about
The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug bindingc-Abl Mediated Tyrosine Phosphorylation of Aha1 Activates Its Co-chaperone Function in Cancer Cells.Mps1 Mediated Phosphorylation of Hsp90 Confers Renal Cell Carcinoma Sensitivity and Selectivity to Hsp90 Inhibitors.Sixth BHD Symposium and First International Upstate Kidney Cancer Symposium: latest scientific and clinical discoveries.Structural and functional basis of protein phosphatase 5 substrate specificity.Asymmetric Hsp90 N domain SUMOylation recruits Aha1 and ATP-competitive inhibitors.The dynamic interactome of human Aha1 upon Y223 phosphorylation.Valproic Acid Alters Angiogenic and Trophic Gene Expression in Human Prostate Cancer Models.Impact of Posttranslational Modifications on the Anticancer Activity of Hsp90 Inhibitors.Targeting Hsp90 in Non-Cancerous Maladies.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.Detecting Posttranslational Modifications of Hsp90.CIP2A and PP2A in human leptomeninges, arachnoid granulations and meningiomas.Sporadic renal angiomyolipoma in a patient with Birt-Hogg-Dubé: chaperones in pathogenesis.The mTOR Independent Function of Tsc1 and FNIPsPost-translational Regulation of FNIP1 Creates a Rheostat for the Molecular Chaperone Hsp90Mutation of the co-chaperone Tsc1 in bladder cancer diminishes Hsp90 acetylation and reduces drug sensitivity and selectivityExtracellular Phosphorylation of TIMP-2 by Secreted c-Src Tyrosine Kinase Controls MMP-2 ActivityCo-chaperones TIMP2 and AHA1 Competitively Regulate Extracellular HSP90:Client MMP2 Activity and Matrix ProteolysisDesign of Disruptors of the Hsp90-Cdc37 Interface
P50
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P50
description
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Mark R Woodford
@ast
Mark R Woodford
@en
Mark R Woodford
@es
Mark R Woodford
@nl
type
label
Mark R Woodford
@ast
Mark R Woodford
@en
Mark R Woodford
@es
Mark R Woodford
@nl
prefLabel
Mark R Woodford
@ast
Mark R Woodford
@en
Mark R Woodford
@es
Mark R Woodford
@nl
P106
P21
P31
P496
0000-0002-6737-2832