{"doi":"10.1002/jcp.1131","title":"Hsp90: Chaperoning signal transduction","abstract":"<jats:title>Abstract</jats:title><jats:p>Hsp90 is an ATP dependent molecular chaperone involved in the folding and activation of an unknown number of substrate proteins. These substrate proteins include protein kinases and transcription factors. Consistent with this task, Hsp90 is an essential protein in all eucaryotes. The interaction of Hsp90 with its substrate proteins involves the transient formation of multiprotein complexes with a set of highly conserved partner proteins. The specific function of each component in the processing of substrates is still unknown. Large ATP‐dependent conformational changes of Hsp90 occur during the hydrolysis reaction and these changes are thought to drive the chaperone cycle. Natural inhibitors of the ATPase activity, like geldanamycin and radicicol, block the processing of Hsp90 substrate proteins. As many of these substrates are critical elements in signal transduction, Hsp90 seems to introduce an additional level of regulation. © 2001 Wiley‐Liss, Inc.</jats:p>","journal":"Journal of Cellular Physiology","year":2001,"id":22930,"datarank":14.894735357964569,"base_score":6.359573868672378,"endowment":6.359573868672378,"self_citation_contribution":0.9539360803008567,"citation_network_contribution":13.940799277663713,"self_endowment_contribution":0.9539360803008567,"citer_contribution":13.940799277663713,"corpus_percentile":null,"corpus_rank":null,"citation_count":577,"citer_count":200,"citers_with_citation_signal":200,"citers_with_endowment":200,"datacite_reuse_total":6,"is_dataset":false,"is_dataset_confidence":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":141322,"name":"Johannes 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shock proteins research","Computational Drug Discovery Methods","Plant biochemistry and biosynthesis","Biology","Medicine","Adenosine Triphosphatases","Adenosine Triphosphate","Amino Acid Motifs","Animals","Enzyme Inhibitors","HSP90 Heat-Shock Proteins","Humans","Models, Molecular","Phosphotransferases","Protein Binding","Protein Conformation","Protein-Tyrosine Kinases","Signal Transduction"],"mesh_terms":["Adenosine Triphosphatases","Adenosine Triphosphate","Animals","Enzyme Inhibitors","Humans","Models, Molecular","Phosphotransferases","Protein Binding","Protein Conformation","Protein-Tyrosine Kinases","Signal Transduction","HSP90 Heat-Shock Proteins","Amino Acid Motifs"],"keywords":["Hsp90","Geldanamycin","CDC37","Chaperone (clinical)","Co-chaperone","Cell biology","Signal transduction","Biochemistry","Biology","ATP hydrolysis","Protein folding","ATPase","Chemistry","Enzyme","Heat shock 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