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
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
TLR6: A novel member of an expanding toll-like receptor family.
Host defense mechanisms triggered by microbial lipoproteins through toll-like receptors.
Discrimination of bacterial lipoproteins by Toll-like receptor 6.
Cutting edge: role of Toll-like receptor 1 in mediating immune response to microbial lipoproteins.
Membrane sorting of toll-like receptor (TLR)-2/6 and TLR2/1 heterodimers at the cell surface determines heterotypic associations with CD36 and intracellular targeting.
Recognition of lipopeptide patterns by Toll-like receptor 2-Toll-like receptor 6 heterodimer.
CD36 ligands promote sterile inflammation through assembly of a Toll-like receptor 4 and 6 heterodimer.
Increased toll-like receptor (TLR) activation and TLR ligands in recently diagnosed type 2 diabetic subjects.
Identification of Drosophila Yin and PEPT2 as evolutionarily conserved phagosome-associated muramyl dipeptide transporters.
TLR2 is a primary receptor for Alzheimer's amyloid β peptide to trigger neuroinflammatory activation.
Isolated Toll-like receptor transmembrane domains are capable of oligomerization.
Divergent roles of amino acid residues inside and outside the BB loop affect human Toll-like receptor (TLR)2/2, TLR2/1 and TLR2/6 responsiveness.
Crystal structure of TIR domain of TLR6 reveals novel dimeric interface of TIR-TIR interaction for toll-like receptor signaling pathway.
Structural and functional understanding of the toll-like receptors.
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
TLR6:TLR2 is recruited to ligand:CD14:CD36
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
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
oxLDL:CD36 binds TLR4:TLR6
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
CD36 coordinates NLRP3 inflammasome activation by facilitating intracellular nucleation of soluble ligands into particulate ligands in sterile inflammation.