{"id":2552,"date":"2023-09-06T15:06:59","date_gmt":"2023-09-06T19:06:59","guid":{"rendered":"https:\/\/www.bates.edu\/chemistry-biochemistry\/?page_id=2552"},"modified":"2023-09-06T15:07:08","modified_gmt":"2023-09-06T19:07:08","slug":"t-glen-lawson","status":"publish","type":"page","link":"https:\/\/www.bates.edu\/chemistry-biochemistry\/t-glen-lawson\/","title":{"rendered":"T. Glen Lawson"},"content":{"rendered":"
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\"\"<\/a><\/figure>\n<\/div>\n\n\n
Charles A. Dana Professor Emeritus<\/h5>\n\n\n\n
Associations<\/h5>\n\n\n\n

Chemistry and Biochemistry<\/strong><\/p>\n\n\n\n

<\/div>\n\n\n\n

tlawson@bates.edu<\/p>\n\n\n\n

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About<\/h4>\n\n\n\n

Ph. D., Purdue University; B.S., Anderson University<\/strong><\/p>\n\n\n\n

Research Interests<\/h5>\n\n\n\n

To learn more about Glen’s research, teaching, and writing, please visit his website<\/a>.<\/p>\n\n\n\n

Selected Publications<\/h5>\n\n\n\n

Carmody, M., Zimmer*, J. T., Cushman*, C. H., Nguyen*, T., and Lawson, T. G. (2018) The Ubiquitin-Protein Ligase E6AP\/UBE3A Supports Early Encephalomyocarditis Virus Replication. Virus Res.<\/em> 252<\/strong>, 48 – 57.<\/p>\n\n\n\n

Carmody, M., Notarianni*, T. P., Sambel*, L. A., Walsh*, S. J., Burke*, J. M., Armstrong*, J. L., and Lawson, T. G. (2017) E6AP\/UBE3A Catalyzes Encephalomyocarditis Virus 3C Protease Polyubiquitylation and Promotes its Concentration Reduction in Virus-infected Cells. Biochem. Biophys. Res. Commun.<\/em> 494<\/strong>, 63 -67.<\/p>\n\n\n\n

Yong Z., Mao, D., Roswit, W. T., Jin, X., Patel, A. C., Patel, D. A., Agapov, E., Wang, Z., Tidwell, R. M., Atkinson, J. J., Huang, G., McCarthy, R., Yu, J., Yun, N. E., Paessler, S., Lawson, T. G., Omattage, N. S., Brett, T. J., and Holtzman, M. J. (2015) PARP9-DTX3L Forms a Dual-Function Ubiquitin Ligase that Controls Host and Pathogen. Nature Immunology<\/em> 16<\/strong>, 1215-1231.<\/p>\n\n\n\n

Papon, L., Oteiza, A., Imaizumi, T., Kato, H., Brocchi, E., Lawson, T. G., Akira, S., and Mechti, N. (2009) The Viral RNA Recognition Sensor RIG-I is Degraded during Encephalomyocarditis Virus (EMCV) Infection. Virology<\/em> 393<\/strong>, 311-318.<\/p>\n\n\n\n

Eldin, P., Papon, L., Oteiza, A., Brocchi, E., Lawson, T. G., and Mechti, N. (2009) TRIMM22 E3 Ubiquitin Ligase Activity is Required to Mediate Antiviral Activity against Encephalomyocarditis Virus (EMCV). J. Gen. Virology<\/em> 90<\/strong>, 536-545.<\/p>\n\n\n\n

Schlax, P. E., Zhang*, J., Lewis*, E., Planchart, A., and Lawson, T. G. (2007) Degradation of the Encephalomyocarditis Virus and and Hepatitis A Virus 3C Proteases by the Ubiquitin\/26S Proteasome System in vivo<\/em>. Virology<\/em> 360<\/strong>, 350-363.<\/p>\n\n\n\n

Losick*, V. P., Schlax, P. E., Emmons*, R. A., and Lawson, T. G. (2003) Signals in Hepatitis A Virus P3 Region Proteins Recognized by the Ubiquitin-mediated Proteolytic System. Virology<\/em> 309<\/strong>, 306-319.<\/p>\n\n\n\n

Lam, Y. A., Lawson, T. G., Velayutham, M., Zweier, J., and Pickart, C. M. (2002) ATPase Subunit of the 26S Proteasome Recognizes Polyubiquitin Chains. Nature<\/em> 416,<\/strong> 763-767.<\/p>\n\n\n\n

Lawson, T. G., Sweep*, M. E., Schlax, P. E., Bohnsack, R. N., and Haas, A. L. (2001) Kinetic Analysis of the Conjugation of Ubiquitin to Picornavirus 3C Proteases Catalyzed by the Mammalian Ubiquitin-Protein Ligase E3alpha. J. Biol. Chem.<\/em> 276<\/strong>, 39629-39637.<\/p>\n\n\n\n

Lawson, T. G., Gronros, D. L., Evans*, P. E., Bastien*, M. C., Michalewich*, K. M., Clark*, J. K., Edmonds*, J. H., Graber*, K. H., Werner*, J. A., Lurvey*, B. A., and Cate*, J. M. (1999) Identification and Characterization of a Protein Destruction Signal in the Encephalomyocarditis Virus 3C Protease. J. Biol. Chem.<\/em> 274<\/strong>, 9871-9880.<\/p>\n\n\n\n

Gladding*, R. L., Haas*, A. L., Gronros, D. L., and Lawson, T. G. (1997) Evaluation of the Susceptibility of the 3C Proteases of Hepatitis A Virus and Poliovirus to Degradation by the Ubiquitin-mediated Proteolytic System. Biochem. Biophys. Res. Commun.<\/em> 238<\/strong>, 119 -125.<\/p>\n\n\n\n

Lawson, T. G. (1995). An Analysis of the Involvement of Purine Ribonucleotides in Eukaryotic Protein Synthesis. An Undergraduate Biochemistry Laboratory Experiment. J. Chem. Educ.<\/em> 72<\/strong>, 1041-1043.<\/p>\n\n\n\n

Lawson, T. G., Gronros, D. L., Werner*, J. A., Wey*, A. C., DiGeorge*, A. M., Lockhart*, J. L., Wilson*, J. W., and Wintrode*, P. L. (1994) The Encephalomyocarditis Virus 3C Protease Is a Substrate for the Ubiquitin-mediated Proteolytic System. J. Biol. Chem.<\/em> 269<\/strong>, 28429-28435.<\/p>\n\n\n\n

Oberst*, M. D., Gollan*, T. J., Gupta*, M., Peura*, S. R., Zydlewski*, J. D., Sudarsanan*, P., and Lawson, T. G. (1993) The Encephalomyocarditis Virus 3C Protease Is Rapidly Degraded by an ATP-Dependent Proteolytic System in Reticulocyte Lysate. Virology<\/em> 193<\/strong>, 28-40.<\/p>\n\n\n\n

Lawson, T. G., Smith, L. L., Palmenberg, A. C., and Thach, R. E. (1989) Inducible Expression of the Encephalomyocarditis Virus 3C Protease Activity in Stably Transformed Mouse Cell Lines. J. Virology<\/em> 63<\/strong>, 5013-5022.<\/p>\n\n\n\n

Lawson, T. G., Lee, K. A., Maimone, M. M., Abramson, R. D., Dever, T. E., Merrick, W. C., and Thach, R. E. (1989) Dissociation of Double-Stranded Polynucleotide Helical Structures by Eukaryotic Initiation Factors, as Revealed by a Novel Assay. Biochemistry<\/em> 28<\/strong>, 4729-4734.<\/p>\n\n\n\n

Lawson, T. G., Cladaras, M. H., Ray, B. K., Lee, K. A., Abramson, R. D., Merrick, W. C., and Thach, R. E. (1988) Discriminatory Interaction of Purified Eukaryotic Initiation Factors 4F Plus 4A with the 5′ Ends of Reovirus Messenger RNAs. J. Biol. Chem.<\/em> 263<\/strong>, 7266-7276.<\/p>\n\n\n\n

Abramson, R. D., Browning, K. S., Dever, T. E., Lawson, T. G., Thach, R. E., Ravel, J. M., and Merrick, W. C. (1988) Initiation Factors that Bind mRNA: A Comparison of Mammalian Factors with Wheat Germ Factors. J. Biol. Chem.<\/em> 263<\/strong>, 5462-5467.<\/p>\n\n\n\n

Abramson, R. D., Dever, T. E., Lawson, T. G., Ray, B. K., Thach, R. E., and Merrick, W. C. (1987) The ATP-Dependent Interaction of Eukaryotic Initiation Factors with mRNA. J. Biol. Chem.<\/em> 262<\/strong>, 3826-3832.<\/p>\n\n\n\n

Lawson, T. G., Ray, B. K., Dodds, J. T., Grifo, J. A., Abramson, R. D., Merrick, W. C., Betsch, D. F., Weith, H. L., and Thach, R. E. (1986) Influence of 5′ Proximal Secondary Structure on the Translational Efficiency of Eukaryotic mRNAs and on Their Interaction with Initiation Factors. J. Biol. Chem.<\/em> 261<\/strong>, 13979-13989.<\/p>\n\n\n\n

Ray, B. K., Lawson, T. G., Abramson, R. D., Merrick, W. C., and Thach, R. E. (1986) Recycling of mRNA Cap Binding Proteins Mediated by eIF-4B. J. Biol. Chem.<\/em> 261<\/strong>, 11466-11470.<\/p>\n\n\n\n

Ray, B. K., Lawson, T. G., Kramer, J. C., Cladaras, M. H., Grifo, J. A., Abramson, R. D., Merrick, W. C., and Thach, R. E. (1985) ATP-Dependent Unwinding of Messenger RNA Structure by Eukaryotic Initiation Factors. J. Biol. Chem.<\/em> 260<\/strong>, 7651-7658.<\/p>\n\n\n\n

(*undergraduate students)<\/p>\n\n\n\n

Links<\/h4>\n\n\n\n
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Research Website<\/a>
<\/p>\n<\/div>\n\n\n\n

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<\/p>\n<\/div>\n<\/div>\n","protected":false},"excerpt":{"rendered":"

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