Clinton E. Leysath, Ph.D.
Affiliations: | 2008 | Institute for Cellular and Molecular Biology | University of Texas at Austin, Austin, Texas, U.S.A. |
Area:
Antibody and Enzyme EngineeringGoogle:
"Clinton Leysath"Mean distance: 8.61 | S | N | B | C | P |
Parents
Sign in to add mentorBrent L. Iverson | grad student | 2008 | UT Austin | |
(Structure and Engineering of Neutralizing Antibodies to Anthrax Toxin.) |
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Publications
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Chen KH, Liu S, Leysath CE, et al. (2016) Anthrax Toxin Protective Antigen Variants that selectively utilize either the CMG2 or TEM8 Receptors for Cellular Uptake and Tumor Targeting. The Journal of Biological Chemistry |
Moayeri M, Leysath CE, Tremblay JM, et al. (2015) A heterodimer of a VHH (variable domains of camelid heavy chain-only) antibody that inhibits anthrax toxin cell binding linked to a VHH antibody that blocks oligomer formation is highly protective in an anthrax spore challenge model. The Journal of Biological Chemistry. 290: 6584-95 |
Tremblay JM, Mukherjee J, Leysath CE, et al. (2013) A single VHH-based toxin-neutralizing agent and an effector antibody protect mice against challenge with Shiga toxins 1 and 2. Infection and Immunity. 81: 4592-603 |
Mukherjee J, Tremblay JM, Leysath CE, et al. (2012) A novel strategy for development of recombinant antitoxin therapeutics tested in a mouse botulism model. Plos One. 7: e29941 |
Leysath CE, Chen KH, Moayeri M, et al. (2011) Mouse monoclonal antibodies to anthrax edema factor protect against infection. Infection and Immunity. 79: 4609-16 |
Radjainia M, Hyun JK, Leysath CE, et al. (2010) Anthrax toxin-neutralizing antibody reconfigures the protective antigen heptamer into a supercomplex. Proceedings of the National Academy of Sciences of the United States of America. 107: 14070-4 |
Leysath CE, Monzingo AF, Maynard JA, et al. (2009) Crystal structure of the engineered neutralizing antibody M18 complexed to domain 4 of the anthrax protective antigen. Journal of Molecular Biology. 387: 680-93 |
Seo MJ, Jeong KJ, Leysath CE, et al. (2009) Engineering antibody fragments to fold in the absence of disulfide bonds. Protein Science : a Publication of the Protein Society. 18: 259-67 |