Any process that activates or increases the frequency, rate or extent of activity of the transcription factor NF-kappaB.

Any process that activates or increases the frequency, rate or extent of activity of the transcription factor NF-kappaB.

Any process that activates or increases the frequency, rate, or extent of T cell cytokine production.

Any process that activates or increases the frequency, rate, or extent of T cell cytokine production.

Any process that initiates the activity of the inactive enzyme cysteine-type endopeptidase in the context of an apoptotic process.

The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell.

The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell.

The process in which a signal is passed on to downstream components within the cell through the I-kappaB-kinase (IKK)-dependent activation of NF-kappaB. The cascade begins with activation of a trimeric IKK complex (consisting of catalytic kinase subunits IKKalpha and/or IKKbeta, and the regulatory scaffold protein NEMO) and ends with the regulation of transcription of target genes by NF-kappaB. In a resting state, NF-kappaB dimers are bound to I-kappaB proteins, sequestering NF-kappaB in the cytoplasm. Phosphorylation of I-kappaB targets I-kappaB for ubiquitination and proteasomal degradation, thus releasing the NF-kappaB dimers, which can translocate to the nucleus to bind DNA and regulate transcription.

The stimulation of the activity of NF-kappaB-inducing kinase through phosphorylation at specific residues.

The stimulation of the activity of NF-kappaB-inducing kinase through phosphorylation at specific residues.

Any process that modulates the rate or extent of the tumor necrosis factor-mediated signaling pathway. The tumor necrosis factor-mediated signaling pathway is the series of molecular signals generated as a consequence of tumor necrosis factor binding to a cell surface receptor.

The removal of one or more ubiquitin groups from a protein.

The chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.

Any process that activates or increases the frequency, rate, or extent of interleukin-2 production.

Any process that activates or increases the frequency, rate, or extent of interleukin-2 production.

A series of molecular signals initiated by the binding of a tumor necrosis factor to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription.

A series of molecular signals initiated by the binding of a tumor necrosis factor to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription.

A series of molecular signals initiated by the binding of a tumor necrosis factor to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription.

A series of molecular signals initiated by the binding of a tumor necrosis factor to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription.

Any process that stops, prevents, or reduces the frequency, rate, or extent of glial cell apoptotic process.

The aggregation, arrangement and bonding together of a set of components to form a protein complex, occurring at the level of an individual cell.

The aggregation, arrangement and bonding together of a set of components to form a protein complex, occurring at the level of an individual cell.

Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stress acting at the endoplasmic reticulum. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen.

Any process that modulates the occurrence or rate of cell death by apoptotic process.

Any process that modulates the occurrence or rate of cell death by apoptotic process.

Any process that modulates the occurrence or rate of cell death by apoptotic process.

Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process.

Any process that activates or increases the frequency, rate or extent of I-kappaB kinase/NF-kappaB signaling.

Any process that activates or increases the frequency, rate or extent of JUN kinase activity.

Any process that activates or increases the frequency, rate or extent of JUN kinase activity.

Any process that activates or increases the frequency, rate or extent of JUN kinase activity.

Any process that modulates the frequency, rate or extent of signal transduction mediated by the JNK cascade.

Any process that modulates the frequency, rate or extent of the regulated release of immunoglobulins from a cell.

Any process that activates or increases the frequency, rate or extent of activity of a transcription factor, any factor involved in the initiation or regulation of transcription.

Any process that activates or increases the frequency, rate or extent of activity of a transcription factor, any factor involved in the initiation or regulation of transcription.

Any process that activates or increases the frequency, rate or extent of activity of the transcription factor NF-kappaB.

The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of component monomers that are not all identical. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer.

The ubiquitination by a protein of one or more of its own amino acid residues, or residues on an identical protein. Ubiquitination occurs on the lysine residue by formation of an isopeptide crosslink.

The ubiquitination by a protein of one or more of its own amino acid residues, or residues on an identical protein. Ubiquitination occurs on the lysine residue by formation of an isopeptide crosslink.

The ubiquitination by a protein of one or more of its own amino acid residues, or residues on an identical protein. Ubiquitination occurs on the lysine residue by formation of an isopeptide crosslink.

The ubiquitination by a protein of one or more of its own amino acid residues, or residues on an identical protein. Ubiquitination occurs on the lysine residue by formation of an isopeptide crosslink.

The aggregation, arrangement and bonding together of a set of macromolecules to form a protein-containing complex.

A series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a cell. The pathway is induced in response to a stimulus indicating endoplasmic reticulum (ER) stress, and ends when the execution phase of apoptosis is triggered. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen.

The formation of a protein homotrimer, a macromolecular structure consisting of three noncovalently associated identical subunits.

The formation of a protein homotrimer, a macromolecular structure consisting of three noncovalently associated identical subunits.

A protein ubiquitination process in which a polymer of ubiquitin, formed by linkages between lysine residues at position 63 of the ubiquitin monomers, is added to a protein. K63-linked ubiquitination does not target the substrate protein for degradation, but is involved in several pathways, notably as a signal to promote error-free DNA postreplication repair.

A protein ubiquitination process in which a polymer of ubiquitin, formed by linkages between lysine residues at position 63 of the ubiquitin monomers, is added to a protein. K63-linked ubiquitination does not target the substrate protein for degradation, but is involved in several pathways, notably as a signal to promote error-free DNA postreplication repair.

A protein ubiquitination process in which a polymer of ubiquitin, formed by linkages between lysine residues at position 63 of the ubiquitin monomers, is added to a protein. K63-linked ubiquitination does not target the substrate protein for degradation, but is involved in several pathways, notably as a signal to promote error-free DNA postreplication repair.

A process of protein complex assembly in which the arrangement and bonding together of the set of components that form the protein complex is mediated by a death domain (DD) interaction, as part of the extrinsic apoptotic signaling pathway.

Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a nitric oxide stimulus.

Any process that increases the frequency, rate or extent of protein homodimerization, interacting selectively with an identical protein to form a homodimer.

Any process that increases the frequency, rate or extent of protein homodimerization, interacting selectively with an identical protein to form a homodimer.

A necrotic cell death process that results from the activation of endogenous cellular processes, such as signaling involving death domain receptors or Toll-like receptors.

Any process that stops, prevents or reduces the frequency, rate or extent of neuron death.

Any process that modulates the frequency, rate or extent of extrinsic apoptotic signaling pathway via death domain receptors.

Any process that stops, prevents or reduces the frequency, rate or extent of extrinsic apoptotic signaling pathway via death domain receptors.

Any process that activates or increases the frequency, rate or extent of tumor necrosis factor-mediated signaling pathway.

Any process that activates or increases the frequency, rate or extent of I-kappaB phosphorylation.

Any process that activates or increases the frequency, rate or extent of extrinsic apoptotic signaling pathway.

Any process that activates or increases the frequency, rate or extent of extrinsic apoptotic signaling pathway.

A series of molecular signals initiated by the binding of a tumor necrosis factor to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription.

Any process that stops, prevents, or reduces the frequency, rate, or extent of glial cell apoptotic process.

The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of component monomers that are not all identical. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer.

The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

A protein complex of the endoplasmic reticulum membrane that consists of IRE1 (Inositol-requiring enzyme-1), TRAF2 (TNF receptor-associated factor 2) and ASK1 (Apoptosis signal-regulating kinase 1, a MAP3K).

All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

Any of the small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes. Small rafts can sometimes be stabilized to form larger platforms through protein-protein and protein-lipid interactions.

A protein complex that includes a ubiquitin-protein ligase and enables ubiquitin protein ligase activity. The complex also contains other proteins that may confer substrate specificity on the complex.

A protein complex that includes a ubiquitin-protein ligase and enables ubiquitin protein ligase activity. The complex also contains other proteins that may confer substrate specificity on the complex.

That part of the nuclear content other than the chromosomes or the nucleolus.

All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

The region of a cell that lies just beneath the plasma membrane and often, but not always, contains a network of actin filaments and associated proteins.

The leaflet the plasma membrane that faces the cytoplasm and any proteins embedded or anchored in it or attached to its surface.

The leaflet the plasma membrane that faces the cytoplasm and any proteins embedded or anchored in it or attached to its surface.

The lipid bilayer surrounding any membrane-bounded vesicle in the cell.

A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.

A protein complex that contains at least CD40 (a cell surface receptor of the tumour necrosis factor receptor (TNFR) superfamily), and other signaling molecules.

A protein complex that contains at least CD40 (a cell surface receptor of the tumour necrosis factor receptor (TNFR) superfamily), and other signaling molecules.

Any of the small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes. Small rafts can sometimes be stabilized to form larger platforms through protein-protein and protein-lipid interactions.

A protein complex comprising tumor necrosis factor (TNF) receptor-associated factor 2 (TRAF2) and glutathione S-transferase pi 1 (GSTP1). This complex is thought to disrupt the TNF signaling cascade, thus down-regulating inflammatory responses.

A protein complex comprising tumor necrosis factor (TNF) receptor-associated factor 2 (TRAF2) and glutathione S-transferase pi 1 (GSTP1). This complex is thought to disrupt the TNF signaling cascade, thus down-regulating inflammatory responses.

A protein complex of the endoplasmic reticulum membrane that consists of IRE1 (Inositol-requiring enzyme-1), TRAF2 (TNF receptor-associated factor 2) and ASK1 (Apoptosis signal-regulating kinase 1, a MAP3K).

The region of a cell that lies just beneath the plasma membrane and often, but not always, contains a network of actin filaments and associated proteins.

A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.

A protein complex of the endoplasmic reticulum membrane that consists of IRE1 (Inositol-requiring enzyme-1), TRAF2 (TNF receptor-associated factor 2) and ASK1 (Apoptosis signal-regulating kinase 1, a MAP3K).