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Article

A proteomic investigation of ligand-dependent HSP90 complexes reveals CHORDC1 as a novel ADP-dependent HSP90-interacting protein.

Molecular & cellular proteomics : MCP - 1 Feb 2010

Gano Jacob J, Simon Julian A

Abstract excerpt

Structural studies of the chaperone HSP90 have revealed that nucleotide and drug ligands induce several distinct conformational states; however, little is known how these conformations affect interactions with co-chaperones and client proteins. Here we use tandem affinity purification and LC-MS/MS to investigate the proteome-wide effects of ATP, ADP, and geldanamycin on the constituents of the human HSP90...

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Source

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Identifiers

PMID: 19875381
DOI: 10.1074/mcp.M900261-MCP200
PMCID: PMC2830838

Genes

CHORDC1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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