Acetylation of Novel Sites in the Nucleosomal Binding Domain of Chromosomal Protein HMG-14 by p300 Alters Its Interaction with Nucleosomes-Reference-Cited by-同舟云学术

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Acetylation of Novel Sites in the Nucleosomal Binding Domain of Chromosomal Protein HMG-14 by p300 Alters Its Interaction with Nucleosomes

Published:2000-04 Issue:15 Volume:275 Page:11514-11520
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Bergel Michael,Herrera Julio E.,Thatcher Bradley J.,Prymakowska-Bosak Marta,Vassilev Alex,Nakatani Yoshihiro,Martin Brian,Bustin Michael

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference39 articles.

1. Structure and Function of the Core Histone N-Termini: More Than Meets the Eye

2. Covalent modifications of histones: expression from chromatin templates

3. Linking histone acetylation to transcriptional regulation

4. Histone acetylation and transcriptional regulatory mechanisms

5. Histone acetyltransferase activity of yeast Gcn5p is required for the activation of target genes in vivo

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3. Protein intrinsic disorder on a dynamic nucleosomal landscape;Progress in Molecular Biology and Translational Science;2021

4. Lysine succinylation on non-histone chromosomal protein HMG-17 (HMGN2) regulates nucleosomal DNA accessibility by disrupting the HMGN2–nucleosome association;RSC Chemical Biology;2021

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