年论文
@wuu
name
Atomic structure of Hsp90-Cdc3 ...... stabilizes an unfolded kinase
@ast
Atomic structure of Hsp90-Cdc3 ...... stabilizes an unfolded kinase
@en
Atomic structure of Hsp90-Cdc3 ...... stabilizes an unfolded kinase
@nl
type
label
Atomic structure of Hsp90-Cdc3 ...... stabilizes an unfolded kinase
@ast
Atomic structure of Hsp90-Cdc3 ...... stabilizes an unfolded kinase
@en
Atomic structure of Hsp90-Cdc3 ...... stabilizes an unfolded kinase
@nl
prefLabel
Atomic structure of Hsp90-Cdc3 ...... stabilizes an unfolded kinase
@ast
Atomic structure of Hsp90-Cdc3 ...... stabilizes an unfolded kinase
@en
Atomic structure of Hsp90-Cdc3 ...... stabilizes an unfolded kinase
@nl
P2093
P2860
P50
P356
P1433
P1476
Atomic structure of Hsp90-Cdc3 ...... stabilizes an unfolded kinase
@en
P2093
Akihiko Arakawa
David A Agard
Kliment A Verba
Ray Yu-Ruei Wang
P2860
P304
P356
10.1126/SCIENCE.AAF5023
P407
P577
2016-06-24T00:00:00Z