Mps1 Mediated Phosphorylation of Hsp90 Confers Renal Cell Carcinoma Sensitivity and Selectivity to Hsp90 Inhibitors. - Wikidata - wikimedia - TriplyDB

Mps1 Mediated Phosphorylation of Hsp90 Confers Renal Cell Carcinoma Sensitivity and Selectivity to Hsp90 Inhibitors.

Mps1 Mediated Phosphorylation of Hsp90 Confers Renal Cell Carcinoma Sensitivity and Selectivity to Hsp90 Inhibitors.

http://www.wikidata.org/entity/Q36951574

about

The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding Structural and functional basis of protein phosphatase 5 substrate specificity.STA-8666, a novel HSP90 inhibitor/SN-38 drug conjugate, causes complete tumor regression in preclinical mouse models of pediatric sarcoma.Critical Roles of Dual-Specificity Phosphatases in Neuronal Proteostasis and Neurological Diseases.Phosphorylation and Ubiquitination Regulate Protein Phosphatase 5 Activity and Its Prosurvival Role in Kidney Cancer.Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facilitates folding of kinase and non-kinase clients.Clinical Evaluation and Biomarker Profiling of Hsp90 Inhibitors.Detecting Posttranslational Modifications of Hsp90.Proteomic interrogation of HSP90 and insights for medical research.Endogenous epitope tagging of heat shock protein 70 isoform Hsc70 using CRISPR/Cas9.Methods to validate Hsp90 inhibitor specificity, to identify off-target effects, and to rethink approaches for further clinical development.Sporadic renal angiomyolipoma in a patient with Birt-Hogg-Dubé: chaperones in pathogenesis.

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P2860

Mps1 Mediated Phosphorylation of Hsp90 Confers Renal Cell Carcinoma Sensitivity and Selectivity to Hsp90 Inhibitors.

http://www.wikidata.org/entity/Q36951574

description

2016 nî lūn-bûn

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2016年の論文

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2016年論文

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2016年論文

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2016年論文

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2016年論文

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2016年论文

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2016年论文

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2016年论文

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Mps1 Mediated Phosphorylation ...... lectivity to Hsp90 Inhibitors.

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Mps1 Mediated Phosphorylation ...... lectivity to Hsp90 Inhibitors.

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Mps1 Mediated Phosphorylation ...... lectivity to Hsp90 Inhibitors.

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J.CELREP.2015.12.084

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Mps1 Mediated Phosphorylation ...... lectivity to Hsp90 Inhibitors.

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Barry Panaretou

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Dawn E Post

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Dimitra Bourboulia

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Donald Wolfgeher

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Gennady Bratslavsky

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Jane B Trepel

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Kristin Beebe

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Len Neckers

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

Mehdi Mollapour

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Mourad Abouelleil

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P2860

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

Targeting the mitotic checkpoint for cancer therapy with NMS-P715, an inhibitor of MPS1 kinase

The spindle-assembly checkpoint in space and time

Cdc55p, the B-type regulatory subunit of protein phosphatase 2A, has multiple functions in mitosis and is required for the kinetochore/spindle checkpoint in Saccharomyces cerevisiae.

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

Activation of the budding yeast spindle assembly checkpoint without mitotic spindle disruption.

The yeast CDC37 gene interacts with MPS1 and is required for proper execution of spindle pole body duplication.

Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1

Stressing the development of small molecules targeting HSP90

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

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872-884

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scholarly article

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10.1016/J.CELREP.2015.12.084

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4

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14

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Chrisostomos Prodromou

Stephen J. Kron

Andrew W Truman

Mark R Woodford

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2016-01-19T00:00:00Z

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291419680

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26804907

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4887101

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