Discovery of Potent and Selective Allosteric Inhibitors of Protein Arginine Methyltransferase 3 (PRMT3).

about

The Methylation Status of the Epigenome: Its Emerging Role in the Regulation of Tumor Angiogenesis and Tumor Growth, and Potential for Drug Targeting

P2860

Q58789495-3D1A166E-3A72-4E47-BDBB-654725B01C2E

P2860

Discovery of Potent and Selective Allosteric Inhibitors of Protein Arginine Methyltransferase 3 (PRMT3).

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http://www.wikidata.org/entity/Q47290345

description

2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年學術文章

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2017年學術文章

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2017年學術文章

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name

Discovery of Potent and Select ...... e Methyltransferase 3 (PRMT3).

@en

Discovery of Potent and Select ...... n Arginine Methyltransferase 3

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type

Item

label

Discovery of Potent and Select ...... e Methyltransferase 3 (PRMT3).

@en

Discovery of Potent and Select ...... n Arginine Methyltransferase 3

@nl

prefLabel

Discovery of Potent and Select ...... e Methyltransferase 3 (PRMT3).

@en

Discovery of Potent and Select ...... n Arginine Methyltransferase 3

@nl

P1476

Discovery of Potent and Select ...... e Methyltransferase 3 (PRMT3).

@en

P2093

Dalia Barsyte-Lovejoy

http://www.w3.org/2001/XMLSchema#string

Elena Dobrovetsky

http://www.w3.org/2001/XMLSchema#string

En Li

http://www.w3.org/2001/XMLSchema#string

Feng He

http://www.w3.org/2001/XMLSchema#string

Fengling Li

http://www.w3.org/2001/XMLSchema#string

H Ümit Kaniskan

http://www.w3.org/2001/XMLSchema#string

Irene Zang

http://www.w3.org/2001/XMLSchema#string

Jennifer Lin-Jones

http://www.w3.org/2001/XMLSchema#string

Kehao Zhao

http://www.w3.org/2001/XMLSchema#string

Keith Schmidt

http://www.w3.org/2001/XMLSchema#string

P2860

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

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

Promiscuous modification of the nuclear poly(A)-binding protein by multiple protein-arginine methyltransferases does not affect the aggregation behavior

Kinetic characterization of human histone H3 lysine 36 methyltransferases, ASH1L and SETD2

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

The tumor suppressor DAL-1/4.1B and protein methylation cooperate in inducing apoptosis in MCF-7 breast cancer cells.

An allosteric inhibitor of protein arginine methyltransferase 3

DAL-1/4.1B tumor suppressor interacts with protein arginine N-methyltransferase 3 (PRMT3) and inhibits its ability to methylate substrates in vitro and in vivo

PRMT3 is essential for dendritic spine maturation in rat hippocampal neurons

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

P304

1204-1217

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P31

scholarly article

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10.1021/ACS.JMEDCHEM.7B01674

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English

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http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

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P577

2017-12-15T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

29244490

http://www.w3.org/2001/XMLSchema#string

P921

allosteric inhibitor

P932

5808361

http://www.w3.org/2001/XMLSchema#string

Discovery of Potent and Selective Allosteric Inhibitors of Protein Arginine Methyltransferase 3 (PRMT3).

about

P2860

P2860

Discovery of Potent and Selective Allosteric Inhibitors of Protein Arginine Methyltransferase 3 (PRMT3).

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P921

P932