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PRMT1介导的蛋白质精氨酸甲基化的生理和病理生理作用。

The physiological and pathophysiological role of PRMT1-mediated protein arginine methylation.

机构信息

Novartis Institutes for Biomedical Research, Cambridge, MA 02139, USA.

出版信息

Pharmacol Res. 2009 Dec;60(6):466-74. doi: 10.1016/j.phrs.2009.07.006. Epub 2009 Jul 28.

Abstract

Post-translational modifications are well-known effectors in DNA damage signaling and epigenetic gene expression. Protein arginine methylation is a covalent modification that results in the addition of methyl groups to the nitrogen atoms of the arginine side chains and is catalyzed by a family of protein arginine methyltransferases (PRMTs). In the past, arginine methylation was mainly observed on abundant proteins such as RNA-binding proteins and histones, but recent advances have revealed a plethora of arginine-methylated proteins implicated in a variety of cellular processes including signal transduction, epigenetic regulation and DNA repair pathways. Herein, we discuss these recent advances, focusing on the role of PRMT1, the major asymmetric arginine methyltransferase, in cellular processes and its link to human diseases.

摘要

翻译后修饰是DNA损伤信号传导和表观遗传基因表达中众所周知的效应器。蛋白质精氨酸甲基化是一种共价修饰,可导致甲基添加到精氨酸侧链的氮原子上,并由蛋白质精氨酸甲基转移酶(PRMT)家族催化。过去,精氨酸甲基化主要在诸如RNA结合蛋白和组蛋白等丰富的蛋白质上观察到,但最近的进展表明,大量精氨酸甲基化蛋白参与了包括信号转导、表观遗传调控和DNA修复途径在内的各种细胞过程。在此,我们讨论这些最新进展,重点关注主要的不对称精氨酸甲基转移酶PRMT1在细胞过程中的作用及其与人类疾病的联系。

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