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Details on Person ESTG binds ESR1:chaperone complex
Class:Id Reaction:8939204 _displayName ESTG binds ESR1:chaperone complex _doRelease TRUE _timestamp 2020-12-15 16:01:35 authored [InstanceEdit:9024061] Rothfels, Karen, 2017-09-29 compartment [Compartment:7660] nucleoplasm created [InstanceEdit:8939206] Rothfels, Karen, 2016-09-16 edited [InstanceEdit:9027686] Rothfels, Karen, 2017-11-03 input [SimpleEntity:1254400] ESTG [nucleoplasm] [Complex:8939185] ESR1:chaperone complex [nucleoplasm] [Homo sapiens] isChimeric FALSE literatureReference [LiteratureReference:8937339] The biological role of estrogen receptors alpha and beta in cancer [LiteratureReference:8937285] Estrogen receptor beta--a new dimension in estrogen mechanism of action [LiteratureReference:8937355] Tissue-specific expression pattern of estrogen receptors (ER): quantification of ER alpha and ER beta mRNA with real-time RT-PCR [LiteratureReference:8937263] Breast cancer, estrogen receptor and ligands [LiteratureReference:8937286] Estrogen receptor transcription and transactivation: Structure-function relationship in DNA- and ligand-binding domains of estrogen receptors [LiteratureReference:8937258] Activities of estrogen receptor alpha- and beta-selective ligands at diverse estrogen responsive gene sites mediating transactivation or transrepression [LiteratureReference:8937307] Molecular mechanisms of estrogen action: selective ligands and receptor pharmacology [LiteratureReference:8937273] Common non-hormone binding component in non-transformed chick oviduct receptors of four steroid hormones [LiteratureReference:8937319] Subunit structure of the nonactivated human estrogen receptor [LiteratureReference:8937314] Role for Hsp90-associated cochaperone p23 in estrogen receptor signal transduction [LiteratureReference:8937324] The N-terminal adenosine triphosphate binding domain of Hsp90 is necessary and sufficient for interaction with estrogen receptor [LiteratureReference:8937277] Control of estrogen receptor ligand binding by Hsp90 [LiteratureReference:8937345] The cochaperone p23 differentially regulates estrogen receptor target genes and promotes tumor cell adhesion and invasion [LiteratureReference:8937304] Minireview: the intersection of steroid receptors with molecular chaperones: observations and questions [LiteratureReference:8937317] Steroid receptor interactions with heat shock protein and immunophilin chaperones [LiteratureReference:8937335] The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation [LiteratureReference:8937253] ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo [LiteratureReference:8937300] In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis modified [InstanceEdit:9024086] Rothfels, Karen, 2017-09-29 [InstanceEdit:9028396] Rothfels, Karen, 2017-11-07 [InstanceEdit:9029195] Rothfels, Karen, 2017-11-14 [InstanceEdit:9038171] Rothfels, Karen, 2018-02-23 [InstanceEdit:9038275] Rothfels, Karen, 2018-02-23 [InstanceEdit:9709548] Jassal, Bijay, 2020-12-15 [InstanceEdit:9830342] Matthews, Lisa, 2023-03-08 name ESTG binds ESR1:chaperone complex output [Complex:8939191] ESTG:ESR1:chaperone complex [nucleoplasm] [Homo sapiens] precedingEvent
releaseDate 2018-03-21 reviewed [InstanceEdit:9038169] Magnani, Luca, 2018-02-23 reviewStatus [ReviewStatus:9821382] five stars species [Species:48887] Homo sapiens stableIdentifier [StableIdentifier:8939210] R-HSA-8939204.3 summation [Summation:8939195] In the nucleus, estrogens bind to estrogen receptors, member... (hasEvent) [Pathway:8939211] ESR-mediated signaling [Homo sapiens] (precedingEvent) [Reaction:8939203] HSP90-dependent ATP hydrolysis promotes release of ESR:ESTG from chaperone complex [Homo sapiens]
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