Matthew E. Lopper, Ph.D.
Affiliations: | 2003 | University of Wisconsin, Madison, Madison, WI |
Area:
Biochemistry, Microbiology BiologyGoogle:
"Matthew Lopper"Parents
Sign in to add mentorTeresa Compton | grad student | 2003 | UW Madison | |
(Molecular mechanisms of human cytomegalovirus entry.) | ||||
James L. Keck | post-doc | 2004-2007 | UW Madison (Chemistry Tree) |
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Publications
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Lopper ME, Boone J, Morrow C. (2015) Deinococcus radiodurans PriA is a Pseudohelicase. Plos One. 10: e0133419 |
Sunchu B, Berg L, Ward HE, et al. (2012) Identification of a small molecule PriA helicase inhibitor. Biochemistry. 51: 10137-46 |
Berg L, Lopper ME. (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: e24494 |
Feng C, Sunchu B, Greenwood ME, et al. (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: 189 |
Dong J, George NP, Duckett KL, et al. (2010) The crystal structure of Neisseria gonorrhoeae PriB reveals mechanistic differences among bacterial DNA replication restart pathways. Nucleic Acids Research. 38: 499-509 |
Lopper M, Boonsombat R, Sandler SJ, et al. (2007) A hand-off mechanism for primosome assembly in replication restart. Molecular Cell. 26: 781-93 |
Cadman CJ, Lopper M, Moon PB, et al. (2005) PriB stimulates PriA helicase via an interaction with single-stranded DNA. The Journal of Biological Chemistry. 280: 39693-700 |
Lopper M, Holton JM, Keck JL. (2004) Crystal structure of PriB, a component of the Escherichia coli replication restart primosome. Structure (London, England : 1993). 12: 1967-75 |
Lopper M, Compton T. (2004) Coiled-coil domains in glycoproteins B and H are involved in human cytomegalovirus membrane fusion. Journal of Virology. 78: 8333-41 |
Lopper M, Compton T. (2002) Disulfide bond configuration of human cytomegalovirus glycoprotein B. Journal of Virology. 76: 6073-82 |