Falcon deep research report on MYD88
Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Automatic assignment of GO terms using logical inference, based on on inter-ontology links
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
The cloning and characterization of human MyD88: a member of an IL-1 receptor related family.
IRAK (Pelle) family member IRAK-2 and MyD88 as proximal mediators of IL-1 signaling.
MyD88: an adapter that recruits IRAK to the IL-1 receptor complex.
MyD88 is an adaptor protein in the hToll/IL-1 receptor family signaling pathways.
The apoptotic signaling pathway activated by Toll-like receptor-2.
Mal (MyD88-adapter-like) is required for Toll-like receptor-4 signal transduction.
Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways.
Characterization of Pellino2, a substrate of IRAK1 and IRAK4.
Toll IL-1 receptors differ in their ability to promote the stabilization of adenosine and uridine-rich elements containing mRNA.
Interferon-alpha induction through Toll-like receptors involves a direct interaction of IRF7 with MyD88 and TRAF6.
Human TLR10 is a functional receptor, expressed by B cells and plasmacytoid dendritic cells, which activates gene transcription through MyD88.
Towards a proteome-scale map of the human protein-protein interaction network.
Localization of TLR2 and MyD88 to Chlamydia trachomatis inclusions. Evidence for signaling by intracellular TLR2 during infection with an obligate intracellular pathogen.
Modulation of TLR4 signaling by a novel adaptor protein signal-transducing adaptor protein-2 in macrophages.
Phosphoinositide-mediated adaptor recruitment controls Toll-like receptor signaling.
Extracellular heat shock protein 70 mediates heat stress-induced epidermal growth factor receptor transactivation in A431 carcinoma cells.
MAPPIT analysis of TLR adaptor complexes.
Hepatitis C virus nonstructural protein 5A modulates the toll-like receptor-MyD88-dependent signaling pathway in macrophage cell lines.
Distinct roles of TIR and non-TIR regions in the subcellular localization and signaling properties of MyD88.
Class-specific regulation of pro-inflammatory genes by MyD88 pathways and IkappaBzeta.
IL-33 induces antigen-specific IL-5+ T cells and promotes allergic-induced airway inflammation independent of IL-4.
Activation of ROS/NF-kappaB and Ca2+/CaM kinase II are necessary for VCAM-1 induction in IL-1beta-treated human tracheal smooth muscle cells.
A TIR domain variant of MyD88 adapter-like (Mal)/TIRAP results in loss of MyD88 binding and reduced TLR2/TLR4 signaling.
Expression of the Bcl-2 protein BAD promotes prostate cancer growth.
AIP1 functions as Arf6-GAP to negatively regulate TLR4 signaling.
Identification of MyD88 as a novel target of miR-155, involved in negative regulation of Helicobacter pylori-induced inflammation.
The transmembrane activator TACI triggers immunoglobulin class switching by activating B cells through the adaptor MyD88.
Aspartate-glutamate-alanine-histidine box motif (DEAH)/RNA helicase A helicases sense microbial DNA in human plasmacytoid dendritic cells.
Clinical features and outcome of patients with IRAK-4 and MyD88 deficiency.
The hepatitis B e antigen (HBeAg) targets and suppresses activation of the toll-like receptor signaling pathway.
Next-generation sequencing to generate interactome datasets.
TIRAP, an adaptor protein for TLR2/4, transduces a signal from RAGE phosphorylated upon ligand binding.
Crystal structure of Toll-like receptor adaptor MAL/TIRAP reveals the molecular basis for signal transduction and disease protection.
Toward an understanding of the protein interaction network of the human liver.
The Brucella TIR-like protein TcpB interacts with the death domain of MyD88.
DOCK8 functions as an adaptor that links TLR-MyD88 signaling to B cell activation.
β-TrCP-mediated IRAK1 degradation releases TAK1-TRAF6 from the membrane to the cytosol for TAK1-dependent NF-κB activation.
HCV-induced miR-21 contributes to evasion of host immune system by targeting MyD88 and IRAK1.
Functional assessment of the mutational effects of human IRAK4 and MyD88 genes.
A proteome-scale map of the human interactome network.
A massively parallel pipeline to clone DNA variants and examine molecular phenotypes of human disease mutations.
Widespread macromolecular interaction perturbations in human genetic disorders.
SARM modulates MyD88-mediated TLR activation through BB-loop dependent TIR-TIR interactions.
Increased Expression of Interleukin-36, a Member of the Interleukin-1 Cytokine Family, in Inflammatory Bowel Disease.
Widespread Expansion of Protein Interaction Capabilities by Alternative Splicing.
Pooled-matrix protein interaction screens using Barcode Fusion Genetics.
Architecture of the human interactome defines protein communities and disease networks.
HDAC6 controls innate immune and autophagy responses to TLR-mediated signalling by the intracellular bacteria Listeria monocytogenes.
An interactome perturbation framework prioritizes damaging missense mutations for developmental disorders.
Selective disruption of TLR2-MyD88 interaction inhibits inflammation and attenuates Alzheimer's pathology.
Understanding early TLR signaling through the Myddosome.
The TLR4 adaptor TRAM controls the phagocytosis of Gram-negative bacteria by interacting with the Rab11-family interacting protein 2.
T-Cell Deletion of MyD88 Connects IL17 and IκBζ to RAS Oncogenesis.
Extensive disruption of protein interactions by genetic variants across the allele frequency spectrum in human populations.
A reference map of the human binary protein interactome.
SARS-CoV-2, SARS-CoV-1, and HIV-1 derived ssRNA sequences activate the NLRP3 inflammasome in human macrophages through a non-classical pathway.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Systematic discovery of mutation-directed neo-protein-protein interactions in cancer.
PAUF Induces Migration of Human Pancreatic Cancer Cells Exclusively via the TLR4/MyD88/NF-κB Signaling Pathway.
Regulation of innate immune signaling by IRAK proteins.
BacSp222 bacteriocin as a novel ligand for TLR2/TLR6 heterodimer.
USP3 plays a critical role in the induction of innate immune tolerance.
OTUD5 promotes the inflammatory immune response by enhancing MyD88 oligomerization and Myddosome formation.
Molecular definition of the endogenous Toll-like receptor signalling pathways.
TLR9 signaling requires ligand-induced phosphorylation of two specific tyrosine residues by EGFR and Syk.
MyD88 forms a complex with TIRAP:activated TLR2/4
IRAK4 binds to the activated TLR receptor:TIRAP:MyD88 complex
IRAK1 or IRAK2 binds to the activated IRAK4 :activated TLR:MyD88:TIRAP complex
First phosphorylation of IRAK1 by IRAK4 bound to activated TLR:MyD88:Mal
Second phosphorylation of IRAK1 by IRAK4 bound to activated TLR:MyD88:TIRAP
Multiple IRAK1 autophosphorylation steps
Dissociation of hp-IRAK1:TRAF6 from the activated TLR:oligo-Myd88:TIRAP:p-IRAK4 complex
IRAK interacts with TRAF6
Dissociation of p-IRAK2:TRAF6 from the activated TLR:oligo-Myd88:TIRAP:p-IRAK4 complex
DHX36 or DHX9 binds MyD88
IRAK4 is activated by autophosphorylation
IL1R1:IL1:IL1RAP:MYD88 homodimer binds IRAK4
IRAK2 is phosphorylated downstream of IRAK4 following IL1 receptor activation
IRAK1 binds to MYD88 within the IL1R complex
IRAK4 phosphorylates IRAK1
IRAK4-activated IRAK1 autophosphorylates
Hyperphosphorylated IRAK1 associates with TRAF6
The Interleukin 1 receptor complex binds Tollip
TRAF6 binding leads to IRAK1:TRAF6 release
IL1R1:IL1:IL1RAP binds MYD88 homodimer
Defective MyD88 does not oligomerize within the complex of activated TLR5
Defective IRAK4 does not bind MyD88:MAL:BTK:activated TLR2/4
Defective MyD88 does not oligomerize within the activated TLR2/4 complex
IRAK4 deficiency blocks formation of the MyD88-IRAK4 Myddosome in the TLR5 pathway
Defective MyD88 does not bind MAL(TIRAP):TLR2/4
IRAK4 autophosphorylation in the complex with activated TLR:MyD88:TIRAP
Phosphorylation of IRAK2 bound to the activated IRAK4:MyD88 oligomer:TIRAP:activated TLR complex
MyD88 oligomerization within the complex of activated TLR:TIRAP:MyD88
MyD88 oligomerization within the complex of activated TLR 7/8 or 9 : MyD88
Dissociation of hp-IRAK1/or IRAK2:TRAF6-oligomer from the p-IRAK4 :oligo-Myd88:activated TLR7/8 or 9 complex
Phosphorylation and release of IRF7 upon TLR7/8 or 9 activation
TRAF6 binds to hp- IRAK1/or p-IRAK2:p-IRAK4:MyD88:activated TLR7/8 or 9
IRAK1/or IRAK2 binds to the activated IRAK4 :MyD88:activated TLR 7/8 or 9
TRAF6 ubiquitinqtes IRF7 within the activated TLR7/8 or 9 complex
Multiple IRAK1 autophosphorylation steps within the complex pIRAK4:MyD88:activated TLR7/8 or 9
Second phosphorylation of IRAK1 by IRAK4 bound to MyD88: activated TLR 7/8 or 9
IRAK4 binds to the activated TLR7/8 or 9 receptor:MyD88 complex
Phosphorylation of IRAK2 bound to the activated IRAK4:MyD88 oligomer:activated TLR 7/8 or 9
IRAK4 autophosphorylation in the complex with MyD88:activated TLR 7/8 or 9
MyD88 interacts with the activated TLR receptor 7, 8 or 9
First phosphorylation of IRAK1 by IRAK4 bound to MyD88:activated TLR 7/8 or 9
TRAF6 interacts with IRF7 upon TLR7/8 or 9 activation
IRAK1/or IRAK2 binds to the activated IRAK4 :oligo MyD88:activated TLR5 or 10 complex
Multiple IRAK1 autophosphorylation within the complex p-IRAK4:oligo MyD88:activated TLR
TRAF6 binds to hp- IRAK1 or p-IRAK2
Phosphorylation of IRAK2 bound to the activated IRAK4:MyD88 oligomerl:activated TLR5 or 10 complex
IRAK4 autophosphorylation within the complex activated TLR:MyD88
MyD88 forms a complex with the activated TLR receptor
IRAK4 binds to MyD88 bound to the activated TLR5 or 10 receptor
Second phosphorylation of IRAK1 by IRAK4 bound to MyD88:activated TLR complex
First phosphorylation of IRAK1 by IRAK4 bound to MyD88:activated TLR
Dissociation of hp-IRAK1:TRAF6 or IRAK2:TRAF6-oligomer from the activated TLR5 or 10:oligo-Myd88:p-IRAK4 complex
MyD88 oligomerization within the complex of activated TLR:MyD88
The pro-atherogenic cytokine interleukin-18 induces CXCL16 expression in rat aortic smooth muscle cells via MyD88, interleukin-1 receptor-associated kinase, tumor necrosis factor receptor-associated factor 6, c-Src, phosphatidylinositol 3-kinase, Akt, c-Jun N-terminal kinase, and activator protein-1 signaling.