dc.creatorda Silva, Viviane C H
dc.creatorRamos, Carlos H I
dc.date2012-Jun
dc.date2015-11-27T13:28:08Z
dc.date2015-11-27T13:28:08Z
dc.date.accessioned2018-03-29T01:14:43Z
dc.date.available2018-03-29T01:14:43Z
dc.identifierJournal Of Proteomics. v. 75, n. 10, p. 2790-802, 2012-Jun.
dc.identifier1876-7737
dc.identifier10.1016/j.jprot.2011.12.028
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/22236519
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/199839
dc.identifier22236519
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1300072
dc.descriptionIn the cell, proteins interact within a network in which a small number of proteins are highly connected nodes or hubs. A disturbance in the hub proteins usually has a higher impact on the cell physiology than a disturbance in poorly connected nodes. In eukaryotes, the cytosolic Hsp90 is considered to be a hub protein as it interacts with molecular chaperones and co-chaperones, and has key regulatory proteins as clients, such as transcriptional factors, protein kinases and hormone receptors. The large number of Hsp90 partners suggests that Hsp90 is involved in very important functions, such as signaling, proteostasis and epigenetics. Some of these functions are dysregulated in cancer, making Hsp90 a potential target for therapeutics. The number of Hsp90 interactors appears to be so large that a precise answer to the question of how many proteins interact with this chaperone has no definitive answer yet, not even if the question refers to specific Hsp90s as one of the human cytosolic forms. Here we review the major chaperones and co-chaperones that interact with cytosolic Hsp90s, highlighting the latest findings regarding client proteins and the role that posttranslational modifications have on the function and interactions of these molecular chaperones. This article is part of a Special Issue entitled: Proteomics: The clinical link.
dc.description75
dc.description2790-802
dc.languageeng
dc.relationJournal Of Proteomics
dc.relationJ Proteomics
dc.rightsfechado
dc.rightsCopyright © 2011 Elsevier B.V. All rights reserved.
dc.sourcePubMed
dc.subjectAmino Acid Sequence
dc.subjectCytosol
dc.subjectHsp90 Heat-shock Proteins
dc.subjectHumans
dc.subjectModels, Molecular
dc.subjectMolecular Chaperones
dc.subjectMolecular Sequence Data
dc.subjectMolecular Targeted Therapy
dc.subjectNeoplasms
dc.subjectProtein Binding
dc.subjectProtein Interaction Domains And Motifs
dc.subjectProtein Interaction Mapping
dc.subjectSequence Homology, Amino Acid
dc.titleThe Network Interaction Of The Human Cytosolic 90 Kda Heat Shock Protein Hsp90: A Target For Cancer Therapeutics.
dc.typeArtículos de revistas


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