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
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
MD-2, a molecule that confers lipopolysaccharide responsiveness on Toll-like receptor 4.
Lipopolysaccharide is in close proximity to each of the proteins in its membrane receptor complex. transfer from CD14 to TLR4 and MD-2.
Secreted MD-2 is a large polymeric protein that efficiently confers lipopolysaccharide sensitivity to Toll-like receptor 4.
Lipoteichoic acid (LTA) of Streptococcus pneumoniae and Staphylococcus aureus activates immune cells via Toll-like receptor (TLR)-2, lipopolysaccharide-binding protein (LBP), and CD14, whereas TLR-4 and MD-2 are not involved.
Separate functional domains of human MD-2 mediate Toll-like receptor 4-binding and lipopolysaccharide responsiveness.
Human TLR10 is a functional receptor, expressed by B cells and plasmacytoid dendritic cells, which activates gene transcription through MyD88.
Crystal structure of the TLR4-MD-2 complex with bound endotoxin antagonist Eritoran.
Allergenicity resulting from functional mimicry of a Toll-like receptor complex protein.
The structural basis of lipopolysaccharide recognition by the TLR4-MD-2 complex.
A critical cysteine is required for HMGB1 binding to Toll-like receptor 4 and activation of macrophage cytokine release.
Morphine activates neuroinflammation in a manner parallel to endotoxin.
Structural basis of species-specific endotoxin sensing by innate immune receptor TLR4/MD-2.
A reference map of the human binary protein interactome.
Structural and functional understanding of the toll-like receptors.
Falcon deep research report on LY96
Transfer of LPS onto TLR4
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
TLR4:LY96:LPS:CD14 recruits TRAM (TICAM2)
TRAM:TLR4:LY96:LPS:CD14 recruits TRIF (TICAM1)
Phosphorylation of IRF-3/IRF7 and their release from the activated TLR complex
IRF3/IRF7 recruitment to p-TBK1/p-IKK epsilon bound to the activated TLR4
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
K63-linked ubiquitination of RIP1 bound to the activated TLR complex
TRIF:activated TLR3/TLR4 complex recruits RIP1
Endocytosis of TLR4:LY96:LPS:CD14
Activated TLR2/4 interacts with MAL (TIRAP)
TIRAP is phosphorylated by BTK
TRAF3 binds TICAM1:activated TLR4 complex
Auto-ubiquitination of TRAF3
Dissociation of p-IRAK2:TRAF6 from the activated TLR:oligo-Myd88:TIRAP:p-IRAK4 complex
Activated TLR2/4:TIRAP interacts with BTK
SARM binds TICAM1:TRAM:TLR4:LY96:LPS:CD14
TLR4-induced ripoptosome assembly
Caspase-8 processing within TLR4 complex
RIP3 binds TRIF to mediate necroptosis
Activated TRAF6 synthesizes unanchored polyubiquitin chains upon TLR stimulation
TANK binds K63-poly-Ub-TRAF3:TICAM1:activated TLR4
TANK is ubiquitinated within TANK:K63polyUb-TRAF3:TRIF:activated TLR4
S100A8:S100A9 binds TLR4:LY96
SFTPA/SFTPD binds TLR4:LY96
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
Cleaved fibrinogen products bind TLR4:LY96
Activated TLR4:TICAM1:K63pUb-TRAF6 recruits TAK1complex
Activation of TAK1 complex bound to activated TLR4 complex
Auto ubiquitination of TRAF6 bound to the activated TLR4 complex
Activated TLR4:TICAM1 recruits TRAF6
IRAK4 autophosphorylation in the complex with activated TLR:MyD88:TIRAP
IKBKG subunit of IKK complex binds polyubiquinated RIP1
Phosphorylation of IRAK2 bound to the activated IRAK4:MyD88 oligomer:TIRAP:activated TLR complex
Phosphorylated TAK1 leaves activated TLR receptor complex
MyD88 oligomerization within the complex of activated TLR:TIRAP:MyD88
Hemes:LY96 activates TLR4
TBK1 is ubiquitinated within TBK1:K63polyUb-TANK:K63polyUb-TRAF3:TRIF:activated TLR4
TBK1 is phosphorylated within the activated TLR4 complex
Recruitment of TBK1 to K63polyUb-TANK:K63polyUb-TRAF3:TRIF:activated TLR4
Recruitment of IKKε (IKBKE) to K63polyUb-TANK:K63polyUb-TRAF3:TRIF:activated TLR4
OPTN binds TBK1 within the activated TLR4 complex
IKKε (IKBKE) is ubiquitinated within the activated TLR4
IKKε (IKBKE) is phosphorylated within the activated TLR4 complex
RSV F binds TLR4:LY96:CD14