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
Mal (MyD88-adapter-like) is required for Toll-like receptor-4 signal transduction.
Involvement of TIRAP/MAL in signaling for the activation of interferon regulatory factor 3 by lipopolysaccharide.
Essential role for TIRAP in activation of the signalling cascade shared by TLR2 and TLR4.
Toll IL-1 receptors differ in their ability to promote the stabilization of adenosine and uridine-rich elements containing mRNA.
Toll-IL-1 receptor domain-containing adaptor protein is critical for early lung immune responses against Escherichia coli lipopolysaccharide and viable Escherichia coli.
Phosphoinositide-mediated adaptor recruitment controls Toll-like receptor signaling.
Protein kinase Cdelta binds TIRAP/Mal to participate in TLR signaling.
MAPPIT analysis of TLR adaptor complexes.
A Mal functional variant is associated with protection against invasive pneumococcal disease, bacteremia, malaria and tuberculosis.
Distinct roles of TIR and non-TIR regions in the subcellular localization and signaling properties of MyD88.
Requirement of TLR2-mediated signaling for the induction of IL-15 gene expression in human monocytic cells by HSV-1.
A TIR domain variant of MyD88 adapter-like (Mal)/TIRAP results in loss of MyD88 binding and reduced TLR2/TLR4 signaling.
Mal connects TLR2 to PI3Kinase activation and phagocyte polarization.
AIP1 functions as Arf6-GAP to negatively regulate TLR4 signaling.
The hepatitis B e antigen (HBeAg) targets and suppresses activation of the toll-like receptor signaling pathway.
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.
Mapping a dynamic innate immunity protein interaction network regulating type I interferon production.
The Brucella TIR-like protein TcpB interacts with the death domain of MyD88.
Crystal structures of the Toll/Interleukin-1 receptor (TIR) domains from the Brucella protein TcpB and host adaptor TIRAP reveal mechanisms of molecular mimicry.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
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
Activated TLR2/4 interacts with MAL (TIRAP)
TIRAP is phosphorylated by BTK
Dissociation of p-IRAK2:TRAF6 from the activated TLR:oligo-Myd88:TIRAP:p-IRAK4 complex
Activated TLR2/4:TIRAP interacts with BTK
TIRAP binds PIP2-rich regions in the plasma membrane
Defective IRAK4 does not bind MyD88:MAL:BTK:activated TLR2/4
Defective MyD88 does not oligomerize within the activated TLR2/4 complex
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
Falcon deep research report on human TIRAP