PRMT2 interacts with splicing factors and regulates the alternative splicing of BCL-X. - Wikidata - thesis-toulmin - TriplyDB

PRMT2 interacts with splicing factors and regulates the alternative splicing of BCL-X.

PRMT2 interacts with splicing factors and regulates the alternative splicing of BCL-X.

http://www.wikidata.org/entity/Q30008797

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Post-Transcriptional Regulation of Anti-Apoptotic BCL2 Family Members.Protein arginine methylation: an emerging regulator of the cell cycle.

P2860

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P2860

PRMT2 interacts with splicing factors and regulates the alternative splicing of BCL-X.

http://www.wikidata.org/entity/Q30008797

description

2017 nî lūn-bûn

@nan

2017 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2017 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

2017年の論文

@ja

2017年論文

@yue

2017年論文

@zh-hant

2017年論文

@zh-hk

2017年論文

@zh-mo

2017年論文

@zh-tw

2017年论文

@wuu

name

PRMT2 interacts with splicing factors and regulates the alternative splicing of BCL-X.

@ast

PRMT2 interacts with splicing factors and regulates the alternative splicing of BCL-X.

@en

type

label

PRMT2 interacts with splicing factors and regulates the alternative splicing of BCL-X.

@ast

PRMT2 interacts with splicing factors and regulates the alternative splicing of BCL-X.

@en

prefLabel

PRMT2 interacts with splicing factors and regulates the alternative splicing of BCL-X.

@ast

PRMT2 interacts with splicing factors and regulates the alternative splicing of BCL-X.

@en

P1433

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P1433

Journal of Biochemistry

P1476

PRMT2 interacts with splicing factors and regulates the alternative splicing of BCL-X.

@en

P2093

Charles E Chalfant

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

Dylan Thomas

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

Magnolia L Pak

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

Margaret A Park

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

Mynol I Vhuiyan

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P2860

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

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

Identification and characterization of novel spliced variants of PRMT2 in breast carcinoma

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

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

PRMT8, a new membrane-bound tissue-specific member of the protein arginine methyltransferase family

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

The arginine methyltransferase PRMT2 binds RB and regulates E2F function

Novel splicing factor RBM25 modulates Bcl-x pre-mRNA 5' splice site selection

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

P304

17-25

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P31

scholarly article

P356

10.1093/JB/MVW102

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P433

1

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P478

162

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Ted M. Lakowski

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2017-07-01T00:00:00Z

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28057797

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P932

5892402

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