Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle.
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Steroid Receptor-Associated Immunophilins: A Gateway to Steroid SignallingThe Hsp90 cochaperones Cpr6, Cpr7, and Cns1 interact with the intact ribosomeSystematic Mutant Analyses Elucidate General and Client-Specific Aspects of Hsp90 FunctionThe FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug bindingSelective targeting of the stress chaperome as a therapeutic strategyAltered cofactor regulation with disease-associated p97/VCP mutationsDifferential 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 humansThe charged linker of the molecular chaperone Hsp90 modulates domain contacts and biological function.c-Abl Mediated Tyrosine Phosphorylation of Aha1 Activates Its Co-chaperone Function in Cancer Cells.Crowding Activates Heat Shock Protein 90.Interaction of heat shock protein 90 and the co-chaperone Cpr6 with Ura2, a bifunctional enzyme required for pyrimidine biosynthesisAsymmetric Hsp90 N domain SUMOylation recruits Aha1 and ATP-competitive inhibitors.Contributions of co-chaperones and post-translational modifications towards Hsp90 drug sensitivity.Targeting Hsp90 and its co-chaperones to treat Alzheimer's diseaseHsp90 activator Aha1 drives production of pathological tau aggregates.Activation of Hsp90 Enzymatic Activity and Conformational Dynamics through Rationally Designed Allosteric Ligands.Alternative approaches to Hsp90 modulation for the treatment of cancer.Hsp90 regulates the dynamics of its cochaperone Sti1 and the transfer of Hsp70 between modules.Differences in conformational dynamics within the Hsp90 chaperone family reveal mechanistic insightsThe Mechanism of Hsp90 ATPase Stimulation by Aha1Novel Entropically Driven Conformation-specific Interactions with Tomm34 Protein Modulate Hsp70 Protein Folding and ATPase Activities.Cooperation of local motions in the Hsp90 molecular chaperone ATPase mechanism.Aha1 can act as an autonomous chaperone to prevent aggregation of stressed proteins.Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facilitates folding of kinase and non-kinase clients.Gene expression regulation by heat-shock proteins: the cardinal roles of HSF1 and Hsp90.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.Computational Modeling of the Hsp90 Interactions with Cochaperones and Small-Molecule Inhibitors.A chemical compound inhibiting the Aha1-Hsp90 chaperone complex.Hsp90 Sensitivity to ADP Reveals Hidden Regulation Mechanisms.Importance of cycle timing for the function of the molecular chaperone Hsp90.The HSP90 chaperone machinery.Mutation of essential Hsp90 co-chaperones SGT1 or CNS1 renders yeast hypersensitive to overexpression of other co-chaperones.
P2860
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P2860
Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle.
description
2013 nî lūn-bûn
@nan
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
2013年论文
@zh
2013年论文
@zh-cn
name
Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle.
@en
type
label
Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle.
@en
prefLabel
Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle.
@en
P2093
P2860
P356
P1476
Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle.
@en
P2093
Jochen Reinstein
Johannes Buchner
P2860
P2888
P304
P356
10.1038/NSMB.2502
P577
2013-02-10T00:00:00Z