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Vanadate inhibits the ATPase activity and DNA binding capability of bacterial MutS. A structural model for the vanadate-MutS interaction at the Walker A motif.
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Vanadate inhibits the ATPase activity and DNA binding capability of bacterial MutS. A structural model for the vanadate-MutS interaction at the Walker A motif.
Vanadate inhibits the ATPase activity and DNA binding capability of bacterial MutS. A structural model for the vanadate-MutS interaction at the Walker A motif. Nucleic Acids Res. 2002 Nov 01; 30(21):4700-8.
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PubMed
subject areas
Adenosine Diphosphate
Adenosine Diphosphate
Adenosine Triphosphatases
Adenosine Triphosphatases
Adenosine Triphosphate
Adenosine Triphosphate
Amino Acid Motifs
Amino Acid Motifs
Amino Acid Sequence
Amino Acid Sequence
Bacterial Proteins
Bacterial Proteins
DNA
DNA
DNA-Binding Proteins
DNA-Binding Proteins
Electrophoretic Mobility Shift Assay
Electrophoretic Mobility Shift Assay
Escherichia coli
Escherichia coli
Escherichia coli Proteins
Escherichia coli Proteins
Ligands
Ligands
Models, Molecular
Models, Molecular
Molecular Sequence Data
Molecular Sequence Data
MutS DNA Mismatch-Binding Protein
MutS DNA Mismatch-Binding Protein
Oligodeoxyribonucleotides
Oligodeoxyribonucleotides
Protein Conformation
Protein Conformation
Pseudomonas aeruginosa
Pseudomonas aeruginosa
Scattering, Radiation
Scattering, Radiation
Temperature
Temperature
Vanadates
Vanadates
authors with profiles
Roberto J Pezza