Thomas Smith

Dr. Tom Smith received his B.S. (1982), M.S. (1984), and Ph.D. (1985) in Biochemistry from the University of Rochester, Rochester, NY. He was a Postdoctoral Research Associate in crystallography (1985-1987), an Assistant Research Scientist (1988-1989), an Assistant Professor (1989-1994), an Associate Professor (1994-1999), and a Professor (1999-2001) at Purdue University, W. Lafayette IN. In 2001, he joined the DDPSC as a Member and Principal Investigator at the same time became an adjunct Professor at Washington University in St. Louis.

RESEARCH | PUBLICATIONS | RESEARCH TEAM | LAB NEWS

Publications

Allen, A., Islamovic, E., Kaur, J., Gold, S., Shah, D., and Smith, T.J. (2011). Transgenic maize plants expressing the Totivirus antifungal protein, KP4, are highly resistant to corn smut. Plant Biotechnol J, doi:10.1111/j.1467-7652.2011.00590.x.
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Bailey, J., Powell, L., Sinanan, L., Neal, J., Li, M., Smith, T., and Bell, E. (2011). A novel mechanism of V-type zinc inhibition of glutamate dehydrogenase results from disruption of subunit interactions necessary for efficient catalysis. FEBS J 278, 3140-3151.
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Higashi, Y., Kutchan, T.M., and Smith, T.J (2011). Atomic structure of salutaridine reductase from the opium poppy (Papaver somniferum). J Biol Chem 286, 6532-6541.
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Li, M., Li, C., Allen, A., Stanley, C.A., and Smith, T.J. (2011). The structure and allosteric regulation of glutamate dehydrogenase. Neurochem Int 59, 445-455.
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Pakrasi, H.B., and Smith, T.J. (2011). Zinc binding protein, ZnuA. In Handbook of Metalloproteins, A. Messerschmidt, ed (Chichester, UK: John Wiley & Sons, Ltd), pp. 746-754.
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Sagaram, U.S., Pandurangi, R., Kaur, J., Smith, T.J., and Shah, D.M. (2011). Structure-Activity Determinants in Antifungal Plant Defensins MsDef1 and MtDef4 with Different Modes of Action against Fusarium graminearum. PLoS ONE 6, e18550.
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Smith, T.J. (2011). Engineering fungal resistance in crop plants using antifungal proteins from viruses. ISB News Report 2011, 8-10.
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Smith, T.J. (2011). Development of fungal resistance in crop plants using genetic engineering and antifungal proteins from viruses. ISB News Report (in press)
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Smith, T.J., and Stanley, C.A. (2011). Glutamate Dehydrogenase. In Amino Acids in Human Nutrition and Health, F. D'Mello, ed (Oxford: CABI Publishing)
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Smith, T.J. (2011). Glutamate dehydrogenase: structure regulation, and its role in insulin homeostasis. Frontiers in Diabetes In press
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Smith, T.J. (2011). Green tea and control of glutamate dehydrogenase activity. In Tea in Health and Disease Prevention V.R. Preedy, ed (San Diego, CA: Academic Press. In press
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Smith, T.J. (2011). Green Tea Polyphenols in drug discovery - a success or failure? Expert Opin Drug Discov 6, 589-595.
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Smith, T.J. (2011). Structural studies on antibody recognition and neutralization of viruses. Current Opinion in Virology 1, 150-156
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Higashi, Y., Smith, T.J., Jez, J.M., and Kutchan, T.M. (2010). Crystallization and preliminary X-ray diffraction analysis of salutaridine reductase from the opium poppy Papaver somniferum. Acta Crystallogr Sect F Struct Biol Cryst Commun 66, 163-166.
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Katpally, U., and Smith, T.J. (2010). The caliciviruses. Curr Top Microbiol Immunol 343, 23-41.
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Katpally, U., Voss, N.R., Cavazza, T., Taube, S., Rubin, J.R., Young, V.L., Stuckey, J., Ward, V.K., Virgin, H.W.t., Wobus, C.E., and Smith, T.J. (2010). High-resolution cryo-electron microscopy structures of murine norovirus 1 and rabbit hemorrhagic disease virus reveal marked flexibility in the receptor binding domains. J Virol 84, 5836-5841.
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Koropatkin, N.M., and Smith, T.J. (2010). SusG: a unique cell-membrane-associated alpha-amylase from a prominent human gut symbiont targets complex starch molecules. Structure 18, 200-215.
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Li, C., Chen, P., Palladino, A., Narayan, S., Russell, L.K., Sayed, S., Xiong, G., Chen, J., Stokes, D., Butt, Y.M., Jones, P.M., Collins, H.W., Cohen, N.A., Cohen, A.S., Nissim, I., Smith, T.J., Strauss, A.W., Matschinsky, F.M., Bennett, M.J., and Stanley, C.A. (2010). Mechanism of hyperinsulinism in short-chain 3-hydroxyacyl-CoA dehydrogenase deficiency involves activation of glutamate dehydrogenase. J Biol Chem 285, 31806-31818.
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Li, M., Li, C., Allen, A., Stanley, C.A., and Smith, T.J (2010). The structure and allosteric regulation of glutamate dehydrogenase. Neurochem Int, doi:10.1016/j.neuint.2010.1010.1017.
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Taube, S., Rubin, J.R., Katpally, U., Smith, T.J., Kendall, A., Stuckey, J.A., and Wobus, C.E. (2010). High-resolution x-ray structure and functional analysis of the murine norovirus 1 capsid protein protruding domain. J Virol 84, 5695-5705.
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Katpally, U., Fu, T.M., Freed, D.C., Casimiro, D.R., and Smith, T.J. (2009). Antibodies to the buried N terminus of rhinovirus VP4 exhibit cross-serotypic neutralization. J Virol 83, 7040-7048
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Koropatkin, N., Martens, E.C., Gordon, J.I., and Smith, T.J. (2009). Structure of a SusD homologue, BT1043, involved in mucin O-glycan utilization in a prominent human gut symbiont. Biochemistry 48, 1532-1542.
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Li, M., Smith, C.J., Walker, M.T., and Smith, T.J. (2009). Novel inhibitors complexed with glutamate dehydrogenase: allosteric regulation by control of protein dynamics. J Biol Chem 284, 22988-23000.
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Martens, E.C., Koropatkin, N.M., Smith, T.J., and Gordon, J.I. (2009). Complex glycan catabolism by the human gut microbiota: the Bacteroidetes Sus-like paradigm. J Biol Chem 284, 24673-24677.
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Smith, T.J. (2009). Glutamate dehydrogenase; structure, evolution, regulation, and role in insulin homeostasis. Amino Acids 37, S119.
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Smith, T.J. (2009). Structural studies on antibody/virus complexes. In Structural Virology Monographs, M. Agbandje-McKanna and R. McKenna, eds (London: Royal Society of Chemistry), pp. 261-283.
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Allen, A., Snyder, A.K., Preuss, M., Nielsen, E.E., Shah, D.M., and Smith, T.J. (2008). Plant defensins and virally encoded fungal toxin KP4 inhibit plant root growth. Planta 227, 331-339.
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Kakani, K., Reade, R., Katpally, U., Smith, T., and Rochon, D. (2008). Induction of particle polymorphism by cucumber necrosis virus coat protein mutants in vivo. J Virol 82, 1547-1557.
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Katpally, U., Wobus, C.E., Dryden, K., Virgin, H.W.t., and Smith, T.J. (2008). Structure of antibody-neutralized murine norovirus and unexpected differences from viruslike particles. J Virol 82, 2079-2088.
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Koropatkin, N.M., Martens, E.C., Gordon, J.I., and Smith, T.J. (2008). Starch catabolism by a prominent human gut symbiont is directed by the recognition of amylose helices. Structure 16, 1105-1115.
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Smith, T.J., and Stanley, C.A. (2008). Untangling the glutamate dehydrogenase allosteric nightmare. Trends Biochem Sci 33, 557-564.
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Asurmendi, S., Berg, R.H., Smith, T.J., Bendahmane, M., and Beachy, R.N. (2007). Aggregation of TMV CP plays a role in CP functions and in coat-protein-mediated resistance. Virology 366, 98-106.
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Goncalves, R.B., Mendes, Y.S., Soares, M.R., Katpally, U., Smith, T.J., Silva, J.L., and Oliveira, A.C (2007). VP4 protein from human rhinovirus 14 is released by pressure and locked in the capsid by the antiviral compound WIN. J Mol Biol 366, 295-306.
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Jez, J.M., Schachtman, D.P., Berg, R.H., Taylor, C.G., Chen, S., Hicks, L.M., Jaworski, J.G., Smith, T.J., Nielsen, E., and Pikaard, C.S. (2007). Developing a new interdisciplinary lab course for undergraduate and graduate students: Plant cells and proteins. Biochemistry and Molecular Biology Education 35, 410-415.
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Katpally, U., and Smith, T.J. (2007). Pocket factors are unlikely to play a major role in the life cycle of human rhinovirus. J Virol 81, 6307-6315.
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Katpally, U., Kakani, K., Reade, R., Dryden, K., Rochon, D., and Smith, T.J. (2007). Structures of T=1 and T=3 particles of cucumber necrosis virus: evidence of internal scaffolding. J Mol Biol 365, 502-512.
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Koropatkin, N.M., Koppenaal, D.W., Pakrasi, H.B., and Smith, T.J. (2007). The structure of a cyanobacterial bicarbonate transport protein, CmpA. J Biol Chem 282, 2606-2614.
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Koropatkin, N., Randich, A.M., Bhattacharyya-Pakrasi, M., Pakrasi, H.B., and Smith, T.J. (2007). The structure of the iron-binding protein, FutA1, from Synechocystis 6803. J Biol Chem 282, 27468-27477.
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Li, M., Allen, A., and Smith, T.J. (2007). High throughput screening reveals several new classes of glutamate dehydrogenase inhibitors. Biochemistry 46, 15089-15102.
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Allen, A., Kwagh, J., Fang, J., Stanley, C.A., and Smith, T.J. (2004). Evolution of glutamate dehydrogenase regulation of insulin homeostasis is an example of molecular exaptation. Biochemistry 43, 14431-14443.
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Wei, B., Randich, A.M., Bhattacharyya-Pakrasi, M., Pakrasi, H.B., and Smith, T.J. (2007). Possible regulatory role for the histidine-rich loop in the zinc transport protein, ZnuA. Biochemistry 46, 8734-8743.
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Koropatkin, N.M., Pakrasi, H.B., and Smith, T.J. (2006). Atomic structure of a nitrate-binding protein crucial for photosynthetic productivity. Proc Natl Acad Sci U S A 103, 9820-9825.
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Koropatkin, N., Pakrasi, H.B., and Smith, T.J. (2006). Iron-Binding Protein FutA1. (John Wiley & Sons, Ltd).
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Li, C., Allen, A., Kwagh, J., Doliba, N.M., Qin, W., Najafi, H., Collins, H.W., Matschinsky, F.M., Stanley, C.A., and Smith, T.J. (2006). Green tea polyphenols modulate insulin secretion by inhibiting glutamate dehydrogenase. J Biol Chem 281, 10214-10221.
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Allen, A., Kwagh, J., Fang, J., Stanley, C.A., and Smith, T.J. (2004). Evolution of glutamate dehydrogenase regulation of insulin homeostasis is an example of molecular exaptation. Biochemistry 43, 14431-14443.
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Ke, J., Schmidt, T., Chase, E., Bozarth, R.F., and Smith, T.J. (2004). Structure of Cowpea mottle virus: a consensus in the genus Carmovirus. Virology 321, 349-358.
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Smith, T.J. (2004). MolViewX: a molecular visualization program for the Macintosh OS X system. Journal of Applied Crystallography 37, 654-657.
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Spelbrink, R.G., Dilmac, N., Allen, A., Smith, T.J., Shah, D.M., and Hockerman, G.H. (2004). Differential Antifungal and Calcium Channel-Blocking Activity among Structurally Related Plant Defensins. Plant Physiol 135, 2055-2067.
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Banerjee, S., Wei, B., Bhattacharyya-Pakrasi, M., Pakrasi, H.B., and Smith, T.J. (2003). Structural determinants of metal specificity in the zinc transport protein ZnuA from synechocystis 6803. J Mol Biol 333, 1061-1069.
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Banerjee, S., Schmidt, T., Fang, J., Stanley, C.A., and Smith, T.J. (2003). Structural studies on ADP activation of mammalian glutamate dehydrogenase and the evolution of regulation. Biochemistry 42, 3446-3456.
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Li, C., Najafi, H., Daikhin, Y., Nissim, I.B., Collins, H.W., Yudkoff, M., Matschinsky, F.M., and Stanley, C.A. (2003). Regulation of leucine-stimulated insulin secretion and glutamine metabolism in isolated rat islets. J Biol Chem 278, 2853-2858.
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Reisdorph, N., Thomas, J.J., Katpally, U., Chase, E., Harris, K., Siuzdak, G., and Smith, T.J. (2003). Human rhinovirus capsid dynamics is controlled by canyon flexibility. Virology 314, 34-44.
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Smith, T.J. (2003). Structural studies on antibody-virus complexes. Adv Protein Chem 64, 409-453.
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Bowman, V.D., Chase, E.S., Franz, A.W., Chipman, P.R., Zhang, X., Perry, K.L., Baker, T.S., and Smith, T.J. (2002). An antibody to the putative aphid recognition site on cucumber mosaic virus recognizes pentons but not hexons. J Virol 76, 12250-12258.
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Fang, J., Hsu, B.Y., MacMullen, C.M., Poncz, M., Smith, T.J., and Stanley, C.A. (2002). Expression, purification and characterization of human glutamate dehydrogenase (GDH) allosteric regulatory mutations. Biochem J 363, 81-87.
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Gage, M.J., Rane, S.G., Hockerman, G.H., and Smith, T.J. (2002). The virally encoded fungal toxin KP4 specifically blocks L-type voltage-gated calcium channels. Mol Pharmacol 61, 936-944.
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Liu, S., He, X., Park, G., Josefsson, C., and Perry, K.L. (2002). A conserved capsid protein surface domain of Cucumber mosaic virus is essential for efficient aphid vector transmission. J Virol 76, 9756-9762.
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Smith, T.J. (2002). Antibody interactions with rhinovirus. In Molecular Biology of Picornaviruses, B.L. Semler and E. Wimmer, eds (Washington, D.C.: ASM Press), pp. 39-49.
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Smith, T.J., Schmidt, T., Fang, J., Wu, J., Siuzdak, G., and Stanley, C.A. (2002). The structure of apo human glutamate dehydrogenase details subunit communication and allostery. J Mol Biol 318, 765-777.
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Broo, K., Wei, J., Marshall, D., Brown, F., Smith, T.J., Johnson, J.E., Schneemann, A., and Siuzdak, G. (2001). Viral capsid mobility: a dynamic conduit for inactivation. Proc Natl Acad Sci U S A 98, 2274-2277.
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Gage, M.J., Bruenn, J., Fischer, M., Sanders, D., and Smith, T.J. (2001). KP4 fungal toxin inhibits growth in Ustilago maydis by blocking calcium uptake. Mol. Microbiol. 41, 775-786.
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MacMullen, C., Fang, J., Hsu, B.Y., Kelly, A., de Lonlay-Debeney, P., Saudubray, J.M., Ganguly, A., Smith, T.J., and Stanley, C.A. (2001). Hyperinsulinism/hyperammonemia syndrome in children with regulatory mutations in the inhibitory guanosine triphosphate-binding domain of glutamate dehydrogenase. J Clin Endocrinol Metab 86, 1782-1787.
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Smith, T.J. (2001). Antibody interactions with rhinovirus; lessons for mechanisms of neutralization and the role of immunity in viral evolution. In Current Topics in Microbiology and Immunology., D.R. Burton, ed (New York: Springer-Verlag), pp. 1-28.
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Smith, T.J., Peterson, P.E., Schmidt, T., Fang, J., and Stanley, C.A. (2001). Structures of bovine glutamate dehydrogenase complexes elucidate the mechanism of purine regulation. J Mol Biol 307, 707-720.
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Smith, T.J., Chase, E., Schmidt, T., and Perry, K.L. (2000). The structure of cucumber mosaic virus and comparison to cowpea chlorotic mottle virus. J Virol 74, 7578-7586.
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Oliveira, A.C., Ishimaru, D., Goncalves, R.B., Smith, T.J., Mason, P., Sa-Carvalho, D., and Silva, J.L. (1999). Low temperature and pressure stability of picornaviruses: implications for virus uncoating. Biophys J 76, 1270-1279.
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Peterson, P.E., and Smith, T.J. (1999). The structure of bovine glutamate dehydrogenase provides insights into the mechanism of allostery. Structure 7, 769-782.
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Smith, T.J., and Baker, T. (1999). Picornaviruses: epitopes, canyons, and pockets. Adv Virus Res 52, 1-23.
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Che, Z., Olson, N.H., Leippe, D., Lee, W.M., Mosser, A.G., Rueckert, R.R., Baker, T.S., and Smith, T.J. (1998). Antibody-mediated neutralization of human rhinovirus 14 explored by means of cryoelectron microscopy and X-ray crystallography of virus-Fab complexes. J Virol 72, 4610-4622.
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Lewis, J.K., Bothner, B., Smith, T.J., and Siuzdak, G. (1998). Antiviral agent blocks breathing of the common cold virus. Proc Natl Acad Sci U S A 95, 6774-6778.
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Lewis, J.K., Bendahmane, M., Smith, T.J., Beachy, R.N., and Siuzdak, G. (1998). Identification of viral mutants by mass spectrometry. Proc Natl Acad Sci U S A 95, 8596-8601.
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Peterson, P.E., Pierce, J., and Smith, T.J. (1997). Crystallization and characterization of bovine liver glutamate dehydrogenase. J Struct Biol 120, 73-77.
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Rossmann, M.G., Greve, J.M., Kolatkar, P.R., Olson, N.H., Smith, T.J., McKinlay, M.A., and Rueckert, R.R. (1997). Rhinovirus attachment and cell entry. In Structural Biology of Viruses, W. Chiu, R. Burnett, and R. Garcea, eds (New York: Oxford University Press), pp. 105-133.
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Smith, T.J., and Mosser, A.G. (1997). Antibody-mediated neutralization of picornaviruses. In Structure Biology of Viruses, W. Chiu, R. Burnett, and R. Garcea, eds (New York: Oxford University Press), pp. 134-156.
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Gu, F., Khimani, A., Rane, S.G., Flurkey, W.H., Bozarth, R.F., and Smith, T.J. (1996). The structure of a virally encoded fungal toxin from Ustilago maydis that inhibits fungal and mammalian Ca2+ channels. In Protein Toxin Structure, M. Parker, ed (New York: Springer), pp. 291-303.
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Smith, T.J., Chase, E.S., Schmidt, T.J., Olson, N.H., and Baker, T.S. (1996). Neutralizing antibody to human rhinovirus 14 penetrates the receptor-binding canyon. Nature 383, 350-354.
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Smith, T.J., Olson, N.H., Zhe, Z., Chase, E., Mosser, A., Leippe, D., Cheng, H., Rueckert, R.R., and Baker, T.S. (1996). Structural studies on virus-antibody interactions. In Cold Spring Harbor Symposium Proceedings (Cold Spring Harbor: Vaccines96), pp. 161-167.
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Gu, F., Khimani, A., Rane, S.G., Flurkey, W.H., Bozarth, R.F., and Smith, T.J. (1995). Structure and function of a virally encoded fungal toxin from Ustilago maydis: a fungal and mammalian Ca2+ channel inhibitor. Structure 3, 805-814.
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Smith, T.J. (1995). Introduction: Antibody recognition in viruses. Semin. Virol. 6, 217-218
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Smith, T.J. (1995). MolView, freeware for analyzing and viewing atomic structures. SciTech Journal 5, 24-25
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Smith, T.J. (1995). MolView: a program to analyze and display atomic structures on the Macintosh personal computer. J. Mol. Graphics 13, 122-125
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Smith, T.J., Cheng, R.H., Olson, N.H., Peterson, P., Chase, E., Kuhn, R.J., and Baker, T.S. (1995). Putative receptor binding sites on alphaviruses as visualized by cryoelectron microscopy. Proc Natl Acad Sci U S A 92, 10648-10652.
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Smith, T.J., Mosser, A.G., and Baker, T.S. (1995). Structural studies on the mechanisms of antibody-mediated neutralization of human rhinovirus. Seminar in Virology 6, 233-242
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Cheng, R.H., Caston, J.R., Wang, G.J., Gu, F., Smith, T.J., Baker, T.S., Bozarth, R.F., Trus, B.L., Cheng, N., Wickner, R.B., and et al. (1994). Fungal virus capsids, cytoplasmic compartments for the replication of double-stranded RNA, formed as icosahedral shells of asymmetric Gag dimers. J Mol Biol 244, 255-258.
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Gu, F., Sullivan, T.S., Che, Z., Ganesa, C., Flurkey, W.H., Bozarth, R.F., and Smith, T.J. (1994). The characterization and crystallization of a virally encoded Ustilago maydis KP4 toxin. J Mol Biol 243, 792-795.
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Liu, H., Smith, T.J., Lee, W.M., Mosser, A.G., Rueckert, R.R., Olson, N.H., Cheng, R.H., and Baker, T.S. (1994). Structure determination of an Fab fragment that neutralizes human rhinovirus 14 and analysis of the Fab-virus complex. J Mol Biol 240, 127-137.
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Saraswat, N., Alleman, J.E., and Smith, T.J. (1994). Enzyme Immunoassay Detection of Nitrosomonas europaea. Appl Environ Microbiol 60, 1969-1973.
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Rossmann, M.G., Smith, T.J., and Rueckert, R.R. (1993). The structure of human rhinovirus 14. Structure Introductory Issue, xxiv-xxv
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Smith, T.J. (1993). MacInPlot II-an updated program to display electron density and atomic models on the MacIntosh personal computer. J. Appl. Cryst. 26, 496-498
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Smith, T.J., Olson, N.H., Cheng, R.H., Chase, E.S., and Baker, T.S. (1993). Structure of a human rhinovirus-bivalently bound antibody complex: implications for viral neutralization and antibody flexibility. Proc Natl Acad Sci U S A 90, 7015-7018.
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Smith, T.J., Olson, N.H., Cheng, R.H., Liu, H., Chase, E.S., Lee, W.M., Leippe, D.M., Mosser, A.G., Rueckert, R.R., and Baker, T.S. (1993). Structure of human rhinovirus complexed with Fab fragments from a neutralizing antibody. J Virol 67, 1148-1158.
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Olson, N.H., Smith, T.J., Kolatkar, P.R., Oliveira, M.A., Rueckert, R.R., Greve, J.M., Rossmann, M.G., and Baker, T.S. (1992). Cryoelectron microscopy of complexes of human rhinovirus with a monoclonal Fab and the viral cellular receptor. Proc. Elect. Microsc. Soc. of Amer. 50, 524-525
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Smith, T.J., and Chase, E.S. (1992). Purification and crystallization of intact human rhinovirus complexed with a neutralizing Fab. Virology 191, 600-606.
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Smith, T.J. (1992). Purification of mouse antibodies and Fab fragments. In Methods in Cell Biology, D. Asai, ed (New York, New York: Academic Press, Inc.), pp. 75-93
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Boege, U., Kobasa, D., Onodera, S., Parks, G.D., Palmenberg, A.C., and Scraba, D.G. (1991). Characterization of Mengo virus neutralization epitopes. Virology 181, 1-13.
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Tsao, J., Chapman, M.S., Agbandje, M., Keller, W., Smith, K., Wu, H., Luo, M., Smith, T.J., Rossmann, M.G., Compans, R.W., and et al. (1991). The three-dimensional structure of canine parvovirus and its functional implications. Science 251, 1456-1464.
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Kim, S., Boege, U., Krishnaswamy, S., Minor, I., Smith, T.J., Luo, M., Scraba, D.G., and Rossmann, M.G. (1990). Conformational variability of a picornavirus capsid: pH-dependent structural changes of Mengo virus related to its host receptor attachment site and disassembly. Virology 175, 176-190.
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Prongay, A.J., Smith, T.J., Rossmann, M.G., Ehrlich, L.S., Carter, C.A., and McClure, J. (1990). Preparation and crystallization of a human immunodeficiency virus p24-Fab complex. Proc Natl Acad Sci U S A 87, 9980-9984.
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Smith, T.J., Badger, J., Kremer, M., Oliveira, M., Rossmann, M.G., McKinlay, M.A., Diana, G.D., Pavear, D.C., Dutko, F.J., Rueckert, R.R., Heinz, B., and Shepard, D. (1990). Crystallographic and pharmacological studies of antiviral agents against human rhinovirus. (New York: Springer-Verlag).
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Smith, T.J. (1990). MacInPlot - a program to display electron density and atomic models on the Macintosh personal computer. J. Appl. Cryst. 23, 141-142
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Willingmann, P., Krishnaswamy, S., McKenna, R., Smith, T.J., Olson, N.H., Rossmann, M.G., Stow, P.L., and Incardona, N.L. (1990). Preliminary investigation of the phage phi X174 crystal structure. J Mol Biol 212, 345-350.
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Badger, J., Minor, I., Oliveira, M.A., Smith, T.J., and Rossmann, M.G. (1989). Structural analysis of antiviral agents that interact with the capsid of human rhinoviruses. Proteins 6, 1-19.
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Boege, U., Cygler, M., Wengler, G., Dumas, P., Tsao, J., Luo, M., Smith, T.J., and Rossmann, M.G. (1989). Sindbis virus core protein crystals. J Mol Biol 208, 79-82.
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Diana, G.D., Otto, M.J., Treasurywala, A.M., McKinlay, M.A., Oglesby, R.C., Maliski, E.G., Rossmann, M.G., and Smith, T.J. (1988). Enantiomeric effects of homologues of disoxaril on the inhibitory activity against human rhinovirus-14. J Med Chem 31, 540-544.
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Heinz, B.A., Rueckert, R.R., Shepard, D.A., Dutko, F.J., McKinlay, M.A., Fancher, M., Rossmann, M.G., Badger, J., and Smith, T.J. (1989). Genetic and molecular analyses of spontaneous mutants of human rhinovirus 14 that are resistant to an antiviral compound. J Virol 63, 2476-2485.
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Kim, S.S., Smith, T.J., Chapman, M.S., Rossmann, M.C., Pevear, D.C., Dutko, F.J., Felock, P.J., Diana, G.D., and McKinlay, M.A. (1989). Crystal structure of human rhinovirus serotype 1A (HRV1A). J Mol Biol 210, 91-111.
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Smith, T.J. (1989). Approaches to antiviral drug design. (New York: Mercel Dekker).
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Badger, J., Minor, I., Kremer, M.J., Oliveira, M.A., Smith, T.J., Griffith, J.P., Guerin, D.M., Krishnaswamy, S., Luo, M., Rossmann, M.G., and et al. (1988). Structural analysis of a series of antiviral agents complexed with human rhinovirus 14. Proc Natl Acad Sci U S A 85, 3304-3308.
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Diana, G.D., Pevear, D.C., Otto, M.J., McKinlay, M.A., Rossmann, M.G., Smith, T., and Badger, J. (1989). Inhibitors of viral uncoating. Pharmacol Ther 42, 289-305.
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Rossmann, M.G., Arnold, E., Kamer, G., Kremer, M.J., Luo, M., Smith, T.J., Vriend, G., Rueckert, R.R., Mosser, A.G., Sherry, B., Boege, U., Scraba, D.G., McKinlay, M.A., and Diana, G.D. (1987). Viral particles at atomic resolution. (New York: Plenum Press).
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Rossmann, M.G., Arnold, E., Kamer, G., Kremer, M.J., Luo, M., Smith, T.J., Vriend, G., Rueckert, R.R., Mosser, A.G., Sherry, B., Boege, U., Scraba, D.G., McKinlay, M.A., and Diana, G.D. (1987). Structure and function of human rhinovirus 14 and Mengo virus: Neutralizing antigenic sites, putative receptor binding site, neutralization by drug binding. (New York: Alan R. Liss).
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Rossmann, M.G., Arnold, E., Griffith, J.P., Kamer, G., Luo, M., Smith, T.J., Vriend, G., Rueckert, R.R., Sherry, B., McKinlay, M.A., Diana, G., and Otto, M. (1987). Common cold viruses. Trends Biochem. Sci. 12, 313-318
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Smith, T.J. (1987). The isolation of the two electrophoretic forms of cowpea mosaic virus using fast protein liquid chromatography. J Virol Methods 16, 263-269.
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Smith, T.J., and Bell, J.E. (1986). An exponential gradient marker for use with minigel polyacrylamide electrophoresis systems. Anal Biochem 152, 74-77.
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Smith, T.J., Kremer, M.J., Luo, M., Vriend, G., Arnold, E., Kamer, G., Rossmann, M.G., McKinlay, M.A., Diana, G.D., and Otto, M.J. (1986). The site of attachment in human rhinovirus 14 for antiviral agents that inhibit uncoating. Science 233, 1286-1293.
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Smith, T.J., and Bell, J.E. (1985). Investigation of the effects of crosslinking glutamate dehydrogenase with dimethyl pimelimidate. Arch Biochem Biophys 239, 63-73.
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Smith, T.J. (1985). The mechanisms of, and roles for site-site interactions in glutamate dehydrogenase. In Biochemisty (Rochester: University of Rochester Medical School).
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Smith, T., and Bell, J.E. (1982). Mechanism of hysteresis in bovine glutamate dehydrogenase: role of subunit interactions. Biochemistry 21, 733-737.
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