| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| Further analysis of mRNA and protein expression levels of apoptosis signaling molecules FADD , receptor interacting protein , hematopoietic cell protein tyrosine phosphatase , Fas associated phosphatase 1 , FLICE , bel 2 , bcl xL , and , bax alpha showed that only the expression level of bcl xL correlated with T cell resistance to CD 95 mediated apoptosis ( day 1 T cells : bcl xhiL ; day 6 T cells : bcl XloL ) . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| The TNF R 1 associated death domain protein interacts with the p 55 TNF R 1 cytoplasmic domain and recruits the Fas associated death domain protein ( which directly activates the apoptotic proteases ) , the protein kinase receptor interacting protein , and TNF receptor associated factor 2 ( TRAF 2 ) . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| RNA expression of Fas receptor ( CD 95 ) associated proteins ( Fas associated phosphatase 1 / FAP 1 , Fas associating protein with death domain / FADD , and receptor interacting protein / RIP ) in human leukaemia / lymphoma cell lines . mRNA expression of Fas ( CD 95 ) associated proteins [ Fas associating protein with death domain ( FADD ) , receptor interacting protein ( RIP ) , and Fas associated phosphatase 1 ( FAP 1 ) ] has been investigated in 26 Fas positive human leukaemia / lymphoma cell lines . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| To clarify the molecular mechanism of apoptosis susceptibility , mRNA expression of FasR associated proteins [ Fas associating protein with death domain ( FADD ) , receptor interacting protein ( RIP ) , and Fas associated phosphatase 1 ( FAP 1 ) ] has been investigated in IL 2 activated T cells . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| The Fas associated signaling protein receptor interacting protein ( RIP ) was expressed by some Fas expressing cells , whereas Fas associated death domain ( FADD ) was undetectable in the early postnatal cerebral cortex . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
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: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| This Fas ligand induced caspase independent death is absent in T cells that are deficient in either Fas associated death domain ( FADD ) or receptor interacting protein ( RIP ) . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| The protein levels of caspase 3 , 8 , and 9 , DFF 45 ( DNA fragmentation factor 45 ) , and FLIP ( Fas associated death domain ( FADD ) like interleukin 1beta converting enzyme inhibitory proteins ) were decreased , whereas those of ARC ( apoptosis repressor with caspase recruitment domain ) and RICK ( Receptor interacting protein ( RIP ) like interacting CLARP kinase ) increased in AD . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
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 . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
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 . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| We also compared the subgroups in terms of the expression of Fas associated death domain protein ( FADD ) , the levels of activation of Receptor Interacting Protein ( RIP ) and caspases , and cleavage of Poly ( ADP Ribose ) Polymerase ( PARP ) . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| However , pretreatment of the cells with the Hsp 90 inhibitor geldanamycin , which leads to proteasome mediated degradation of receptor interacting protein 1 ( RIP 1 ) , reverts FKBP FADD induced necrosis to apoptosis . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| The signalling pathway incorporating FADD is largely independent of Toll like receptor 3 and the dsRNA dependent kinase PKR , but seems to require receptor interacting protein 1 as well as Tank binding kinase 1 mediated activation of the transcription factor IRF 3 . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| Furthermore , down regulating the receptor interacting protein , RIP , with geldanamycin treatment , which is essential for TNF alpha signalling , markedly inhibited AICD in FADD ( / ) Jurkat T cells . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| In mammals , DR signalling is mediated by the recruitment of several DD ( death domain ) containing molecules , such as FADD ( Fas associated DD ) and RIP 1 ( receptor interacting protein 1 ) . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
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 . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
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: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| RIP and FADD : two `` death domain ' ' containing proteins can induce apoptosis by convergent , but dissociable , pathways . ^^^ With use of the yeast two hybrid system , the proteins RIP and FADD / MORT1 have been shown to interact with the `` death domain ' ' of the Fas receptor . ^^^ Furthermore , RIP and FADD appear to activate different apoptotic pathways since RIP is able to induce cell death in a cell line that is resistant to the apoptotic effects of Fas , tumor necrosis factor , and FADD . ^^^ Consistent with this , a dominant negative mutant of FADD , lacking its N terminal domain , blocks apoptosis induced by RIP but not by FADD . ^^^ Since both pathways are blocked by CrmA , the interleukin 1 beta converting enzyme family protease inhibitor , these results suggest that FADD and RIP can act along separable pathways that nonetheless converge on a member of the interleukin 1 beta converting enzyme family of cysteine proteases . . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| An analysis of cells reconstituted with mutant forms of RIP reveals similarities between the action of RIP and FADD / MORT 1 , a Fas associated death domain protein . . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| Finally , both receptors can interact with FADD , TRADD , and RIP . ^^^ Thus , both DR 5 and DR 4 use FADD , TRADD , and RIP in their signal transduction pathways , and FADD is the common mediator of apoptosis by all known death domain containing receptors . . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| The intracellular domain of Fas interacts with several proteins including FADD ( MORT 1 ) , DAXX , RIP , FAF 1 , FAP 1 and Sentrin . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| On the other hand , bcl 2 or certain novel proteins ( including FADD , RIP , TRADD and sentrin ) prevent apoptosis . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
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: Q13546 and Q13158 |
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: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| Immunoprecipitates of fas antigen from membrane preparations made from control or castrated rat prostates were analyzed for coprecipitation of FADD and RIP proteins to assess the activation state of the fas antigen before and after castration . ^^^ Immunoprecipitates of fas antigen from membranes of ventral prostates from castrated rats contained significantly increased amounts of both FADD and RIP proteins when compared to those of intact or control operated rats . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| A dominant negative mutant of RIP inhibits FADD and caspase 8 induced but not Casper induced NF kappaB activation . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
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 . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| RIP 3 mediated apoptosis was inhibited by Bcl 2 , Bcl 10 ( L ) , dominant negative FADD , as well as the general caspase inhibitor Z VAD . ^^^ This region is similar , but distinct , to the death domain found in many pro apoptotic receptors and adapter proteins , including FAS , FADD , TNFR 1 , and RIP . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| 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: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| The C terminal of TRADD comprises the `` death domain ' ' that is responsible for association of TNFR 1 and other death domain containing proteins such as FADD and RIP . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| In contrast to Fas associated death domain ( FADD ) or caspase 8 , FADD like interleukin 1 converting enzyme inhibitory protein ( FLIP ) and RIP protein levels rapidly decreased upon treatment with CHX or ActD , indicating that both molecules have a high turnover rate . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
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 . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| Transfection of livin in HeLa cells resulted in protection from apoptosis induced by expression of FADD , Bax , RIP , RIP 3 , and DR 6 . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| Up regulation of surface FasL expression , accompanied by a down regulation of Fas associated proteins ( FADD , DAXX , and RIP ) , was observed 72 h after infection . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
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 . ^^^ 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 . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
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 . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| FasL , Fas , FADD , RIP , caspase 8 , caspase 3 , Bid , FLIP ( S+L ) , FLASH and FAP 1 , proteins known to act within the Fas apoptosis cascade , showed no changes in their expression levels in cells treated with butyrate compared with untreated cells . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| Both cell lines express almost the same levels of FADD , RIP , c FLIP , FAP 1 , Bax , Bcl 2 and Bcl XL . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| Furthermore , Jurkat cell lines deficient in RIP , caspase 8 , or FADD were as susceptible as wild type Jurkat cells to HIV 1 cytopathicity . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
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: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| The point of bifurcation of this pathway and the decision making molecules FADD , TRAF 2 and RIP are discussed . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| Here , we show that ectopic expression of the death receptor signaling protein RIP ( receptor interactive protein ) triggers apoptosis via a FAS associated death domain protein ( FADD ) and caspase 8 dependent pathway . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| Expression of FADD dominant negative in HEK 293 cells that prevents the recruitment of caspase 8 and RIP to TRAIL death receptors also eliminates this increase . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| 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 . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
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 . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| Ligation of CD 95 instigates the formation of a complex known as the `` death inducing signaling complex ' ' or DISC , which is composed of molecules including FADD ( Fas associated with death domain ) and RIP ( receptor interacting kinase ) , as well as procaspases 8 and 10 , and a caspase 8 like molecule that lacks proteolytic activity called c FLIP . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| Moreover , using the yeast two hybrid system , we tested whether p75NTR intracellular domain was able to dimerize or interact with known DD containing proteins including FADD , RIP , RAIDD and TRADD . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| In this study , we utilized gene knockout mouse embryonic fibroblasts cells and found that tumor necrosis factor receptor ( TNFR ) 1 mediates TNF induced necrotic cell death , and that RIP , FADD , and TRAF 2 are critical components of the signaling cascade of this TNF induced necrotic cell death . ^^^ Interestingly , during TNF induced necrotic cell death , the cellular ROS level was significantly elevated in wild type , but not in RIP ( / ) , TRAF 2 ( / ) , and FADD ( / ) cells . ^^^ These results suggest that RIP , TRAF 2 , and FADD are crucial in mediating ROS accumulation in TNF induced necrotic cell death . . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| Bcl 2 , RIP , FADD ) were not affected . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| NFkappaB activation by Fas is mediated through FADD , caspase 8 , and RIP and is inhibited by FLIP . ^^^ Here , we show that Fas activates NFkappaB via a pathway involving RIP , FADD , and caspase 8 . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
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 . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| Several proteins , including FADD , the death domain kinase RIP and the TNF receptor associated factor TRAF 2 have been identified as the key effectors of TNF signaling . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| This was established by showing that CIN 85 was co precipitated with TNFR 1 , TRADD , cIAP 1 and TARF1 / 2 , but not with FADD , RIP , caspase 8 or TRAF 6 . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| Ceramide analogs also induced cell death in Jurkat mutants that are deficient in cell death signaling proteins , including FADD , caspase 8 and 10 , and RIP . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| In a second step , TRADD and RIP 1 associate with FADD and caspase 8 , forming a cytoplasmic complex ( complex 2 ) . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
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: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| The secondary complex retained the DISC components FADD and caspase 8 , but recruited several factors involved in kinase activation by TNF , namely , RIP 1 , TRAF 2 , and NEMO / IKKgamma . ^^^ |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13546 and Q13158 |
Pubmed |
SVM Score :0.0 |
| NA |
|