中文核心期刊
中国科技核心期刊
CSCD核心期刊
CN:31-1600/Q
ISSN:1004-0374
2019基因编辑学术研讨会 《生命科学》入编《中文核心期刊要目总览》2017年版 第29卷第11期第1197-1204页一文撤稿声明 第29卷第7期第941-945页一文撤稿声明
《生命科学》 2018, 30(4): 455-461
组蛋白赖氨酸酰化新修饰研究进展
谭敏佳*,朱明睿
(中国科学院上海药物研究所新药研究国家重点实验室,上海 201203)
摘 要:蛋白质的翻译后修饰是细胞生命活动的基本形式之一,对蛋白质生物功能的发挥具有极为重要的影响,包括细胞的生长、分化、代谢等生命过程。赖氨酸酰化修饰是重要研究内容之一,其广泛参与细胞分化、细胞代谢等重要生理活动,成为生命科学领域研究热点。随着生物质谱的扫描速度、灵敏度、分辨率的不断提高,近几年来许多新的赖氨酸酰化修饰被研究者鉴定。该文总结了琥珀酰化、巴豆酰化、丙二酰化、戊二酰化、2- 羟基异丁酰化、β- 羟基丁酰化等新型赖氨酸酰化修饰的发现确证、修饰调控酶、底物鉴定和生理病理功能等方面的最新研究进展。
 
Progress in characterization of novel lysine acyl modifications
TAN Min-Jia*, ZHU Ming-Rui
(The State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China)
Abstract: Protein post-translational modifications (PTMs) play fundamental and diverse biological functions in cells, such as cell growth, differentiation and metabolism. Lysine acyl modifications are an important class of PTMs, which is widely involved in cell differentiation, energy metabolism and other important physiological activities. In recent years, due to the development of high sensitive and high resolution mass spectrometry-based proteomics technologies, many novel lysine acyl modifications with unique biological functions have been discovered. This review summarized the recent advances of the identification of novel lysine acyl modifications (including succinylation, crotonylation, malonylation, glutarylation, 2-hydroxyisobutyrylation, β-hydroxybutyrylation), their regulatory enzymes, substrates, and roles in physiology and pathology.
 
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