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Publications by Rafael Núñez-Ramírez

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

Nature Communications

English

Image Processing for Electron Microscopy Single-Particle Analysis Using XMIPP

English

Related publications

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

English

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

Biophysical Journal

Biophysics

2018

English

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

Theoretical Chemistry

Pharmaceutical Science

English

Crystal Structure of the PXR–T1317 Complex Provides a Scaffold to Examine the Potential for Receptor Antagonism

Bioorganic and Medicinal Chemistry

Clinical Biochemistry

Pharmaceutical Science

Drug Discovery

2007

English

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

Journal of Biological Chemistry

English

Targeting the Hsp90-Cdc37-Client Protein Interaction to Disrupt Hsp90 Chaperone Machinery

Journal of Hematology and Oncology

English

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

Science advances

Multidisciplinary

2019

English

Toxoplasma Gondii Sis1-Like J-Domain Protein Is a Cytosolic Chaperone Associated to HSP90/HSP70 Complex

International Journal of Biological Macromolecules

English

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

English

Amanote Research

Discover open access scientific publications

Search, annotate, share and cite publications

Publications by Rafael Núñez-Ramírez

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

Image Processing for Electron Microscopy Single-Particle Analysis Using XMIPP

Related publications

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

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

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

Crystal Structure of the PXR–T1317 Complex Provides a Scaffold to Examine the Potential for Receptor Antagonism

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

Targeting the Hsp90-Cdc37-Client Protein Interaction to Disrupt Hsp90 Chaperone Machinery

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

Toxoplasma Gondii Sis1-Like J-Domain Protein Is a Cytosolic Chaperone Associated to HSP90/HSP70 Complex

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