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Molecular Microbiology|December 14, 1999
Helicase motifs: the engine that powers DNA unwindingM C Hall, S W MatsonThe Journal of Biological Chemistry|January 9, 1999
The Escherichia coli MutL protein physically interacts with MutH and stimulates the MutH-associated endonuclease activityM C Hall, S W MatsonThe Journal of Biological Chemistry|July 25, 1997
Mutation of a highly conserved arginine in motif IV of Escherichia coli DNA helicase II results in an ATP-binding defectM C Hall, S W MatsonJournal of Molecular Biology|June 6, 1998
Site-directed mutations in motif VI of Escherichia coli DNA helicase II result in multiple biochemical defects: evidence for the involvement of motif VI in the coupling of ATPase and DNA binding activities via conformational changesM C Hall, A Z Ozsoy, S W MatsonThe EMBO Journal|April 18, 1998
Evidence for a physical interaction between the Escherichia coli methyl-directed mismatch repair proteins MutL and UvrDM C Hall, J R Jordan, S W MatsonThe Journal of Biological Chemistry|April 23, 1999
Escherichia coli DNA helicase II is active as a monomerL E Mechanic, M C Hall, S W MatsonThe Journal of Biological Chemistry|August 5, 1986
Escherichia coli helicase II (urvD gene product) translocates unidirectionally in a 3' to 5' directionS W MatsonProceedings of the National Academy of Sciences of the United States of America|June 1, 1989
Escherichia coli DNA helicase II (uvrD gene product) catalyzes the unwinding of DNA.RNA hybrids in vitroS W MatsonProgress in Nucleic Acid Research and Molecular Biology|January 1, 1991
DNA helicases of Escherichia coliS W MatsonJournal of Bacteriology|April 1, 1981
Short deoxyribonucleic acid repair patch length in Escherichia coli is determined by the processive mechanism of deoxyribonucleic acid polymerase IS W Matson, R A BambaraPageof 13