Ubc9 interacts with the androgen receptor and activates receptor-dependent transcription (Q28138255)

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P Aarnisalo

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U Karvonen

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J J Palvimo

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O A Jänne

Journal of Biological Chemistry

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language of work or name

English

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publication date

2 July 1999

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published in

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volume

274

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issue

27

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page(s)

19441-6

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cites work

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Androgen receptor-mediated transcriptional regulation in the absence of direct interaction with a specific DNA element

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Mutual transcriptional interference between RelA and androgen receptor

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The partial agonist activity of antagonist-occupied steroid receptors is controlled by a novel hinge domain-binding coactivator L7/SPA and the corepressors N-CoR or SMRT

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Activation of androgen receptor function by a novel nuclear protein kinase

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TLS (Translocated-in-Liposarcoma) Is a High-Affinity Interactor for Steroid, Thyroid Hormone, and Retinoid Receptors

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A testis-specific androgen receptor coregulator that belongs to a novel family of nuclear proteins

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The function of steroid hormone receptors is inhibited by the hsp90-specific compound geldanamycin

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Ubch9 conjugates SUMO but not ubiquitin

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Ubc9p is the conjugating enzyme for the ubiquitin-like protein Smt3p

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Preferential interaction of sentrin with a ubiquitin-conjugating enzyme, Ubc9.

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The ubiquitin-like proteins SMT3 and SUMO-1 are conjugated by the UBC9 E2 enzyme

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Molecular cloning of the cDNA and chromosome localization of the gene for human ubiquitin-conjugating enzyme 9

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