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

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		Property / cites work
			Methylation of histone H4 by arginine methyltransferase PRMT1 is essential in vivo for many subsequent histone modifications
		Property / cites work: Methylation of histone H4 by arginine methyltransferase PRMT1 is essential in vivo for many subsequent histone modifications / rank
			Normal rank
		Property / cites work: Methylation of histone H4 by arginine methyltransferase PRMT1 is essential in vivo for many subsequent histone modifications / reference
			stated in: Crossref reference URL: https://api.crossref.org/works/10.1042%2FBJ20090268 retrieved: 21 January 2018 Timestamp +2018-01-21T00:00:00Z Timezone +00:00 Calendar Gregorian Precision 1 day Before 0 After 0
		Property / cites work
			Identification and mapping of a novel human gene, HRMT1L1, homologous to the rat protein arginine N-methyltransferase 1 (PRMT1) gene
		Property / cites work: Identification and mapping of a novel human gene, HRMT1L1, homologous to the rat protein arginine N-methyltransferase 1 (PRMT1) gene / rank
			Normal rank
		Property / cites work: Identification and mapping of a novel human gene, HRMT1L1, homologous to the rat protein arginine N-methyltransferase 1 (PRMT1) gene / reference
			stated in: Crossref reference URL: https://api.crossref.org/works/10.1042%2FBJ20090268 retrieved: 21 January 2018 Timestamp +2018-01-21T00:00:00Z Timezone +00:00 Calendar Gregorian Precision 1 day Before 0 After 0
		Property / cites work
			Heterogeneous nuclear ribonucleoprotein E1B-AP5 is methylated in its Arg-Gly-Gly (RGG) box and interacts with human arginine methyltransferase HRMT1L1
		Property / cites work: Heterogeneous nuclear ribonucleoprotein E1B-AP5 is methylated in its Arg-Gly-Gly (RGG) box and interacts with human arginine methyltransferase HRMT1L1 / rank
			Normal rank
		Property / cites work: Heterogeneous nuclear ribonucleoprotein E1B-AP5 is methylated in its Arg-Gly-Gly (RGG) box and interacts with human arginine methyltransferase HRMT1L1 / reference
			stated in: Crossref reference URL: https://api.crossref.org/works/10.1042%2FBJ20090268 retrieved: 21 January 2018 Timestamp +2018-01-21T00:00:00Z Timezone +00:00 Calendar Gregorian Precision 1 day Before 0 After 0
		Property / cites work
			A kinetic study of human protein arginine N-methyltransferase 6 reveals a distributive mechanism
		Property / cites work: A kinetic study of human protein arginine N-methyltransferase 6 reveals a distributive mechanism / rank
			Normal rank
		Property / cites work: A kinetic study of human protein arginine N-methyltransferase 6 reveals a distributive mechanism / reference
			stated in: Crossref reference URL: https://api.crossref.org/works/10.1042%2FBJ20090268 retrieved: 21 January 2018 Timestamp +2018-01-21T00:00:00Z Timezone +00:00 Calendar Gregorian Precision 1 day Before 0 After 0
		Property / cites work
			Kinetic mechanism of protein arginine methyltransferase 1.
		Property / cites work: Kinetic mechanism of protein arginine methyltransferase 1. / rank
			Normal rank
		Property / cites work: Kinetic mechanism of protein arginine methyltransferase 1. / reference
			stated in: Crossref reference URL: https://api.crossref.org/works/10.1042%2FBJ20090268 retrieved: 21 January 2018 Timestamp +2018-01-21T00:00:00Z Timezone +00:00 Calendar Gregorian Precision 1 day Before 0 After 0
		Property / cites work
			Protein arginine methyltransferase 1: positively charged residues in substrate peptides distal to the site of methylation are important for substrate binding and catalysis
		Property / cites work: Protein arginine methyltransferase 1: positively charged residues in substrate peptides distal to the site of methylation are important for substrate binding and catalysis / rank
			Normal rank
		Property / cites work: Protein arginine methyltransferase 1: positively charged residues in substrate peptides distal to the site of methylation are important for substrate binding and catalysis / reference
			stated in: Crossref reference URL: https://api.crossref.org/works/10.1042%2FBJ20090268 retrieved: 21 January 2018 Timestamp +2018-01-21T00:00:00Z Timezone +00:00 Calendar Gregorian Precision 1 day Before 0 After 0
		Property / cites work
			RNase treatment of yeast and mammalian cell extracts affects in vitro substrate methylation by type I protein arginine N-methyltransferases.
		Property / cites work: RNase treatment of yeast and mammalian cell extracts affects in vitro substrate methylation by type I protein arginine N-methyltransferases. / rank
			Normal rank
		Property / cites work: RNase treatment of yeast and mammalian cell extracts affects in vitro substrate methylation by type I protein arginine N-methyltransferases. / reference
			stated in: Crossref reference URL: https://api.crossref.org/works/10.1042%2FBJ20090268 retrieved: 21 January 2018 Timestamp +2018-01-21T00:00:00Z Timezone +00:00 Calendar Gregorian Precision 1 day Before 0 After 0
		Property / cites work
			A protein-domain microarray identifies novel protein-protein interactions
		Property / cites work: A protein-domain microarray identifies novel protein-protein interactions / rank
			Normal rank
		Property / cites work: A protein-domain microarray identifies novel protein-protein interactions / reference
			stated in: Crossref reference URL: https://api.crossref.org/works/10.1042%2FBJ20090268 retrieved: 21 January 2018 Timestamp +2018-01-21T00:00:00Z Timezone +00:00 Calendar Gregorian Precision 1 day Before 0 After 0
		Property / cites work
			A mass spectrometry based method for distinguishing between symmetrically and asymmetrically dimethylated arginine residues
		Property / cites work: A mass spectrometry based method for distinguishing between symmetrically and asymmetrically dimethylated arginine residues / rank
			Normal rank
		Property / cites work: A mass spectrometry based method for distinguishing between symmetrically and asymmetrically dimethylated arginine residues / reference
			stated in: Crossref reference URL: https://api.crossref.org/works/10.1042%2FBJ20090268 retrieved: 21 January 2018 Timestamp +2018-01-21T00:00:00Z Timezone +00:00 Calendar Gregorian Precision 1 day Before 0 After 0
		Property / cites work
			Fragmentation pathways of N(G)-methylated and unmodified arginine residues in peptides studied by ESI-MS/MS and MALDI-MS.
		Property / cites work: Fragmentation pathways of N(G)-methylated and unmodified arginine residues in peptides studied by ESI-MS/MS and MALDI-MS. / rank
			Normal rank
		Property / cites work: Fragmentation pathways of N(G)-methylated and unmodified arginine residues in peptides studied by ESI-MS/MS and MALDI-MS. / reference
			stated in: Crossref reference URL: https://api.crossref.org/works/10.1042%2FBJ20090268 retrieved: 21 January 2018 Timestamp +2018-01-21T00:00:00Z Timezone +00:00 Calendar Gregorian Precision 1 day Before 0 After 0
		Property / cites work
			Type I Arginine Methyltransferases PRMT1 and PRMT-3 Act Distributively.
		Property / cites work: Type I Arginine Methyltransferases PRMT1 and PRMT-3 Act Distributively. / rank
			Normal rank
		Property / cites work: Type I Arginine Methyltransferases PRMT1 and PRMT-3 Act Distributively. / reference
			stated in: Crossref reference URL: https://api.crossref.org/works/10.1042%2FBJ20090268 retrieved: 21 January 2018 Timestamp +2018-01-21T00:00:00Z Timezone +00:00 Calendar Gregorian Precision 1 day Before 0 After 0
		Property / cites work
			Substrate profiling of PRMT1 reveals amino acid sequences that extend beyond the "RGG" paradigm
		Property / cites work: Substrate profiling of PRMT1 reveals amino acid sequences that extend beyond the "RGG" paradigm / rank
			Normal rank
		Property / cites work: Substrate profiling of PRMT1 reveals amino acid sequences that extend beyond the "RGG" paradigm / reference
			stated in: Crossref reference URL: https://api.crossref.org/works/10.1042%2FBJ20090268 retrieved: 21 January 2018 Timestamp +2018-01-21T00:00:00Z Timezone +00:00 Calendar Gregorian Precision 1 day Before 0 After 0
		Property / cites work
			Human protein arginine methyltransferases in vivo--distinct properties of eight canonical members of the PRMT family
		Property / cites work: Human protein arginine methyltransferases in vivo--distinct properties of eight canonical members of the PRMT family / rank
			Normal rank
		Property / cites work: Human protein arginine methyltransferases in vivo--distinct properties of eight canonical members of the PRMT family / reference
			stated in: Crossref reference URL: https://api.crossref.org/works/10.1042%2FBJ20090268 retrieved: 21 January 2018 Timestamp +2018-01-21T00:00:00Z Timezone +00:00 Calendar Gregorian Precision 1 day Before 0 After 0

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Revision as of 22:05, 22 October 2018

scientific article

Language	Label	Description	Also known as
English	Kinetic analysis of human protein arginine N-methyltransferase 2: formation of monomethyl- and asymmetric dimethyl-arginine residues on histone H4	scientific article

Statements

instance of

scholarly article

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title

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

series ordinal

1

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Adam Frankel

series ordinal

2

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language of work or name

English

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publication date

15 July 2009

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published in

Biochemical Journal

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volume

421

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issue

2

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page(s)

253-61

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cites work

The language of covalent histone modifications

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Crossref

reference URL

https://api.crossref.org/works/10.1042/BJ20090268

retrieved

21 April 2017

Methylation at arginine 17 of histone H3 is linked to gene activation

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reference URL

https://api.crossref.org/works/10.1042/BJ20090268

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21 April 2017

Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by the nuclear receptor coactivator PRMT1

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1042/BJ20090268

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21 April 2017

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

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reference URL

https://api.crossref.org/works/10.1042/BJ20090268

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21 April 2017

Protein methyltransferase 2 inhibits NF-kappaB function and promotes apoptosis

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reference URL

https://api.crossref.org/works/10.1042/BJ20090268

retrieved

21 April 2017

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

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reference URL

https://api.crossref.org/works/10.1042/BJ20090268

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21 April 2017

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

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reference URL

https://api.crossref.org/works/10.1042/BJ20090268

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21 April 2017

Identification and characterization of two putative human arginine methyltransferases (HRMT1L1 and HRMT1L2)

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reference URL

https://api.crossref.org/works/10.1042/BJ20090268

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21 April 2017

The arginine methyltransferase PRMT2 binds RB and regulates E2F function

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1042/BJ20090268

retrieved

21 April 2017

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

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1042/BJ20090268

retrieved

21 April 2017

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

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stated in

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reference URL

https://api.crossref.org/works/10.1042/BJ20090268

retrieved

21 April 2017

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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reference URL

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21 April 2017

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

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stated in

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reference URL

https://api.crossref.org/works/10.1042/BJ20090268

retrieved

21 April 2017

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

1 reference

stated in

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reference URL

https://api.crossref.org/works/10.1042/BJ20090268

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21 April 2017

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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stated in

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reference URL

https://api.crossref.org/works/10.1042/BJ20090268

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21 April 2017

The predominant protein-arginine methyltransferase from Saccharomyces cerevisiae

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stated in

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reference URL

https://api.crossref.org/works/10.1042/BJ20090268

retrieved

21 April 2017

Insights into histone code syntax from structural and biochemical studies of CARM1 methyltransferase

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stated in

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reference URL

https://api.crossref.org/works/10.1042/BJ20090268

retrieved

21 April 2017

Structural and functional insights into O-methyltransferase from Bacillus cereus

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stated in

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reference URL

https://api.crossref.org/works/10.1042/BJ20090268

retrieved

21 April 2017

PRMT7, a new protein arginine methyltransferase that synthesizes symmetric dimethylarginine

1 reference

stated in

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reference URL

https://api.crossref.org/works/10.1042/BJ20090268

retrieved

21 April 2017

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

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1042%2FBJ20090268

retrieved

21 April 2017

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

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1042%2FBJ20090268

retrieved

21 April 2017

Methylation of histone H4 by arginine methyltransferase PRMT1 is essential in vivo for many subsequent histone modifications

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1042%2FBJ20090268

retrieved

21 January 2018

Identification and mapping of a novel human gene, HRMT1L1, homologous to the rat protein arginine N-methyltransferase 1 (PRMT1) gene

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1042%2FBJ20090268

retrieved

21 January 2018

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

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1042%2FBJ20090268

retrieved

21 January 2018

A kinetic study of human protein arginine N-methyltransferase 6 reveals a distributive mechanism

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1042%2FBJ20090268

retrieved

21 January 2018

Kinetic mechanism of protein arginine methyltransferase 1.

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1042%2FBJ20090268

retrieved

21 January 2018

Protein arginine methyltransferase 1: positively charged residues in substrate peptides distal to the site of methylation are important for substrate binding and catalysis

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1042%2FBJ20090268

retrieved

21 January 2018

RNase treatment of yeast and mammalian cell extracts affects in vitro substrate methylation by type I protein arginine N-methyltransferases.

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1042%2FBJ20090268

retrieved

21 January 2018

A protein-domain microarray identifies novel protein-protein interactions

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1042%2FBJ20090268

retrieved

21 January 2018

A mass spectrometry based method for distinguishing between symmetrically and asymmetrically dimethylated arginine residues

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1042%2FBJ20090268

retrieved

21 January 2018

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

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1042%2FBJ20090268

retrieved

21 January 2018

Type I Arginine Methyltransferases PRMT1 and PRMT-3 Act Distributively.

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1042%2FBJ20090268

retrieved

21 January 2018

Substrate profiling of PRMT1 reveals amino acid sequences that extend beyond the "RGG" paradigm

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1042%2FBJ20090268

retrieved

21 January 2018

Human protein arginine methyltransferases in vivo--distinct properties of eight canonical members of the PRMT family

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1042%2FBJ20090268

retrieved

21 January 2018

Identifiers

DOI

10.1042/BJ20090268

0 references

PubMed publication ID

19405910

0 references

 

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