Structure and function of molecular chaperone HSP90

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Transcript of Structure and function of molecular chaperone HSP90

Page 1: Structure and function of molecular chaperone HSP90
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Peroxisomal Proteostasis Involves a Lon Family Protein That Functions as Protease and Chaperone

Peroxisomal Proteostasis Involves a Lon Family Protein That Functions as Protease and Chaperone

Influence of the conserved disulphide bond, exposed to the putative binding pocket, on the structure and function of the immunoglobulin-like molecular chaperone Caf1M of Yersinia pestis

Influence of the conserved disulphide bond, exposed to the putative binding pocket, on the structure and function of the immunoglobulin-like molecular chaperone Caf1M of Yersinia pestis

Hsp90 inhibitors as new leads to target parasitic diarrheal diseases

Hsp90 inhibitors as new leads to target parasitic diarrheal diseases

MGR Hash Function

MGR Hash Function

Hsp90 Inhibition Accelerates Cell Lysis: ANTI-Hsp90 RIBOZYME REVEALS A COMPLEX MECHANISM OF Hsp90 INHIBITORS INVOLVING BOTH SUPEROXIDE- AND Hsp90-DEPENDENT EVENTS

Hsp90 Inhibition Accelerates Cell Lysis: ANTI-Hsp90 RIBOZYME REVEALS A COMPLEX MECHANISM OF Hsp90 INHIBITORS INVOLVING BOTH SUPEROXIDE- AND Hsp90-DEPENDENT EVENTS

Characterization of Arabidopsis thaliana AtFKBP42 that is membrane-bound and interacts with Hsp90

Characterization of Arabidopsis thaliana AtFKBP42 that is membrane-bound and interacts with Hsp90

Chaperone-like activity and hydrophobicity of α-crystallin

Chaperone-like activity and hydrophobicity of α-crystallin

Role for Hsp70 Chaperone in Saccharomyces cerevisiae Prion Seed Replication

Role for Hsp70 Chaperone in Saccharomyces cerevisiae Prion Seed Replication

Association between HSP90 and Her2 in Gastric and Gastroesophageal Carcinomas

Association between HSP90 and Her2 in Gastric and Gastroesophageal Carcinomas

Elucidation of the Hsp90 C-terminal inhibitor binding site

Elucidation of the Hsp90 C-terminal inhibitor binding site

Tuning of chaperone activity of Hsp70 proteins by modulation of nucleotide exchange

Tuning of chaperone activity of Hsp70 proteins by modulation of nucleotide exchange

Complex Function Theory

Complex Function Theory

DnaJ/hsp40 chaperone domain of SV40 large T antigen promotes efficient viral DNA replication

DnaJ/hsp40 chaperone domain of SV40 large T antigen promotes efficient viral DNA replication

Nucleotide utilization requirements that render ClpB active as a chaperone

Nucleotide utilization requirements that render ClpB active as a chaperone

Clusterin is a secreted mammalian chaperone

Clusterin is a secreted mammalian chaperone

Language Function

Language Function

The Smarandache Function

The Smarandache Function

Discovery of (2,4-Dihydroxy-5-isopropylphenyl)-[5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl]methanone (AT13387), a Novel Inhibitor of the Molecular Chaperone Hsp90 by

Discovery of (2,4-Dihydroxy-5-isopropylphenyl)-[5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl]methanone (AT13387), a Novel Inhibitor of the Molecular Chaperone Hsp90 by

Function – Installation

Function – Installation

Hop: An Hsp70/Hsp90 Co-Chaperone That Functions Within and Beyond Hsp70/Hsp90 Protein Folding Pathways

Hop: An Hsp70/Hsp90 Co-Chaperone That Functions Within and Beyond Hsp70/Hsp90 Protein Folding Pathways