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首页> 外文期刊>Angewandte Chemie >Site-Specific Incorporation of ε-N-CrotonyIlysiee into Histones
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Site-Specific Incorporation of ε-N-CrotonyIlysiee into Histones

机译:特定位置将ε-N-CrotonyIlysiee掺入组蛋白中

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摘要

Histones, the major protein components of chromatin, are extensively altered by post-translational modifications (PTMs). Deciphering distinctive patterns of these PTMs (namely the "histone code") is key to understanding the epigenetic regulation of diverse biological processes. For example, lysine acetylation is one of the most common PTMs found in histones, and its regulation has been demonstrated to be closely related to DNA replication/repair, transcriptional regulation of genes, and the status of chromatin assembly. Misregulation of chromatin PTM is linked to various human diseases such as cancer, central nervous system (CNS) disorders,1 and autoimmune diseases. Therefore, the enzymes responsible for lysine acetyl modifications, including histone acetyltransferases (HATs) and histone deacetylases (HDACs), are regarded as important drug targets.
机译:组蛋白是染色质的主要蛋白质成分,可通过翻译后修饰(PTM)进行广泛改变。理解这些PTM的独特模式(即“组蛋白代码”)是理解各种生物过程的表观遗传调控的关键。例如,赖氨酸乙酰化是在组蛋白中发现的最常见的PTM之一,其调节已被证明与DNA复制/修复,基因的转录调节以及染色质组装状态密切相关。染色质PTM的失调与多种人类疾病有关,例如癌症,中枢神经系统(CNS)疾病1和自身免疫性疾病。因此,负责赖氨酸乙酰基修饰的酶,包括组蛋白乙酰转移酶(HATs)和组蛋白脱乙酰基酶(HDACs),被视为重要的药物靶标。

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