M
Martin Renatus
Researcher at Novartis
Publications - 55
Citations - 5859
Martin Renatus is an academic researcher from Novartis. The author has contributed to research in topics: Caspase & Plasminogen activator. The author has an hindex of 18, co-authored 51 publications receiving 5491 citations. Previous affiliations of Martin Renatus include Sanford-Burnham Institute for Medical Research & École Normale Supérieure.
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Journal ArticleDOI
A unified model for apical caspase activation.
Kelly M. Boatright,Martin Renatus,Fiona L. Scott,Sabina Sperandio,Hwain Shin,Irene M. Pedersen,Jean-Ehrland Ricci,Wade Edris,Daniel P. Sutherlin,Douglas R. Green,Guy S. Salvesen +10 more
TL;DR: A unified caspase activation hypothesis is proposed whereby apical caspases are activated by dimerization of monomeric zymogens, and single amino acid substitutions at the dimer interface abrogate the activity of caspased-8 and -9 introduced into recipient mammalian cells.
Journal ArticleDOI
Structural Basis for the Inhibition of Caspase-3 by XIAP
Stefan J. Riedl,Martin Renatus,Robert Schwarzenbacher,Qiao Zhou,Chaohong Sun,Stephen W. Fesik,Robert C. Liddington,Guy S. Salvesen +7 more
TL;DR: The crystal structure of the second BIR domain of XIAP (BIR2) in complex with caspase-3, at a resolution of 2.7 A, is reported, revealing the structural basis for inhibition and the mechanism of inhibition is due to a steric blockade prohibitive of substrate binding.
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Structural basis for the activation of flaviviral NS3 proteases from dengue and West Nile virus.
Paul Erbel,Nikolaus Schiering,Allan D'Arcy,Martin Renatus,M. Kroemer,Siew Pheng Lim,Zheng Yin,Thomas H. Keller,Subhash G. Vasudevan,Ulrich Hommel +9 more
TL;DR: In this article, the crystal structures of a dengue NS2B-NS3pro complex and a West Nile virus NS2b-NS 3pro complex with a substrate-based inhibitor were reported.
Journal ArticleDOI
Dimer formation drives the activation of the cell death protease caspase 9.
TL;DR: Observations support a model in which recruitment by Apaf-1 creates high local concentrations of caspase 9 to provide a pathway for dimer-induced activation, with interactions at the dimer interface promoting reorientation of the activation loop.
Journal ArticleDOI
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.