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
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4.5K
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148
Authors
43
Institutions
Publications per year
2017–2026
9
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38
Structural Biology of Rad50 ATPase
Karl‐Peter Hopfner, Annette Kärcher, David Shin et al. · Cell · 2000 · 913 citations · Full text
The Mre11:Rad50 Structure Shows an ATP-Dependent Molecular Clamp in DNA Double-Strand Break Repair
Katja Lammens, Derk Bemeleit, Carolin Möckel et al. · Cell · 2011 · 209 citations · Full text
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Ludwig-Maximilians-Universität München
Munich, Germany
7 h-index
41 publications
5K citations
Center for Integrated Protein Science Munich
Munich, Germany
6 h-index
10 publications
1.3K citations
Scripps Research Institute
San Diego, United States
5 h-index
25 publications
9.3K citations
National Institutes of Health
Bethesda, United States
4 h-index
6 publications
1.6K citations
The University of Texas at Austin
Austin, United States
4 h-index
17 publications
1.8K citations
Iowa State University
Ames, United States
4 h-index
12 publications
343 citations

Lawrence Berkeley National Laboratory
Berkeley, United States
3 h-index
9 publications
1.7K citations

Tel Aviv University
Tel Aviv, Israel
3 h-index
10 publications
254 citations
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8 publications · 418 citations
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JBC · 5 publications · 199 citations
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5 publications · 510 citations
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3 publications · 383 citations
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3 publications · 1.6K citations
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