PubMed:24550389 / 1095-1501 JSONTXT

Annnotations TAB JSON ListView MergeView

    c_corpus

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of an Msh2-Msh6/Msh3 chimeric protein and mutant Msh2-Msh3 complexes showed that the nucleotide binding domain and communicating regions but not the mispair binding domain of Msh2-Msh3 are responsible for the extremely rapid dissociation of Msh2-Msh3 sliding clamps from DNA relative to that seen for Msh2-Msh6, and that amino acid residues predicted to stabilize Msh2-Msh3 interactions with bent,"}

    UseCases_ArguminSci_Discourse

    {"project":"UseCases_ArguminSci_Discourse","denotations":[{"id":"T12","span":{"begin":0,"end":406},"obj":"DRI_Approach"}],"text":"Analysis of an Msh2-Msh6/Msh3 chimeric protein and mutant Msh2-Msh3 complexes showed that the nucleotide binding domain and communicating regions but not the mispair binding domain of Msh2-Msh3 are responsible for the extremely rapid dissociation of Msh2-Msh3 sliding clamps from DNA relative to that seen for Msh2-Msh6, and that amino acid residues predicted to stabilize Msh2-Msh3 interactions with bent,"}

    PubMed_ArguminSci

    {"project":"PubMed_ArguminSci","denotations":[{"id":"T8","span":{"begin":0,"end":406},"obj":"DRI_Approach"}],"text":"Analysis of an Msh2-Msh6/Msh3 chimeric protein and mutant Msh2-Msh3 complexes showed that the nucleotide binding domain and communicating regions but not the mispair binding domain of Msh2-Msh3 are responsible for the extremely rapid dissociation of Msh2-Msh3 sliding clamps from DNA relative to that seen for Msh2-Msh6, and that amino acid residues predicted to stabilize Msh2-Msh3 interactions with bent,"}