E
Emad S. Alnemri
Researcher at Thomas Jefferson University
Publications - 228
Citations - 75133
Emad S. Alnemri is an academic researcher from Thomas Jefferson University. The author has contributed to research in topics: Apoptosis & Caspase. The author has an hindex of 106, co-authored 223 publications receiving 67441 citations. Previous affiliations of Emad S. Alnemri include QIMR Berghofer Medical Research Institute & Laval University.
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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.
Journal ArticleDOI
The AIM2 inflammasome is critical for innate immunity to Francisella tularensis
Teresa Fernandes-Alnemri,Je-Wook Yu,Je-Wook Yu,Christine Juliana,Leobaldo Solorzano,Seokwon Kang,Jianghong Wu,Pinaki Datta,Margaret E. McCormick,Lan Huang,Erin McDermott,Laurence C. Eisenlohr,Carlisle P. Landel,Emad S. Alnemri +13 more
TL;DR: This study identifies AIM2 as a crucial sensor of F. tularensis infection and provides genetic proof of its critical role in host innate immunity to intracellular pathogens.
Journal ArticleDOI
Identification and Molecular Cloning of Two Novel Receptors for the Cytotoxic Ligand TRAIL
Marion MacFarlane,Manzoor Ahmad,Srinivasa M. Srinivasula,Teresa Fernandes-Alnemri,Gerald M. Cohen,Emad S. Alnemri +5 more
TL;DR: TRAIL receptor-3 may function as an antagonistic decoy receptor to attenuate the cytotoxic effect of TRAIL in most tissues that are TRAIL+, DR4+, and DR5+.
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Structural Basis of Caspase-7 Inhibition by XIAP
Jijie Chai,Eric N. Shiozaki,Srinivasa M. Srinivasula,Qi Wu,Pinaki Dataa,Emad S. Alnemri,Yigong Shi +6 more
TL;DR: The biochemical and structural analyses reveal that the BIR domains are dispensable for the inhibition of caspase-3 and -7, and provides a structural basis for the design of the next-generation caspases.
Journal ArticleDOI
Non-transcriptional Priming and Deubiquitination Regulate NLRP3 Inflammasome Activation
Christine Juliana,Teresa Fernandes-Alnemri,Seokwon Kang,Andrew Farias,Fengsong Qin,Emad S. Alnemri +5 more
TL;DR: In mouse macrophages, signaling by the pattern recognition receptor TLR4 through MyD88 can rapidly and non-transcriptionally prime NLRP3 by stimulating its deubiquitination, which could explain how NL RP3 is activated by diverse danger signals.