Mechanisms of caspase activation.
By K. Boatright, G. Salvesen. Current Opinion in Cell Biology, 2003
1,448 citations recorded by the source corpus.
Subfields: Cancer Research, Epidemiology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/235c4932cdb7720bbfe23f13687e6163c9ac4af4
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Citations in the corpus
- Structural Mechanism for GSDMD Targeting by Autoprocessed Caspases in Pyroptosis. (2020, background): “The downstream caspase-3/6/7 are intrinsic dimers but their activation also requires cleavage between the p20 and the p10 to adopt an active conformation (Boatright and Salvesen, 2003; Riedl andShi, 2004).”
- Apoptosis as anticancer mechanism: function and dysfunction of its modulators and targeted therapeutic strategies (2016, background): “The role of adapter proteins (FADD/TRADD) is to sequester, at level of this protein complex, the initiator pro-caspase-8 and/or -10 resulting in the formation of the so-called death-inducing signaling complex (DISC), increasing the local concentration of pro-caspase and promoting the mutual auto-act”
- Transcriptomic responses to heat stress and bleaching in the elkhorn coral Acropora palmata (2010, background): “This likely reflects previous findings that caspase-3, which is an executioner caspase, requires activation via post-translational modification (Boatright & Salvesen 2003).”
- The apoptosome: signalling platform of cell death (2007, background): “The contrasting hypotheses, including recent revisions of the models, have been reviewed extensivel”
- The inflammasomes: guardians of the body. (2009, background): “These platforms integrate cellular signals, recruit initiator caspases via their death-fold domain, and promote dimerization of the caspases, which all lead to the formation of an active enzyme proficient enough to initiate specific signaling cascades (74).”
- Apoptosis, Pyroptosis, and Necrosis: Mechanistic Description of Dead and Dying Eukaryotic Cells (2005, background): “composed of two large subunits and two small subunits (6).”
- Mixed lineage kinase domain-like is a key receptor interacting protein 3 downstream component of TNF-induced necrosis (2012, background): “FADD recruits and induces dimerization and activation of the autocatalytic activation of the initiator cysteine proteases caspases 8 and 10, which drive apoptosis (11, 12).”