TNF-R1 Signaling: A Beautiful Pathway

By Guoqing Chen, D. Goeddel. Science, 2002

2,003 citations recorded by the source corpus.

Subfields: Cancer Research, Immunology, Oncology

View Paper: https://www.semanticscholar.org/paper/76e6098abe5717f2a1af33413f6472fae880795a

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Citations in the corpus

Tumor Necrosis Factor Alpha: A Link between Neuroinflammation and Excitotoxicity (2014, positive): “This latter protein mediates recruitment and activation of caspases 8 and 10 that initiate a protease cascade that leads to apoptosis [31].”
Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes. (2003, neutral): “It is currently believed that engagement of TNFR1 triggers the recruitment of the DD-containing adapter molecule TRADD followed by the DDcontaining Ser/Thr kinase RIP1 (Ashkenazi and Dixit, 1998; Chen and Goeddel, 2002).”
Autocrine Tumor Necrosis Factor Alpha Links Endoplasmic Reticulum Stress to the Membrane Death Receptor Pathway through IRE1α-Mediated NF-κB Activation and Down-Regulation of TRAF2 Expression (2006, methodology): “IRE1 induces JNK activation through interaction with TRAF2 in ER stress, which is a pathway similar to that used by cells in response to TNF- (38), and it is known that in TNF- signaling, TRAF2 is required for both JNK and NF- B activation (3).”
Chronic Inflammation and Cytokines in the Tumor Microenvironment (2014, background): “Trimerization occurs upon TNF-𝛼 binding to TNF-𝛼-Rs, leading to activation of at least four signaling pathways: a proapoptotic pathway induced by caspase8 interaction with Fas-associated death domain (FADD); an antiapoptotic platform activated by cellular inhibitor of apoptosis protein-1 (cIAP-1) ”
Caspase-8 induces cleavage of gasdermin D to elicit pyroptosis during Yersinia infection (2018, background): “TNF receptor signaling engages the TNF receptor-associated adaptor TRADD to recruit RIP1 via death domain (DD) interactions (4), forming complex I.”
Regulation of reactive oxygen species generation in cell signaling (2011, background): “TRADD recruits TNF receptor-associated factor 2 (TRAF2), receptor-interacting protein 1 (RIP1), and cellular inhibitor of apoptosis proteins to form TNF-αinduced signaling complex I (Chen and Goeddel, 2002; Karin and Lin, 2002).”
3D Complex: A Structural Classification of Protein Complexes (2006, background): “It can also serve as a template for bringing together proteins and triggering a function, as in the case of the tumor necrosis factor [44].”
Mixed lineage kinase domain-like is a key receptor interacting protein 3 downstream component of TNF-induced necrosis (2012, background): “TRADD (TNF-R1–associated death domain protein) is the first protein to interact with the receptor through its death domain and recruits other effector proteins, such as RIP1 (receptor interacting protein) and TRAF2 (TNFR-associated factor 2) to form the TNF-R1 signaling complex leading to the activa”