(PDF) Deep Structural Analysis of RPAP3 and PIH1D1, Two

Deep Structural Analysis of RPAP3 and PIH1D1, Two Components of the HSP90 Co-Chaperone R2TP Complex

Structure - United States

doi 10.1016/j.str.2018.06.002

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Date

September 1, 2018

Authors

Christelle Aigueperse

Florian Georgescauld

Franck Vandermoere

Rénette Saint-Fort

Isabelle Behm-Ansmant

Bruno Charpentier

Bérengère Pradet-Balade

Publisher

Elsevier BV

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Deep Structural Analysis of RPAP3 and PIH1D1, Two Components of the HSP90 Co-Chaperone R2TP Complex

Structure - United States

doi 10.1016/j.str.2018.06.002

Full Text

Abstract

Categories

Date

Authors

Publisher

Related search

RPAP3 Provides a Flexible Scaffold for Coupling HSP90 to the Human R2TP Co-Chaperone Complex

Structural Insights Into the Regulation Mechanism of HSP90 by Co-Chaperone AHA1

Structural Mechanism for Regulation of the AAA-ATPases RUVBL1-RUVBL2 in the R2TP Co-Chaperone Revealed by Cryo-Em

The Hsp90 Kinase Co-Chaperone Cdc37 Regulates Tau Stability and Phosphorylation Dynamics

Stability of the Human Hsp90-P50Cdc37 Chaperone Complex Against Nucleotides and Hsp90 Inhibitors, and the Influence of Phosphorylation by Casein Kinase 2

Conformational Dynamics of the Molecular Chaperone Hsp90

The Hsp90 Chaperone Complex Is Both a Facilitator and a Repressor of the dsRNA-dependent Kinase PKR

Polypeptide Release by Hsp90 Involves ATP Hydrolysis and Is Enhanced by the Co-Chaperone P23

The Sch9 Protein Kinase Regulates Hsp90 Chaperone Complex Signal Transduction Activity in Vivo