The Rad50 zinc-hook is a structure joining Mre11 complexes in DNA recombination and repair

By K. Hopfner, L. Craig, G. Moncalián, Robert A. Zinkel, Takehiko Usui, B. Owen, A. Karcher, B. Henderson, J. Bodmer, C. McMurray and 3 more. Nature, 2002

608 citations recorded by the source corpus.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/3eb530161ce778d3f5cb21921b08e41078ca165c

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In Molecular Biology

1. T. Stracker
2. J. Petrini
3. B. O. Krogh
4. L. Symington
5. Thomas Helleday

Citations in the corpus

• The Physiological, Biochemical, and Molecular Roles of Zinc Transporters in Zinc Homeostasis and Metabolism. (2015, background): “Intermolecular zinc-binding sites consisting of an interface between two or more proteins are generally difficult to identify (7, 265), although a number of important examples have been found (165, 361).”
• Recombination proteins in yeast. (2004, methodology): “PfRad50 forms homodimers in the presence of ATP (75, 78).”
• The MRE11 complex: starting from the ends (2011, background): “At the apex of the RAD50 coils, where the N-terminal and C-terminal stretches fold back on themselves, is a domain called the RAD50 hoo”
• DNA double-strand break repair: from mechanistic understanding to cancer treatment. (2007, background): “The Mre11, Rad50 and Nbs1 protein complex may facilitate tethering of the two DNA ends, and may be less critical under conditions where ends can be directly ligated than under conditions when ends require processing [19–21].”