Phosphorylation of steroidogenic factor 1 is mediated by cyclin-dependent kinase 7.

No abstract is available for this paper.

• Publication year

  2008

• Venue

  Molecular Endocrinology

• Publication date

  Unknown publication date

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1210/ME.2006-0478PMID 17901130PMCID PMC5419630
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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• Cyclin H binding to the RARalpha activation function (AF)-2 domain directs phosphorylation of the AF-1 domain by cyclin-dependent kinase 7.

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• cAMP-dependent Protein Kinase Enhances CYP17 Transcription via MKP-1 Activation in H295R Human Adrenocortical Cells*

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• The nuclear receptor coactivators p300/CBP/cointegrator-associated protein (p/CIP) and transcription intermediary factor 2 (TIF2) differentially regulate PKA-stimulated transcriptional activity of steroidogenic factor 1.

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  2000influential reference
• Phosphorylation of human progesterone receptors at serine-294 by mitogen-activated protein kinase signals their degradation by the 26S proteasome.

  2000cited by this paper
• Activation of estrogen receptor alpha by S118 phosphorylation involves a ligand-dependent interaction with TFIIH and participation of CDK7.

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• Regulation of the Transcriptional Activity of the Peroxisome Proliferator-activated Receptor α by Phosphorylation of a Ligand-independent trans-Activating Domain*

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• Identification of a Novel Inhibitor of Mitogen-activated Protein Kinase Kinase*

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