Crystal Structure of MutS2 Endonuclease Domain and the Mechanism of Homologous Recombination Suppression
Open Access
- 1 November 2008
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 283 (48) , 33417-33427
- https://doi.org/10.1074/jbc.m806755200
Abstract
No abstract availableKeywords
This publication has 56 references indexed in Scilit:
- Analysis of a nuclease activity of catalytic domain of Thermus thermophilus MutS2 by high-accuracy mass spectrometryNucleic Acids Research, 2007
- Nuclease activity of the MutS homologue MutS2 from Thermus thermophilus is confined to the Smr domainNucleic Acids Research, 2007
- Pfam: clans, web tools and servicesNucleic Acids Research, 2006
- Molecular Mechanisms of Mammalian Global Genome Nucleotide Excision RepairChemical Reviews, 2005
- Mechanisms of, and Barriers to, Horizontal Gene Transfer between BacteriaNature Reviews Microbiology, 2005
- Comparative and Evolutionary Analysis of the Bacterial Homologous Recombination SystemsPLoS Genetics, 2005
- Coot: model-building tools for molecular graphicsActa Crystallographica Section D-Biological Crystallography, 2004
- Refinement of Macromolecular Structures by the Maximum-Likelihood MethodActa Crystallographica Section D-Biological Crystallography, 1997
- [20] Processing of X-ray diffraction data collected in oscillation modePublished by Elsevier ,1997
- Endonuclease VII of Phage T4 Triggers Mismatch Correction in VitroJournal of Molecular Biology, 1993