Publications

Found 37 results
Filters: Author is Tanner, John J  [Clear All Filters]
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Korasick, D. A., Singh, H., Pemberton, T. A., Luo, M., Dhatwalia, R., and Tanner, J. J. (2017) Biophysical investigation of type A PutAs reveals a conserved core oligomeric structure. FEBS J. 10.1111/febs.14165
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Ostrander, E. L., Larson, J. D., Schuermann, J. P., and Tanner, J. J. (2009) A conserved active site tyrosine residue of proline dehydrogenase helps enforce the preference for proline over hydroxyproline as the substrate. Biochemistry. 48, 951-9
Robinson, R., Qureshi, I. A., Klancher, C. A., Rodriguez, P. J., Tanner, J. J., and Sobrado, P. (2015) Contribution to catalysis of ornithine binding residues in ornithine N5-monooxygenase. Arch Biochem Biophys. 585, 25-31
Da Fonseca, I., Qureshi, I. A., Mehra-Chaudhary, R., Kizjakina, K., Tanner, J. J., and Sobrado, P. (2014) Contributions of unique active site residues of eukaryotic UDP-galactopyranose mutases to substrate recognition and active site dynamics. Biochemistry. 53, 7794-804
Campbell, A. C., Becker, D. F., Gates, K. S., and Tanner, J. J. (2020) Covalent Modification of the Flavin in Proline Dehydrogenase by Thiazolidine-2-Carboxylate. ACS Chem Biol. 10.1021/acschembio.9b00935
Dhatwalia, R., Singh, H., Reilly, T. J., and Tanner, J. J. (2015) Crystal structure and tartrate inhibition of Legionella pneumophila histidine acid phosphatase. Arch Biochem Biophys. 585, 32-38
Mehra-Chaudhary, R., Mick, J., Tanner, J. J., Henzl, M. T., and Beamer, L. J. (2011) Crystal structure of a bacterial phosphoglucomutase, an enzyme involved in the virulence of multiple human pathogens. Proteins. 79, 1215-29
Liu, L. - K., and Tanner, J. J. (2018) Crystal Structure of Aldehyde Dehydrogenase 16 Reveals Trans-Hierarchical Structural Similarity and a New Dimer. J Mol Biol. 10.1016/j.jmb.2018.11.030
Luo, M., Arentson, B. W., Srivastava, D., Becker, D. F., and Tanner, J. J. (2012) Crystal structures and kinetics of monofunctional proline dehydrogenase provide insight into substrate recognition and conformational changes associated with flavin reduction and product release. Biochemistry. 51, 10099-108
Dhatwalia, R., Singh, H., Oppenheimer, M., Karr, D. B., Nix, J. C., Sobrado, P., and Tanner, J. J. (2012) Crystal structures and small-angle x-ray scattering analysis of UDP-galactopyranose mutase from the pathogenic fungus Aspergillus fumigatus. J Biol Chem. 287, 9041-51
Singh, H., Felts, R. L., Schuermann, J. P., Reilly, T. J., and Tanner, J. J. (2009) Crystal Structures of the histidine acid phosphatase from Francisella tularensis provide insight into substrate recognition. J Mol Biol. 394, 893-904
Dhatwalia, R., Singh, H., Oppenheimer, M., Sobrado, P., and Tanner, J. J. (2012) Crystal structures of Trypanosoma cruzi UDP-galactopyranose mutase implicate flexibility of the histidine loop in enzyme activation. Biochemistry. 51, 4968-79
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Daudu, O. I., Meeks, K. R., Zhang, L., Seravalli, J., Tanner, J. J., and Becker, D. F. (2023) Functional Impact of a Cancer-Related Variant in Human Δ-Pyrroline-5-Carboxylate Reductase 1.. ACS Omega. 8, 3509-3519
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Dhatwalia, R., Singh, H., Solano, L. M., Oppenheimer, M., Robinson, R. M., Ellerbrock, J. F., Sobrado, P., and Tanner, J. J. (2012) Identification of the NAD(P)H binding site of eukaryotic UDP-galactopyranose mutase. J Am Chem Soc. 134, 18132-8
Wyatt, J. W., Korasick, D. A., Qureshi, I. A., Campbell, A. C., Gates, K. S., and Tanner, J. J. (2020) Inhibition, crystal structures, and in-solution oligomeric structure of aldehyde dehydrogenase 9A1. Arch Biochem Biophys. 691, 108477
Zhu, W., Haile, A. M., Singh, R. K., Larson, J. D., Smithen, D., Chan, J. Y., Tanner, J. J., and Becker, D. F. (2013) Involvement of the β3-α3 loop of the proline dehydrogenase domain in allosteric regulation of membrane association of proline utilization A.. Biochemistry. 52, 4482-91
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Lyons, N. S., Bogner, A. N., Tanner, J. J., and Sobrado, P. (2022) Kinetic and Structural Characterization of a Flavin-Dependent Putrescine -Hydroxylase from . Biochemistry. 61, 2607-2620
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Meeks, K. R., Ji, J., Protopopov, M. V., Tarkhanova, O. O., Moroz, Y. S., and Tanner, J. J. (2024) Novel Fragment Inhibitors of PYCR1 from Docking-Guided X-ray Crystallography. J Chem Inf Model. 64, 1704-1718
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Campbell, A. C., Prater, A. R., Bogner, A. N., Quinn, T. P., Gates, K. S., Becker, D. F., and Tanner, J. J. (2021) Photoinduced Covalent Irreversible Inactivation of Proline Dehydrogenase by S-Heterocycles. ACS Chem Biol. 10.1021/acschembio.1c00427
Pemberton, T. A., Still, B. R., Christensen, E. M., Singh, H., Srivastava, D., and Tanner, J. J. (2012) Proline: Mother Nature's cryoprotectant applied to protein crystallography. Acta Crystallogr D Biol Crystallogr. 68, 1010-8
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Singh, H., Schuermann, J. P., Reilly, T. J., Calcutt, M. J., and Tanner, J. J. (2010) Recognition of nucleoside monophosphate substrates by Haemophilus influenzae class C acid phosphatase. J Mol Biol. 404, 639-49
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Meeks, K. R., Bogner, A. N., and Tanner, J. J. (2024) Screening a knowledge-based library of low molecular weight compounds against the proline biosynthetic enzyme 1-pyrroline-5-carboxylate 1 (PYCR1). Protein Sci. 33, e5072
Christensen, E. M., Bogner, A. N., Vandekeere, A., Tam, G. S., Patel, S. M., Becker, D. F., Fendt, S. - M., and Tanner, J. J. (2020) Screening for Proline Analog Inhibitors of the Proline Cycle Enzyme PYCR1. J Biol Chem. 10.1074/jbc.RA120.016106
Korasick, D. A., Končitíková, R., Kopečná, M., Hájková, E., Vigouroux, A., Moréra, S., Becker, D. F., Šebela, M., Tanner, J. J., and Kopečný, D. (2019) Structural and Biochemical Characterization of Aldehyde Dehydrogenase 12, the Last Enzyme of Proline Catabolism in Plants. J Mol Biol. 431, 576-592
Valentino, H., Korasick, D. A., Bohac, T. J., Shapiro, J. A., Wencewicz, T. A., Tanner, J. J., and Sobrado, P. (2021) Structural and Biochemical Characterization of the Flavin-Dependent Siderophore-Interacting Protein from . ACS Omega. 6, 18537-18547

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