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Article

In vivo potentiation of human oestrogen receptor alpha by Cdk7-mediated phosphorylation.

Genes to cells : devoted to molecular & cellular mechanisms - 1 Oct 2004

Ito Saya, Takeyama Ken-ichi, Yamamoto Ayako, Sawatsubashi Shun, Shirode Yuko, Kouzmenko Alexander, Tabata Tetsuya, Kato Shigeaki

Abstract excerpt

Phosphorylation of the Ser(118) residue in the N-terminal A/B domain of the human oestrogen receptor alpha (hERalpha) by mitogen-activated protein kinase (MAPK), stimulated via growth factor signalling pathways, is known to potentiate ERalpha ligand-induced transactivation function. Besides MAPK, cyclin dependent kinase 7 (Cdk7) in the TFIIH complex has also been found to potentiate hERalpha transactivation in...

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PMID: 15461668
DOI: 10.1111/j.1365-2443.2004.00777.x

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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In vivo potentiation of human oestrogen receptor alpha by Cdk7-mediated phosphorylation.PMID 15461668Read ↗

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