Apo2L/TRAIL and its death and decoy receptors

By Heidi N. Leblanc, A. Ashkenazi. Cell Death and Differentiation, 2003

888 citations recorded by the source corpus.

Subfields: Cancer Research, Immunology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/e4bac76c5641e0a0728f130be71c51cd9eaab503

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cancer Research

1. K. Debatin
2. A. Ashkenazi
3. Simone Fulda

In Immunology

1. Alexandru Almasan
2. Simone Fulda
3. K. Debatin
4. A. Ashkenazi

In Molecular Biology

1. Simone Fulda
2. K. Debatin
3. Alexandru Almasan
4. A. Ashkenazi

Citations in the corpus

• Apo2L/TRAIL: apoptosis signaling, biology, and potential for cancer therapy. (2003, background): “Importantly, in the Bcl-2/Bcl-XL overexpression studies, Apo2L/TRAIL-dependent killing does not necessarily recapitulate the Type I/II model described for Fas, since in Type II cell lines ectopic Bcl-2 expression does not block activation of caspase-8 and apoptosis following Apo2L/TRAIL addition [45”
• Extrinsic versus intrinsic apoptosis pathways in anticancer chemotherapy (2006, background): “In contrast, TRAIL appears to be a relatively safe and promising candidate for clinical application, particularly in its non-tagged, zinc-bound homotrimeric form (LeBlanc and Ashkenazi, 2003).”
• Apoptosis as anticancer mechanism: function and dysfunction of its modulators and targeted therapeutic strategies (2016, background): “Owing to its different toxicity for transformed as opposed to normal cells, Apo2/TRAIL shows promise as potential cancer therapy agent [80,81].”
• REACTIVE OXYGEN SPECIES, CELLULAR REDOX SYSTEMS AND APOPTOSIS (2010, neutral): “TRAIL-R3, TRAIL-R4 and soluble receptor, osteoprotegerin lack functional cytosolic domains and are decoy receptors where ligand binding does not transmit an apoptotic signal [98].”
• A cytokine-mediated link between innate immunity, inflammation, and cancer. (2007, neutral): “The TNF superfamily member TRAIL can bind five different receptors, two of which, death receptor 4 (DR4) and DR5, have cytoplasmic death domains that deliver caspase-dependent apoptotic signals to the cell on which they are expressed (52).”