Dr. David D. Boehr
Department of Chemistry
The Pennsylvania State University, USA
Assistant Professor
Email: ddb12@psu.edu
Qualifications
2004 Ph.D., McMaster University, Biochemistry
1997 B.Sc., University of Lethbridge, Biochemistry
Publications (selected)
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Liu X., Yang X., Lee C.A., Moustafa I.M., Smidansky E.D., Lum D., Arnold J.J., Cameron C.E. and Boehr D.D. (2013), Vaccine-derived mutation in motif D of poliovirus RNA-dependent RNA polymerase lowers nucleotide incorporation fidelity. J. Biol. Chem., in press.
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Boehr D.D., Schnell J.R., McElheny D., Bae S.H., Duggan B.M., Benkovic S.J., Dyson H.J. and Wright P.E. (2013), A distal mutation perturbs dynamic amino acid networks in dihydrofolate reductase. Biochemistry, 52, 4605-4619.
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Zaccardi M.J., Yezdimer E.M. and Boehr D.D. (2013), Functional identification of the general acid and base in the dehydration step of indole-3-glycerol phosphate synthase catalysis. J. Biol. Chem., 288, 26350-26356.
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Axe J.M. and Boehr D.D. (2013), Long-range interactions in the alpha subunit of tryptophan synthase help to coordinate ligand binding, catalysis and substrate channeling, J. Mol. Biol, 425, 1527-1545.
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Yang X., Smidansky E.D., Maksimchuk K.R., Lum D., Welch J.L., Arnold J.J., Cameron C.E. and Boehr D.D. (2012), Motif D of viral RNA-dependent RNA polymerases determines efficiency and fidelity of nucleotide addition, Structure, 20, 1519-1527.
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Weikl T.R. and Boehr D.D. (2012), Conformational selection and induced changes along the catalytic cycle of Escherichia.coli dihydrofolate reductase. Proteins, 80, 2369-2383.
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Zaccardi M.J., Mannweiler O. and Boehr D.D. (2012), Differences in the catalytic mechanisms of mesophilic and thermophilic indole-3-glycerol phosphate synthase enzymes at their adaptive temperatures, Biochem. Biophys. Res. Comm., 418, 324-329.
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D.D. Boehr (2011), Promiscuity in protein-RNA interactions: Conformational ensembles facilitate molecular recognition in the spliceosome: Conformational diversity in U2AF(65) facilitates binding to diverse RNA sequences, Bioessays, 34, 174-180.
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Yang X., Welch J.L., Arnold J.J. and Boehr D.D. (2010) Long-range interaction networks in the function and fidelity of poliovirus RNA-dependent RNA polymerase studied by nuclear magnetic resonance, Biochemistry, 49, 9361-9371.
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Boehr D.D., McElheny D., Dyson H.J. and Wright P.E. (2010), Millisecond timescale fluctuations in dihydrofolate reductase are exquisitely sensitive to the bound ligands, Proc. Natl. Acad. Sci., 107, 1373-1378.
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Boehr, D.D. (2009), During transitions proteins make fleeting bonds, Cell, 139, 1049-1051.
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Boehr D.D., Nussinov R. and Wright P.E. (2009), The role of dynamic conformational ensembles in biomolecular recognition, Nat. Chem. Biol., 5, 789-796.
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Boehr D.D. and Wright P.E. (2008), How do proteins interact? Science, 320, 1429-1430.
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Boehr D.D., Dyson H.J. and Wright P.E. (2008), Conformational relaxation following hydride transfer plays a limiting role in dihydrofolate reductase catalysis, Biochemistry, 47, 9227-9233.
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Boehr D.D., McElheny D., Dyson H.J. and Wright P.E. (2006), The dynamic energy landscape of dihydrofolate reductase catalysis, Science, 313, 1638-1642.
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Boehr D.D., Dyson H.J. and Wright P.E. (2006), An NMR perspective on enzyme dynamics, Chem. Rev., 106, 3055-3079.
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Boehr D.D., Farley A.R., LaRonde F.J., Murdock T.R., Wright G.D. and Cox J.R. (2005), Establishing the principles of recognition in the adenine-binding region of an aminoglycoside antibiotic kinase [APH(3’)-IIIa], Biochemistry, 44, 12445-12453.
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Boehr D.D., Daigle D.M. and Wright G.D. (2004), Domain-domain interactions in the aminoglycoside antibiotic resistance enzyme AAC(6')-APH(2"), Biochemistry, 43, 9846-9855.
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Draker K.A., Boehr D.D., Elowe N.H., Noga T.J. and Wright G.D. (2003), Functional annotation of putative aminoglycoside antibiotic modifying proteins in Mycobacterium tuberculosis H37Rv., J. Antibiot., 56, 135-142.
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Boehr D.D., Draker K.A., Koteva K., Bains M., Hancock R.E. and Wright G.D. (2003), Broad-spectrum peptide inhibitors of aminoglycoside antibiotic resistance enzymes, Chem. Biol., 10, 189-196.
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Boehr D.D., Jenkins S.I. and Wright G.D. (2003), 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, J. Biol. Chem., 278, 12873-12880.
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Boehr D.D., Farley A.R., Wright G.D. and Cox J.R. (2002), Analysis of the pi-pi stacking interactions between the aminoglycoside antibiotic kinase APH(3')-IIIa and its nucleotide ligands, Chem. Biol, 9, 1209-1217.
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Thompson P.R., Boehr D.D., Berghuis A.M. and Wright G.D. (2002), Mechanism of aminoglycoside antibiotic kinase APH(3')-IIIa: role of the nucleotide positioning loop, Biochemistry, 41, 7001-7007.
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Boehr D.D., Lane W.S. and Wright G.D. (2001), Active site labeling of the gentamicin resistance enzyme AAC(6')-APH(2") by the lipid kinase inhibitor wortmannin, Chem. Biol., 8, 791-800.
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Boehr D.D., Thompson P.R. and Wright G.D. (2001), Molecular mechanism of aminoglycoside antibiotic kinase APH(3')-IIIa: roles of conserved active site residues, J. Biol. Chem., 276, 23929-23936. 26. Sucheck S.J., Wong A.L., Koeller K.M., Boehr D.D., Draker K.A., Sears P., Wright G.D. and Wong C.H. (2000), Design of bifunctional antibiotics that target bacterial rRNA and inhibit resistance-causing enzymes, J. Am. Chem. Soc. 122, 5230-5231.