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 Article
Cell Permeable Bcl-2 Binding Peptides: A Chemical Approach to Apoptosis Induction in Tumor Cells
Jia-Lun Wang,ZhiJia Zhang,Swati Choksi,Simei Shan,Zhixian Lu,Carlo M. Croce,Emad S. Alnemri,Robert Korngold,Ziwei Huang +8 more
TL;DR: A cell permeable Bcl-2 binding peptide, cpm-1285, was designed by chemically attaching a fatty acid to a peptide derived from the proapoptotic protein Bad and had in vivo activity in slowing human myeloid leukemia growth in severe combined immunodeficient mice.
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Regulation of IL-1β generation by Pseudo-ICE and ICEBERG, two dominant negative caspase recruitment domain proteins
TL;DR: The data suggest that Pseudo-ICE and ICEBERG are intracellular regulators of caspase-1 activation and could play a role in the regulation of IL-1β secretion and NF-κB activation during the pro-inflammatory cytokine response.
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Calpain activation is upstream of caspases in radiation- induced apoptosis
Nigel J. Waterhouse,Debra M Finucane,Douglas R. Green,John S. Elce,Sharad Kumar,Emad S. Alnemri,Gerald Litwack,Kum Kum Khanna,Martin F. Lavin,Martin F. Lavin,Dianne Watters +10 more
TL;DR: A role for calpain in the early phases of the radiation-induced apoptosis pathway, upstream of the caspases is supported, as was the calpain-mediated hydrolysis of casein in the Burkitts' Lymphoma cell line BL30A.
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Inflammasome Priming by Lipopolysaccharide Is Dependent upon ERK Signaling and Proteasome Function
Mohammed G. Ghonime,Mohammed G. Ghonime,Obada R. Shamaa,S. Das,Ramadan A. El-Domany,Teresa Fernandes-Alnemri,Emad S. Alnemri,Mikhail A. Gavrilin,Mark D. Wewers +8 more
TL;DR: Findings suggest that ERK1-mediated posttranslational modifications license the NLRP3 inflammasome to respond to the second signal ATP by inducing post translational events that are independent of new production of pro–IL-1β and NOD-like receptor components.
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Activation of the IκB Kinases by RIP via IKKγ/NEMO-mediated Oligomerization
Jean-Luc Poyet,Srinivasa M. Srinivasula,Jun-Hsiang Lin,Teresa Fernandes-Alnemri,Shoji Yamaoka,Philip N. Tsichlis,Emad S. Alnemri +6 more
TL;DR: Gel filtration analysis of the IKK complex revealed that TNFα stimulation induces a large increase in the size of this complex, suggesting oligomerization, and data suggest that IKKγ functions as a signaling adaptor between the upstream regulators such as RIP and the Ikks and that oligomersization of theIKK complex by upstream regulators is a critical step in activation of thiscomplex.