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Distinct requirements within the Msh3 nucleotide binding pocket for mismatch and double-strand break repair.

Kumar C, Williams GM, Havens B, Dinicola MK, Surtees JA.

J Mol Biol. 2013 Jun 12;425(11):1881-98. doi: 10.1016/j.jmb.2013.02.024. Epub 2013 Feb 28.


ATP binding and hydrolysis by Saccharomyces cerevisiae Msh2-Msh3 are differentially modulated by mismatch and double-strand break repair DNA substrates.

Kumar C, Eichmiller R, Wang B, Williams GM, Bianco PR, Surtees JA.

DNA Repair (Amst). 2014 Jun;18:18-30. doi: 10.1016/j.dnarep.2014.03.032. Epub 2014 Apr 18.


Mispair-specific recruitment of the Mlh1-Pms1 complex identifies repair substrates of the Saccharomyces cerevisiae Msh2-Msh3 complex.

Srivatsan A, Bowen N, Kolodner RD.

J Biol Chem. 2014 Mar 28;289(13):9352-64. doi: 10.1074/jbc.M114.552190. Epub 2014 Feb 18.


Msh2 separation of function mutations confer defects in the initiation steps of mismatch repair.

Kijas AW, Studamire B, Alani E.

J Mol Biol. 2003 Aug 1;331(1):123-38.


Role of Saccharomyces cerevisiae Msh2 and Msh3 repair proteins in double-strand break-induced recombination.

Sugawara N, Pâques F, Colaiácovo M, Haber JE.

Proc Natl Acad Sci U S A. 1997 Aug 19;94(17):9214-9.


Saccharomyces cerevisiae Msh2-Msh3 acts in repair of base-base mispairs.

Harrington JM, Kolodner RD.

Mol Cell Biol. 2007 Sep;27(18):6546-54. Epub 2007 Jul 16.


Redundancy of Saccharomyces cerevisiae MSH3 and MSH6 in MSH2-dependent mismatch repair.

Marsischky GT, Filosi N, Kane MF, Kolodner R.

Genes Dev. 1996 Feb 15;10(4):407-20.


Multiple factors insulate Msh2-Msh6 mismatch repair activity from defects in Msh2 domain I.

Kumar C, Piacente SC, Sibert J, Bukata AR, O'Connor J, Alani E, Surtees JA.

J Mol Biol. 2011 Aug 26;411(4):765-80. doi: 10.1016/j.jmb.2011.06.030. Epub 2011 Jun 25.


The nucleotide binding dynamics of human MSH2-MSH3 are lesion dependent.

Owen BA, H Lang W, McMurray CT.

Nat Struct Mol Biol. 2009 May;16(5):550-7. doi: 10.1038/nsmb.1596. Epub 2009 Apr 19. Erratum in: Nat Struct Mol Biol. 2009 Aug;16(8):897.


Functional studies and homology modeling of Msh2-Msh3 predict that mispair recognition involves DNA bending and strand separation.

Dowen JM, Putnam CD, Kolodner RD.

Mol Cell Biol. 2010 Jul;30(13):3321-8. doi: 10.1128/MCB.01558-09. Epub 2010 Apr 26.


Analysis of yeast MSH2-MSH6 suggests that the initiation of mismatch repair can be separated into discrete steps.

Bowers J, Tran PT, Liskay RM, Alani E.

J Mol Biol. 2000 Sep 15;302(2):327-38.


Requirement of the yeast MSH3 and MSH6 genes for MSH2-dependent genomic stability.

Johnson RE, Kovvali GK, Prakash L, Prakash S.

J Biol Chem. 1996 Mar 29;271(13):7285-8.


Application of stopped-flow kinetics methods to investigate the mechanism of action of a DNA repair protein.

Biro FN, Zhai J, Doucette CW, Hingorani MM.

J Vis Exp. 2010 Mar 31;(37). pii: 1874. doi: 10.3791/1874.


(CAG)(n)-hairpin DNA binds to Msh2-Msh3 and changes properties of mismatch recognition.

Owen BA, Yang Z, Lai M, Gajec M, Badger JD 2nd, Hayes JJ, Edelmann W, Kucherlapati R, Wilson TM, McMurray CT.

Nat Struct Mol Biol. 2005 Aug;12(8):663-70. Epub 2005 Jul 17. Erratum in: Nat Struct Mol Biol. 2005 Sep;12(9):824. Gajek, Maciez [corrected to Gajec, Maciej].


The yeast gene MSH3 defines a new class of eukaryotic MutS homologues.

New L, Liu K, Crouse GF.

Mol Gen Genet. 1993 May;239(1-2):97-108.


Functional interaction of proliferating cell nuclear antigen with MSH2-MSH6 and MSH2-MSH3 complexes.

Clark AB, Valle F, Drotschmann K, Gary RK, Kunkel TA.

J Biol Chem. 2000 Nov 24;275(47):36498-501.

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