Kinetic analysis of human protein arginine N-methyltransferase 2: formation of monomethyl- and asymmetric dimethyl-arginine residues on histone H4 (Q24320243)

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English	Kinetic analysis of human protein arginine N-methyltransferase 2: formation of monomethyl- and asymmetric dimethyl-arginine residues on histone H4	scientific article

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scholarly article

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Kinetic analysis of human protein arginine N-methyltransferase 2: formation of monomethyl- and asymmetric dimethyl-arginine residues on histone H4 (English)

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author name string

Ted M Lakowski

1

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Adam Frankel

2

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original language of film or TV show

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publication date

15 July 2009

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Biochemical Journal

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421

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2

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253-61

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

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Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa

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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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Accurate localization and relative quantification of arginine methylation using nanoflow liquid chromatography coupled to electron transfer dissociation and orbitrap mass spectrometry

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PRMT7, a new protein arginine methyltransferase that synthesizes symmetric dimethylarginine

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

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Methylation of histone H4 at arginine 3 facilitating transcriptional activation by nuclear hormone receptor

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Identifiers

10.1042/BJ20090268

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