Publications

Found 33 results
Filters: Author is Tanner, John J  [Clear All Filters]
2009
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
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
2010
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
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
2011
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
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
2012
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
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
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
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
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
2013
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
2014
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
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., 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
2015
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
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
Luo, M., and Tanner, J. J. (2015) Structural Basis of Substrate Recognition by Aldehyde Dehydrogenase 7A1. Biochemistry. 54, 5513-22
2017
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
2018
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
2019
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
2020
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
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
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

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