Broad domains of histone H3 lysine 4 trimethylation in transcriptional regulation and disease-Reference-Cited by-同舟云学术

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Broad domains of histone H3 lysine 4 trimethylation in transcriptional regulation and disease

Published:2020-02-04 Issue:14 Volume:287 Page:2891-2902
ISSN:1742-464X
Container-title:The FEBS Journal
language:en
Short-container-title:FEBS J

Author:

Park Shinae¹²,Kim Go Woon³,Kwon So Hee³⁴,Lee Jung‐Shin¹²^ORCID

Affiliation:

1. Department of Molecular Bioscience College of Biomedical Science Kangwon National University Chuncheon Korea

2. Critical Zone Frontier Research Laboratory Kangwon National University Chuncheon Korea

3. College of Pharmacy Yonsei Institute of Pharmaceutical Sciences Yonsei University Incheon Korea

4. Department of Integrated OMICS for Biomedical Science Yonsei University Seoul Korea

Funder

National Research Foundation of Korea

Publisher

Wiley

Subject

Cell Biology,Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1111/febs.15219

Reference82 articles.

1. Regulation of chromatin by histone modifications

2. Expression switching in thestevorandPfmc-2TMsuperfamilies inPlasmodium falciparum

3. Studies of the DNA binding properties of histone H4 amino terminus. Thermal denaturation studies reveal that acetylation markedly reduces the binding constant of the H4 “tail” to DNA;Hong L;J Biol Chem,1993

4. A positive role for histone acetylation in transcription factor access to nucleosomal DNA

5. Acetylation of histone H4 plays a primary role in enhancing transcription factor binding to nucleosomal DNA in vitro.

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