Gene Ontology annotation through association of InterPro records with GO terms
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
Structural basis for signal transduction by the Toll/interleukin-1 receptor domains.
The repertoire for pattern recognition of pathogens by the innate immune system is defined by cooperation between toll-like receptors.
IFNs activate toll-like receptor gene expression in viral infections.
Cutting edge: role of Toll-like receptor 1 in mediating immune response to microbial lipoproteins.
Human TLR10 is a functional receptor, expressed by B cells and plasmacytoid dendritic cells, which activates gene transcription through MyD88.
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.
Structural and functional evidence for the role of the TLR2 DD loop in TLR1/TLR2 heterodimerization and signaling.
Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide.
Recognition of lipopeptide patterns by Toll-like receptor 2-Toll-like receptor 6 heterodimer.
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.
Structural and functional understanding of the toll-like receptors.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
A family of human receptors structurally related to Drosophila Toll.
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
TLR1:TLR2 is recruited to ligand:CD14
Beta defensin 103 activates TLR1:TLR2
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
SFTPA/SFTPD binds TLR2:TLR1
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
TLR2:TLR1 binds SARS-CoV-2 E pentamer
Falcon deep research report for human TLR1