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Histone mimics: more tales to read.
Yu, Yucong; Wen, Hong; Shi, Xiaobing.
  • Yu Y; Department of Epigenetics, Van Andel Institute, 333 Bostwick Ave. NE, Grand Rapids, Michigan 49503, U.S.A.
  • Wen H; Department of Epigenetics, Van Andel Institute, 333 Bostwick Ave. NE, Grand Rapids, Michigan 49503, U.S.A.
  • Shi X; Department of Epigenetics, Van Andel Institute, 333 Bostwick Ave. NE, Grand Rapids, Michigan 49503, U.S.A.
Biochem J ; 478(14): 2789-2791, 2021 07 30.
Article in English | MEDLINE | ID: covidwho-1526112
ABSTRACT
Post-translational modifications (PTMs) on histone proteins are known as epigenetic marks that demarcate the status of chromatin. These modifications are 'read' by specific reader proteins, which in turn recruit additional factors to modulate chromatin accessibility and the activity of the underlying DNA. Accumulating evidence suggests that these modifications are not restricted solely to histones, many non-histone proteins may function in a similar way through mimicking the histones. In this commentary, we briefly discuss a systematic study of the discovery of histone H3 N-terminal mimicry proteins (H3TMs), and their implications in chromatin regulation and drug discoveries.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: DNA / Chromatin / Histones / Protein Processing, Post-Translational Type of study: Systematic review/Meta Analysis Limits: Animals / Humans Language: English Journal: Biochem J Year: 2021 Document Type: Article Affiliation country: BCJ20210357

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Full text: Available Collection: International databases Database: MEDLINE Main subject: DNA / Chromatin / Histones / Protein Processing, Post-Translational Type of study: Systematic review/Meta Analysis Limits: Animals / Humans Language: English Journal: Biochem J Year: 2021 Document Type: Article Affiliation country: BCJ20210357