Swe1Wee1-dependent tyrosine phosphorylation of Hsp90 regulates distinct facets of chaperone function. - Wikidata - wikimedia - TriplyDB

Swe1Wee1-dependent tyrosine phosphorylation of Hsp90 regulates distinct facets of chaperone function.

Swe1Wee1-dependent tyrosine phosphorylation of Hsp90 regulates distinct facets of chaperone function.

http://www.wikidata.org/entity/Q33669025

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Mechanisms of Hsp90 regulation Role of Heat-Shock Proteins in Cellular Function and in the Biology of Fungi The 'active life' of Hsp90 complexes Targeting Hsp90 in urothelial carcinoma Raf-interactome in tuning the complexity and diversity of Raf function.C-terminal phosphorylation of Hsp70 and Hsp90 regulates alternate binding to co-chaperones CHIP and HOP to determine cellular protein folding/degradation balances Posttranslational modification and conformational state of heat shock protein 90 differentially affect binding of chemically diverse small molecule inhibitors Threonine 22 phosphorylation attenuates Hsp90 interaction with cochaperones and affects its chaperone activity The co-chaperone Hch1 regulates Hsp90 function differently than its homologue Aha1 and confers sensitivity to yeast to the Hsp90 inhibitor NVP-AUY922 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.An Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humans WEE1 inhibition sensitizes osteosarcoma to radiotherapy 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.H2B Tyr37 phosphorylation suppresses expression of replication-dependent core histone genes iTRAQ-based quantitative proteome and phosphoprotein characterization reveals the central metabolism changes involved in wheat grain development.The molecular chaperone Hsp90 is required for cell cycle exit in Drosophila melanogaster.An in vivo photo-cross-linking approach reveals a homodimerization domain of Aha1 in S. cerevisiae 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 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.Hsp90 molecular chaperone inhibitors: are we there yet?Complex regulation of Hsf1-Skn7 activities by the catalytic subunits of PKA in Saccharomyces cerevisiae: experimental and computational evidences.Advances in the discovery and development of heat-shock protein 90 inhibitors for cancer treatment.The Effects of Hsp90α1 Mutations on Myosin Thick Filament Organization The response to heat shock and oxidative stress in Saccharomyces cerevisiae Nitration of Hsp90 on Tyrosine 33 Regulates Mitochondrial Metabolism Safety control for apoptotic irreversibility Combined inhibition of Wee1 and Hsp90 activates intrinsic apoptosis in cancer cells Tumor-intrinsic and tumor-extrinsic factors impacting hsp90- targeted therapy.Uncovering a region of heat shock protein 90 important for client binding in E. coli and chaperone function in yeast.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.Interaction of heat shock protein 90 and the co-chaperone Cpr6 with Ura2, a bifunctional enzyme required for pyrimidine biosynthesis Hsp90, an unlikely ally in the war on cancer.The Role of Sulfhydryl Reactivity of Small Molecules for the Activation of the KEAP1/NRF2 Pathway and the Heat Shock Response Wee1 kinase as a target for cancer therapy.The regulatory mechanism of a client kinase controlling its own release from Hsp90 chaperone machinery through phosphorylation

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Swe1Wee1-dependent tyrosine phosphorylation of Hsp90 regulates distinct facets of chaperone function.

http://www.wikidata.org/entity/Q33669025

description

2010 nî lūn-bûn

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2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年学术文章

@wuu

2010年学术文章

@zh-cn

2010年学术文章

@zh-hans

2010年学术文章

@zh-my

2010年学术文章

@zh-sg

2010年學術文章

@yue

name

Swe1Wee1-dependent tyrosine ph ...... facets of chaperone function.

@ast

Swe1Wee1-dependent tyrosine ph ...... facets of chaperone function.

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type

label

Swe1Wee1-dependent tyrosine ph ...... facets of chaperone function.

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Swe1Wee1-dependent tyrosine ph ...... facets of chaperone function.

@en

prefLabel

Swe1Wee1-dependent tyrosine ph ...... facets of chaperone function.

@ast

Swe1Wee1-dependent tyrosine ph ...... facets of chaperone function.

@en

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J.MOLCEL.2010.01.005

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Swe1Wee1-dependent tyrosine ph ...... facets of chaperone function.

@en

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Alison C Donnelly

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

Barry Panaretou

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

Bradley T Scroggins

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

Brian S Blagg

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

Dimitra Bourboulia

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

Giorgio Colombo

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

Giulia Morra

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

Jane B Trepel

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

Kristin Beebe

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

Laurence H Pearl

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

P2860

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

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

Human Wee1 kinase inhibits cell division by phosphorylating p34cdc2 exclusively on Tyr15

Modeling signal propagation mechanisms and ligand-based conformational dynamics of the Hsp90 molecular chaperone full-length dimer

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

Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone

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

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

In vivo analysis of the Hsp90 cochaperone Sti1 (p60)

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333-343

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scholarly article

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10.1016/J.MOLCEL.2010.01.005

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3

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37

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Chrisostomos Prodromou

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2010-02-01T00:00:00Z

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41451350

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20159553

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phosphorylation

molecular chaperones

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2824606

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