A network of allosterically coupled residues in the bacteriophage T4 Mre11–Rad50 complex
Author:
Affiliation:
1. Department of Biochemistry, Biophysics, and Molecular BiologyIowa State UniversityAmes Iowa50011
Funder
Carver Trust Young Investigator
National Science Foundation
Publisher
Wiley
Subject
Molecular Biology,Biochemistry
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1002/pro.3028
Reference43 articles.
1. The Mre11/Rad50/Nbs1 complex: Recent insights into catalytic activities and ATP-driven conformational changes
2. Biochemical mechanisms of chromosomal translocations resulting from DNA double-strand breaks
3. Tethering on the brink: the evolutionarily conserved Mre11–Rad50 complex
4. Mre11 Dimers Coordinate DNA End Bridging and Nuclease Processing in Double-Strand-Break Repair
5. Structural Biochemistry and Interaction Architecture of the DNA Double-Strand Break Repair Mre11 Nuclease and Rad50-ATPase
Cited by 4 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. The dynamic nature of the Mre11-Rad50 DNA break repair complex;Progress in Biophysics and Molecular Biology;2021-08
2. Adjacent mutations in the archaeal Rad50 ABC ATPase D-loop disrupt allosteric regulation of ATP hydrolysis through different mechanisms;Nucleic Acids Research;2019-12-31
3. Double-mutant cycles: new directions and applications;Current Opinion in Structural Biology;2019-10
4. A dynamic allosteric pathway underlies Rad50 ABC ATPase function in DNA repair;Scientific Reports;2018-01-26
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