Disruption of the Bacteriophage T4 Mre11 Dimer Interface Reveals a Two-state Mechanism for Exonuclease Activity
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference40 articles.
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1. Mutation of Conserved Mre11 Residues Alter Protein Dynamics to Separate Nuclease Functions;Journal of Molecular Biology;2020-05
2. Functional evaluation of the C-terminal region of bacteriophage T4 Rad50;Biochemical and Biophysical Research Communications;2020-05
3. 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
4. The bacterial Mre11–Rad50 homolog SbcCD cleaves opposing strands of DNA by two chemically distinct nuclease reactions;Nucleic Acids Research;2018-10-02
5. Kinetic Analysis of the Exonuclease Activity of the Bacteriophage T4 Mre11–Rad50 Complex;Methods in Enzymology;2018
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