Publications

Found 760 results
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Journal Article
Hudson, J. D., Tamilselvan, E., Sotomayor, M., and Cooper, S. R. (2021) A complete Protocadherin-19 ectodomain model for evaluating epilepsy-causing mutations and potential protein interaction sites. Structure. 29, 1128-1143.e4
Liu, D. S., Nivón, L. G., Richter, F., Goldman, P. J., Deerinck, T. J., Yao, J. Z., Richardson, D., Phipps, W. S., Ye, A. Z., Ellisman, M. H., Drennan, C. L., Baker, D., and Ting, A. Y. (2014) Computational design of a red fluorophore ligase for site-specific protein labeling in living cells. Proc Natl Acad Sci U S A. 111, E4551-9
Bryan, C. M., Rocklin, G. J., Bick, M. J., Ford, A., Majri-Morrison, S., Kroll, A. V., Miller, C. J., Carter, L., Goreshnik, I., Kang, A., DiMaio, F., Tarbell, K. V., and Baker, D. (2021) Computational design of a synthetic PD-1 agonist. Proc Natl Acad Sci U S A. 10.1073/pnas.2102164118
Todd, R. C., and Lippard, S. J. (2010) Consequences of cisplatin binding on nucleosome structure and dynamics. Chem Biol. 17, 1334-43
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
Tabtiang, R. K., Cezairliyan, B. O., Grant, R. A., Cochrane, J. C., and Sauer, R. T. (2005) Consolidating critical binding determinants by noncyclic rearrangement of protein secondary structure. Proc Natl Acad Sci U S A. 102, 2305-9
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
Durek, T., Torbeev, V. Yu, and Kent, S. B. H. (2007) Convergent chemical synthesis and high-resolution x-ray structure of human lysozyme. Proc Natl Acad Sci U S A. 104, 4846-51
Fetherolf, M. M., Boyd, S. D., Taylor, A. B., Kim, H. Jong, Wohlschlegel, J. A., Blackburn, N. J., P Hart, J., Winge, D. R., and Winkler, D. D. (2017) Copper-zinc superoxide dismutase is activated through a sulfenic acid intermediate at a copper ion entry site. J Biol Chem. 292, 12025-12040
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
Cavalier, M. C., Pierce, A. D., Wilder, P. T., Alasady, M. J., Hartman, K. G., Neau, D. B., Foley, T. L., Jadhav, A., Maloney, D. J., Simeonov, A., Toth, E. A., and Weber, D. J. (2014) Covalent small molecule inhibitors of Ca(2+)-bound S100B. Biochemistry. 53, 6628-40
Padayatti, P. S., Leung, J. H., Mahinthichaichan, P., Tajkhorshid, E., Ishchenko, A., Cherezov, V., S Soltis, M., J Jackson, B., C Stout, D., Gennis, R. B., and Zhang, Q. (2017) Critical Role of Water Molecules in Proton Translocation by the Membrane-Bound Transhydrogenase. Structure. 25, 1111-1119.e3
Teplova, M., Falschlunger, C., Krasheninina, O., Egger, M., Ren, A., Patel, D. J., and Micura, R. (2019) Crucial Roles of Two Hydrated Mg Ions in Reaction Catalysis of the Pistol Ribozyme. Angew Chem Int Ed Engl. 10.1002/anie.201912522
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
Rashid, R., Liang, B., Baker, D. L., Youssef, O. A., He, Y., Phipps, K., Terns, R. M., Terns, M. P., and Li, H. (2006) Crystal structure of a Cbf5-Nop10-Gar1 complex and implications in RNA-guided pseudouridylation and dyskeratosis congenita. Mol Cell. 21, 249-60
Rashid, R., Liang, B., Baker, D. L., Youssef, O. A., He, Y., Phipps, K., Terns, R. M., Terns, M. P., and Li, H. (2006) Crystal structure of a Cbf5-Nop10-Gar1 complex and implications in RNA-guided pseudouridylation and dyskeratosis congenita. Mol Cell. 21, 249-60
Tu, D., Li, Y., Song, H. Kyu, Toms, A. V., Gould, C. J., Ficarro, S. B., Marto, J. A., Goode, B. L., and Eck, M. J. (2011) Crystal structure of a coiled-coil domain from human ROCK I. PLoS One. 6, e18080
Tu, D., Li, Y., Song, H. Kyu, Toms, A. V., Gould, C. J., Ficarro, S. B., Marto, J. A., Goode, B. L., and Eck, M. J. (2011) Crystal structure of a coiled-coil domain from human ROCK I. PLoS One. 6, e18080
Robart, A. R., Chan, R. T., Peters, J. K., Rajashankar, K. R., and Toor, N. (2014) Crystal structure of a eukaryotic group II intron lariat. Nature. 514, 193-7
Chan, R. T., Robart, A. R., Rajashankar, K. R., Pyle, A. Marie, and Toor, N. (2012) Crystal structure of a group II intron in the pre-catalytic state. Nat Struct Mol Biol. 19, 555-7
Maderbocus, R., Fields, B. L., Hamilton, K., Luo, S., Tran, T. H., Dietrich, L. E. P., and Tong, L. (2017) Crystal structure of a Pseudomonas malonate decarboxylase holoenzyme hetero-tetramer. Nat Commun. 8, 160
Maderbocus, R., Fields, B. L., Hamilton, K., Luo, S., Tran, T. H., Dietrich, L. E. P., and Tong, L. (2017) Crystal structure of a Pseudomonas malonate decarboxylase holoenzyme hetero-tetramer. Nat Commun. 8, 160
Toor, N., Keating, K. S., Taylor, S. D., and Pyle, A. Marie (2008) Crystal structure of a self-spliced group II intron. Science. 320, 77-82

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