Asymmetric Hsp90 N domain SUMOylation recruits Aha1 and ATP-competitive inhibitors. - Wikidata - wikimedia - TriplyDB

Asymmetric Hsp90 N domain SUMOylation recruits Aha1 and ATP-competitive inhibitors.

Asymmetric Hsp90 N domain SUMOylation recruits Aha1 and ATP-competitive inhibitors.

http://www.wikidata.org/entity/Q37661597

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Mechanisms of Hsp90 regulation Direct and/or Indirect Roles for SUMO in Modulating Alpha-Synuclein Toxicity Targeting Hsp90 in urothelial carcinoma Mechanistic Asymmetry in Hsp90 Dimers The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding Selective targeting of the stress chaperome as a therapeutic strategy An Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humans Hsp90 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 Grp94 Pharmacoproteomics 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 Racket Structural 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 Aha1 Symmetry 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.

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Asymmetric Hsp90 N domain SUMOylation recruits Aha1 and ATP-competitive inhibitors.

http://www.wikidata.org/entity/Q37661597

description

article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on January 2014

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

@cs

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

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J.MOLCEL.2013.12.007

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Asymmetric Hsp90 N domain SUMOylation recruits Aha1 and ATP-competitive inhibitors.

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Ailan Guo

http://www.w3.org/2001/XMLSchema#string

Anthony Hoang

http://www.w3.org/2001/XMLSchema#string

Barry Panaretou

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Dimitra Bourboulia

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Elham Fotooh-Abadi

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Gennady Bratslavsky

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Jane B Trepel

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Kristin Beebe

http://www.w3.org/2001/XMLSchema#string

Len Neckers

http://www.w3.org/2001/XMLSchema#string

Mehdi Mollapour

http://www.w3.org/2001/XMLSchema#string

P2860

In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis

Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone

Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis

Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1

Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome

The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains

The 'active life' of Hsp90 complexes

Function and regulation of SUMO proteases

Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions

Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent

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317-329

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scholarly article

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10.1016/J.MOLCEL.2013.12.007

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2

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53

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Chrisostomos Prodromou

William G Stetler-Stevenson

Mark R Woodford

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2014-01-01T00:00:00Z

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259916853

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24462205

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3964875

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