Rad50 Atpase Function

RAD50 ATPase Function is a molecular enzymatic activity that belongs to the ATPase family of proteins and specifically mediates the hydrolysis of ATP to regulate structural dynamics and DNA end tethering during DNA double-strand break repair within the context of the MRN complex.

38

Publications

4.5K

Citations

148

Authors

43

Institutions

Publications per year

2017–2026

9

Authors

148

  1. KH
    Karl‐Peter Hopfner

    Ludwig-Maximilians-Universität München, Germany

    10 publications · 2.2K citations

    10

    h-index

  2. KL
    Katja Lammens

    Ludwig-Maximilians-Universität München, Germany

    7 publications · 688 citations

    7

    h-index

  3. JA
    John A. Tainer

    Scripps Research Institute, United States

    5 publications · 1.8K citations

    5

    h-index

  4. TT
    Tanya T. Paull

    The University of Texas at Austin, United States

    5 publications · 932 citations

    5

    h-index

  5. SW
    Scott W. Nelson

    Iowa State University, United States

    4 publications · 118 citations

    4

    h-index

1–5 of 148

Venues

  1. Nucleic Acids Research

    8 publications · 418 citations

    8

    h-index

  2. Journal of Biological Chemistry

    JBC · 5 publications · 199 citations

    5

    h-index

  3. The EMBO Journal

    5 publications · 510 citations

    5

    h-index

  4. Nature Structural & Molecular Biology

    3 publications · 383 citations

    3

    h-index

  5. Cell

    3 publications · 1.6K citations

    3

    h-index

1–5