(Q27690032)

2

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Jun-Dal Kim

3

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Akiyoshi Fukamizu

4

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Toshiyuki Shimizu

Protein arginine methylation in mammals: who, what, and why

5

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language of work or name

English

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publication date

21 May 2014

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published in

FEBS Letters

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volume

588

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issue

10

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page(s)

1942-8

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cites work

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.03.053

Human protein arginine methyltransferase 7 (PRMT7) is a type III enzyme forming ω-NG-monomethylated arginine residues.

21 January 2018

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Mammalian protein arginine methyltransferase 7 (PRMT7) specifically targets RXR sites in lysine- and arginine-rich regions

21 January 2018

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Protein arginine methyltransferases and cancer

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The role of arginine methylation in the DNA damage response

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Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteins

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Protein arginine methyltransferase 7 regulates cellular response to DNA damage by methylating promoter histones H2A and H4 of the polymerase δ catalytic subunit gene, POLD1

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Nuclear proteome analysis of undifferentiated mouse embryonic stem and germ cells.

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Trans-tail regulation of MLL4-catalyzed H3K4 methylation by H4R3 symmetric dimethylation is mediated by a tandem PHD of MLL4

21 January 2018

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

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

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Processing of X-ray diffraction data collected in oscillation mode

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Phasercrystallographic software

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Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7

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Coot: model-building tools for molecular graphics

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Refinement of macromolecular structures by the maximum-likelihood method

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PROCHECK: a program to check the stereochemical quality of protein structures

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Crystal structure of the conserved core of protein arginine methyltransferase PRMT3

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Structural insights into protein arginine symmetric dimethylation by PRMT5

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Crystal structure of the human PRMT5:MEP50 complex

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

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PRIMUS: a Windows PC-based system for small-angle scattering data analysis

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