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MADD, a novel death domain protein that interacts with the type 1 tumor necrosis factor receptor and activates mitogen-activated protein kinase (Q24315104)

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English	MADD, a novel death domain protein that interacts with the type 1 tumor necrosis factor receptor and activates mitogen-activated protein kinase	scientific article

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scholarly article

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MADD, a novel death domain protein that interacts with the type 1 tumor necrosis factor receptor and activates mitogen-activated protein kinase (English)

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MAP kinase activating death domain

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GOA release 2020-03-11

regulation of extrinsic apoptotic signaling pathway via death domain receptors

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GOA release 2020-03-11

author name string

A R Schievella

1

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J H Chen

2

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J R Graham

3

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L L Lin

4

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publication date

2 May 1997

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language of work or name

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Journal of Biological Chemistry

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272

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18

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12069-75

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The TNF receptor superfamily of cellular and viral proteins: activation, costimulation, and death

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The polypeptide encoded by the cDNA for human cell surface antigen Fas can mediate apoptosis

1 reference

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A novel domain within the 55 kd TNF receptor signals cell death

1 reference

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Characterization of binding and biological effects of monoclonal antibodies against a human tumor necrosis factor receptor

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The two different receptors for tumor necrosis factor mediate distinct cellular responses

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The stress-activated protein kinase subfamily of c-Jun kinases

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Independent human MAP-kinase signal transduction pathways defined by MEK and MKK isoforms

1 reference

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Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine

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Tumor necrosis factor receptor-mediated signaling pathways

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The TNF receptor 1-associated protein TRADD signals cell death and NF-kappa B activation

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TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways

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TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex

1 reference

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TRAF2-mediated activation of NF-kappa B by TNF receptor 2 and CD40

1 reference

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RIP: a novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death

1 reference

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A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain

1 reference

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FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis

1 reference

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Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death

1 reference

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FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death--inducing signaling complex

1 reference

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A new class of yeast transcriptional activators

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Filamentous coliphage M13 as a cloning vehicle: insertion of a HindII fragment of the lac regulatory region in M13 replicative form in vitro

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Improved vectors for stable expression of foreign genes in mammalian cells by use of the untranslated leader sequence from EMC virus

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A novel arachidonic acid-selective cytosolic PLA2 contains a Ca(2+)-dependent translocation domain with homology to PKC and GAP

1 reference

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Cdi1, a human G1 and S phase protein phosphatase that associates with Cdk2

1 reference

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The death domain: a module shared by proteins with diverse cellular functions.

1 reference

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The leucine zipper: a hypothetical structure common to a new class of DNA binding proteins

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The regulation of AP-1 activity by mitogen-activated protein kinases

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Transcription factor ATF2 regulation by the JNK signal transduction pathway

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Cyclic AMP-Independent ATF Family Members Interact with NF-κB and Function in the Activation of the E-Selectin Promoter in Response to Cytokines

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Signals and receptors involved in recruitment of inflammatory cells

1 reference

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Tumor necrosis factor alpha gene regulation in activated T cells involves ATF-2/Jun and NFATp

1 reference

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cPLA2 is phosphorylated and activated by MAP kinase

1 reference

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Cytoplasmic phospholipase A2 activity and gene expression are stimulated by tumor necrosis factor: dexamethasone blocks the induced synthesis

1 reference

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Cytosolic phospholipase A2 is coupled to hormonally regulated release of arachidonic acid

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Contenders in FasL/TNF death signaling

1 reference

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Dissection of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis while NF-kappaB activation prevents cell death

1 reference

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How MAP kinases are regulated

1 reference

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JNK1: a protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain

1 reference

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The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signaling pathway

1 reference

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Selective activation of the JNK signaling cascadeand c-Jun transcriptional activity by the small GTPases Rac and Cdc42Hs

1 reference

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Cdc42 and PAK-mediated signaling leads to Jun kinase and p38 mitogen-activated protein kinase activation

1 reference

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Requirement for ceramide-initiated SAPK/JNK signalling in stress-induced apoptosis.

1 reference

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Integration of MAP kinase signal transduction pathways at the serum response element

1 reference

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A mitogen-activated protein kinase independent pathway involved in the phosphorylation and activation of cytosolic phospholipase A2 in human neutrophils stimulated with tumor necrosis factor-alpha

1 reference

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7 January 2021

based on heuristic

inferred from DOI database lookup

Self-association of the Death Domains of the p55 Tumor Necrosis Factor (TNF) Receptor and Fas/APO1 Prompts Signaling for TNF and Fas/APO1 Effects

1 reference

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7 January 2021

based on heuristic

inferred from DOI database lookup

Cytosolic Phospholipase A2 Is Phosphorylated in Collagen- and Thrombin-stimulated Human Platelets Independent of Protein Kinase C and Mitogen-activated Protein Kinase

1 reference

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based on heuristic

inferred from DOI database lookup

Thrombin induces activation of p38 MAP kinase in human platelets

1 reference

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based on heuristic

inferred from DOI database lookup

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10.1074/JBC.272.18.12069

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