Type |
Details |
Score |
Publication |
First Author: |
Koymans KJ |
Year: |
2015 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
Structural basis for inhibition of TLR2 by staphylococcal superantigen-like protein 3 (SSL3). |
Volume: |
112 |
Issue: |
35 |
Pages: |
11018-23 |
|
•
•
•
•
•
|
Publication |
First Author: |
Jeyaseelan S |
Year: |
2006 |
Journal: |
J Immunol |
Title: |
Toll/IL-1R domain-containing adaptor protein (TIRAP) is a critical mediator of antibacterial defense in the lung against Klebsiella pneumoniae but not Pseudomonas aeruginosa. |
Volume: |
177 |
Issue: |
1 |
Pages: |
538-47 |
|
•
•
•
•
•
|
Publication |
First Author: |
Hope C |
Year: |
2014 |
Journal: |
Blood |
Title: |
TPL2 kinase regulates the inflammatory milieu of the myeloma niche. |
Volume: |
123 |
Issue: |
21 |
Pages: |
3305-15 |
|
•
•
•
•
•
|
Publication |
First Author: |
Zahoor A |
Year: |
2020 |
Journal: |
J Cell Physiol |
Title: |
Gas6 negatively regulates the Staphylococcus aureus-induced inflammatory response via TLR signaling in the mouse mammary gland. |
Volume: |
235 |
Issue: |
10 |
Pages: |
7081-7093 |
|
•
•
•
•
•
|
Publication |
First Author: |
Jang YH |
Year: |
2017 |
Journal: |
J Invest Dermatol |
Title: |
House Dust Mite Increases pro-Th2 Cytokines IL-25 and IL-33 via the Activation of TLR1/6 Signaling. |
Volume: |
137 |
Issue: |
11 |
Pages: |
2354-2361 |
|
•
•
•
•
•
|
Publication |
First Author: |
Huh JW |
Year: |
2014 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
UNC93B1 is essential for the plasma membrane localization and signaling of Toll-like receptor 5. |
Volume: |
111 |
Issue: |
19 |
Pages: |
7072-7 |
|
•
•
•
•
•
|
Publication |
First Author: |
McCurdy JD |
Year: |
2001 |
Journal: |
J Leukoc Biol |
Title: |
Toll-like receptor 4-mediated activation of murine mast cells. |
Volume: |
70 |
Issue: |
6 |
Pages: |
977-84 |
|
•
•
•
•
•
|
Publication |
First Author: |
Rousseau S |
Year: |
2008 |
Journal: |
J Cell Sci |
Title: |
TPL2-mediated activation of ERK1 and ERK2 regulates the processing of pre-TNF alpha in LPS-stimulated macrophages. |
Volume: |
121 |
Issue: |
Pt 2 |
Pages: |
149-54 |
|
•
•
•
•
•
|
Publication |
First Author: |
Mayer AK |
Year: |
2007 |
Journal: |
J Immunol |
Title: |
Differential recognition of TLR-dependent microbial ligands in human bronchial epithelial cells. |
Volume: |
178 |
Issue: |
5 |
Pages: |
3134-42 |
|
•
•
•
•
•
|
Publication |
First Author: |
Satta N |
Year: |
2007 |
Journal: |
Blood |
Title: |
The role of TLR2 in the inflammatory activation of mouse fibroblasts by human antiphospholipid antibodies. |
Volume: |
109 |
Issue: |
4 |
Pages: |
1507-14 |
|
•
•
•
•
•
|
Publication |
First Author: |
Pore D |
Year: |
2010 |
Journal: |
Mol Immunol |
Title: |
34 kDa MOMP of Shigella flexneri promotes TLR2 mediated macrophage activation with the engagement of NF-kappaB and p38 MAP kinase signaling. |
Volume: |
47 |
Issue: |
9 |
Pages: |
1739-46 |
|
•
•
•
•
•
|
Publication |
First Author: |
Schroder K |
Year: |
2012 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
Conservation and divergence in Toll-like receptor 4-regulated gene expression in primary human versus mouse macrophages. |
Volume: |
109 |
Issue: |
16 |
Pages: |
E944-53 |
|
•
•
•
•
•
|
Publication |
First Author: |
Rose JA |
Year: |
2011 |
Journal: |
Am J Reprod Immunol |
Title: |
Peptidoglycan induces necrosis and regulates cytokine production in murine trophoblast stem cells. |
Volume: |
66 |
Issue: |
3 |
Pages: |
209-22 |
|
•
•
•
•
•
|
Publication |
First Author: |
Westwell-Roper C |
Year: |
2016 |
Journal: |
J Biol Chem |
Title: |
Differential Activation of Innate Immune Pathways by Distinct Islet Amyloid Polypeptide (IAPP) Aggregates. |
Volume: |
291 |
Issue: |
17 |
Pages: |
8908-17 |
|
•
•
•
•
•
|
Publication |
First Author: |
Khan S |
Year: |
2021 |
Journal: |
Elife |
Title: |
SARS-CoV-2 spike protein induces inflammation via TLR2-dependent activation of the NF-κB pathway. |
Volume: |
10 |
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Brightbill HD |
Year: |
1999 |
Journal: |
Science |
Title: |
Host defense mechanisms triggered by microbial lipoproteins through toll-like receptors. |
Volume: |
285 |
Issue: |
5428 |
Pages: |
732-6 |
|
•
•
•
•
•
|
Publication |
First Author: |
Mattos KA |
Year: |
2011 |
Journal: |
J Immunol |
Title: |
TLR6-driven lipid droplets in Mycobacterium leprae-infected Schwann cells: immunoinflammatory platforms associated with bacterial persistence. |
Volume: |
187 |
Issue: |
5 |
Pages: |
2548-58 |
|
•
•
•
•
•
|
Publication |
First Author: |
Zahoor A |
Year: |
2020 |
Journal: |
Immunobiology |
Title: |
MerTK negatively regulates Staphylococcus aureus induced inflammatory response via SOCS1/SOCS3 and Mal. |
Volume: |
225 |
Issue: |
4 |
Pages: |
151960 |
|
•
•
•
•
•
|
Publication |
First Author: |
Wang J |
Year: |
2006 |
Journal: |
J Biol Chem |
Title: |
The functional effects of physical interactions among Toll-like receptors 7, 8, and 9. |
Volume: |
281 |
Issue: |
49 |
Pages: |
37427-34 |
|
•
•
•
•
•
|
Publication |
First Author: |
Banerjee P |
Year: |
2008 |
Journal: |
Int Immunol |
Title: |
Porin-incorporated liposome induces Toll-like receptors 2- and 6-dependent maturation and type 1 response of dendritic cell. |
Volume: |
20 |
Issue: |
12 |
Pages: |
1551-63 |
|
•
•
•
•
•
|
Publication |
First Author: |
O'Neill LA |
Year: |
2007 |
Journal: |
Nat Rev Immunol |
Title: |
The family of five: TIR-domain-containing adaptors in Toll-like receptor signalling. |
Volume: |
7 |
Issue: |
5 |
Pages: |
353-64 |
|
•
•
•
•
•
|
Publication |
First Author: |
Leulier F |
Year: |
2008 |
Journal: |
Nat Rev Genet |
Title: |
Toll-like receptors--taking an evolutionary approach. |
Volume: |
9 |
Issue: |
3 |
Pages: |
165-78 |
|
•
•
•
•
•
|
Publication |
First Author: |
West AP |
Year: |
2006 |
Journal: |
Annu Rev Cell Dev Biol |
Title: |
Recognition and signaling by toll-like receptors. |
Volume: |
22 |
|
Pages: |
409-37 |
|
•
•
•
•
•
|
Publication |
First Author: |
Medzhitov R |
Year: |
1997 |
Journal: |
Curr Opin Immunol |
Title: |
Innate immunity: impact on the adaptive immune response. |
Volume: |
9 |
Issue: |
1 |
Pages: |
4-9 |
|
•
•
•
•
•
|
Publication |
First Author: |
Kaisho T |
Year: |
2006 |
Journal: |
J Allergy Clin Immunol |
Title: |
Toll-like receptor function and signaling. |
Volume: |
117 |
Issue: |
5 |
Pages: |
979-87; quiz 988 |
|
•
•
•
•
•
|
Publication |
First Author: |
Moresco EM |
Year: |
2011 |
Journal: |
Curr Biol |
Title: |
Toll-like receptors. |
Volume: |
21 |
Issue: |
13 |
Pages: |
R488-93 |
|
•
•
•
•
•
|
Publication |
First Author: |
Hashimoto C |
Year: |
1988 |
Journal: |
Cell |
Title: |
The Toll gene of Drosophila, required for dorsal-ventral embryonic polarity, appears to encode a transmembrane protein. |
Volume: |
52 |
Issue: |
2 |
Pages: |
269-79 |
|
•
•
•
•
•
|
Publication |
First Author: |
Keith FJ |
Year: |
1990 |
Journal: |
EMBO J |
Title: |
The Drosophila membrane receptor Toll can function to promote cellular adhesion. |
Volume: |
9 |
Issue: |
13 |
Pages: |
4299-306 |
|
•
•
•
•
•
|
Publication |
First Author: |
Lemaitre B |
Year: |
1996 |
Journal: |
Cell |
Title: |
The dorsoventral regulatory gene cassette spätzle/Toll/cactus controls the potent antifungal response in Drosophila adults. |
Volume: |
86 |
Issue: |
6 |
Pages: |
973-83 |
|
•
•
•
•
•
|
Publication |
First Author: |
Weber AN |
Year: |
2003 |
Journal: |
Nat Immunol |
Title: |
Binding of the Drosophila cytokine Spätzle to Toll is direct and establishes signaling. |
Volume: |
4 |
Issue: |
8 |
Pages: |
794-800 |
|
•
•
•
•
•
|
Publication |
First Author: |
Beutler B |
Year: |
2001 |
Journal: |
Nat Immunol |
Title: |
Toll we meet again.... |
Volume: |
2 |
Issue: |
1 |
Pages: |
9-10 |
|
•
•
•
•
•
|
Publication |
First Author: |
Underhill D |
Year: |
2003 |
Journal: |
Nat Immunol |
Title: |
Toll gets tied in a knot. |
Volume: |
4 |
Issue: |
8 |
Pages: |
723-4 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
This entry represents toll-like receptors (TLRs), which are key regulators of immune responses. They recognise pathogen-associated molecular patterns (PAMPs) such as bacterial lipopeptides (TLR1/2/6), bacterial flagellin (TLR5), and lipopolysaccharide (TLR4) []. In highervertebrates, TLRs are essential not only for sensing microbes by the innate immune system, but also for inducing adaptive immune system responses mediated by B and T cells [].TLRs are expressed at the cell membrane and in subcellular compartments such as the endosome. TLRs are type-I transmembrane proteins with extracellular leucine-rich repeat (LRR) motifs and an intracellular Toll/interleukin-1 receptor (TIR) domain. Members of the TLR family contribute both to cell-cell interactions and to signalling, linking extracellular signals to specific gene-expression programmes [, ]. Binding of ligands to the extracellular domains causes rearrangement of the receptor complexes and triggers the recruitment of specific adaptor proteins to the intracellular TIR domain, leading to nuclear factor-kappa B (NF-kappaB) activation and initiation of both innate and adaptive immune responses. Signalling by TLRs involves five adaptor proteins known as MyD88, MAL, TRIF, TRAM and SARM []. TLRs form homodimers or heterodimers induced by the binding of ligands to residues in the LRRs of distinct receptor chains. In mice and humans combined there are 13 paralogous TLRs; 10 in humans and 12 in mice. TLR10 is only present in humans, and TLR11-13 are only present in mice []. This entry represents some toll-like receptors, which includes TLR1, TLR2, TLR4, TLR5, TLR6 and TLR10.In Drosophila, the Toll receptor plays a role in development as well as immunity [, ]. Toll is a component of the extracellular signaling pathway that establishes the dorsal-ventral pathway of the embryo []. Three proteases; ndl, gd and snk process easter to create active easter. Active easter defines cell identities along the dorsal-ventral continuum by activating the Spz ligand for the Tl receptor in the ventral region of the embryo []. Toll promotes heterophilic cellular adhesion []. The Drosophila Toll receptor is essential in initiating innate immune defenses to fungi and Gram-positive bacteria in adult flies []. Spz C-106 in the hemolymph controls expression of the antifungal peptide Drosomycin (Drs) by acting as a ligand of Tl and inducing an intracellular signaling pathway []. |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
86
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
105
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
154
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
784
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
784
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
784
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
784
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
661
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
661
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
180
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
991
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
905
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
926
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
795
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
835
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
906
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
859
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
749
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
748
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
749
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
748
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
749
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
749
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
748
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
748
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
748
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
748
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
748
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
748
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
748
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
859
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
835
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
749
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
748
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
905
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
748
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
749
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
873
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
905
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
835
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
748
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
748
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
748
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
749
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
926
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
727
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
835
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
835
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
853
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
931
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
906
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
748
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
748
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
604
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
748
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
795
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
748
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
749
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
859
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
748
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
748
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
748
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
748
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
748
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
748
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
748
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
748
 |
Fragment?: |
true |
|
•
•
•
•
•
|