Histone Biotinylation
Histone Biotinylation is a post-translational modification in which biotin is covalently attached to specific lysine residues on histone proteins, thereby influencing chromatin structure and gene regulation.
40
Publications
2.3K
Citations
131
Authors
46
Institutions
Publications per year
2017–2026
0
40
Jeanne Hymes, Kristin Fleischhauer, Barry Wolf · Biochemical and Molecular Medicine · 1995 · 166 citations
K8 and K12 are biotinylated in human histone H4
Gabriela Camporeale, Elizabeth E. Shubert, Gautam Sarath et al. · European Journal of Biochemistry · 2004 · 106 citations · Full text
1–5 of 40
131
19
h-index
6
h-index
6
h-index
University of Nebraska–Lincoln, United States
5 publications · 364 citations
5
h-index
5
h-index
1–5 of 131
46
University of Nebraska–Lincoln
Lincoln, United States
19 h-index
76 publications
4.6K citations

Saint Louis University
St Louis, United States
4 h-index
8 publications
512 citations

University of Arkansas for Medical Sciences
Little Rock, United States
3 h-index
4 publications
251 citations
University of Nebraska Medical Center
Omaha, United States
3 h-index
9 publications
504 citations
Nutrition Sciences (Belgium)
Ghent, Belgium
3 h-index
3 publications
193 citations

University of Calgary
Calgary, Canada
3 h-index
8 publications
388 citations

Arkansas Children's Hospital
Little Rock, United States
3 h-index
4 publications
251 citations
United States Department of Agriculture
Washington, United States
2 h-index
2 publications
114 citations
1–8 of 46
JN · 7 publications · 344 citations
7
h-index
JNB · 5 publications · 241 citations
5
h-index
3 publications · 163 citations
3
h-index
3 publications · 142 citations
3
h-index
EJB · 2 publications · 280 citations
2
h-index
1–5