Asymmetric Hsp90 N domain SUMOylation recruits Aha1 and ATP-competitive inhibitors.
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Mechanisms of Hsp90 regulationDirect and/or Indirect Roles for SUMO in Modulating Alpha-Synuclein ToxicityTargeting Hsp90 in urothelial carcinomaMechanistic Asymmetry in Hsp90 DimersThe FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug bindingSelective targeting of the stress chaperome as a therapeutic strategyAn Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humansHsp90 C-terminal inhibitors exhibit antimigratory activity by disrupting the Hsp90α/Aha1 complex in PC3-MM2 cells.Sumoylated HSP90 is a dominantly inherited plasma cell dyscrasias risk factor.Structure-activity relationship in a purine-scaffold compound series with selectivity for the endoplasmic reticulum Hsp90 paralog Grp94Pharmacoproteomics identifies combinatorial therapy targets for diffuse large B cell lymphoma.c-Abl Mediated Tyrosine Phosphorylation of Aha1 Activates Its Co-chaperone Function in Cancer Cells.Chemical Tools to Investigate Mechanisms Associated with HSP90 and HSP70 in Disease.A Remodeled Hsp90 Molecular Chaperone Ensemble with the Novel Cochaperone Aarsd1 Is Required for Muscle Differentiation.Heat Shock Proteins Promote Cancer: It's a Protection RacketStructural and functional basis of protein phosphatase 5 substrate specificity.Heat Shock Protein (HSP) Drug Discovery and Development: Targeting Heat Shock Proteins in Disease.Extensive functional redundancy in the regulation of Candida albicans drug resistance and morphogenesis by lysine deacetylases Hos2, Hda1, Rpd3 and Rpd31.The dynamic interactome of human Aha1 upon Y223 phosphorylation.Activation of Hsp90 Enzymatic Activity and Conformational Dynamics through Rationally Designed Allosteric Ligands.Targeting the Diabetic Chaperome to Improve Peripheral Neuropathy.Alternative approaches to Hsp90 modulation for the treatment of cancer.Regulation of Cellular Processes by SUMO: Understudied Topics.The activity of the glucocorticoid receptor is regulated by SUMO conjugation to FKBP51.Protein SUMOylation is Involved in Cell-cycle Progression and Cell Morphology in Giardia lamblia.The Mechanism of Hsp90 ATPase Stimulation by Aha1Symmetry broken and rebroken during the ATP hydrolysis cycle of the mitochondrial Hsp90 TRAP1.Diverging Novobiocin Anti-Cancer Activity from Neuroprotective Activity through Modification of the Amide Tail.A Novel HSP90 Inhibitor-Drug Conjugate to SN38 Is Highly Effective in Small Cell Lung Cancer.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.Detecting Posttranslational Modifications of Hsp90.Methods to validate Hsp90 inhibitor specificity, to identify off-target effects, and to rethink approaches for further clinical development.The HSP90 chaperone machinery.Molecular mechanism of bacterial Hsp90 pH-dependent ATPase activity.A switch point in the molecular chaperone Hsp90 responding to client interaction.Mutation of essential Hsp90 co-chaperones SGT1 or CNS1 renders yeast hypersensitive to overexpression of other co-chaperones.Four-colour FRET reveals directionality in the Hsp90 multicomponent machinery.
P2860
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P2860
Asymmetric Hsp90 N domain SUMOylation recruits Aha1 and ATP-competitive inhibitors.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
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artigo científico
@pt
bilimsel makale
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scientific article published on January 2014
@en
vedecký článok
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vetenskaplig artikel
@sv
videnskabelig artikel
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vědecký článek
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name
Asymmetric Hsp90 N domain SUMOylation recruits Aha1 and ATP-competitive inhibitors.
@en
Asymmetric Hsp90 N domain SUMOylation recruits Aha1 and ATP-competitive inhibitors.
@nl
type
label
Asymmetric Hsp90 N domain SUMOylation recruits Aha1 and ATP-competitive inhibitors.
@en
Asymmetric Hsp90 N domain SUMOylation recruits Aha1 and ATP-competitive inhibitors.
@nl
prefLabel
Asymmetric Hsp90 N domain SUMOylation recruits Aha1 and ATP-competitive inhibitors.
@en
Asymmetric Hsp90 N domain SUMOylation recruits Aha1 and ATP-competitive inhibitors.
@nl
P2093
P2860
P50
P1433
P1476
Asymmetric Hsp90 N domain SUMOylation recruits Aha1 and ATP-competitive inhibitors.
@en
P2093
Anthony Hoang
Barry Panaretou
Dimitra Bourboulia
Elham Fotooh-Abadi
Gennady Bratslavsky
Jane B Trepel
Kristin Beebe
Len Neckers
Mehdi Mollapour
P2860
P304
P356
10.1016/J.MOLCEL.2013.12.007
P577
2014-01-01T00:00:00Z