| URN | urn:agi-Binding:inout-urn:agi-llid:8737:inout-urn:agi-llid:8717::unknown |
|---|---|
| References | 97 |
| Connectivity | 2 |
| Effect | unknown |
| TextRef | info:pmid/8612133#abs:2 |
|---|---|
| MedLine Reference | 8612133:1 |
| Sentence | Here, we show that TRADD interacts strongly with RIP, another death domain protein that was shown previously to associate with Fas antigen. |
| TextRef | info:pmid/10848577#abs:7 |
|---|---|
| MedLine Reference | 10848577:6 |
| Sentence | Examination of Stat1-deficient cells showed an apparent increase in TNF-alpha-induced TRADD-RIP and TRADD-TRAF2 complex formation, while interaction between TRADD and FADD was unaffected. |
| CellLineName | HeLa |
| TextRef | info:pmid/15115707#abs:13 |
|---|---|
| MedLine Reference | 15115707:12 |
| Sentence | These results suggest that delta-PKC and PI 3-kinase regulate TNF antiapoptotic signaling at the level of the TNFR-1 through control of assembly of a TNFR-1-TRADD-RIP-TRAF2 complex. |
| TextRef | info:pmid/12773372#body:136 |
|---|---|
| MedLine Reference | 12773372:1135 |
| Sentence | RIP is recruited into the TNF-R1 complex by the TNF adapter protein, TRADD ( T NF- R 1- a ssociated d eath d omain protein). |
| Organ | Liver |
| Organism | dog |
| CellType | macrophage |
| CellLineName | NIH 3T3 |
| Tissue | epithelia |
| Journal | Mol. Endocrin |
| Journal Reference | v93 i24 p13973 (1996) |
| Journal Link | http://www.pnas.org/cgi/content/full/93/24/13973 |
| Source | Curated |
| TextRef | info:pmid/11861282#body:136 |
|---|---|
| MedLine Reference | 11861282:1135 |
| Sentence | Surface death-receptor expression on CD4 and CD8 T cells from healthy donors and HIV-infected patients Increased TNFR1- and TNFR2-induced apoptosis in HIV infection is not associated with altered expression of the adapter proteins TRADD, TRAF-2, and RIP The binding of TNF to TNFR1 leads to the recruitment of TRADD that serves as a platform to recruit FADD, TRAF-2, and RIP, which interact with TRADD directly. 24 Recent studies showed that, in human T cells, RIP is needed for TNFR1- and TNFR2-mediated cell death, RIP playing an indispensable role in converting cells from life to death in response to TNF treatment. 26 , 32 To further explore the factors responsible for the increased susceptibility of patients' T cells to TNFR-induced apoptosis, messenger RNA (mRNA) and protein expression of TRADD, RIP, and TRAF-2 were analyzed in freshly purified CD2 T cells from control donors and HIV + subjects. |
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| Source | Curated |
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| MedLine Reference | 12882979:2 |
| CellLineName | TF1 |
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| MedLine Reference | 15572679:10159 |
| Journal | Mol. Cell. Biol |
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| Journal Link | http://mcb.asm.org/cgi/content/full/24/24/10757 |
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| MedLine Reference | 16219681:10060 |
| Journal | Cell Sci |
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| Journal | Genes & Dev |
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| Organism | Mus musculus |
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| Organism | Mus musculus |
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| Organism | Mus musculus |
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| MedLine Reference | 15590916:10031 |
| Organism | Rattus norvegicus |
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| Journal | Genes & Dev |
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| MedLine Reference | 9712898:10301 |
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| MedLine Reference | 11479302:10024 |
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| Journal | Carcinogenesis |
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| Organism | mouse |
| CellLineName | NIH 3T3 |
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| Journal | Mol. Endocrin |
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| MedLine Reference | 15075251:10213 |
| Organism | Mus musculus |
| Journal | Gastr. Liver Phys |
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| Organism | Mus musculus |
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| Organism | Mus musculus |
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| Journal | Blood |
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| Journal | Cell |
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| Organ | Lung |
| Organism | mouse |
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| Sentence | In another pathway, RIP binds to TRADD and transduces an apoptotic signal through the death domain. |
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