A facile strategy for selective incorporation of phosphoserine into histones.
A facile strategy for selective incorporation of phosphoserine into histones.
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DOI：
10.1002/anie.201300531
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发表时间：
2013-05-27
影响因子：
16.6
通讯作者：
Park, Hee-Sung
中科院分区：
文献类型：
--
作者：
Lee, Sangsik;Oh, Seunghee;Yang, Aerin;Kim, Jihyo;Soell, Dieter;Lee, Daeyoup;Park, Hee-Sung
组蛋白是染色质的主要蛋白质成分。它们经历了许多翻译后修饰，包括磷酸化、乙酰化和甲基化，这些经常相互影响[1，2]。这种组蛋白修饰的交叉调节被认为在许多生理过程中发挥着核心作用。组蛋白H3在丝氨酸10位的磷酸化(H3S10)和组蛋白H3的N末端赖氨酸残基的乙酰化是真核细胞转录激活的典型标志。许多体内研究表明，这些修饰之间可能存在联系[3-5]，但这种联系尚未建立。早期使用合成H3小肽的体外研究提供了关于磷酸化和乙酰化之间的联系的混合和相互矛盾的结果[3，4，6]，而最近的多肽实验没有发现任何相关性[7]。然而，由于合成肽不同于经过修饰的生理底物，它们
Histones are the main protein components of chromatin. They undergo numerous posttranslational modifications, including phosphorylation, acetylation, and methylation, which often affect each other [1, 2]. Such cross-regulation of histone modification is known to play a central role in many physiological processes. Phosphorylation of histone H3 at serine 10 (H3S10) and acetylation of N-terminal lysine residues in histone H3 are representative markers of transcriptional activation in eukaryotic cells. Many in vivo studies have suggested a possible link between these modifications [3-5], but this association is not yet established. Early in vitro studies using small synthetic H3 peptides provided mixed and conflicting results regarding the association between phosphorylation and acetylation [3, 4, 6], and recent peptide experiments have failed to find any correlation [7]. However, since synthetic peptides differ from the physiological substrates that undergo modifications, they
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影响因子：
3.5
作者：
Heinemann IU;Rovner AJ;Aerni HR;Rogulina S;Cheng L;Olds W;Fischer JT;Söll D;Isaacs FJ;Rinehart J
通讯作者：
Rinehart J
影响因子：
16
作者：
Lo, WS;Trievel, RC;Berger, SL
通讯作者：
Berger, SL
影响因子：
56.9
作者：
DAWSON, PE;MUIR, TW;KENT, SBH
通讯作者：
KENT, SBH
DOI：
10.1101/sqb.2004.69.219
发表时间：
2004-01-01
期刊：
COLD SPRING HARBOR SYMPOSIA ON QUANTITATIVE BIOLOGY
影响因子：
--
作者：
Fry, CJ;Shogren-Knaak, MA;Peterson, CL
通讯作者：
Peterson, CL
影响因子：
4.8
作者：
Grant, PA;Eberharter, A;Workman, JL
通讯作者：
Workman, JL