Histone Deimination
Histone Deimination is a post-translational modification in which arginine residues on histone tails are converted to citrulline through enzymatic deimination, thereby altering chromatin structure and regulating gene expression.
59
Publications
6.6K
Citations
362
Authors
129
Institutions
Publications per year
2017–2026
15
Variants
Histone Citrullination
Parents
59
Human PAD4 Regulates Histone Arginine Methylation Levels via Demethylimination
Yanming Wang, Joanna Wysocka, Joyce Sayegh et al. · Science · 2004 · 995 citations
Histone Deimination Antagonizes Arginine Methylation
Graeme L. Cuthbert, Sylvain Daujat, Andrew Snowden et al. · Cell · 2004 · 823 citations · Full text
Regulation of Extracellular Chromatin Release from Neutrophils
Indira Neeli, Nishant Dwivedi, Salar N. Khan et al. · Journal of Innate Immunity · 2009 · 277 citations · Full text
1–5 of 59
362
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h-index
University of Massachusetts Chan Medical School, United States
8 publications · 836 citations
8
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6
h-index
5
h-index
University of Tennessee Health Science Center, United States
4 publications · 1.1K citations
4
h-index
1–5 of 362
129

Yokohama City University
Yokohama, Japan
9 h-index
34 publications
6.1K citations

Cornell University
Ithaca, United States
9 h-index
35 publications
16.3K citations
Scripps Research Institute
San Diego, United States
5 h-index
9 publications
634 citations
University of Tennessee Health Science Center
Memphis, United States
4 h-index
11 publications
3.3K citations
University College London
London, United Kingdom
3 h-index
10 publications
872 citations
University of South Carolina
Columbia, United States
3 h-index
11 publications
2K citations

Nanjing Medical University
Nanjing, China
3 h-index
17 publications
1.2K citations
University of Westminster
London, United Kingdom
3 h-index
7 publications
302 citations
1–8 of 129
JBC · 4 publications · 671 citations
4
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JACS · 4 publications · 299 citations
4
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3 publications · 383 citations
3
h-index
3 publications · 328 citations
3
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MCB · 2 publications · 112 citations
2
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1–5