Exploring the Influence of Domain Architecture on the Catalytic Function of Diterpene Synthases von Pemberton, Travis A, Chen, Mengbin, Harris, Golda G, Chou, Wayne K. W, Duan, Lian, Köksal, Mustafa, Genshaft, Alex S, Cane, David E, Christianson, David W

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Multi-domain terpenoid cyclase architecture and prospects for proximity in bifunctional catalysis von Chen, Mengbin, Harris, Golda G, Pemberton, Travis A, Christianson, David W

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General base-general acid catalysis by terpenoid cyclases von Pemberton, Travis A, Christianson, David W

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Structural Basis for the Substrate Inhibition of Proline Utilization A by Proline von Korasick, David A, Pemberton, Travis A, Arentson, Benjamin W, Becker, Donald F, Tanner, John J

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Structural Studies of Yeast Δ1‑Pyrroline-5-carboxylate Dehydrogenase (ALDH4A1): Active Site Flexibility and Oligomeric State von Pemberton, Travis A, Srivastava, Dhiraj, Sanyal, Nikhilesh, Henzl, Michael T, Becker, Donald F, Tanner, John J

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Biophysical investigation of type A PutAs reveals a conserved core oligomeric structure von Korasick, David A., Singh, Harkewal, Pemberton, Travis A., Luo, Min, Dhatwalia, Richa, Tanner, John J.

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Structural basis of substrate selectivity of Δ(1)-pyrroline-5-carboxylate dehydrogenase (ALDH4A1): semialdehyde chain length von Pemberton, Travis A, Tanner, John J

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Crystal Structure of Cucumene Synthase, a Terpenoid Cyclase That Generates a Linear Triquinane Sesquiterpene von Blank, Patrick N, Pemberton, Travis A, Chow, Jeng-Yeong, Poulter, C. Dale, Christianson, David W

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Structural studies of yeast Δ(1)-pyrroline-5-carboxylate dehydrogenase (ALDH4A1): active site flexibility and oligomeric state von Pemberton, Travis A, Srivastava, Dhiraj, Sanyal, Nikhilesh, Henzl, Michael T, Becker, Donald F, Tanner, John J

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Kinetic and Structural Characterization of Tunnel-Perturbing Mutants in Bradyrhizobium japonicum Proline Utilization A von Arentson, Benjamin W, Luo, Min, Pemberton, Travis A, Tanner, John J, Becker, Donald F

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Structural Studies of Geosmin Synthase, a Bifunctional Sesquiterpene Synthase with αα Domain Architecture That Catalyzes a Unique Cyclization–Fragmentation Reaction Sequence von Harris, Golda G, Lombardi, Patrick M, Pemberton, Travis A, Matsui, Tsutomu, Weiss, Thomas M, Cole, Kathryn E, Köksal, Mustafa, Murphy, Frank V, Vedula, L. Sangeetha, Chou, Wayne K. W, Cane, David E, Christianson, David W

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Structural basis of substrate selectivity of Δ1-pyrroline-5-carboxylate dehydrogenase (ALDH4A1): Semialdehyde chain length von Pemberton, Travis A., Tanner, John J.

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Proline: Mother Nature's cryoprotectant applied to protein crystallography von Pemberton, Travis A., Still, Brady R., Christensen, Emily M., Singh, Harkewal, Srivastava, Dhiraj, Tanner, John J.

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Structural Studies of Geosmin Synthase, a Bifunctional Sesquiterpene Synthase with Alpha-Alpha Domain Architecture that Catalyzes a Unique Cyclization-Fragmentation Reaction Sequen... von Harris, Golda G., Lombardi, Patrick M., Pemberton, Travis A., Matsui, Tsutomu, Weiss, Thomas M., Cole, Kathryn E., Köksal, Mustafa, Murphy, Frank V., Vedula, L. Sangeetha, Chou, Wayne K.W., Cane, David E., Christianson, David W.

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Structural Studies of Yeast Delta super(1)-Pyrroline-5-carboxylate Dehydrogenase (ALDH4A1): Active Site Flexibility and Oligomeric State von Pemberton, Travis A, Srivastava, Dhiraj, Sanyal, Nikhilesh, Henzl, Michael T, Becker, Donald F, Tanner, John J

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Structural Studies of Yeast Δ 1 -Pyrroline-5-carboxylate Dehydrogenase (ALDH4A1): Active Site Flexibility and Oligomeric State von Pemberton, Travis A., Srivastava, Dhiraj, Sanyal, Nikhilesh, Henzl, Michael T., Becker, Donald F., Tanner, John J.

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Structural Studies of Geosmin Synthase, a Bifunctional Sesquiterpene Synthase with αα Domain Architecture That Catalyzes a Unique Cyclization–Fragmentation Reaction Sequence von Harris, Golda G., Lombardi, Patrick M., Pemberton, Travis A., Matsui, Tsutomu, Weiss, Thomas M., Cole, Kathryn E., Köksal, Mustafa, Murphy, Frank V., Vedula, L. Sangeetha, Chou, Wayne K. W., Cane, David E., Christianson, David W.

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SARS-CoV-2 vaccination for patients with inflammatory bowel diseases: recommendations from an international consensus meeting von Siegel, Corey A, Melmed, Gil Y, McGovern, Dermot PB, Rai, Victoria, Krammer, Florian, Rubin, David T, Abreu, Maria T, Dubinsky, Marla C, Ahuja, Vineet, Allez, Matthieu, Ananthakrishnan, Ashwin N, Bernstein, Charles N, Braun, Jonathan, Chowers, Yehuda, Colombel, Jean-Frederic, Danese, Silvio, Dignass, Axel, Dotan, Iris, Fleshner, Phillip R, Gasche, Christoph, Gearry, Richard B, Ghosh, Subrata, Griffiths, Anne M, Hanauer, Stephen B, Hart, Ailsa L, Kaplan, Gilaad G, Kaser, Arthur, Kotze, Paulo G, Koutroubakis, Ioannis E, Kruis, Wolfgang, Lakatos, Peter L, Levine, Arie, Lewis, James D, Lindsay, James O, Loftus, Jr, Edward V, Louis, Edouard, Lukas, Milan, Magro, Fernando, Mahadevan, Uma, Mantzaris, Gerasimos J, Moum, Bjørn A, Munkholm, Pia, Ng, Siew C, O’Morain, Colm, Oresland, Tom, Panaccione, Remo, Panes, Julian, Pemberton, John H, Prantera, Cosimo, Ran, Zhihua, Reinisch, Walter, Rogler, Gerhard, Sandborn, William J, Sands, Bruce E, Sartor, Balfour, Schölmerich, Jürgen, Siegmund, Britta, Silverberg, Mark S, Sood, Ajit, Spinelli, Antonino, Steinwurz, Flavio, Travis, Simon, Turner, Dan, Tysk, Curt, Vatn, Morten H, Vermeire, Severine, Yamamoto, Takayuki, Yamamoto-Furusho, Jesus K, Panis, Yves

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Multianalyte Physiological Microanalytical Devices von Davis, Anna Nix, Travis, Adam R, Miller, Dusty R, Cliffel, David E

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The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature von Silverman, G A, Bird, P I, Carrell, R W, Church, F C, Coughlin, P B, Gettins, P G, Irving, J A, Lomas, D A, Luke, C J, Moyer, R W, Pemberton, P A, Remold-O'Donnell, E, Salvesen, G S, Travis, J, Whisstock, J C

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