Human inhibitor of apoptosis proteins: why XIAP is the black sheep of the family
By Brendan P. Eckelman, G. Salvesen, F. Scott. EMBO Reports, 2006
845 citations recorded by the source corpus.
Subfields: Epidemiology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/07894e8a1cc11af86eb880e6586292222ae39983
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In Epidemiology
In Molecular Biology
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- D. Klionsky
Citations in the corpus
- Tumor resistance to apoptosis (2009, background): “signaling by binding to active caspase-3 and -7 and by preventing caspase-9 activation.(71) XIAP also regulates other signaling cascades, for example the NF-jB pathway.”
- Cell Death Signaling. (2015, background): “XIAP further dampens intrinsic apoptosis induction through direct ubiquitylation and proteasomal degradation of active caspases (Eckelman et al. 2006).”
- IAPs: from caspase inhibitors to modulators of NF-κB, inflammation and cancer (2010, background): “Of all IAPs, mammalian XIAP is the only IAP that functions as a direct caspase inhibitor in a strict biochemical sens”
- The Ripoptosome, a signaling platform that assembles in response to genotoxic stress and loss of IAPs. (2011, background): “Although genotoxic stress triggers depletion of cIAPs and XIAP, it remains unclear whether etoposide-mediated depletion of cIAPs and XIAP contributes to cell death, particularly because cIAPs reportedly are unable to regulate caspases (Eckelman et al., 2006).”
- Molecular mechanisms of cell death: recommendations of the Nomenclature Committee on Cell Death 2018 (2018, background): “XIAP is the only IAP protein family member that counteracts the apoptotic cascade by stably binding to and hence physically blocking caspases [184, 185].”
- HECT and RING finger families of E3 ubiquitin ligases at a glance (2012, background): “Inhibitor of apoptosis proteins (IAPs) are RING E3s that prevent apoptosis at the level of caspase activation (Eckelman et al., 2006).”