Year |
Citation |
Score |
2023 |
D'Amico RN, Boehr DD. Allostery, engineering and inhibition of tryptophan synthase. Current Opinion in Structural Biology. 82: 102657. PMID 37467527 DOI: 10.1016/j.sbi.2023.102657 |
0.318 |
|
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 |
0.34 |
|
2020 |
D'Amico RN, Murray AM, Boehr DD. Driving Protein Conformational Cycles in Physiology and Disease: "Frustrated" Amino Acid Interaction Networks Define Dynamic Energy Landscapes: Amino Acid Interaction Networks Change Progressively Along Alpha Tryptophan Synthase's Catalytic Cycle. Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology. e2000092. PMID 32720327 DOI: 10.1002/Bies.202000092 |
0.344 |
|
2020 |
Gorman SD, Winston DS, Sahu D, Boehr DD. Different Solvent and Conformational Entropy Contributions to the Allosteric Activation and Inhibition Mechanisms of Yeast Chorismate Mutase. Biochemistry. PMID 32538627 DOI: 10.1021/Acs.Biochem.0C00277 |
0.395 |
|
2020 |
Gorman SD, Winston DS, Sahu D, Boehr DD. A Six-State Binding Model Gives Rise to Dynamic Activity and Energy Landscapes in Yeast Chorismate Mutase Biophysical Journal. 118: 519a. DOI: 10.1016/J.Bpj.2019.11.2856 |
0.318 |
|
2019 |
Gorman SD, D'Amico RN, Winston DS, Boehr DD. Engineering Allostery into Proteins. Advances in Experimental Medicine and Biology. 1163: 359-384. PMID 31707711 DOI: 10.1007/978-981-13-8719-7_15 |
0.312 |
|
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 |
0.304 |
|
2019 |
Gorman SD, Boehr DD. Energy and Enzyme Activity Landscapes of Yeast Chorismate Mutase at Cellular Concentrations of Allosteric Effectors. Biochemistry. 58: 4058-4069. PMID 31498992 DOI: 10.1021/Acs.Biochem.9B00721 |
0.448 |
|
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 |
0.351 |
|
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 |
0.373 |
|
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 |
0.401 |
|
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 |
0.315 |
|
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 |
0.463 |
|
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 |
0.352 |
|
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 |
0.35 |
|
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 |
0.31 |
|
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 |
0.372 |
|
2016 |
O’Rourke K, Jelowicki A, Boehr D. Controlling Active Site Loop Dynamics in the (β/α)8 Barrel Enzyme Indole-3-Glycerol Phosphate Synthase Catalysts. 6: 129. DOI: 10.3390/Catal6090129 |
0.43 |
|
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 |
0.3 |
|
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 |
0.385 |
|
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 |
0.439 |
|
2015 |
O’Rourke KF, Axe JM, Kerstetter NE, Boehr DD. The Impact of Perturbing Dynamic Amino Acid Networks in a (β/α)8 Barrel Enzyme Biophysical Journal. 108: 528a. DOI: 10.1016/J.Bpj.2014.11.2897 |
0.43 |
|
2015 |
Chan YM, Boehr DD. Allosteric Functional Switch in Poliovirus 3C Protease Biophysical Journal. 108: 528a. DOI: 10.1016/J.Bpj.2014.11.2893 |
0.345 |
|
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 |
0.417 |
|
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 |
0.327 |
|
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 |
0.383 |
|
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 |
0.473 |
|
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 |
0.327 |
|
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 |
0.319 |
|
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 |
0.448 |
|
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 |
0.747 |
|
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 |
0.439 |
|
2013 |
Chan YM, Yang X, Boehr DD. The Role of Phosphatidylinositol Phosphates (PIPs) in Poliovirus Replication Complexes Trafficking to Viral Replication Organelles Biophysical Journal. 104: 98a. DOI: 10.1016/J.Bpj.2012.11.578 |
0.34 |
|
2013 |
Moustafa IM, Korneeva VS, Arnold JJ, Smidansky ED, Marcotte LL, Yang X, Sanchez Farran MA, Maranas JK, Boehr DD, Hogle JM, Colina CM, Cameron CE. Nanosecond-Timescale Dynamics of the Viral RNA-Dependent RNA Polymerase as a Determinant of Incorporation Fidelity Biophysical Journal. 104: 213a. DOI: 10.1016/J.Bpj.2012.11.1204 |
0.411 |
|
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 |
0.335 |
|
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 |
0.406 |
|
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 |
0.401 |
|
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 |
0.346 |
|
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 |
0.372 |
|
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 |
0.574 |
|
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 |
0.506 |
|
2009 |
Boehr DD, Nussinov R, Wright PE. Erratum: The role of dynamic conformational ensembles in biomolecular recognition Nature Chemical Biology. 5: 954-954. DOI: 10.1038/Nchembio1209-954D |
0.478 |
|
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 |
0.546 |
|
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 |
0.466 |
|
2007 |
Wright PE, Boehr DD, McElheny D, Dyson HJ. The Dynamic Energy Landscape of Enzyme Catalysis The Faseb Journal. 21. DOI: 10.1096/Fasebj.21.5.A90-A |
0.537 |
|
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 |
0.51 |
|
2006 |
Boehr DD, Dyson HJ, Wright PE. An NMR perspective on enzyme dynamics. Chemical Reviews. 106: 3055-79. PMID 16895318 DOI: 10.1021/Cr050312Q |
0.552 |
|
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 |
0.605 |
|
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 |
0.763 |
|
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 |
0.727 |
|
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 |
0.744 |
|
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 |
0.671 |
|
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 |
0.599 |
|
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 |
0.685 |
|
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 |
0.65 |
|
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 |
0.684 |
|
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 |
0.731 |
|
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