S
Stefan J. Riedl
Researcher at Princeton University
Publications - 6
Citations - 3164
Stefan J. Riedl is an academic researcher from Princeton University. The author has contributed to research in topics: Apoptosis & Apoptosome. The author has an hindex of 6, co-authored 6 publications receiving 3002 citations.
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Journal ArticleDOI
Molecular mechanisms of caspase regulation during apoptosis
Stefan J. Riedl,Yigong Shi +1 more
TL;DR: The present understanding of caspase regulation during apoptosis is described and biochemical and structural studies have led to important advances in understanding the underlying molecular mechanisms of cispase regulation.
Journal ArticleDOI
Mechanism of XIAP-Mediated Inhibition of Caspase-9
Eric N. Shiozaki,Jijie Chai,Daniel J. Rigotti,Stefan J. Riedl,Pingwei Li,Srinivasa M. Srinivasula,Emad S. Alnemri,Robert Fairman,Yigong Shi +8 more
TL;DR: It is demonstrated that monomeric caspase-9 is catalytically inactive due to the absence of a supporting sequence element that could be provided by homodimerization, which defines a unified mechanism for the activation of all caspases.
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Structure of the apoptotic protease-activating factor 1 bound to ADP
TL;DR: The 2.2-Å crystal structure of an ADP-bound, WD40-deleted Apaf-1 is reported, which reveals the molecular mechanism by which Apf-1 exists in an inactive state before ATP binding, and drives conformational changes that are essential for the formation of the apoptosome and the activation of caspase-9.
Journal ArticleDOI
A structure of the human apoptosome at 12.8 A resolution provides insights into this cell death platform.
Xinchao Yu,Devrim Acehan,Jean-François Ménétret,Christopher R. Booth,Steven J. Ludtke,Stefan J. Riedl,Yigong Shi,Xiaodong Wang,Christopher W. Akey +8 more
TL;DR: It is found that seven caspase recruitment domains (CARDs) form a central ring within the apoptosome and how a CARD ring and the central hub combine to create a platform for procaspase-9 activation is revealed.
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Structure-activity based study of the Smac-binding pocket within the BIR3 domain of XIAP
TL;DR: A small series of peptide mimics was designed and synthesized to contain a heterocyclic ring in place of the potentially labile N-terminal peptide bond of the tetrapeptide containing the Smac-XIAP-binding motif.