Threonine 22 phosphorylation attenuates Hsp90 interaction with cochaperones and affects its chaperone activity - Wikidata - wikimedia - TriplyDB

Threonine 22 phosphorylation attenuates Hsp90 interaction with cochaperones and affects its chaperone activity

Threonine 22 phosphorylation attenuates Hsp90 interaction with cochaperones and affects its chaperone activity

http://www.wikidata.org/entity/Q28307703

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Mechanisms of Hsp90 regulation The 'active life' of Hsp90 complexes Raf-interactome in tuning the complexity and diversity of Raf function.The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding Posttranslational modification and conformational state of heat shock protein 90 differentially affect binding of chemically diverse small molecule inhibitors Mapping the Hsp90 genetic interaction network in Candida albicans reveals environmental contingency and rewired circuitry The co-chaperone Hch1 regulates Hsp90 function differently than its homologue Aha1 and confers sensitivity to yeast to the Hsp90 inhibitor NVP-AUY922 Regulation and function of the human HSP90AA1 gene LPS induces pp60c-src-mediated tyrosine phosphorylation of Hsp90 in lung vascular endothelial cells and mouse lung.Differential 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.Δ9-THC increases endogenous AHA1 expression in rat cerebellum and may modulate CB1 receptor function during chronic use Toxoplasma gondii Hsp90: potential roles in essential cellular processes of the parasite.Probing molecular mechanisms of the Hsp90 chaperone: biophysical modeling identifies key regulators of functional dynamics.De-acetylation and degradation of HSPA5 is critical for E1A metastasis suppression in breast cancer cells.The molecular chaperone Hsp90 is required for cell cycle exit in Drosophila melanogaster.HSP90 functions in the circadian clock through stabilization of the client F-box protein ZEITLUPE.Stability of the human Hsp90-p50Cdc37 chaperone complex against nucleotides and Hsp90 inhibitors, and the influence of phosphorylation by casein kinase 2 UBR1 promotes protein kinase quality control and sensitizes cells to Hsp90 inhibition.Post-translational modifications of Hsp90 and their contributions to chaperone regulation Casein kinase 2 phosphorylation of Hsp90 threonine 22 modulates chaperone function and drug sensitivity.Charged linker sequence modulates eukaryotic heat shock protein 90 (Hsp90) chaperone activity Quantitative proteomics of the yeast Hsp70/Hsp90 interactomes during DNA damage reveal chaperone-dependent regulation of ribonucleotide reductase.The Effects of Hsp90α1 Mutations on Myosin Thick Filament Organization Dual action antifungal small molecule modulates multidrug efflux and TOR signaling c-Abl Mediated Tyrosine Phosphorylation of Aha1 Activates Its Co-chaperone Function in Cancer Cells.Fungal Hsp90: a biological transistor that tunes cellular outputs to thermal inputs.Mps1 Mediated Phosphorylation of Hsp90 Confers Renal Cell Carcinoma Sensitivity and Selectivity to Hsp90 Inhibitors.The myosin-binding UCS domain but not the Hsp90-binding TPR domain of the UNC-45 chaperone is essential for function in Caenorhabditis elegans Comprehensive Analysis of the Membrane Phosphoproteome Regulated by Oligogalacturonides in Arabidopsis thaliana Structural and functional basis of protein phosphatase 5 substrate specificity.Hsp90, an unlikely ally in the war on cancer.The regulatory mechanism of a client kinase controlling its own release from Hsp90 chaperone machinery through phosphorylation Extensive functional redundancy in the regulation of Candida albicans drug resistance and morphogenesis by lysine deacetylases Hos2, Hda1, Rpd3 and Rpd31.Asymmetric Hsp90 N domain SUMOylation recruits Aha1 and ATP-competitive inhibitors.Biochemistry, proteomics, and phosphoproteomics of plant mitochondria from non-photosynthetic cells Contributions of co-chaperones and post-translational modifications towards Hsp90 drug sensitivity.Molecular cochaperones: tumor growth and cancer treatment.Probing the N-terminal sequence of spinach PsbO: evidence that essential threonine residues bind to different functional sites in eukaryotic photosystem II.HSP90 promotes Burkitt lymphoma cell survival by maintaining tonic B-cell receptor signaling.

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P2860

Threonine 22 phosphorylation attenuates Hsp90 interaction with cochaperones and affects its chaperone activity

http://www.wikidata.org/entity/Q28307703

description

2011 nî lūn-bûn

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2011 թուականի Մարտին հրատարակուած գիտական յօդուած

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2011 թվականի մարտին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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Threonine 22 phosphorylation a ...... affects its chaperone activity

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Threonine 22 phosphorylation a ...... affects its chaperone activity

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Threonine 22 phosphorylation a ...... affects its chaperone activity

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J.MOLCEL.2011.02.011

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Threonine 22 phosphorylation a ...... affects its chaperone activity

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Andrew W Truman

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Anna Konstantinova

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Barry Panaretou

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Cara K Vaughan

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Jane B Trepel

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Len Neckers

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Mehdi Mollapour

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Peter W Piper

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Shinji Tsutsumi

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Srinivas Vourganti

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

P2860

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

A two-hybrid screen of the yeast proteome for Hsp90 interactors uncovers a novel Hsp90 chaperone requirement in the activity of a stress-activated mitogen-activated protein kinase, Slt2p (Mpk1p).

Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase.

Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast.

The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90

Intra- and intermonomer interactions are required to synergistically facilitate ATP hydrolysis in Hsp90.

Targeting the dynamic HSP90 complex in cancer

Structure and mechanism of the Hsp90 molecular chaperone machinery

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672-81

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406034

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10.1016/J.MOLCEL.2011.02.011

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6

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Chrisostomos Prodromou

Laurence H Pearl

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2011-03-18T00:00:00Z

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50592989

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21419342

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phosphorylation

molecular chaperones

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3062913

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