David D Boehr

Summary

Affiliation: The Scripps Research Institute
Country: USA

Publications

  1. ncbi Biochemistry. How do proteins interact?
    David D Boehr
    Department of Molecular Biology and Skaggs Institute for Chemical Biology, Scripps Research Institute, La Jolla, CA 92037, USA
    Science 320:1429-30. 2008
  2. pmc Millisecond timescale fluctuations in dihydrofolate reductase are exquisitely sensitive to the bound ligands
    David D Boehr
    Department of Molecular Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines, La Jolla, CA 92037, USA
    Proc Natl Acad Sci U S A 107:1373-8. 2010
  3. pmc Conformational relaxation following hydride transfer plays a limiting role in dihydrofolate reductase catalysis
    David D Boehr
    Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA
    Biochemistry 47:9227-33. 2008
  4. ncbi The dynamic energy landscape of dihydrofolate reductase catalysis
    David D Boehr
    Department of Molecular Biology and Skaggs Institute for Chemical Biology, Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    Science 313:1638-42. 2006
  5. ncbi An NMR perspective on enzyme dynamics
    David D Boehr
    Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA
    Chem Rev 106:3055-79. 2006
  6. ncbi Analysis of the pi-pi stacking interactions between the aminoglycoside antibiotic kinase APH(3')-IIIa and its nucleotide ligands
    David D Boehr
    Antimicrobial Research Centre, Department of Biochemistry, McMaster University, 1200 Main Street West, Hamilton, Ontario L8N 3Z5, Canada
    Chem Biol 9:1209-17. 2002
  7. ncbi The molecular basis of the expansive substrate specificity of the antibiotic resistance enzyme aminoglycoside acetyltransferase-6'-aminoglycoside phosphotransferase-2". The role of ASP-99 as an active site base important for acetyl transfer
    David D Boehr
    Antimicrobial Research Centre, Department of Biochemistry, McMaster University, Hamilton, Ontario L8N 3Z5, Canada
    J Biol Chem 278:12873-80. 2003
  8. ncbi Establishing the principles of recognition in the adenine-binding region of an aminoglycoside antibiotic kinase [APH(3')-IIIa]
    David D Boehr
    Antimicrobial Research Centre, Department of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, Ontario, Canada
    Biochemistry 44:12445-53. 2005

Detail Information

Publications8

  1. ncbi Biochemistry. How do proteins interact?
    David D Boehr
    Department of Molecular Biology and Skaggs Institute for Chemical Biology, Scripps Research Institute, La Jolla, CA 92037, USA
    Science 320:1429-30. 2008
  2. pmc Millisecond timescale fluctuations in dihydrofolate reductase are exquisitely sensitive to the bound ligands
    David D Boehr
    Department of Molecular Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines, La Jolla, CA 92037, USA
    Proc Natl Acad Sci U S A 107:1373-8. 2010
    ....
  3. pmc Conformational relaxation following hydride transfer plays a limiting role in dihydrofolate reductase catalysis
    David D Boehr
    Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA
    Biochemistry 47:9227-33. 2008
    ....
  4. ncbi The dynamic energy landscape of dihydrofolate reductase catalysis
    David D Boehr
    Department of Molecular Biology and Skaggs Institute for Chemical Biology, Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    Science 313:1638-42. 2006
    ..Thus, the modulation of the energy landscape by the bound ligands funnels the enzyme through its reaction cycle along a preferred kinetic path...
  5. ncbi An NMR perspective on enzyme dynamics
    David D Boehr
    Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA
    Chem Rev 106:3055-79. 2006
  6. ncbi Analysis of the pi-pi stacking interactions between the aminoglycoside antibiotic kinase APH(3')-IIIa and its nucleotide ligands
    David D Boehr
    Antimicrobial Research Centre, Department of Biochemistry, McMaster University, 1200 Main Street West, Hamilton, Ontario L8N 3Z5, Canada
    Chem Biol 9:1209-17. 2002
    ..This type of information concerning the forces that govern nucleotide binding in APH(3')-IIIa will facilitate inhibitor design strategies that target the nucleotide binding site of APH-type enzymes...
  7. ncbi The molecular basis of the expansive substrate specificity of the antibiotic resistance enzyme aminoglycoside acetyltransferase-6'-aminoglycoside phosphotransferase-2". The role of ASP-99 as an active site base important for acetyl transfer
    David D Boehr
    Antimicrobial Research Centre, Department of Biochemistry, McMaster University, Hamilton, Ontario L8N 3Z5, Canada
    J Biol Chem 278:12873-80. 2003
    ..The prominent role of this residue in aminoglycoside modification can be exploited as an anchoring site for the development of compounds capable of reversing antibiotic resistance in vivo...
  8. ncbi Establishing the principles of recognition in the adenine-binding region of an aminoglycoside antibiotic kinase [APH(3')-IIIa]
    David D Boehr
    Antimicrobial Research Centre, Department of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, Ontario, Canada
    Biochemistry 44:12445-53. 2005
    ..The principles governing adenine recognition established in this study may be applied to other protein-ligand complexes and used to navigate future studies directed at discovering potent and selective inhibitors of APH-type enzymes...