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Matt Lopper

Associate Professor

Full-Time Faculty

College of Arts and Sciences: Chemistry; School of Engineering: Bioengineering Graduate Program

Contact

Email: Matt Lopper
Phone: 937-229-2674
SC 265

Degrees

  • Ph.D., Biomolecular Chemistry, University of Wisconsin, 2003
  • B.S., Biochemistry, University of Dayton, 1998

Profile

Dr. Matthew Lopper joined the chemistry department in 2007 after doing his Ph.D. thesis work in virology and post-graduate work in structural biology at the University of Wisconsin-Madison. Dr. Lopper returned to the chemistry department at UD where he obtained his undergraduate degree in biochemistry in 1998. His undergraduate research experience was instrumental in his decision to pursue further graduate studies. Hence, he understands the value and impact mentors can have on students. Throughout his scientific career, Dr. Lopper has presented his work at scientific meetings, published his work in peer-reviewed journals, and successfully competed for grants to fund his research. Dr. Lopper firmly believes that the ability to clearly communicate is an essential element of a successful scientist, and he is committed to training students on their path toward becoming independent scientific investigators as well as effective communicators of science.

Faculty perspective

"My students at UD have taught me a great deal about what it means to teach. I have learned that listening to students is just as important as lecturing to them. Students want to know that their ideas and concerns are valued and being a good listener makes a teacher approachable. I think the best way to stimulate curiosity is to make students feel at ease asking questions, and a student who feels confident to question things in the world has taken an important step towards becoming an independent and responsible thinker."

Courses taught

  • CHM 123: General Chemistry
  • CHM 124: General Chemistry
  • CHM 420: Biochemistry
  • CHM 451: General Biochemistry I
  • CHM 452: General Biochemistry II
  • CHM 454: Rational Drug Design
  • CHM 462L: Biochemistry Laboratory

Research interests

  • Discovery of novel inhibitors of bacterial efflux pumps as a way to combat multi-drug resistance in bacteria

Selected publications

Lopper, M. E., Boone, J., Morrow, C. (2015). Deinococcus radiodurans PriA is a pseudohelicase. PLOS ONE, 13. http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0133419

Sunchu, B., Berg, L., Ward, H. E., Lopper, M. E. (2012). Identification of a small molecule PriA helicase inhibitor. Biochemistry, 51, 10137-46. http://pubs.acs.org/doi/abs/10.1021/bi301100w

Berg, L., Lopper, M. E. (2011). The priB Gene of Klebsiella pneumoniae Encodes a 104-Amino Acid Protein That Is Similar in Structure and Function to Escherichia coli PriB. PLoS ONE, 6(9), 4. www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0024494

Feng, C., Sunchu, B., Greenwood, M. E., Lopper, M. E. (2011). A bacterial PriB with weak single-stranded DNA binding activity can stimulate the DNA unwinding activity of its cognate PriA helicase. BMC Microbiology, 11(1), 11. www.biomedcentral.com/1471-2180/11/189

Dong, J., George, N.P., Duckett, K.L., DeBeer, M.A. and Lopper, M.E. (2009) The crystal structure of Neisseria gonorrhoeae PriB reveals mechanistic differences among bacterial DNA replication restart pathways. Nucleic Acids Res, 38, 499-509.

Lopper, M., Boonsombat, R., Sandler, S.J., and Keck, J.L. (2007). "A hand-off mechanism for primosome assembly in replication restart." Mol. Cell, 26: 781-793.

Lopper, M. and Keck, J.L. (2006). "Protein-protein interactions: identification." Encyclopedia of Life Sciences. John Wiley and Sons, Ltd: Chichester. [DOI: 10.1002/9780470015902.a0020491].

Cadman, C.J., Lopper, M., Moon, P.B., Keck, J.L., and McGlynn, P. (2005). "PriB stimulates PriA helicase via an interaction with single-stranded DNA." J Biol Chem. 280: 39693-700.

Lopper, M., Holton, J., and Keck, J.L. (2004). "Crystal structure of PriB, a component of the Escherichia coli replication restart primosome." Structure. 12: 1967-75.

Lopper, M. and Compton, T. (2004). "Coiled-coil domains in glycoproteins B and H are involved in human cytomegalovirus membrane fusion." J Virol. 78:8333-41.

Lopper, M. and Compton, T. (2002). "Disulfide bond configuration of human cytomegalovirus glycoprotein B." J Virol. 76:6073-82.

Simmen, K. A., Singh, J., Luukkonen, B. G., Lopper, M., Bittner, A., Miller, N. E., Jackson, M. R., Compton, T., Fruh, K. (2001). "Global modulation of cellular transcription by human cytomegalovirus is initiated by viral glycoprotein B." PNAS. 98:7140-5.