Phosphorylation-Driven Assembly of the RIP1-RIP3 Complex Regulates Programmed Necrosis and Virus-Induced Inflammation
Top Cited Papers
- 1 June 2009
- Vol. 137 (6) , 1112-1123
- https://doi.org/10.1016/j.cell.2009.05.037
Abstract
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This publication has 41 references indexed in Scilit:
- Identification of a Molecular Signaling Network that Regulates a Cellular Necrotic Cell Death PathwayCell, 2008
- Cytomegalovirus M45 Cell Death Suppression Requires Receptor-interacting Protein (RIP) Homotypic Interaction Motif (RHIM)-dependent Interaction with RIP1Journal of Biological Chemistry, 2008
- How dying cells alert the immune system to dangerNature Reviews Immunology, 2008
- Genetic variation in 1253 immune and inflammation genes and risk of non-Hodgkin lymphomaBlood, 2007
- Necrostatin: A Potentially Novel Cardioprotective Agent?Cardiovascular Drugs and Therapy, 2007
- Innate immunity against vaccinia virus is mediated by TLR2 and requires TLR-independent production of IFN-βBlood, 2006
- Competitive Control of Independent Programs of Tumor Necrosis Factor Receptor-Induced Cell Death by TRADD and RIP1Molecular and Cellular Biology, 2006
- Inflammation and cancerNature, 2002
- The RIP‐like kinase, RIP3, induces apoptosis and NF‐κB nuclear translocation and localizes to mitochondriaFEBS Letters, 2000
- Identification of RIP3, a RIP-like kinase that activates apoptosis and NFκBCurrent Biology, 1999