PRMT2, a member of the protein arginine methyltransferase family, is a coactivator of the androgen receptor (Q24313208)

Protein arginine methyltransferase 2

GOA release 2020-03-11

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regulation of androgen receptor signaling pathway

GOA release 2020-03-11

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The Journal of Steroid Biochemistry and Molecular Biology

GOA release 2020-03-11

author name string

Rene Meyer

series ordinal

1

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Siegmund S Wolf

series ordinal

2

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Maik Obendorf

series ordinal

3

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language of work or name

English

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publication date

October 2007

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published in

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volume

107

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page(s)

1-14

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issue

1-2

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cites work

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Characterization of the nontransformed and transformed androgen receptor and heat shock protein 90 with high-performance hydrophobic-interaction chromatography

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SH3 domains direct cellular localization of signaling molecules

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Steroid hormone receptors: many actors in search of a plot

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Actin monomer enhances supervillin-modulated androgen receptor transactivation.

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Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53

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Arginine methylation an emerging regulator of protein function

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WW and SH3 domains, two different scaffolds to recognize proline-rich ligands

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Pure antiandrogens disrupt the recruitment of coactivator GRIP1 to colocalize with androgen receptor in nuclei

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RNA and protein interactions modulated by protein arginine methylation.

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Nuclear receptor coactivators: multiple enzymes, multiple complexes, multiple functions.

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Structure of the Predominant Protein Arginine Methyltransferase PRMT1 and Analysis of Its Binding to Substrate Peptides

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Characterization of the interaction between androgen receptor and a new transcriptional inhibitor, SHP.

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SHP represses transcriptional activity via recruitment of histone deacetylases.

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Heterogeneous nuclear ribonucleoprotein E1B-AP5 is methylated in its Arg-Gly-Gly (RGG) box and interacts with human arginine methyltransferase HRMT1L1

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Effects of ligand activation of peroxisome proliferator-activated receptor gamma in human prostate cancer

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CREB binding protein acts synergistically with steroid receptor coactivator-1 to enhance steroid receptor-dependent transcription

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Interaction between the amino- and carboxyl-terminal regions of the rat androgen receptor modulates transcriptional activity and is influenced by nuclear receptor coactivators.

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PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation

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Unusual sites of arginine methylation in Poly(A)-binding protein II and in vitro methylation by protein arginine methyltransferases PRMT1 and PRMT3

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JAB1 interacts with both the progesterone receptor and SRC-1

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PRMT7, a new protein arginine methyltransferase that synthesizes symmetric dimethylarginine

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Crystal structure of the conserved core of protein arginine methyltransferase PRMT3

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Translating the Histone Code

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The AF1 and AF2 domains of the androgen receptor interact with distinct regions of SRC1

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release_tbtohl7jovehbdflrt35kncoiy

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https://api.fatcat.wiki/v0/release/tbtohl7jovehbdflrt35kncoiy

24 November 2022