Life and death by death receptors

By M. E. Guicciardi, G. Gores. The FASEB Journal, 2009

670 citations recorded by the source corpus.

Subfields: Immunology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/a1888ace0b2792a627d0f106773df08352c51138

How researchers see this paper

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

In Immunology

1. Chao Yang
2. H. Kim
3. Monica S. Thakar
4. Hyun Sook Hwang
5. Alex M. Abel
6. S. Malarkannan

In Molecular Biology

1. H. Kim
2. Hyun Sook Hwang

Citations in the corpus

• Pattern Recognition Receptors and the Host Cell Death Molecular Machinery (2018, background): “The extrinsic pathway, in comparison, is initiated by the interaction of trimeric, extracellular ligands (TNF-α, CD95L, and TRAIL) to their cognate receptors (TNFR1, CD95 and TRAILRI, or TRAILRII, respectively) present on the plasma membrane (10, 22, 23).”
• Chondrocyte Apoptosis in the Pathogenesis of Osteoarthritis (2015, background): “Fas and/or TNF-related apoptosis-inducing ligand (TRAIL) receptors, members of tumor necrosis factor (TNF) receptor superfamily, are highly upregulated in many carcinomas, such as hepatocellular, ovarian, renal, colorectal and pancreatic cancers [11].”
• Natural Killer Cells: Development, Maturation, and Clinical Utilization (2018, background): “The death receptor superfamily is characterized by the utilization of a cytoplasmic death domain which enables these receptors to activate the apoptotic machinery including initiator caspases-8 and 10 (141, 142).”
• Apoptosis and Molecular Targeting Therapy in Cancer (2014, background): “Conflict of Interests The authors declare that there is no conflict of interests regarding the publication of this paper.”
• Apoptosis as anticancer mechanism: function and dysfunction of its modulators and targeted therapeutic strategies (2016, background): “Upon death receptor stimulation by its corresponding ligand, the same receptor undergoes oligomerization and a conformational change to reveal its cytoplasmic DD to support homotypic interactions with other DD-containing proteins [21].”