Results 161 to 170 of about 8,519 (204)

CIITA/PRMT5 promote CD4<sup>+</sup>Gzma<sup>+</sup> T cell activation via H3R2me2-mediated endothelial expression of MHC class II in smoking-induced atherosclerosis. [PDF]

open access: yesBMC Med
Chen Y   +23 more
europepmc   +1 more source

Regulation of a PRMT5/NF-κB Axis by Phosphorylation of PRMT5 at Serine 15 in Colorectal Cancer [PDF]

open access: yesInternational Journal of Molecular Sciences, 2020
The overexpression of PRMT5 is highly correlated to poor clinical outcomes for colorectal cancer (CRC) patients. Importantly, our previous work demonstrated that PRMT5 overexpression could substantially augment activation of the nuclear factor kappa B (NF-κB) via methylation of arginine 30 (R30) on its p65 subunit, while knockdown of PRMT5 showed the ...
Tao Lu, Lakshmi Prabhu, Yunlong Liu
exaly   +4 more sources

Discovery of a Dual PRMT5–PRMT7 Inhibitor

open access: yesACS Medicinal Chemistry Letters, 2015
The protein arginine methyltransferases PRMT7 and PRMT5, respectively, monomethylate and symmetrically dimethylate arginine side-chains of proteins involved in diverse cellular mechanisms, including chromatin-mediated control of gene transcription ...
Masoud Vedadi   +2 more
exaly   +2 more sources
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PRMT5 promotes retinoblastoma development

Human Cell, 2022
Epigenetic mechanism, including DNA methylation and histone modifications, contributes to alterations in the expression patterns of genes regulating malignant phenotype of cancer cells. However, the epigenetic modulation of vascular endothelial growth factor-A (VEGFA) in retinoblastoma (RB) has not been clearly established.
Yu, Jiang   +2 more
openaire   +2 more sources

A New Move for PRMT5

Nature Reviews Molecular Cell Biology, 2011
Joanna E Huddleston
exaly   +2 more sources

The Where and the How of PRMT5

Current Molecular Biology Reports, 2015
The post-translational modification (PTM) of proteins is an important mechanism for regulating and modulating their functional repertoire. PTMs can alter the charge, hydrophobicity, or physical structure of a peptide, resulting in altered protein-RNA, protein-DNA, and protein-protein interactions.
Cheryl M. Koh   +2 more
openaire   +1 more source

PRMT5 INHIBITORS

2020
NAIR PRATHAP SREEDHARAN   +8 more
  +20 more sources

Medicinal Chemistry Strategies Targeting PRMT5 for Cancer Therapy

European Journal of Medicinal Chemistry, 2022
Liang Ouyang, Jifa Zhang, Congcong Lin
exaly  

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