Regulation of protein arginine methyltransferase 8 (PRMT8) activity by its N-terminal domain (Q34699830)

4 August 2017

Regulation of protein arginine methyltransferase 8 (PRMT8) activity by its N-terminal domain (English)

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Protein arginine methyltransferase 8

4 August 2017

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protein-arginine omega-N asymmetric methyltransferase activity

GOA release 2020-03-11

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GOA release 2020-03-11

author name string

Joyce Sayegh

1

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4 August 2017

Kristofor Webb

2

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4 August 2017

Donghang Cheng

3

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4 August 2017

Mark T Bedford

4

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4 August 2017

Steven G Clarke

5

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4 August 2017

language of work or name

English

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publication date

9 October 2007

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Journal of Biological Chemistry

4 August 2017

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4 August 2017

282

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4 August 2017

36444-36453

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4 August 2017

50

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Arginine methylation an emerging regulator of protein function

4 August 2017

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704650200

Protein arginine methylation: Cellular functions and methods of analysis

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M704650200

Protein arginine methyltransferases: evolution and assessment of their pharmacological and therapeutic potential

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704650200

Protein arginine methyltransferases: from unicellular eukaryotes to humans

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704650200

Arginine methylation inhibits the binding of proline-rich ligands to Src homology 3, but not WW, domains

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704650200

Methylation of Smad6 by protein arginine N-methyltransferase 1

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704650200

Specific protein methylation defects and gene expression perturbations in coactivator-associated arginine methyltransferase 1-deficient mice

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704650200

Arginine methyltransferase CARM1 is a promoter-specific regulator of NF-kappaB-dependent gene expression

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704650200

The arginine methyltransferase CARM1 regulates the coupling of transcription and mRNA processing.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704650200

Signal-dependent control of gluconeogenic key enzyme genes through coactivator-associated arginine methyltransferase 1

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704650200

Coactivator-associated arginine methyltransferase 1 (CARM1) is a positive regulator of the Cyclin E1 gene

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704650200

The activity and stability of the transcriptional coactivator p/CIP/SRC-3 are regulated by CARM1-dependent methylation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704650200

Negative regulation of transcription by the type II arginine methyltransferase PRMT5

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704650200

Transcriptional down-regulation through nuclear exclusion of EWS methylated by PRMT1.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704650200

Conserved SR protein kinase functions in nuclear import and its action is counteracted by arginine methylation in Saccharomyces cerevisiae

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704650200

PRMT3 is a ribosomal protein methyltransferase that affects the cellular levels of ribosomal subunits

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704650200

Ribosomal protein S2 is a substrate for mammalian PRMT3 (protein arginine methyltransferase 3)

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704650200

delta-N-methylarginine is a novel posttranslational modification of arginine residues in yeast proteins.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704650200

PRMT1 is the predominant type I protein arginine methyltransferase in mammalian cells

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704650200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704650200

Regulation of transcription by a protein methyltransferase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704650200

The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704650200

PRMT8, a new membrane-bound tissue-specific member of the protein arginine methyltransferase family

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704650200

PRMT5 (Janus Kinase-binding Protein 1) Catalyzes the Formation of Symmetric Dimethylarginine Residues in Proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704650200

FBXO11/PRMT9, a new protein arginine methyltransferase, symmetrically dimethylates arginine residues

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704650200

PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704650200

PRMT7, a new protein arginine methyltransferase that synthesizes symmetric dimethylarginine

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704650200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704650200

Identification and phylogenetic analyses of the protein arginine methyltransferase gene family in fish and ascidians.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704650200

Specific regional distribution of protein arginine methyltransferase 8 (PRMT8) in the mouse brain.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704650200

The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704650200

S-Adenosylmethionine-dependent methylation in Saccharomyces cerevisiae. Identification of a novel protein arginine methyltransferase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704650200

In vivo and in vitro arginine methylation of RNA-binding proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704650200

A protein-domain microarray identifies novel protein-protein interactions

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704650200

Altered levels of S-adenosylmethionine and S-adenosylhomocysteine in the brains of L-isoaspartyl (D-Aspartyl) O-methyltransferase-deficient mice

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704650200

Fragmentation pathways of N(G)-methylated and unmodified arginine residues in peptides studied by ESI-MS/MS and MALDI-MS.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704650200

A motif-based profile scanning approach for genome-wide prediction of signaling pathways

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704650200

Alternative splicing yields protein arginine methyltransferase 1 isoforms with distinct activity, substrate specificity, and subcellular localization.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704650200

Organization of the SH3-SH2 unit in active and inactive forms of the c-Abl tyrosine kinase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704650200

21 January 2018

Identifiers

DOI

10.1074/JBC.M704650200

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4 August 2017

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