Histone Formylation

Histone Formylation is a post-translational modification in which a formyl group is covalently attached to specific amino acid residues on histone proteins, thereby altering chromatin structure and function through chemical modification of the histone tail.

7

Publications

781

Citations

42

Authors

30

Institutions

Publications per year

2017–2026

2

Authors

42

  1. KC
    Kuo‐Chen Chou

    The Gordon Life Science Institute, United States

    1 publications · 172 citations

    1

    h-index

  2. ZX
    Zhaochun Xu

    Harbin Institute of Technology, China

    1 publications · 172 citations

    1

    h-index

  3. FL
    Fahui Li

    Chinese Academy of Sciences, China

    1 publications · 28 citations

    1

    h-index

  4. PK
    Pirkko‐Liisa Kellokumpu‐Lehtinen

    1 publications · 134 citations

    1

    h-index

  5. TP
    Thorsten Pfirrmann

    Martin Luther University Halle-Wittenberg, Germany

    1 publications · 55 citations

    1

    h-index

1–5 of 42

Venues

  1. Proceedings of the National Academy of Sciences

    PNAS · 1 publications · 207 citations

    1

    h-index

  2. ChemBioChem

    1 publications · 28 citations

    1

    h-index

  3. Scientific Reports

    1 publications · 55 citations

    1

    h-index

  4. Planta

    1 publications · 21 citations

    1

    h-index

  5. Nucleic Acids Research

    1 publications · 164 citations

    1

    h-index

1–5