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David D. Boehr - Publications

Chemistry Pennsylvania State University, State College, PA, United States 
protein dynamics in enzyme function, coordination and regulation

47 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2021 D'Amico RN, Bosken YK, O'Rourke KF, Murray AM, Admasu W, Chang CA, Boehr DD. Substitution of a Surface-Exposed Residue Involved in an Allosteric Network Enhances Tryptophan Synthase Function in Cells. Frontiers in Molecular Biosciences. 8: 679915. PMID 34124159 DOI: 10.3389/fmolb.2021.679915  0.8
2020 O'Rourke KF, D'Amico RN, Sahu D, Boehr DD. Distinct conformational dynamics and allosteric networks in alpha tryptophan synthase during active catalysis. Protein Science : a Publication of the Protein Society. PMID 33314435 DOI: 10.1002/pro.4011  0.8
2019 Boehr AK, Arnold JJ, Oh HS, Cameron CE, Boehr DD. 2'-C-Methylated nucleotides terminate virus RNA synthesis by preventing active site closure of the viral RNA-dependent RNA polymerase. The Journal of Biological Chemistry. PMID 31575662 DOI: 10.1074/Jbc.Ra119.010214  0.4
2019 Shi J, Perryman JM, Yang X, Liu X, Musser DM, Boehr AK, Moustafa IM, Arnold JJ, Cameron CE, Boehr DD. Rational control of poliovirus RNA-dependent RNA polymerase fidelity by modulating motif D loop conformational dynamics. Biochemistry. PMID 31424194 DOI: 10.1021/Acs.Biochem.9B00497  0.4
2019 O'Rourke KF, Sahu D, Bosken YK, D'Amico RN, Chang CA, Boehr DD. Coordinated Network Changes across the Catalytic Cycle of Alpha Tryptophan Synthase. Structure (London, England : 1993). PMID 31257109 DOI: 10.1016/J.Str.2019.05.013  0.8
2018 O'Rourke KF, Axe JM, D'Amico RN, Sahu D, Boehr DD. Millisecond Timescale Motions Connect Amino Acid Interaction Networks in Alpha Tryptophan Synthase. Frontiers in Molecular Biosciences. 5: 92. PMID 30467546 DOI: 10.3389/Fmolb.2018.00092  0.8
2018 Gorman SD, Sahu D, O'Rourke KF, Boehr DD. Assigning methyl resonances for protein solution-state NMR studies. Methods (San Diego, Calif.). PMID 29958930 DOI: 10.1016/J.Ymeth.2018.06.010  0.8
2018 Boehr DD, D'Amico RN, O'Rourke KF. Engineered control of enzyme structural dynamics and function. Protein Science : a Publication of the Protein Society. PMID 29380452 DOI: 10.1002/Pro.3379  0.8
2017 Shengjuler D, Chan YM, Sun S, Moustafa IM, Li ZL, Gohara DW, Buck M, Cremer PS, Boehr DD, Cameron CE. The RNA-Binding Site of Poliovirus 3C Protein Doubles as a Phosphoinositide-Binding Domain. Structure (London, England : 1993). 25: 1875-1886.e7. PMID 29211985 DOI: 10.1016/J.Str.2017.11.001  0.56
2017 Yang X, Liu X, Musser DM, Moustafa IM, Arnold JJ, Cameron CE, Boehr DD. Triphosphate Re-orientation of the Incoming Nucleotide as a Fidelity Checkpoint in Viral RNA-dependent RNA polymerases. The Journal of Biological Chemistry. PMID 28100782 DOI: 10.1074/Jbc.M116.750638  0.4
2016 O'Rourke KF, Gorman SD, Boehr DD. Biophysical and computational methods to analyze amino acid interaction networks in proteins. Computational and Structural Biotechnology Journal. 14: 245-51. PMID 27441044 DOI: 10.1016/J.Csbj.2016.06.002  0.8
2016 Chan YM, Moustafa IM, Arnold JJ, Cameron CE, Boehr DD. Long-Range Communication between Different Functional Sites in the Picornaviral 3C Protein. Structure (London, England : 1993). 24: 509-17. PMID 27050688 DOI: 10.1016/J.Str.2016.02.019  1
2015 Liu X, Musser DM, Lee CA, Yang X, Arnold JJ, Cameron CE, Boehr DD. Nucleobase but not Sugar Fidelity is Maintained in the Sabin I RNA-Dependent RNA Polymerase. Viruses. 7: 5571-5586. PMID 26516899 DOI: 10.3390/V7102894  1
2015 van der Linden L, Vives-Adrián L, Selisko B, Ferrer-Orta C, Liu X, Lanke K, Ulferts R, De Palma AM, Tanchis F, Goris N, Lefebvre D, De Clercq K, Leyssen P, Lacroix C, Pürstinger G, ... ... Boehr DD, et al. The RNA template channel of the RNA-dependent RNA polymerase as a target for development of antiviral therapy of multiple genera within a virus family. Plos Pathogens. 11: e1004733. PMID 25799064 DOI: 10.1371/Journal.Ppat.1004733  1
2015 Axe JM, O'Rourke KF, Kerstetter NE, Yezdimer EM, Chan YM, Chasin A, Boehr DD. Severing of a hydrogen bond disrupts amino acid networks in the catalytically active state of the alpha subunit of tryptophan synthase. Protein Science : a Publication of the Protein Society. 24: 484-94. PMID 25377949 DOI: 10.1002/Pro.2598  1
2014 Moustafa IM, Korboukh VK, Arnold JJ, Smidansky ED, Marcotte LL, Gohara DW, Yang X, Sánchez-Farrán MA, Filman D, Maranas JK, Boehr DD, Hogle JM, Colina CM, Cameron CE. Structural dynamics as a contributor to error-prone replication by an RNA-dependent RNA polymerase. The Journal of Biological Chemistry. 289: 36229-48. PMID 25378410 DOI: 10.1074/Jbc.M114.616193  1
2014 Boehr DD, Liu X, Yang X. Targeting structural dynamics of the RNA-dependent RNA polymerase for anti-viral strategies. Current Opinion in Virology. 9: 194-200. PMID 25224392 DOI: 10.1016/J.Coviro.2014.08.006  1
2014 Axe JM, Yezdimer EM, O'Rourke KF, Kerstetter NE, You W, Chang CE, Boehr DD. Amino acid networks in a (β/α)₈ barrel enzyme change during catalytic turnover. Journal of the American Chemical Society. 136: 6818-21. PMID 24766576 DOI: 10.1021/Ja501602T  1
2014 Zaccardi MJ, O'Rourke KF, Yezdimer EM, Loggia LJ, Woldt S, Boehr DD. Loop-loop interactions govern multiple steps in indole-3-glycerol phosphate synthase catalysis. Protein Science : a Publication of the Protein Society. 23: 302-11. PMID 24403092 DOI: 10.1002/Pro.2416  1
2014 Boehr DD. The ins and outs of viral RNA polymerase translocation. Journal of Molecular Biology. 426: 1373-6. PMID 24394889 DOI: 10.1016/J.Jmb.2013.12.030  1
2013 Liu X, Yang X, Lee CA, Moustafa IM, Smidansky ED, Lum D, Arnold JJ, Cameron CE, Boehr DD. Vaccine-derived mutation in motif D of poliovirus RNA-dependent RNA polymerase lowers nucleotide incorporation fidelity. The Journal of Biological Chemistry. 288: 32753-65. PMID 24085299 DOI: 10.1074/Jbc.M113.484428  1
2013 Zaccardi MJ, Yezdimer EM, Boehr DD. Functional identification of the general acid and base in the dehydration step of indole-3-glycerol phosphate synthase catalysis. The Journal of Biological Chemistry. 288: 26350-6. PMID 23900843 DOI: 10.1074/Jbc.M113.487447  1
2013 Boehr DD, Schnell JR, McElheny D, Bae SH, Duggan BM, Benkovic SJ, Dyson HJ, Wright PE. A distal mutation perturbs dynamic amino acid networks in dihydrofolate reductase. Biochemistry. 52: 4605-19. PMID 23758161 DOI: 10.1021/Bi400563C  1
2013 Axe JM, Boehr DD. Long-range interactions in the α subunit of tryptophan synthase help to coordinate ligand binding, catalysis, and substrate channeling. Journal of Molecular Biology. 425: 1527-45. PMID 23376097 DOI: 10.1016/J.Jmb.2013.01.030  1
2012 Yang X, Smidansky ED, Maksimchuk KR, Lum D, Welch JL, Arnold JJ, Cameron CE, Boehr DD. Motif D of viral RNA-dependent RNA polymerases determines efficiency and fidelity of nucleotide addition. Structure (London, England : 1993). 20: 1519-27. PMID 22819218 DOI: 10.1016/J.Str.2012.06.012  1
2012 Weikl TR, Boehr DD. Conformational selection and induced changes along the catalytic cycle of Escherichia coli dihydrofolate reductase. Proteins. 80: 2369-83. PMID 22641560 DOI: 10.1002/Prot.24123  1
2012 Zaccardi MJ, Mannweiler O, Boehr DD. Differences in the catalytic mechanisms of mesophilic and thermophilic indole-3-glycerol phosphate synthase enzymes at their adaptive temperatures. Biochemical and Biophysical Research Communications. 418: 324-9. PMID 22274606 DOI: 10.1016/J.Bbrc.2012.01.020  1
2012 Boehr DD. Promiscuity in protein-RNA interactions: conformational ensembles facilitate molecular recognition in the spliceosome: conformational diversity in U2AF⁶⁵ facilitates binding to diverse RNA sequences. Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology. 34: 174-80. PMID 22144099 DOI: 10.1002/Bies.201100152  1
2010 Yang X, Welch JL, Arnold JJ, Boehr DD. Long-range interaction networks in the function and fidelity of poliovirus RNA-dependent RNA polymerase studied by nuclear magnetic resonance. Biochemistry. 49: 9361-71. PMID 20860410 DOI: 10.1021/Bi100833R  1
2010 Boehr DD, McElheny D, Dyson HJ, Wright PE. Millisecond timescale fluctuations in dihydrofolate reductase are exquisitely sensitive to the bound ligands. Proceedings of the National Academy of Sciences of the United States of America. 107: 1373-8. PMID 20080605 DOI: 10.1073/Pnas.0914163107  1
2009 Boehr DD. During transitions proteins make fleeting bonds. Cell. 139: 1049-51. PMID 20005798 DOI: 10.1016/J.Cell.2009.11.031  1
2009 Boehr DD, Nussinov R, Wright PE. The role of dynamic conformational ensembles in biomolecular recognition. Nature Chemical Biology. 5: 789-96. PMID 19841628 DOI: 10.1038/Nchembio.232  1
2008 Boehr DD, Dyson HJ, Wright PE. Conformational relaxation following hydride transfer plays a limiting role in dihydrofolate reductase catalysis. Biochemistry. 47: 9227-33. PMID 18690714 DOI: 10.1021/Bi801102E  1
2008 Boehr DD, Wright PE. Biochemistry. How do proteins interact? Science (New York, N.Y.). 320: 1429-30. PMID 18556537 DOI: 10.1126/Science.1158818  1
2006 Boehr DD, McElheny D, Dyson HJ, Wright PE. The dynamic energy landscape of dihydrofolate reductase catalysis. Science (New York, N.Y.). 313: 1638-42. PMID 16973882 DOI: 10.1126/Science.1130258  1
2006 Boehr DD, Dyson HJ, Wright PE. An NMR perspective on enzyme dynamics. Chemical Reviews. 106: 3055-79. PMID 16895318 DOI: 10.1021/Cr050312Q  1
2005 Boehr DD, Farley AR, LaRonde FJ, Murdock TR, Wright GD, Cox JR. Establishing the principles of recognition in the adenine-binding region of an aminoglycoside antibiotic kinase [APH(3')-IIIa]. Biochemistry. 44: 12445-53. PMID 16156657 DOI: 10.1021/Bi051085P  1
2004 Boehr DD, Daigle DM, Wright GD. Domain-domain interactions in the aminoglycoside antibiotic resistance enzyme AAC(6')-APH(2''). Biochemistry. 43: 9846-55. PMID 15274639 DOI: 10.1021/Bi049135Y  1
2003 Draker KA, Boehr DD, Elowe NH, Noga TJ, Wright GD. Functional annotation of putative aminoglycoside antibiotic modifying proteins in Mycobacterium tuberculosis H37Rv. The Journal of Antibiotics. 56: 135-42. PMID 12715873 DOI: 10.7164/Antibiotics.56.135  1
2003 Boehr DD, Draker KA, Koteva K, Bains M, Hancock RE, Wright GD. Broad-spectrum peptide inhibitors of aminoglycoside antibiotic resistance enzymes. Chemistry & Biology. 10: 189-96. PMID 12618191 DOI: 10.1016/S1074-5521(03)00026-7  1
2003 Boehr DD, Jenkins SI, Wright GD. 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. The Journal of Biological Chemistry. 278: 12873-80. PMID 12566434 DOI: 10.1074/Jbc.M211680200  1
2002 Boehr DD, Farley AR, Wright GD, Cox JR. Analysis of the pi-pi stacking interactions between the aminoglycoside antibiotic kinase APH(3')-IIIa and its nucleotide ligands. Chemistry & Biology. 9: 1209-17. PMID 12445771 DOI: 10.1016/S1074-5521(02)00245-4  1
2002 Thompson PR, Boehr DD, Berghuis AM, Wright GD. Mechanism of aminoglycoside antibiotic kinase APH(3')-IIIa: role of the nucleotide positioning loop. Biochemistry. 41: 7001-7. PMID 12033933 DOI: 10.1021/Bi0256680  1
2001 Boehr DD, Lane WS, Wright GD. Active site labeling of the gentamicin resistance enzyme AAC(6')-APH(2") by the lipid kinase inhibitor wortmannin. Chemistry & Biology. 8: 791-800. PMID 11514228 DOI: 10.1016/S1074-5521(01)00051-5  1
2001 Boehr DD, Thompson PR, Wright GD. Molecular mechanism of aminoglycoside antibiotic kinase APH(3')-IIIa: roles of conserved active site residues. The Journal of Biological Chemistry. 276: 23929-36. PMID 11279088 DOI: 10.1074/Jbc.M100540200  1
2000 Weselake RJ, Kazala EC, Cianflone K, Boehr DD, Middleton CK, Rennie CD, Laroche A, Recnik I. Human acylation stimulating protein enhances triacylglycerol biosynthesis in plant microsomes. Febs Letters. 481: 189-92. PMID 10996321 DOI: 10.1016/S0014-5793(00)01996-7  1
2000 Sucheck SJ, Wong AL, Koeller KM, Boehr DD, Draker KA, Sears P, Wright GD, Wong CH. Design of bifunctional antibiotics that target bacterial rRNA and inhibit resistance-causing enzymes [11] Journal of the American Chemical Society. 122: 5230-5231. DOI: 10.1021/Ja000575W  1
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