Rossmann Folds

Rossmann Fold is a structural motif characterized by a repeated β-α-β pattern that forms a conserved nucleotide-binding domain primarily involved in binding dinucleotide cofactors such as NAD+ or FAD in dehydrogenases and other oxidoreductases.

164

Publications

9.7K

Citations

844

Authors

296

Institutions

Publications per year

2017–2026

32

Authors

844

  1. NV
    Nick V. Grishin

    The University of Texas Southwestern Medical Center, United States

    6 publications · 552 citations

    6

    h-index

  2. SY
    Shigeyuki Yokoyama

    The University of Tokyo, Japan

    4 publications · 512 citations

    4

    h-index

  3. AM
    Allan Matte

    Biotechnology Research Institute, Canada

    3 publications · 134 citations

    3

    h-index

  4. LA
    L. Aravind

    National Center for Biotechnology Information, United States

    3 publications · 432 citations

    3

    h-index

  5. AH
    Akira Hara

    Gifu University, Japan

    3 publications · 148 citations

    3

    h-index

1–5 of 844

Venues

  1. Journal of Biological Chemistry

    JBC · 20 publications · 1.3K citations

    18

    h-index

  2. Biochemistry

    18 publications · 859 citations

    15

    h-index

  3. Proceedings of the National Academy of Sciences

    PNAS · 12 publications · 890 citations

    12

    h-index

  4. Nucleic Acids Research

    10 publications · 430 citations

    10

    h-index

  5. Proteins Structure Function and Bioinformatics

    10 publications · 431 citations

    10

    h-index

1–5