S
Stefan J. Riedl
Researcher at Sanford-Burnham Institute for Medical Research
Publications - 45
Citations - 5143
Stefan J. Riedl is an academic researcher from Sanford-Burnham Institute for Medical Research. The author has contributed to research in topics: Caspase & Apoptosis. The author has an hindex of 27, co-authored 45 publications receiving 4722 citations. Previous affiliations of Stefan J. Riedl include Discovery Institute & Max Planck Society.
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Journal ArticleDOI
The apoptosome: signalling platform of cell death
Stefan J. Riedl,Guy S. Salvesen +1 more
TL;DR: The formation of the apoptosome and the activation of its effector, caspase-9, reveals a sophisticated mechanism that might be more common than was initially thought.
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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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XIAP inhibits caspase‐3 and ‐7 using two binding sites: evolutionarily conserved mechanism of IAPs
Fiona L. Scott,Jean-Bernard Denault,Stefan J. Riedl,Hwain Shin,Martin Renatus,Guy S. Salvesen +5 more
TL;DR: It is shown that the BIR2 domain contributes substantially to inhibition of executioner caspases, and it is predicted that the origin of the death stimulus should dictate the efficiency of inhibition by XIAP.
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The Fas–FADD death domain complex structure unravels signalling by receptor clustering
Fiona L. Scott,Boguslaw Stec,Cristina Pop,Małgorzata K. Dobaczewska,JeongEun J. Lee,Edward Monosov,Howard Robinson,Guy S. Salvesen,Robert Schwarzenbacher,Stefan J. Riedl +9 more
TL;DR: The result is a regulatory Fas–FADD complex bridge governed by weak protein–protein interactions revealing a model where the complex itself functions as a mechanistic switch that prevents accidental DISC assembly, yet allows for highly processive DISC formation and clustering upon a sufficient stimulus.
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The Nod-like receptor (NLR) family: a tale of similarities and differences.
TL;DR: It is revealed that NLRs posses a domain architecture similar to the apoptotic initiator protein Apaf-1, suggesting a similar biochemical behaviour in catalytic activity and oligomerization for individual NLRs.