PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity (Q24320263)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15044439%20AND%20SRC:MED&resulttype=core&format=json

26 December 2019

title

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

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15044439%20AND%20SRC:MED&resulttype=core&format=json

Protein arginine methyltransferase 7

26 December 2019

main subject

1 reference

regulation of protein binding

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

author

Adam Frankel

3

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15044439%20AND%20SRC:MED&resulttype=core&format=json

26 December 2019

author name string

Tina Branscombe Miranda

1

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15044439%20AND%20SRC:MED&resulttype=core&format=json

26 December 2019

Mark Miranda

2

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15044439%20AND%20SRC:MED&resulttype=core&format=json

26 December 2019

Steven Clarke

4

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15044439%20AND%20SRC:MED&resulttype=core&format=json

26 December 2019

language of work or name

English

0 references

publication date

24 March 2004

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15044439%20AND%20SRC:MED&resulttype=core&format=json

Journal of Biological Chemistry

26 December 2019

published in

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15044439%20AND%20SRC:MED&resulttype=core&format=json

26 December 2019

volume

279

1 reference

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26 December 2019

issue

22

1 reference

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26 December 2019

page(s)

22902-22907

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15044439%20AND%20SRC:MED&resulttype=core&format=json

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

26 December 2019

cites work

1 reference

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Protein-arginine methyltransferase I, the predominant protein-arginine methyltransferase in cells, interacts with and is regulated by interleukin enhancer-binding factor 3

21 January 2018

1 reference

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Arginine methylation of STAT1 regulates its dephosphorylation by T cell protein tyrosine phosphatase

21 January 2018

1 reference

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Regulation of transcription by a protein methyltransferase

21 January 2018

1 reference

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Negative regulation of transcription by the type II arginine methyltransferase PRMT5

21 January 2018

1 reference

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

21 January 2018

1 reference

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Analysis of the yeast arginine methyltransferase Hmt1p/Rmt1p and its in vivo function. Cofactor binding and substrate interactions.

21 January 2018

1 reference

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The methylosome, a 20S complex containing JBP1 and pICln, produces dimethylarginine-modified Sm proteins

21 January 2018

1 reference

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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.M312904200

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

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The predominant protein-arginine methyltransferase from Saccharomyces cerevisiae

21 January 2018

1 reference

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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.M312904200

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

21 January 2018

1 reference

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

21 January 2018

1 reference

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Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha

21 January 2018

1 reference

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A human protein selected for interference with Ras function interacts directly with Ras and competes with Raf1

21 January 2018

1 reference

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Crystal structure of the conserved core of protein arginine methyltransferase PRMT3

21 January 2018

1 reference

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Gapped BLAST and PSI-BLAST: a new generation of protein database search programs

21 January 2018

1 reference

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Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312904200

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

21 January 2018

1 reference

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Biological significance of endogenous methylarginines that inhibit nitric oxide synthases

21 January 2018

1 reference

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Endogenous methylarginines regulate neuronal nitric-oxide synthase and prevent excitotoxic injury

21 January 2018

1 reference

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RNA and protein interactions modulated by protein arginine methylation.

21 January 2018

1 reference

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inferred from DOI database lookup

7 January 2021

based on heuristic

Automated identification of putative methyltransferases from genomic open reading frames

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312904200