Publications

Found 38 results
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Campbell, A. C., Stiers, K. M., Del Campo, J. S. Martin, Mehra-Chaudhary, R., Sobrado, P., and Tanner, J. J. (2020) Trapping conformational states of a flavin-dependent N-monooxygenase in crystallo reveals protein and flavin dynamics. J Biol Chem. 10.1074/jbc.RA120.014750
Srivastava, D., Singh, R. K., Moxley, M. A., Henzl, M. T., Becker, D. F., and Tanner, J. J. (2012) The three-dimensional structural basis of type II hyperprolinemia. J Mol Biol. 420, 176-89
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Singh, H., Arentson, B. W., Becker, D. F., and Tanner, J. J. (2014) Structures of the PutA peripheral membrane flavoenzyme reveal a dynamic substrate-channeling tunnel and the quinone-binding site. Proc Natl Acad Sci U S A. 111, 3389-94
Bogner, A. N., Ji, J., and Tanner, J. J. (2022) Structure-based engineering of minimal Proline dehydrogenase domains for inhibitor discovery. Protein Eng Des Sel. 10.1093/protein/gzac016
Bogner, A. N., and Tanner, J. J. (2022) Structure-affinity relationships of reversible proline analog inhibitors targeting proline dehydrogenase. Org Biomol Chem. 10.1039/d1ob02328d
Schuermann, J. P., Tan, A., Tanner, J. J., and Henzl, M. T. (2010) Structure of avian thymic hormone, a high-affinity avian beta-parvalbumin, in the Ca2+-free and Ca2+-bound states. J Mol Biol. 397, 991-1002
Valentino, H., Campbell, A. C., Schuermann, J. P., Sultana, N., Nam, H. G., LeBlanc, S., Tanner, J. J., and Sobrado, P. (2020) Structure and function of a flavin-dependent S-monooxygenase from garlic (). J Biol Chem. 295, 11042-11055
Pemberton, T. A., Srivastava, D., Sanyal, N., Henzl, M. T., Becker, D. F., and Tanner, J. J. (2014) Structural studies of yeast Δ(1)-pyrroline-5-carboxylate dehydrogenase (ALDH4A1): active site flexibility and oligomeric state.. Biochemistry. 53, 1350-9
Singh, H., Reilly, T. J., and Tanner, J. J. (2011) Structural basis of the inhibition of class C acid phosphatases by adenosine 5'-phosphorothioate. FEBS J. 278, 4374-81
Luo, M., and Tanner, J. J. (2015) Structural Basis of Substrate Recognition by Aldehyde Dehydrogenase 7A1. Biochemistry. 54, 5513-22
Bogner, A. N., Stiers, K. M., McKay, C. M., Becker, D. F., and Tanner, J. J. (2021) Structural Basis for the Stereospecific Inhibition of the Dual Proline/Hydroxyproline Catabolic Enzyme ALDH4A1 by Trans-4-Hydroxy-L-Proline. Protein Sci. 10.1002/pro.4131
Korasick, D. A., Owuocha, L. F., Kandoth, P. K., Tanner, J. J., Mitchum, M. G., and Beamer, L. J. (2023) Structural and functional analysis of two SHMT8 variants associated with soybean cyst nematode resistance. FEBS J. 10.1111/febs.16971
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
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
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
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
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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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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
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
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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
Tanner, J. J., Ji, J., Bogner, A. N., Scott, G. K., Patel, S. M., Seravalli, J., Gates, K. S., Benz, C. C., and Becker, D. F. (2024) Noncovalent Inhibition and Covalent Inactivation of Proline Dehydrogenase by Analogs of -Propargylglycine. Biochemistry. 63, 2855-2867
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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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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
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
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

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