Pubmed abstracts for Protein-Protein Interaction search result :


Interacting proteins: Q13546 and Q15628 Pubmed SVM Score :0.73500223
Here , we show that TRADD interacts strongly with RIP , another death domain protein that was shown previously to associate with Fas antigen . 0.73500223^^^
Interacting proteins: Q13546 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: Q13546 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 . ^^^
Interacting proteins: Q13546 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 . ^^^
Interacting proteins: Q13546 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 . ^^^
Interacting proteins: Q13546 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 . ^^^
Interacting proteins: Q13546 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 . ^^^
Interacting proteins: Q13546 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: Q13546 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: Q13546 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 . ^^^
Interacting proteins: Q13546 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 . ^^^
Interacting proteins: Q13546 and Q15628 Pubmed SVM Score :0.0
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 . ^^^
Interacting proteins: Q13546 and Q15628 Pubmed SVM Score :0.0
An important regulatory step in control of antiapoptotic signaling is the assembly of the TNFR 1 TNFR 1 associated death domain protein ( TRADD ) TNFR associated factor 2 ( TRAF 2 ) receptor interacting protein ( RIP ) complex that controls NF kappaB activation . ^^^
Interacting proteins: Q13546 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 . ^^^
Interacting proteins: Q13546 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 ) . . ^^^
Interacting proteins: Q13546 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 ) . ^^^
Interacting proteins: Q13546 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 . ^^^
Interacting proteins: Q13546 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: Q13546 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: Q13546 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 . ^^^
Interacting proteins: Q13546 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 . ^^^
Interacting proteins: Q13546 and Q15628 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 Q15628 Pubmed SVM Score :0.0
TNFR 1 recruits and assembles a signaling complex containing a number of death domain ( DD ) containing proteins , including the adaptor protein TRADD and the serine / threonine kinase RIP , which mediates TNF induced NF kappa B activation . ^^^
Interacting proteins: Q13546 and Q15628 Pubmed SVM Score :0.0
TNFRI has been recently shown to activate NF kappaB through association with TRADD , RIP , and TRAF 2 ; activation of the NF kappaB inducing kinase ( NIK ) ; activation of the IkappaB alpha kinases ( IKKalpha and IKKbeta ) ; and phosphorylation of IkappaB alpha . ^^^
Interacting proteins: Q13546 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: Q13546 and Q15628 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 Q15628 Pubmed SVM Score :0.0
Isolation and characterization of death domain containing proteins ( TRADD , FADD / MORT 1 , RIP ) , TRAF domain containing proteins ( TRAF 1 6 ) as well as new members and adaptor proteins such as DAXX have provided new insights to our understanding of signaling mechanisms associated with this family of receptors . ^^^
Interacting proteins: Q13546 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: Q13546 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: Q13546 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 ) . ^^^ To investigate the importance of the 60 % of the LMP 1 carboxyl terminus that lies between the TES 1 TRAF and TES 2 TRADD and RIP binding sites , an EBV recombinant was made that contains a specific deletion of LMP 1 codons 232 to 351 . ^^^ Mutant and wt LMP 1 proteins were also similar in their constitutive association with TRAF 1 , TRAF 2 , TRAF 3 , TRADD , and RIP . ^^^
Interacting proteins: Q13546 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 . ^^^
Interacting proteins: Q13546 and Q15628 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 Q15628 Pubmed SVM Score :0.0
The involvement of the death adaptor proteins FADD / MORT1 , TRADD , and RIP and the apoptosis initiating caspases 8 and 10 in death signaling by the two death inducing TRAIL receptors 1 and 2 ( TRAIL R 1 and TRAIL R 2 ) are controversial . ^^^
Interacting proteins: Q13546 and Q15628 Pubmed SVM Score :0.0
TRADD alternatively recruits the NF kappaB inducing adaptor RIP . ^^^ TRADD and RIP , which bound TNFR 1 , did not bind DR 4 and DR 5 . ^^^
Interacting proteins: Q13546 and Q15628 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 Q15628 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 Q15628 Pubmed SVM Score :0.0
We show the EGFR forms a complex with a TNFR interacting protein ( RIP ) , which plays a key role in TNFR induced NF kappaB activation , but not with TRADD , an adaptor protein which serves to recruit RIP to the TNFR . ^^^
Interacting proteins: Q13546 and Q15628 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 Q15628 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 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: Q13546 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: Q13546 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 . ^^^ We show here that the zinc finger protein A 20 is an NF kappaB inducible gene that can protect the IKKgamma deficient cells from TNF induced apoptosis by disrupting the recruitment of the death domain signaling molecules TRADD and RIP to the receptor signaling complex . ^^^
Interacting proteins: Q13546 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 . ^^^
Interacting proteins: Q13546 and Q15628 Pubmed SVM Score :0.0
TL1A induced the formation of a DR 3 signaling complex containing TRADD , TRAF 2 , and RIP and activated the NF kappaB and the ERK , JNK , and p 38 mitogen activated protein kinase pathways . ^^^
Interacting proteins: Q13546 and Q15628 Pubmed SVM Score :0.0
TRAFs , TRADD , RIP , JAK 3 , BRAM 1 , and p 85 . ^^^
Interacting proteins: Q13546 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 . ^^^
Interacting proteins: Q13546 and Q15628 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 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: Q13546 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: Q13546 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: Q13546 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: Q13546 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 . ^^^
Interacting proteins: Q13546 and Q15628 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 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: Q13546 and Q15628 Pubmed SVM Score :0.0
The initial plasma membrane bound complex ( complex 1 ) consists of TNFR 1 , the adaptor TRADD , the kinase RIP 1 , and TRAF 2 and rapidly signals activation of NF kappa B . ^^^ In a second step , TRADD and RIP 1 associate with FADD and caspase 8 , forming a cytoplasmic complex ( complex 2 ) . ^^^
Interacting proteins: Q13546 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: Q13546 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 . ^^^
Interacting proteins: Q13546 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 . ^^^ We found that TRADD is required for TNFR 1 to induce NF kappaB activation and caspase 8 dependent apoptosis but is dispensable for TNFR 1 initiated , RIP 1 dependent necrosis . ^^^ Our data also show that TRADD and RIP 1 compete for recruitment to the TNFR 1 signaling complex and the distinct programs of cell death . ^^^ Thus , TNFR 1 initiated intracellular signals diverge at a very proximal level by the independent association of two death domain containing proteins , RIP 1 and TRADD . ^^^
Interacting proteins: Q13546 and Q15628 Pubmed SVM Score :0.0
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Interacting proteins: Q13546 and Q15628 Pubmed SVM Score :0.0
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Interacting proteins: Q13546 and Q15628 Pubmed SVM Score :0.0
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