Stephen H. Leppla
National Institutes of Health
335 Papers
5.5K Citations
Stephen H. Leppla is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Bacillus anthracis & Anthrax toxin. The author has an hindex of 84, co-authored 325 publications. Previous affiliations of Stephen H. Leppla include Government of the United States of America & Laboratory of Molecular Biology.
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Papers
Proteolytic Inactivation of MAP-Kinase-Kinase by Anthrax Lethal Factor
Nicholas S. Duesbery,Craig P. Webb,Stephen H. Leppla,Valery M. Gordon,Kurt Klimpel,Terry D. Copeland,Natalie G. Ahn,M Oskarsson,Kenji Fukasawa,Ken D. Paull,George F. Vande Woude +10 more
TL;DR: It is shown that LF is a protease that cleaves the amino terminus of mitogen-activated protein kinase kinases 1 and 2 and that this cleavage inactivates MAPKK1 and inhibits the MAPK signal transduction pathway.
1K
Anthrax toxin edema factor: a bacterial adenylate cyclase that increases cyclic AMP concentrations of eukaryotic cells.
TL;DR: It is shown here that EF is an adenylate cyclase [ATP pyrophosphate-lyase (cyclizing), EC 4.6.1] produced by Bacillus anthracis in an inactive form and nearly equals that of the most active known cyclase.
976
Crystal structure of the anthrax toxin protective antigen.
TL;DR: A model of pH-dependent membrane insertion involving the formation of a porin-like, membrane-spanning β-barrel is proposed and proposed for use as a general protein delivery system is proposed.
812
Rapid induction of inflammatory lipid mediators by the inflammasome in vivo
Jakob von Moltke,Norver J. Trinidad,Mahtab Moayeri,Alexander F. Kintzer,Samantha Wang,Nico van Rooijen,Charles R. Brown,Bryan A. Krantz,Stephen H. Leppla,Karsten Gronert,Russell E. Vance +10 more
TL;DR: It is shown that systemic inflammasome activation by flagellin leads to a loss of vascular fluid into the intestine and peritoneal cavity, resulting in rapid death in mice, which identifies eicosanoids as a previously unrecognized cell-type-specific signalling output of the inflammaome with marked physiological consequences in vivo.
452
Crystal structure of the anthrax lethal factor
A.D. Pannifer,T.Y. Wong,Robert Schwarzenbacher,Martin Renatus,Carlo Petosa,Carlo Petosa,Jadwiga Bienkowska,Jadwiga Bienkowska,D.B. Lacy,Robert J. Collier,Sukjoon Park,Stephen H. Leppla,Philip C. Hanna,Robert C. Liddington +13 more
TL;DR: The crystal structure of LF reveals a protein that has evolved through a process of gene duplication, mutation and fusion, into an enzyme with high and unusual specificity.