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Interaction IDMol ATypeSpeciesVerbNatureMol BTypeSpecies
26212FASProteinHomo sapiens-eIncreases translocationindirectDAXXProteinHomo sapiens-e
However, HSP27 blocked Fas-induced translocation of Daxx from the nucleus to the cytoplasm and Fas-induced Daxx- and Ask1-dependent apoptosis.
Regulator
26213DAXXProteinHomo sapiens-eBinddirectFASProteinHomo sapiens-e
Here we show that phosphorylated dimers of HSP27 interact with Daxx, a mediator of Fas-induced apoptosis, preventing the interaction of Daxx with both Ask1 and Fas and blocking Daxx-mediated apoptosis.
Regulator
57364TNFProteinHomo sapiens-eIncreases expressionindirectFasProteinMus musculus
Fas is constitutively expressed by primary murine microglia at a low level and significantly up-regulated by TNF-alpha or IFN-gamma stimulation. / TNF-alpha and IFN-gamma induced Fas mRNA by approximately 20-fold.
77850Activator protein 1Multi subunitHomo sapiens-eIncreases activitydirectFASDNAHomo sapiens
Our present study identified an upstream enhancer element (between nucleotide positions -862 and -682) containing a GA-binding protein (GABP) site and a low affinity activating protein-1 (AP-1)-binding site. T cell activation increased the DNA binding of GABP and AP-1 to this enhancer site. / Taken together, these results suggest that the transcription factors GABP and AP-1 play a critical role in the induction of Fas gene expression in T cell antigen receptor.CD3-stimulated Jurkat cells.
Structure
83907FasProteinMus musculusIncreases phosphorylationindirectNfkbiaProteinMus musculus
In fibroblast strains derived from these embryos, the TNF receptors, Fas/Apo1, and DR3 were able to activate the Jun N-terminal kinase and to trigger IkappaB alpha phosphorylation and degradation.
83911FasProteinMus musculusIncreases degradationindirectNfkbiaProteinMus musculus
In fibroblast strains derived from these embryos, the TNF receptors, Fas/Apo1, and DR3 were able to activate the Jun N-terminal kinase and to trigger IkappaB alpha phosphorylation and degradation.
210293FASProteinHomo sapiens-eIncreases cleavageindirectCASP3ProteinHomo sapiens-e
In the present studies, we found that stimulation of CD95 receptors, with either agonistic antibody or CD95 ligand, resulted in the activation of caspase-8, which in turn processed caspase-3 between its large and small subunits.
Regulator