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Arginine methyltransferases as novel therapeutic targets for breast cancer

Arginine methyltransferases as novel therapeutic targets for breast cancer

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Biological Chemistry and Functionality of Protein Sulfenic Acids and Related Thiol Modifications Global mapping of CARM1 substrates defines enzyme specificity and substrate recognition.Tudor Domain Containing Protein 3 Promotes Tumorigenesis and Invasive Capacity of Breast Cancer Cells PRMT1-mediated methylation of MICU1 determines the UCP2/3 dependency of mitochondrial Ca(2+) uptake in immortalized cells.Transition state mimics are valuable mechanistic probes for structural studies with the arginine methyltransferase CARM1.Discovery and optimization of selective inhibitors of protein arginine methyltransferase 5 by docking-based virtual screening.Hijacking DNA methyltransferase transition state analogues to produce chemical scaffolds for PRMT inhibitors

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Arginine methyltransferases as novel therapeutic targets for breast cancer

http://www.wikidata.org/entity/Q26851594

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2015 nî lūn-bûn

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2015 թուականի Մարտին հրատարակուած գիտական յօդուած

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2015 թվականի մարտին հրատարակված գիտական հոդված

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年论文

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name

Arginine methyltransferases as novel therapeutic targets for breast cancer

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Arginine methyltransferases as novel therapeutic targets for breast cancer

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Arginine methyltransferases as novel therapeutic targets for breast cancer

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type

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Arginine methyltransferases as novel therapeutic targets for breast cancer

@ast

Arginine methyltransferases as novel therapeutic targets for breast cancer

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Arginine methyltransferases as novel therapeutic targets for breast cancer

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prefLabel

Arginine methyltransferases as novel therapeutic targets for breast cancer

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Arginine methyltransferases as novel therapeutic targets for breast cancer

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Arginine methyltransferases as novel therapeutic targets for breast cancer

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Arginine methyltransferases as novel therapeutic targets for breast cancer

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Alan Morettin

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R Mitchell Baldwin

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P2860

The testis-specific factor CTCFL cooperates with the protein methyltransferase PRMT7 in H19 imprinting control region methylation

The Hallmarks of Cancer

Relationships of the antiproliferative proteins BTG1 and BTG2 with CAF1, the human homolog of a component of the yeast CCR4 transcriptional complex: involvement in estrogen receptor alpha signaling pathway

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

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

The AT-hook of the chromatin architectural transcription factor high mobility group A1a is arginine-methylated by protein arginine methyltransferase 6

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

Aberrant expression of CARM1, a transcriptional coactivator of androgen receptor, in the development of prostate carcinoma and androgen-independent status

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

Methylation of ribosomal protein S10 by protein-arginine methyltransferase 5 regulates ribosome biogenesis

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177-189

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scholarly article

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3474125

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10.1093/MUTAGE/GEU039

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2

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30

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25688111

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