ESTG binds the ESR:chaperone complex - Wikidata - thesis-toulmin - TriplyDB

ESTG binds the ESR:chaperone complex

ESTG binds the ESR:chaperone complex

http://www.wikidata.org/entity/Q55219860

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ESR-mediated signaling

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Q55230930-2C745049-D819-48DD-875B-D8D2EECF1EA4

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ESTG binds the ESR:chaperone complex

http://www.wikidata.org/entity/Q55219860

description

An instance of the biological ...... perone complex in Homo sapiens

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biologisch proces

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name

ESTG binds the ESR:chaperone complex

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type

label

ESTG binds the ESR:chaperone complex

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prefLabel

ESTG binds the ESR:chaperone complex

@en

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In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis

Role for Hsp90-associated cochaperone p23 in estrogen receptor signal transduction

The N-terminal adenosine triphosphate binding domain of Hsp90 is necessary and sufficient for interaction with estrogen receptor

Estrogen receptor transcription and transactivation: Structure-function relationship in DNA- and ligand-binding domains of estrogen receptors

The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation

Steroid receptor interactions with heat shock protein and immunophilin chaperones

Estrogen receptor beta--a new dimension in estrogen mechanism of action.

ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo.

Molecular mechanisms of estrogen action: selective ligands and receptor pharmacology.

Common non-hormone binding component in non-transformed chick oviduct receptors of four steroid hormones.

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reactome:R-HSA-8939204

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biological process

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ESR-mediated signaling

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R-HSA-8939204

http://www.w3.org/2001/XMLSchema#string

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ESRs:chaperone complex

ESTG:ESRs:chaperone complex

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