| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.86478342 |
| Here , we show that TRADD interacts strongly with RIP , another death domain protein that was shown previously to associate with Fas antigen . 0.86478342^^^ |
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| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| Fas binds FADD directly , whereas TNFR 1 binds FADD indirectly , through TRADD . ^^^ |
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| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| The expression patterns of pro apoptotic genes ( Fas , FasL , TRADD , FADD ) and caspases 2 , 3 , 8 , 9 were studied using PCR . ^^^ |
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| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| Multiplex RT PCR was used to analyze FLICE , FAS , FADD and TRADD mRNAs before and after CD 40 triggering . ^^^ |
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| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| Using the ribonuclease ( RNase ) protection assay and the reverse transcriptase polymerase chain reaction ( RT PCR ) method , we confirmed that TNF receptor 1 ( TNFR 1 ) , TNFR 1 associated death domain protein ( TRADD ) , Fas receptor associated intracellular protein with death domain ( FADD ) , and FADD like interleukin 1beta converting enzyme ( FLICE ) were expressed in the pancreatic beta cell line , MIN 6 cells . ^^^ |
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| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| Isolation and characterization of death domain ( TNF RI , Fas , TRADD , FADD / MORT 1 , RIP ) and TRAF domain containing proteins ( TRAF 1 , TRAF 2 , TRAF 3 ) have partially bridged a large molecular gap within one of several signaling pathways which originate at the plasma membrane and terminate in the nucleus . ^^^ |
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| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| Expression in cells of kinase deficient NIK mutants fails to stimulate NF kappaB and blocks its induction by TNF , by either of the two TNF receptors or by the receptor CD 95 ( Fas / Apo 1 ) , and by TRADD , RIP and MORT1 / FADD , which are adaptor proteins that bind to these receptors . ^^^ |
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| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| The flow of death signals from TNFR 1 occurs through the adaptor molecule tumor necrosis factor receptor associated death domain protein ( TRADD ) to FADD to FLICE , whereas for CD 95 the receptor directly communicates with FADD and then FLICE . ^^^ MC 159 and E 8 inhibited both TNFR 1 and CD 95 induced apoptosis as well as killing mediated by overexpression of the downstream adaptors TRADD and FADD . ^^^ |
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| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| The tumor necrosis factor receptor 1 ( TNFR 1 ) and the Fas receptor recruit complexes formed by the interactions between RIP kinase , TRADD , FADD and RAIDD adaptor proteins that contain death domains which in turn recruit other proteins to initiate signaling [ 1 ] [ 2 ] [ 3 ] [ 4 ] [ 5 ] . ^^^ |
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| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| Transcriptional expression of TNFR 1 ( p 55 ) , as well as that of FLICE , Fas , FADD , DR 3 , FAF , TRADD , and RIP was similar in these cell lines , indicating that the susceptibility to TNFalpha induced apoptosis may not be determined by the constitutive expression level of these factors . ^^^ |
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| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| FADD DD provides the site of FADD recruitment to death receptor complexes at the plasma membrane by , for example , interaction with the Fas receptor cytoplasmic death domain ( Fas DD ) , or binding of the TNF R 1 adapter molecule TRADD . ^^^ |
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| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| The C terminal fragment of RIP also enhanced the association between TNFR 1 and death domain proteins including TNFR 1 associated death domain ( TRADD ) and Fas associated death domain ( FADD ) , resulting in the activation of caspase 8 and stimulation of apoptosis . ^^^ |
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| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| These families may include receptor / ligand molecules such as Fas , Fas ligand , tumor necrosis factor receptor 1 ( TNFR 1 ) , and TNF related apoptosis inducing ligand ( TRAIL ) ; signal transduction adapter molecules such as Fas associated death domain ( FADD ) , TNFR 1 associated death domain ( TRADD ) , receptor interacting protein ( RIP ) , Fas associated factor ( FAF ) , and Fas associated phosphatase ( FAP ) ; or effector molecules such as caspases . ^^^ To detect the expression of apoptosis related molecules , ribonuclease protection assay was used with specific antisense RNA probes for Fas , Fas ligand , TNFR 1 , TRAIL , FADD , TRADD , RIP , FAF , FAP , and caspase 8 . ^^^ Immunostaining for Fas , Fas ligand , TRAIL , TRADD , RIP , and caspase 8 was also performed . ^^^ Compared with control and contralateral kidneys , the ligated kidneys displayed a dynamic expression of mRNAs for many apoptosis related molecules , which included an up to threefold increase for Fas , Fas ligand , TNF R 1 , TRAIL , TRADD , RIP , and caspase 8 , and an up to twofold increase for FADD and FAP , but there was little change for FAF . ^^^ |
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| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| The serine / threonine kinase HIPK 2 interacts with TRADD , but not with CD 95 or TNF R 1 in 293T cells . ^^^ Under the conditions where HIPK2 / TRADD association was found , no direct interaction of HIPK 2 with CD 95 , TNF R 1 , FADD or caspase 8 could be detected . ^^^ |
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| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| Our aim was to expand these searches by looking for mutations in the death domains of FAS , FADD , TNFR , TRADD , and RIP , in the promoter region of FAS , and in the protease domain of caspase 10 , in a larger variety of hematological malignancies , some of which express an apoptosis resistant phenotype . ^^^ RESULTS : Five polymorphic patterns were found : three in the death domain of the FAS gene in CML patients , one in the promoter of this gene in a CLL patient , and the fifth in the death domain of the TRADD gene in a CML patient . ^^^ CONCLUSIONS : These observations imply that mutations in the death domains of FAS , FADD , TNFR , TRADD , and RIP and in the protease domain of caspase 10 are not a major cause for failure of apoptosis in hematological malignancies , mainly CML and CLL . ^^^ |
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| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| This activity is independent of FADD DN ' s ability to bind to three known interacting proteins , Fas , TRADD or RIP suggesting that it is distinct from FADD ' s functions at activated death receptors . ^^^ |
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| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| Expression of TNF receptor 55 and TNF receptor associated death domain ( TRADD ) was increased , with no changes in Fas signaling molecules , Fas , Fas ligand ( FasL ) , Fas associated death domain ( FADD ) and Fas associated protein factor ( FAF ) . ^^^ |
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| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| Blood and liver were analyzed for plasma aminotransferase activity , liver histology , liver apoptotic nuclei , mRNA of several cytokines ( tumor necrosis factor [ TNF ] alpha , interleukin [ IL ] 1beta , IL 6 , and IL 10 ) , apoptotic ligands ( TRAIL ) , cytokine receptors ( TNFRp 55 ) , pro and antiapoptotic regulators / adaptors ( Fas receptor , FasL , FADD , TRADD , RIP , Bak , Bax , Bcl 10 , Bcl 2 and Bcl w ) , and caspase 8 . ^^^ |
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| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| The FADD death domain binds to activated receptors such as Fas or other adapters such as TRADD , whereas the FADD death effector domain binds to procaspase 8 . ^^^ FADD death domain interactions with Fas and TRADD are thought to occur on the same surface ; however , the regulation of these interactions is poorly understood . ^^^ Using this method , we identified mutations in FADD that prevent binding to Fas but do not affect binding to TRADD . ^^^ |
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| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| Furthermore , IL 12 induced apoptosis was associated with caspase 3 , caspase 2 , caspase 7 , DNA fragmentation factor 45 ( DFF 45 ) and Fas associated death domain ( FADD ) whereas TNF receptor associated death domain ( TRADD ) and receptor interacting protein ( RIP ) were not . ^^^ |
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| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| CD 95 , TNF related apoptosis inducing ligand ( TRAIL R 1 ) , and TRAIL R 2 bind FADD directly , whereas recruitment to TNF R 1 is indirect through another adaptor TNF receptor associated death domain protein ( TRADD ) . ^^^ |
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| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| RESULTS : ACEI resulted in a significant induction of Fas , FADD , and TRADD mRNAs in renal transplant patients with or without PTE . ^^^ ACEI also resulted in a significant upregulation of Fas , FADD and TRADD protein expression , and their localization predominantly at the plasma membrane . ^^^ |
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| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| While recruitment of death domain ( DD ) containing adaptors such as Fas associated death domain ( FADD ) and TNFR associated DD ( TRADD ) can lead to the activation of a signal transduction pathway that induces apoptosis , recruitment of TRAF family proteins can lead to the activation of transcription factors such as , NF kappaB and JNK thereby promoting cell survival and differentiation as well as immune and inflammatory responses . ^^^ |
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| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| FB 1 did not alter CD 95 expression in either strain ; however , expressions of TRAIL , and downstream signaling factors FADD , TRADD , and caspase 8 were higher in FB 1 treated TKO mice than in the corresponding WT animals . ^^^ |
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| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| Interestingly , Par 4 is predicted to contain a death domain homologous to that of Fas or TRADD , and may therefore trigger a death cascade analogous to that of the death domain proteins . ^^^ |
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| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| These cytokines induce cell death through sequential recruitment by the death receptors TNFR 1 associated death domain protein ( TRADD ) , Fas associated death domain protein ( FADD ) , FADD like interleukin 1beta converting enzyme ( FLICE ) , and downstream caspases . ^^^ |
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| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| Members of the TNFR family lack intrinsic kinase activity and thus they initiate signaling by interacting intracellular signaling molecules such as TNFR associated factor ( TRAF ) , TNFR associated death domain ( TRADD ) and Fas associated death domain ( FADD ) . ^^^ |
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| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| AIM : To evaluate the expressions of apoptotic signal proteins FADD , TRADD , FasL , Fas , and NFkappaB in gastric carcinoma tissues and their clinical significance . ^^^ METHODS : Western blot immune trace method was adopted to detect the expressions of apoptotic signal proteins FADD , TRADD , FasL , Fas , and NFkappaB in 55 tissue specimens of gastric carcinoma . ^^^ Expressions of the FADD , FasL , Fas , and NFkappaB proteins reduced with increase of the volume of tumor with the exception of increased expression the TRADD protein ( 64 . 7 71 . 1 % , P = 0 . 031 ) . ^^^ With gradual increase of the malignancy of gastric carcinoma tissues , expressions of the FADD , FasL , and Fas proteins decreased ( 78 . 6 28 . 0 % , P = 0 . 008 ; 78 . 6 65 . 9 % , P = 0 . 071 ; 100 . 0 46 . 3 % , P = 0 . 014 ) , while expressions of the TRADD and NFkappaB proteins increased ( 42 . 9 78 . 1 % , P = 0 . 063 ; 78 . 6 79 . 1 % , P = 0 . 134 ) . ^^^ With gradual increase of serum CEA , expression of the FADD protein decreased ( 62 . 5 34 . 0 % , P = 0 . 073 ) , but expressions of the TRADD , FasL , Fas , and NFkappaB proteins increased ( 0 . 0 80 . 8 % , P = 0 . 005 ; 62 . 5 70 . 2 % , P = 0 . 093 ; 0 . 0 70 . 2 % , P = 0 . 003 ; 62 . 5 80 . 9 % , P = 0 . 075 ) . ^^^ |
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| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| Comparing the topology of protein protein interactions for FADD complexes to TRADD complexes reveals that FADD uses a Tube like surface in each of its death motifs to engage either CD 95 or TRADD . ^^^ |
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| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| Some members of the DR family , CD 95 and the TRAIL receptors DR 4 and DR 5 , directly bind FADD , whereas others , such as TNF receptor 1 and DR 3 , initially bind another adaptor protein , TRADD , which then recruits FADD . ^^^ |
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| Interacting proteins: Q15628 and P25445 |
Pubmed |
SVM Score :0.0 |
| Hepatic mRNA levels were measured for several pro apoptotic adaptors / regulators , including FasL , Fas receptor , FADD , TRADD , Bad , Bak , Bax , and Bcl 10 ( S ) , and anti apoptotic regulators , including Bcl w , Bcl 10 ( L ) , Bcl 2 , and Bfl 1 . ^^^ |
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