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Henning R. Stennicke
Researcher at Novo Nordisk
Publications - 100
Citations - 13937
Henning R. Stennicke is an academic researcher from Novo Nordisk. The author has contributed to research in topics: Caspase & Apoptosis. The author has an hindex of 37, co-authored 100 publications receiving 13633 citations. Previous affiliations of Henning R. Stennicke include Discovery Institute & Massachusetts Institute of Technology.
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Journal ArticleDOI
Regulation of Cell Death Protease Caspase-9 by Phosphorylation
Michael H. Cardone,Natalie Roy,Henning R. Stennicke,Guy S. Salvesen,Thomas F. Franke,Eric J. Stanbridge,Steven M. Frisch,John C. Reed +7 more
TL;DR: In this paper, the kinase Akt and p21-Ras, an Akt activator, induced phosphorylation of pro-caspase-9 (pro-Casp9) in cells.
Journal ArticleDOI
IAPs block apoptotic events induced by caspase‐8 and cytochrome c by direct inhibition of distinct caspases
Quinn Deveraux,Natalie Roy,Henning R. Stennicke,Todd Van Arsdale,Qiao Zhou,Srinivasa M. Srinivasula,Emad S. Alnemri,Guy S. Salvesen,John C. Reed +8 more
TL;DR: It is demonstrated that IAPs can suppress different apoptotic pathways by inhibiting distinct caspases and identify pro‐caspase‐9 as a new target for IAP‐mediated inhibition of apoptosis.
Journal ArticleDOI
An Induced Proximity Model for Caspase-8 Activation
TL;DR: It is hypothesized that the FLICE zymogen possesses intrinsic enzymatic activity such that when approximated, it autoprocesses to the active protease.
Journal ArticleDOI
Pro-caspase-3 Is a Major Physiologic Target of Caspase-8
Henning R. Stennicke,Juliane M. Jürgensmeier,Hwain Shin,Quinn Deveraux,Beni B. Wolf,Xiaohe Yang,Qiao Zhou,H. Michael Ellerby,Lisa M. Ellerby,Dale E. Bredesen,Douglas R. Green,John C. Reed,Christopher J. Froelich,Guy S. Salvesen +13 more
TL;DR: In a purified system, the initiator caspases-8 and -10 directly process the executioner pro-caspase-3 with activation rates of 8.7 × 105 and 2.8 × 105 m −1 s−1, respectively, which are of sufficient magnitude to indicate direct processing in vivo.
Journal ArticleDOI
Cleavage of human inhibitor of apoptosis protein XIAP results in fragments with distinct specificities for caspases
TL;DR: It is demonstrated that endogenous XIAP is cleaved into two fragments during apoptosis induced by the tumor necrosis factor family member Fas (CD95), and cleavage of XIAP may be one mechanism by which cell death programs circumvent the anti‐apoptotic barrier posed by XIAP.