| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.79303359 |
| The death domain of tumor necrosis factor ( TNF ) receptor 1 ( TNFR 1 ) triggers distinct signaling pathways leading to apoptosis and NF kappa B activation through its interaction with the death domain protein TRADD . 0.79303359^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.76570256 |
| These results indicate that K 18 may sequester TRADD to attenuate interactions between TRADD and activated TNFR 1 and moderate TNF induced apoptosis in simple epithelial cells . . 0.76570256^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| TIAF 1 inhibits the cytotoxic effects of TNF alpha and overexpressed TNF receptor adaptors TRADD , FADD , and RIP . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| Systematic mutational analysis of the death domain of the tumor necrosis factor receptor 1 associated protein TRADD . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| Competitive control of independent programs of tumor necrosis factor receptor induced cell death by TRADD and RIP 1 . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| TRADD TRAF 2 and TRADD FADD interactions define two distinct TNF receptor 1 signal transduction pathways . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| TNF alpha signaling involves the recruitment of at least three proteins ( TRADD , RIP , and TRAF 2 ) to the type 1 TNF alpha receptor tail , leading to the sequential activation of the downstream NF kappaB inducing kinase ( NIK ) and IkappaB specific kinases ( IKKalpha and IKKbeta ) . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| These results suggest that TNF alpha can cause apoptosis in pancreatic beta cells through TNFR 1 linked apoptotic factors , TRADD , FADD , and FLICE , and TNF induced ceramide production may be involved in the pathways . . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| In combination with TNF alpha , however , ceramide potentiated , whereas NO inhibited , TNF alpha induced TRADD recruitment and caspase 8 activity . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| Activated tumor necrosis factor alpha ( TNF alpha ) receptor 1 ( TNFR 1 ) recruits TNFR 1 associated death domain protein ( TRADD ) , which in turn triggers two opposite signaling pathways leading to caspase activation for apoptosis induction and NF kappaB activation for antiapoptosis gene upregulation . ^^^ TNFR 1 signaling factors TRADD and Fas associated death domain protein ( FADD ) were also found to interact with Stat 1 in a TNF alpha dependent process . ^^^ Examination of Stat 1 deficient cells showed an apparent increase in TNF alpha induced TRADD RIP and TRADD TRAF 2 complex formation , while interaction between TRADD and FADD was unaffected . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| Tumor necrosis factor alpha ( TNF alpha ) induced activation of MAPKs has been shown to involve the death domain proteins ( TRADD , FADD , MADD ) and TRAFs . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| The TRAF C region interacts with TNF alpha receptors and TNF receptor associated death domain ( TRADD ) proteins ; however , our findings indicate that these interactions are unlikely to be mimicked by Siah . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| However , TRADD and RIP , which are essential for the TNF alpha induced NF kappaB activation , were not involved in the FasL induced NF kappaB activation . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| In these cells , MEKK 3 DD substitutes for RIP and directly associates with TRADD in TNF receptor complexes following TNF alpha stimulation . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| Moreover , we found that with progression of the disease process leading to neuronal cell death , an up regulation of genes involved in the TNF alpha death pathway caspase 8 , FADD , TNFRp 55 , TRADD , and RIP by an RNA protection assay . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| The analysed factors included TNF alpha , TNFR 1 , TNF receptor associated death domain ( TRADD ) , caspase 3 , caspase 8 , TNF receptor associated factor 2 ( TRAF 2 ) and receptor interactive protein ( RIP ) , all of which are involved in the TNF alpha / TNFR 1 signalling pathway mediated apoptosis . ^^^ The quantitative RT PCR indicated that the infected muscle tissues up regulate the expression of pro apoptosis genes ( TNF alpha , TNFR 1 and TRADD , caspase 3 and caspase 8 ) , and anti apoptosis genes ( TRAF 2 and RIP ) at the beginning of cyst formation . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| The constitutive expression of mRNA for TNF alpha receptors ( TNFR 1 and TNFR 2 ) and the adapter molecules , such as the TNF receptor associated death domain protein ( TRADD ) , Fas associated death domain protein ( FADD ) , receptor interacting protein ( RIP ) , and TNF receptor associated factor 2 ( TRAF 2 ) were analyzed by reverse transcriptase PCR ( RT PCR ) in PBMCs from control and RA cases . ^^^ PBMCs of RA patients showed a significant increase in TNF alpha and TNFR 1 expression as compared with that from control subjects along with significantly increased constitutive expression of TRADD , RIP , and TRAF 2 mRNA . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| Interaction of the p 55 tumor necrosis factor receptor 1 ( TNF R 1 ) associated signal transducer TRADD with FADD signals apoptosis , whereas the TNF receptor associated factor 2 protein ( TRAF 2 ) is required for activation of the nuclear transcription factor nuclear factor kappa B . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
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 . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| A yeast two hybrid screen identified TES 2 interacting proteins , including the tumor necrosis factor receptor associated death domain protein ( TRADD ) . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| Fas / Apo1 and other cytotoxic receptors of the tumor necrosis factor receptor ( TNFR ) family contain a cytoplasmic death domain ( DD ) [ 1 ] [ 2 ] [ 3 ] [ 4 ] [ 5 ] [ 6 ] [ 7 ] [ 8 ] [ 9 ] [ 10 ] [ 11 ] that activates the apoptotic process by interacting with the DD containing adaptor proteins TNFR associated DD protein ( TRADD ) [ 12 ] [ 13 ] and Fas associated DD protein ( FADD / MORT1 ) [ 14 ] [ 15 ] , leading to the activation of cysteine proteases of the caspase family [ 16 ] . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| The ability of CTAR 1 to activate NF kappaB appears to be attributable to the direct interaction of tumor necrosis factor ( TNF ) receptor associated factor 2 ( TRAF 2 ) , while recent work indicates that CTAR 2 induced NF kappaB is mediated through its association with TNF receptor associated death domain ( TRADD ) . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| The 55 kDa receptor for tumor necrosis factor ( TR 55 ) triggers multiple signaling cascades initiated by adapter proteins like TRADD and FAN . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| The Epstein Barr virus latent membrane protein 1 ( LMP 1 ) binds tumor necrosis factor receptor ( TNFR ) associated factors ( TRAFs ) and the TNFR associated death domain protein ( TRADD ) . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
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 ] . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| Mutational analysis of the LMP 1 cytoplasmic COOH terminus revealed that p 38 activation occurs from both the tumor necrosis factor receptor associated factor ( TRAF ) interacting , membrane proximal COOH terminal activating region ( CTAR ) 1 domain ( amino acids 186 231 ) and the extreme tumor necrosis factor receptor associated death domain ( TRADD ) binding CTAR 2 region ( amino acids 351 386 ) . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| Members of the tumor necrosis factor receptor superfamily induce apoptosis via interaction with FADD and regulate cell growth and differentiation through TRADD and TRAFs molecules . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| The Epstein Barr virus oncoprotein latent membrane protein 1 engages the tumor necrosis factor receptor associated proteins TRADD and receptor interacting protein ( RIP ) but does not induce apoptosis or require RIP for NF kappaB activation . ^^^ A site in the Epstein Barr virus ( EBV ) transforming protein LMP 1 that constitutively associates with the tumor necrosis factor receptor 1 ( TNFR 1 ) associated death domain protein TRADD to mediate NF kappaB and c Jun N terminal kinase activation is critical for long term lymphoblastoid cell proliferation . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| LMP 1 spontaneously aggregates in the plasma membrane and enables two transformation effector sites ( TES 1 and TES 2 ) within the 200 amino acid cytoplasmic carboxyl terminus to constitutively engage the tumor necrosis factor receptor ( TNFR ) associated factors TRAF 1 , TRAF 2 , TRAF 3 , and TRAF 5 and the TNFR associated death domain proteins TRADD and RIP , thereby activating NF kappaB and c Jun N terminal kinase ( JNK ) . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| The underexpressed genes and their relative expression compared with normal scar were defender against cell death 1 ( DAD 1 ) ( 34 . 1 % of normal scar ) ; nucleoside diphosphate kinase B ( c myc transcription factor ) ( 24 . 7 % ) ; glutathione S transferase ( 17 . 9 % ) ; glutathione S transferase microsomal ( 28 . 1 % ) ; glutathione peroxidase ( 47 . 2 % ) ; tumor necrosis factor receptor 1 associated protein ( TRADD ) ( 51 . 0 % ) ; 19 kDa interacting protein 3 ( NIP 3 ) ( 36 . 0 % ) ; and cytoplasmic dynein light chain 1 ( HDLC 1 ) ( 47 . 7 % ) . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
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 . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| Here we describe that HIPK 2 can also associate with TRADD , a protein that interacts with tumor necrosis factor receptor type 1 ( TNF R 1 ) . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| Tumor necrosis factor ( TNF ) receptor associated factor ( TRAF ) 2 is an intracellular adapter protein , which , upon TNF stimulation , is directly recruited to the intracellular region of TNF receptor 2 ( TNFR 2 ) or indirectly , via TRADD , to the intracellular region of TNF receptor 1 ( TNFR 1 ) . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| TES 2 mediates the interaction with tumor necrosis factor receptor associated death domain protein ( TRADD ) and plays a key role in transactivating NF kappa B and AP 1 . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| Expression of receptor interacting protein ( RIP ) associated Ich 1 homologous protein with death domain ( RAIDD ) was increased following seizures , whereas expression of RIP and tumor necrosis factor receptor associated protein with death domain ( TRADD ) , other components thought to be linked to the caspase 2 activation and signaling mechanism , were unchanged . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| Hepatitis C virus core protein enhances FADD mediated apoptosis and suppresses TRADD signaling of tumor necrosis factor receptor . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| The adaptor protein FADD directly , or indirectly via another adaptor called TRADD , recruits caspase 8 to death receptors of the tumor necrosis factor receptor family . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| Rather , CARDINAL potently suppressed NF kappaB activation associated with overexpression of TRAIL R 1 , TRAIL R 2 , RIP , RICK , Bcl 10 , and TRADD , or through ligand induced stimulation of the interleukin 1 or tumor necrosis factor receptors . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| The adapter protein tumor necrosis factor receptor ( TNFR ) 1 associated death domain ( TRADD ) plays an essential role in recruiting signaling molecules to the TNFRI receptor complex at the cell membrane . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
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 . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| A 20 inhibits tumor necrosis factor ( TNF ) alpha induced apoptosis by disrupting recruitment of TRADD and RIP to the TNF receptor 1 complex in Jurkat T cells . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| With a cDNA microarray , we revealed that tumor necrosis factor receptor associated death domain ( tradd ) gene expression was elevated in response to Akt inactivation . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| The oncogenic Epstein Barr virus ( EBV ) encoded latent infection membrane protein 1 ( LMP 1 ) mimics a constitutive active tumor necrosis factor ( TNF ) family receptor in its ability to recruit TNF receptor associated factors ( TRAFs ) and TNF receptor associated death domain protein ( TRADD ) in a ligand independent manner . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| We show here that the tumor necrosis factor receptor associated death domain protein ( TRADD ) interacts with p 75 ( NTR ) upon nerve growth factor ( NGF ) stimulation . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| Overexpression of TRAF 1 , however , had no effect on the interaction of TRADD and TRAF 2 , known to be important for tumor necrosis factor receptor 1 ( TNF R 1 ) mediated NF kappaB activation . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| LMP 1 activates the IkappaB kinase complex and NF kappaB through two cytoplasmic signaling domains that engage tumor necrosis factor receptor associated factor ( TRAF ) 1 / 2 / 3 / 5 or TRADD and RIP . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| Tumor necrosis factor receptor 1 ( TNFR 1 ) associated death domain protein ( TRADD ) is essential in recruiting signaling molecules to the TNFR 1 receptor complex . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| These inclusions , formed from the collapse of fibrils , together with their associated components , also contain ubiquitinated proteins , vimentin , heat shock protein 72 , and tumor necrosis factor receptor type 1 associated death domain protein . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| TNAP specifically inhibits NF kappaB activation induced by tumor necrosis factor ( TNF ) alpha , TNF receptor 1 , TRADD , RIP , TRAF 2 , and NIK but does not affect IKK 1 and IKK 2 mediated NF kappaB activation . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| Although XEDAR induced apoptosis can be blocked by dominant negative Fas associated death domain ( FADD ) protein and FADD small interfering RNA , XEDAR does not directly bind to FADD , tumor necrosis factor receptor associated death domain ( TRADD ) protein , or RIP 1 . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| Tumor necrosis factor ( TNF ) receptor 1 associated death domain protein ( TRADD ) is an adaptor protein known to be involved in the TNF signaling pathway as well as signaling of other members of the TNF receptor superfamily , including DR 3 , DR 6 , p 75 ( NTR ) , and the Epstein Barr virus latent membrane protein 1 . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| It initiates the activation of signalling pathways , such as NF kappaB , mitogen activated protein kinase ( MAPK ) , and JAK / STAT cascade by adaptor proteins including the tumor necrosis factor ( TNF ) receptor associated factors ( TRAFs ) and the TNF receptor associated death domain protein ( TRADD ) . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| We investigated hepatitis B virus ( HBV ) DNA integration and expression of several proteins involved in the cell cycle and apoptosis , including cyclin A , retinoblastoma protein ( pRB ) , Fas associated death domain protein ( FADD ) , tumor necrosis factor receptor associated death domain protein ( TRADD ) , and nuclear factor kappaB ( NF kappaB ) in HBV associated hepatocellular carcinoma ( HCC ) and liver cirrhosis ( LC ) . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| CRT on RK ( 13 ) cell surface ( srCRT ) forms complex ( es ) with tumor necrosis factor receptor 1 ( TNFR 1 ) and TNFR associated death domain ( TRADD ) protein of the cell membrane . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| PAK 4 functions in tumor necrosis factor ( TNF ) alpha induced survival pathways by facilitating TRADD binding to the TNF receptor . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| We identified tumor necrosis factor receptor type 1 associated death domain protein ( TRADD ) as a keratin 18 binding protein . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| The authors tried to determine the responsible molecules ; however , expression of TRAIL receptors ; pro caspase 3 / 8 / 9 ; Fas associated death domain protein ( FADD ) ; tumor necrosis factor receptor 1 associated death domain protein ( TRADD ) ; silencer of death domain ( SODD ) ; FLICE inhibitory protein ( FLIP ) ; and Bcl 2 , Bcl xL , and Bax in FLS was not modulated by IFN gamma . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| BACKGROUND : Tumor necrosis factor receptor 1 recruits tumor necrosis factor receptor associated death domain ( TRADD ) and multiple kinases that ultimately phosphorylate inhibitor kappa B ( IKB alpha ) . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| The TNF receptor 1 associated protein TRADD signals cell death and NF kappa B activation . ^^^ Overexpression of TRADD leads to two major TNF induced responses , apoptosis and activation of NF kappa B . ^^^ However , NF kappa B activation by TRADD is not inhibited by crmA expression , demonstrating that the signaling pathways for TNF induced cell death and NF kappa B activation are distinct . . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
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 . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| One , MORT 1 ( also called FADD ) , binds to Fas / APO1 but not to p 55 R ; another , TRADD , binds to the p 55 TNF receptor but not to Fas / APO1 ; and the third , RIP , binds weakly to both receptors . ^^^ The regions within these proteins that are involved in binding to the receptors and the receptor regions to which they bind share a common sequence motif , that of the `` death domain . ' ' This study shows that the death domain motifs in MORT 1 , TRADD , and RIP bind effectively to each other , a mode of binding that may allow `` cross talk ' ' between the functional expression of the p 55 TNF receptor and Fas / APO1 . . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| Interaction of TRAF 2 with TNF R 2 and TRADD requires sequences at the C terminus of the TRAF C domain , whereas interaction with the protein kinase receptor interacting protein 5 ( RIP ) occurs via sequences at the N terminus of the TRAF C domain . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| The human TNF R 1 associated death domain protein ( TRADD ) induces cell death and NF kappa B activation when overexpressed . ^^^ Mouse TRADD specifically interacts with wild type TNF R 1 but not with a truncated mutant TNF R 1 lacking its C terminal 20 amino acids . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| The association of TRADD , a 34 kDa cytoplasmic protein containing a C terminal death domain , with aggregated TNF receptor 1 ( TNF R 1 ) through their respective death domains leads to NF kappa B activation and programmed cell death . ^^^ The recruitment of TRAF 2 and c IAP 1 to TNF R 1 is TNF dependent , is mediated by TRADD , and is independent of TNF R 2 . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| Association of the Fas / APO1 interacting protein MORT1 / FADD with the p 55 TNF receptor interacting protein TRADD , and the association of both MORT1 / FADD and TRADD with a third protein , RIP , provide potential cross talk mechanisms between Fas / APO1 and the p 55 TNF receptor . ^^^ TRAF 2 , a cytoplasmic protein that binds to the p 75 TNF receptor , as well as to several other receptors of the TNF / NGF family , also binds to TRADD , thus further extending the range of receptors of this family that can share common signaling mechanisms . ^^^ |
|
| Interacting proteins: P01375 and Q15628 |
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: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| The cloning of members of these gene families and the identification of the protein interaction motifs found within their gene products has initiated the molecular identity of factors ( TRADD , FADD / MORT , RIP , FLICE / MACH , and TRAFs ) associated with both of the p 60 and p 80 forms of the TNF receptor and with other members of the TNF receptor superfamily . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| Thus , MyD 88 plays the same role in IL 1 signaling as TRADD and Tube do in TNF and Toll pathways , respectively : it couples a serine / threonine protein kinase to the receptor complex . . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| TNF receptor death domain associated proteins TRADD and FADD signal activation of acid sphingomyelinase . ^^^ Here we describe the TNF dependent activation of acid SMase ( A SMase ) through the p 55 TNF receptor associated proteins TRADD and FADD . ^^^ Overexpression of TRADD and FADD in 293 cells did not change basal activity of A SMase but enhanced TNF induced stimulation of A SMase . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| In their cytoplasmic region , some of these receptors share a conserved sequence motif the ' death domain ' which is required for transduction of the apoptotic signal by recruiting other death domain containing adaptor molecules like the Fas associated protein FADD / MORT1 or the TNF receptor associated protein TRADD [ 2 4 ] . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| The adapter protein TRADD binds to TNF R 55 in a ligand dependent manner and serves as anchor for the subsequent recruitment of other proteins into the signaling complex that directly lead to cell death or nuclear factor kappaB ( NF kappaB ) induction . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| TNF treatment released SODD from TNF R 1 , permitting the recruitment of proteins such as TRADD and TRAF 2 to the active TNF R 1 signaling complex . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| TNF recruits TRADD to the plasma membrane but not the trans Golgi network , the principal subcellular location of TNF R 1 . ^^^ The subcellular interactions of TNF R 1 and the TRADD ( TNFR associated death domain protein ) adaptor protein have been analyzed in the human monocyte cell line U 937 and the human endothelial cell line ECV 304 by confocal immunofluorescence microscopy and by Western blot analysis of fractionated cell extracts . ^^^ In untreated cells , in which TNF R 1 is found on the cell surface but principally localizes to the trans Golgi network , TRADD is concentrated in the cis or medial Golgi region , but separates from the Golgi during cell fractionation . ^^^ Coimmunoprecipitation studies have shown that TRADD binds to TNF R 1 within 1 min of TNF treatment in a cell fraction containing plasma membrane . ^^^ In contrast , no association is detected between TRADD and TNF R 1 in the Golgi in response to exogenous TNF at any time examined . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| The constitutive expression of TNF receptors ( TNFRI and TNFRII ) and the adapter molecules , including TNFR associated death domain protein ( TRADD ) , TNFR associated factor 2 ( TRAF 2 ) , and receptor interacting protein ( RIP ) , were analyzed both at the protein level by flow cytometry or Western blotting , and at the mRNA level using quantitative PCR or Northern blotting in lymphocytes from aged and young subjects . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| No changes in the levels or molecular weights of the adaptor proteins TRADD ( TNF receptor associated death domain ) , RIP ( receptor interacting protein ) , or TRAF 2 ( TNF receptor associated factor 2 ) were caused by apoptogenic drugs . ^^^ Furthermore , TNF dependent recruitment of TRADD to surface TNFR 1 was also inhibited . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| Moreover , NF kappaB activation induced by overexpression of the TNF receptor associated proteins TNF receptor associated death domain protein ( TRADD ) , receptor interacting protein ( RIP ) , and TNF recep tor associated factor 2 ( TRAF 2 ) was also inhibited by expression of A 20 , whereas NF kappaB activation induced by overexpression of NF kappaB inducing kinase ( NIK ) or the human T cell leukemia virus type 1 ( HTLV 1 ) Tax was unaffected . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| RIPc , one of the cleavage products , enhanced interaction between TRADD and FADD / MORT1 and increased cells ' sensitivity to TNF . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| Death receptors belong to the TNF receptor family and are characterised by an intracellular death domain that serves to recruit adapter proteins such as TRADD and FADD and cysteine proteases such as Caspase 8 . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| They can be recruited to activated TNF receptors either by direct interactions with the receptors or indirectly via the adaptor protein TRADD . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| A combination of NMR , BIAcore , and mutagenesis experiments was used to help identify the site of interaction of N TRADD with C TRAF 2 , providing a framework for future attempts to selectively inhibit the TNF signaling pathways . . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
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: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| In parallel with this observation , WOX 1 also enhanced TRADD ( TNF receptor associated death domain protein ) mediated cell death in transient expression experiments . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| The expression of adapter molecules TNF receptor associated death domain ( TRADD ) , Fas associated death domain ( FADD ) and TNF associated factor 2 ( TRAF 2 ) and caspase 3 was analyzed by Western blotting . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| Furthermore , we demonstrate that HCV core protein does not compete with TNF receptor associated death domain ( TRADD ) for its interaction with the death domain of TNFR 1 . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| TNFalpha induced inhibition of the EpCAM expression is mediated by TNF receptor 1 through the TNF receptor associated death domain protein ( TRADD ) and by the activation of nuclear factor kappaB ( NF kappaB ) , and it can be blocked by dominant negative variants of TRADD and the NF kappaB inhibitor , IkappaB . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
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: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| Our data indicate that the resistance of p 53 mutated cl . 1001 cells to TNF induced cell death was not due to a defect in the expression of TRADD and FADD , yet correlated with a reduced caspase 8 activation as well as a deficient mitochondrial membrane permeabilization . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| The most well known apoptotic pathway regulated by TNF involves the TNFR 1 associated death domain protein , Fas associated death domain protein , and caspase 8 . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
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: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| Thus in PC 12 pheochromocytoma cells , ceramide appears to amplify the death signal and there appears to be a sequence of events : TNF ; TRADD , pro caspase 8 , caspase 8 , sphingomyelinase , ceramide , caspase 3 , apoptosis . . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| AD cases had increased levels of proapoptotic markers including tumor necrosis factor alpha ( TNFalpha ) , TNF receptor type 1 ( TNF R 1 ) , TNF receptor associated death domain ( TRADD ) , and caspase 3 , 2 to 10 fold higher ( P < . 01 ) than age matched controls and 1 to 3 times higher than transitional cases . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| The constitutive expression of mRNA for TNF receptors ( TNFR ) , including TNFRI and TNFRII , and the adapter molecules , such as the TNF receptor associated death domain protein ( TRADD ) , Fas associated death domain protein ( FADD ) , receptor interacting protein ( RIP ) and TNF receptor associated factor 2 ( TRAF 2 ) were analyzed by reverse transcriptase ( RT ) PCR in bone marrow samples from control , MDS and AML cases . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
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 ) . ^^^ TRADD also binds two other adaptors receptor interacting protein ( RIP ) and TNF receptor associated factor 2 ( TRAF 2 ) , which are required for TNF induced NF kappaB and c Jun N terminal kinase activation , respectively . ^^^ Analysis of the native TNF signaling complex revealed the recruitment of RIP , TRADD , and TRAF 2 but not FADD or caspase 8 . ^^^ In an in vitro binding assay , the intracellular domain of TNF R 1 bound TRADD , RIP , and TRAF 2 but did not bind FADD or caspase 8 . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| LMP 1 associates simultaneously with lipid rafts and with its signaling molecules , tumor necrosis factor receptor ( TNF R ) associated factors ( TRAFs ) and TNF R 1 associated death domain protein ( TRADD ) intracellularly , although it can be detected at low levels at the plasma membrane , indicating that most of LMP 1 ' s signaling complex resides in intracellular compartments . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| The first complex ( complex 1 ) is formed at the membrane by TNF R 1 , TRADD , RIP , TRAF 2 and c IAP 1 , while the second complex ( complex 2 ) , formed in the cytosol , predominantly contains FADD and pro caspases 8 / 10 but lacks TNF R 1 . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| SCH 66336 also inhibited the NF kappaB dependent reporter gene expression activated by TNF , TNFR 1 , TRADD , TRAF 2 , NIK , and IKK but not that activated by the p 65 subunit of NF kappaB . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| 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 TRAF 2 complex . . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| TNF binding induces release of AIP 1 from TNFR 1 , resulting in cytoplasmic translocation and concomitant formation of an intracellular signaling complex comprised of TRADD , RIP 1 , TRAF 2 , and AIPl . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| NF kappaB dependent reporter gene transcription induced by TNF , TNFR 1 , TRADD , TRAF 2 , NIK , and IKK was also blocked by guggulsterone but without affecting p 65 mediated gene transcription . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| We demonstrate here that within minutes internalized TNF R 1 ( TNF receptosomes ) recruits TRADD , FADD , and caspase 8 to establish the `` death inducing signaling complex ' ' ( DISC ) . ^^^ In contrast , aggregation of TRADD , FADD , and caspase 8 to establish the TNF R 1 associated DISC is critically dependent on receptor endocytosis . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| In the normal rat cortex , a portion of TNFR 1 was present in lipid raft microdomains , where it associated with the adaptor proteins TRADD ( TNF receptor associated death domain ) , TNF receptor associated factor 2 ( TRAF 2 ) , the Ser / Thr kinase RIP ( receptor interacting protein ) , TRAF 1 , and cIAP 1 ( cellular inhibitor of apoptosis protein 1 ) , forming a survival signaling complex . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| In contrast , transiently expressed Zfra could enhance or inhibit the cytotoxicity of overexpressed death domain proteins TRADD , FADD , and RIP of the TNF signaling pathway . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| Evodiamine also inhibited the NF kappaB dependent reporter gene expression activated by TNF , TNFR 1 , TRADD , TRAF 2 , NIK , and IKK but not that activated by the p 65 subunit of NF kappaB . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| Zerumbone also inhibited the NF kappaB dependent reporter gene expression activated by TNF , TNFR 1 , TRADD , TRAF 2 , NIK , and IKK but not that activated by the p 65 subunit of NF kappaB . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
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: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| Furthermore , SAHA inhibited the NF kappaB dependent reporter gene expression activated by TNF , TNFR 1 , TRADD , TRAF 2 , NF kappaB inducing kinase , IkappaBalpha kinase , and the p 65 subunit of NF kappaB . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| AhR sense / antisense transfection studies demonstrated that AhR contents influenced susceptibility to the pro apoptotic effects of TNFalpha + CHX . 1c1c7 cells and all variants expressed comparable amounts of TNF receptor 1 and TRADD . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| Modeling of six homotypic DD interactions involved in the TNF signaling pathway implicates that the DD of RIP ( Receptor interacting protein kinase 1 ) is capable of interacting with the DD of TRADD ( TNFR 1 associated death domain protein ) in two different , exclusive ways : one that subsequently recruits CRADD ( apoptosis / inflammation ) and another that recruits NFkappaB ( survival / proliferation ) . . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| In vivo protein protein interaction studies displayed an association between TNF receptor 1 ( TNFR 1 ) and TNFR 1 associated death domain protein ( TRADD ) , suggesting that the core protein does not perturb this interaction . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| K 17 interacts with TNF receptor 1 ( TNFR 1 ) associated death domain protein ( TRADD ) , a death adaptor essential for TNFR 1 dependent signal relay , suggesting a functional link between this keratin and TNFalpha signaling . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| Analysis of the upstream signaling events affected by PMA revealed that it markedly inhibited the TNF induced recruitment of TNFR 1 associated death domain protein ( TRADD ) and receptor interacting protein ( RIP ) to TNFR 1 , subsequently inhibiting TNF induced activation of nuclear factor kappaB and c Jun NH 2 terminal kinase ( JNK ) . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
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: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| Here we show that upon TNFalpha binding , TNFR 1 translocates to cholesterol and sphingolipid enriched membrane microdomains , termed lipid rafts , where it associates with the Ser / Thr kinase RIP and the adaptor proteins TRADD and TRAF 2 , forming a signaling complex . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| Furthermore , mutation in K 14 reduced its affinity to TNFalpha receptor associated death domain ( TRADD ) , suggesting that the susceptibility of keratinocytes to caspase 8 mediated apoptosis is increased in mutated K 14 because of impairment of the cytoprotective mechanism mediated by K 14 TRADD interaction . . ^^^ |
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| Interacting proteins: P01375 and Q15628 |
Pubmed |
SVM Score :0.0 |
| Seven proteins were identified , including TRADD , TRAP 2 , and TRAF 2 , which are three proteins known to be recruited to TNFalpha receptors . ^^^ |
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