HMG proteins 14 and 17 become cross-linked to the globular domain of histone H3 near the nucleosome core particle dyad
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00117a008
Reference31 articles.
1. Primary organization of nucleosomal core particles is invariable in repressed and active nuclei from animal, plant and yeast cells
2. Structure of nucleosomes and organization of internucleosomal DNA in chromatin
3. Crystal structure of the nucleosome core particle at 16 Å resolution
4. Proteolytic Digestion Studies of Chromatin Core-Histone Structure. Identification of the Limit Peptides of Histones H3 and H4
5. The presence of F3-F2a1 dimers and F1 oligomers in chromatin
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1. HMGN1 and 2 remodel core and linker histone tail domains within chromatin;Nucleic Acids Research;2017-07-07
2. Regulation of chromatin structure and function By HMGN proteins;Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms;2010-01
3. HMGN1 Modulates Estrogen-Mediated Transcriptional Activation through Interactions with Specific DNA-Binding Transcription Factors;Molecular and Cellular Biology;2007-12-15
4. Chromosomal protein HMGN1 enhances the acetylation of lysine 14 in histone H3;The EMBO Journal;2005-08-11
5. The role of HMGN proteins in chromatin function;Chromatin Structure and Dynamics: State-of-the-Art;2004
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