Type |
Details |
Score |
Publication |
First Author: |
Aviello G |
Year: |
2014 |
Journal: |
Am J Physiol Gastrointest Liver Physiol |
Title: |
MyD88 adaptor-like (Mal) regulates intestinal homeostasis and colitis-associated colorectal cancer in mice. |
Volume: |
306 |
Issue: |
9 |
Pages: |
G769-78 |
|
•
•
•
•
•
|
Publication |
First Author: |
Strickson S |
Year: |
2017 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
Roles of the TRAF6 and Pellino E3 ligases in MyD88 and RANKL signaling. |
Volume: |
114 |
Issue: |
17 |
Pages: |
E3481-E3489 |
|
•
•
•
•
•
|
Publication |
First Author: |
Kenny EF |
Year: |
2009 |
Journal: |
J Immunol |
Title: |
MyD88 adaptor-like is not essential for TLR2 signaling and inhibits signaling by TLR3. |
Volume: |
183 |
Issue: |
6 |
Pages: |
3642-51 |
|
•
•
•
•
•
|
Publication |
First Author: |
Xie L |
Year: |
2016 |
Journal: |
J Natl Cancer Inst |
Title: |
Targeting of MyD88 Homodimerization by Novel Synthetic Inhibitor TJ-M2010-5 in Preventing Colitis-Associated Colorectal Cancer. |
Volume: |
108 |
Issue: |
4 |
|
|
•
•
•
•
•
|
Publication |
First Author: |
Bosschaerts T |
Year: |
2010 |
Journal: |
PLoS Pathog |
Title: |
Tip-DC development during parasitic infection is regulated by IL-10 and requires CCL2/CCR2, IFN-gamma and MyD88 signaling. |
Volume: |
6 |
Issue: |
8 |
Pages: |
e1001045 |
|
•
•
•
•
•
|
Publication |
First Author: |
Corr SC |
Year: |
2014 |
Journal: |
Mucosal Immunol |
Title: |
MyD88 adaptor-like (Mal) functions in the epithelial barrier and contributes to intestinal integrity via protein kinase C. |
Volume: |
7 |
Issue: |
1 |
Pages: |
57-67 |
|
•
•
•
•
•
|
Interaction Experiment |
Description: |
MyD88 and Trif target Beclin 1 to trigger autophagy in macrophages. |
|
•
•
•
•
•
|
Interaction Experiment |
Description: |
SPOP promotes ubiquitination and degradation of MyD88 to suppress the innate immune response. |
|
•
•
•
•
•
|
Publication |
First Author: |
Popovic ZV |
Year: |
2011 |
Journal: |
J Immunol |
Title: |
The proteoglycan biglycan enhances antigen-specific T cell activation potentially via MyD88 and TRIF pathways and triggers autoimmune perimyocarditis. |
Volume: |
187 |
Issue: |
12 |
Pages: |
6217-26 |
|
•
•
•
•
•
|
Publication |
First Author: |
Semaan N |
Year: |
2008 |
Journal: |
J Immunol |
Title: |
Etk/BMX, a Btk family tyrosine kinase, and Mal contribute to the cross-talk between MyD88 and FAK pathways. |
Volume: |
180 |
Issue: |
5 |
Pages: |
3485-91 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
241
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Guillamot M |
Year: |
2019 |
Journal: |
Nat Immunol |
Title: |
The E3 ubiquitin ligase SPOP controls resolution of systemic inflammation by triggering MYD88 degradation. |
Volume: |
20 |
Issue: |
9 |
Pages: |
1196-1207 |
|
•
•
•
•
•
|
Publication |
First Author: |
Lopez Kostka S |
Year: |
2022 |
Journal: |
J Invest Dermatol |
Title: |
Exclusive Expression of MyD88 on Dendritic Cells Is Sufficient to Induce Protection against Experimental Leishmaniasis. |
Volume: |
142 |
Issue: |
4 |
Pages: |
1230-1233 |
|
•
•
•
•
•
|
Publication |
First Author: |
Janssens S |
Year: |
2002 |
Journal: |
Trends Biochem Sci |
Title: |
A universal role for MyD88 in TLR/IL-1R-mediated signaling. |
Volume: |
27 |
Issue: |
9 |
Pages: |
474-82 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
119
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Zhao Y |
Year: |
2018 |
Journal: |
Mol Cell |
Title: |
OTUD4 Is a Phospho-Activated K63 Deubiquitinase that Regulates MyD88-Dependent Signaling. |
Volume: |
69 |
Issue: |
3 |
Pages: |
505-516.e5 |
|
•
•
•
•
•
|
Pathway |
|
•
•
•
•
•
|
Pathway |
|
•
•
•
•
•
|
Interaction Experiment |
Description: |
Integrin CD11b negatively regulates TLR-triggered inflammatory responses by activating Syk and promoting degradation of MyD88 and TRIF via Cbl-b. |
|
•
•
•
•
•
|
Publication |
First Author: |
Lysakova-Devine T |
Year: |
2010 |
Journal: |
J Immunol |
Title: |
Viral inhibitory peptide of TLR4, a peptide derived from vaccinia protein A46, specifically inhibits TLR4 by directly targeting MyD88 adaptor-like and TRIF-related adaptor molecule. |
Volume: |
185 |
Issue: |
7 |
Pages: |
4261-71 |
|
•
•
•
•
•
|
Publication |
First Author: |
Gravina HD |
Year: |
2016 |
Journal: |
J Biol Chem |
Title: |
MyD88 Adapter-like (Mal)/TIRAP Is Required for Cytokine Production by Splenic Ly6CloTLR2hi but Not by Ly6ChiTLR2hi Monocytes during Trypanosoma cruzi Infection. |
Volume: |
291 |
Issue: |
45 |
Pages: |
23832-23841 |
|
•
•
•
•
•
|
GO Term |
|
•
•
•
•
•
|
GO Term |
|
•
•
•
•
•
|
Publication |
First Author: |
Janssens S |
Year: |
2002 |
Journal: |
Curr Biol |
Title: |
Regulation of interleukin-1- and lipopolysaccharide-induced NF-kappaB activation by alternative splicing of MyD88. |
Volume: |
12 |
Issue: |
6 |
Pages: |
467-71 |
|
•
•
•
•
•
|
HT Experiment |
Series Id: |
GSE17438 |
Experiment Type: |
transcription profiling by array |
Study Type: |
WT vs. Mutant |
Source: |
ArrayExpress |
|
•
•
•
•
•
|
Publication |
First Author: |
Yu X |
Year: |
2018 |
Journal: |
Cancer Res |
Title: |
MYD88 L265P Mutation in Lymphoid Malignancies. |
Volume: |
78 |
Issue: |
10 |
Pages: |
2457-2462 |
|
•
•
•
•
•
|
Publication |
First Author: |
Muzio M |
Year: |
1997 |
Journal: |
Science |
Title: |
IRAK (Pelle) family member IRAK-2 and MyD88 as proximal mediators of IL-1 signaling. |
Volume: |
278 |
Issue: |
5343 |
Pages: |
1612-5 |
|
•
•
•
•
•
|
Allele |
Name: |
myeloid differentiation primary response gene 88; endonuclease-mediated mutation 2, Shanghai Model Organisms Center |
Allele Type: |
Endonuclease-mediated |
Attribute String: |
Null/knockout |
|
•
•
•
•
•
|
Publication |
First Author: |
Shi CS |
Year: |
2008 |
Journal: |
J Biol Chem |
Title: |
MyD88 and Trif target Beclin 1 to trigger autophagy in macrophages. |
Volume: |
283 |
Issue: |
48 |
Pages: |
33175-82 |
|
•
•
•
•
•
|
Publication |
First Author: |
Li Q |
Year: |
2020 |
Journal: |
PLoS Pathog |
Title: |
SPOP promotes ubiquitination and degradation of MyD88 to suppress the innate immune response. |
Volume: |
16 |
Issue: |
5 |
Pages: |
e1008188 |
|
•
•
•
•
•
|
GO Term |
|
•
•
•
•
•
|
GO Term |
|
•
•
•
•
•
|
GO Term |
|
•
•
•
•
•
|
Allele |
Name: |
myeloid differentiation primary response gene 88; endonuclease-mediated mutation 1, Shanghai Model Organisms Center |
Allele Type: |
Endonuclease-mediated |
Attribute String: |
Conditional ready, No functional change |
|
•
•
•
•
•
|
Strain |
Attribute String: |
coisogenic, mutant strain, endonuclease-mediated mutation |
|
•
•
•
•
•
|
DO Term |
|
•
•
•
•
•
|
Publication |
First Author: |
Loiarro M |
Year: |
2007 |
Journal: |
J Leukoc Biol |
Title: |
Pivotal Advance: Inhibition of MyD88 dimerization and recruitment of IRAK1 and IRAK4 by a novel peptidomimetic compound. |
Volume: |
82 |
Issue: |
4 |
Pages: |
801-10 |
|
•
•
•
•
•
|
GO Term |
|
•
•
•
•
•
|
Ontology Term |
|
•
•
•
•
•
|
Publication |
First Author: |
Choi KC |
Year: |
2006 |
Journal: |
Nat Immunol |
Title: |
Smad6 negatively regulates interleukin 1-receptor-Toll-like receptor signaling through direct interaction with the adaptor Pellino-1. |
Volume: |
7 |
Issue: |
10 |
Pages: |
1057-65 |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Allele |
Name: |
transgene insertion 1, Lora Hooper |
Allele Type: |
Transgenic |
Attribute String: |
Inserted expressed sequence |
|
•
•
•
•
•
|
Strain |
Attribute String: |
coisogenic, endonuclease-mediated mutation, mutant strain |
|
•
•
•
•
•
|
Publication |
First Author: |
Pauls E |
Year: |
2013 |
Journal: |
J Immunol |
Title: |
Two phases of inflammatory mediator production defined by the study of IRAK2 and IRAK1 knock-in mice. |
Volume: |
191 |
Issue: |
5 |
Pages: |
2717-30 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
622
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Allele |
Name: |
myeloid differentiation primary response gene 88; targeted mutation 1, Anthony L DeFranco |
Allele Type: |
Targeted |
Attribute String: |
Conditional ready, No functional change |
|
•
•
•
•
•
|
Strain |
Attribute String: |
coisogenic, mutant strain, transgenic |
|
•
•
•
•
•
|
Publication |
First Author: |
Gantier MP |
Year: |
2008 |
Journal: |
J Immunol |
Title: |
TLR7 is involved in sequence-specific sensing of single-stranded RNAs in human macrophages. |
Volume: |
180 |
Issue: |
4 |
Pages: |
2117-24 |
|
•
•
•
•
•
|
Publication |
First Author: |
Alexopoulou L |
Year: |
2002 |
Journal: |
Nat Med |
Title: |
Hyporesponsiveness to vaccination with Borrelia burgdorferi OspA in humans and in TLR1- and TLR2-deficient mice. |
Volume: |
8 |
Issue: |
8 |
Pages: |
878-84 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
Toll-like receptor 7 (TLR7) is a key component of innate and adaptive immunity. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. TLR7 is a nucleotide-sensing TLR, which is activated by single-stranded RNA, acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response [, ]. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
Toll-like receptor 1 (TLR1) participates in the innate immune response to microbial agents. TLR1 cooperates with TLR2 to mediate the innate immune response to bacterial lipoproteins or lipopeptides [, ]. It acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Strain |
Attribute String: |
major histocompatibility congenic, congenic, mutant strain, spontaneous mutation, targeted mutation |
|
•
•
•
•
•
|
Strain |
Attribute String: |
targeted mutation, mutant strain, congenic |
|
•
•
•
•
•
|
Strain |
Attribute String: |
targeted mutation, mutant strain, congenic |
|
•
•
•
•
•
|
Strain |
Attribute String: |
congenic, targeted mutation |
|
•
•
•
•
•
|
Genotype |
Symbol: |
Myd88/Myd88 |
Background: |
B6.129P2(SJL)-Myd88/J |
Zygosity: |
hm |
Has Mutant Allele: |
true |
|
•
•
•
•
•
|
Publication |
First Author: |
Takeuchi O |
Year: |
2002 |
Journal: |
J Immunol |
Title: |
Cutting edge: role of Toll-like receptor 1 in mediating immune response to microbial lipoproteins. |
Volume: |
169 |
Issue: |
1 |
Pages: |
10-4 |
|
•
•
•
•
•
|
Publication |
First Author: |
Ferrao R |
Year: |
2012 |
Journal: |
Curr Opin Struct Biol |
Title: |
Helical assembly in the death domain (DD) superfamily. |
Volume: |
22 |
Issue: |
2 |
Pages: |
241-7 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
This entry represents the Death Domain (DD) of Myeloid Differentiation primary response protein 88 (MyD88). MyD88 is an adaptor protein involved in interleukin-1 receptor (IL-1R)- and Toll-like receptor (TLR)-induced activation of nuclear factor-kappaB (NF-kB) and mitogen activated protein kinase pathways that lead to the induction of proinflammatory cytokines []. It is a key component in the signaling pathway of pathogen recognition in the innate immune system. MyD88 contains an N-terminal DD and a C-terminal Toll/IL-1 Receptor (TIR) homology domain that mediates interaction with TLRs and IL-1R [].In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN []. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes []. |
|
•
•
•
•
•
|
Publication |
First Author: |
Bauer S |
Year: |
2001 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
Human TLR9 confers responsiveness to bacterial DNA via species-specific CpG motif recognition. |
Volume: |
98 |
Issue: |
16 |
Pages: |
9237-42 |
|
•
•
•
•
•
|
Publication |
First Author: |
Chuang TH |
Year: |
2002 |
Journal: |
J Leukoc Biol |
Title: |
Toll-like receptor 9 mediates CpG-DNA signaling. |
Volume: |
71 |
Issue: |
3 |
Pages: |
538-44 |
|
•
•
•
•
•
|
Publication |
First Author: |
Anderson AE |
Year: |
2007 |
Journal: |
Eur J Immunol |
Title: |
TLR9 polymorphisms determine murine lymphocyte responses to Helicobacter: results from a genome-wide scan. |
Volume: |
37 |
Issue: |
6 |
Pages: |
1548-61 |
|
•
•
•
•
•
|
Publication |
First Author: |
Takeshita F |
Year: |
2001 |
Journal: |
J Immunol |
Title: |
Cutting edge: Role of Toll-like receptor 9 in CpG DNA-induced activation of human cells. |
Volume: |
167 |
Issue: |
7 |
Pages: |
3555-8 |
|
•
•
•
•
•
|
Publication |
First Author: |
Huang X |
Year: |
2010 |
Journal: |
Expert Opin Ther Targets |
Title: |
Targeting the TLR9-MyD88 pathway in the regulation of adaptive immune responses. |
Volume: |
14 |
Issue: |
8 |
Pages: |
787-96 |
|
•
•
•
•
•
|
Publication |
First Author: |
Nyman T |
Year: |
2008 |
Journal: |
J Biol Chem |
Title: |
The crystal structure of the human toll-like receptor 10 cytoplasmic domain reveals a putative signaling dimer. |
Volume: |
283 |
Issue: |
18 |
Pages: |
11861-5 |
|
•
•
•
•
•
|
Publication |
First Author: |
Hasan U |
Year: |
2005 |
Journal: |
J Immunol |
Title: |
Human TLR10 is a functional receptor, expressed by B cells and plasmacytoid dendritic cells, which activates gene transcription through MyD88. |
Volume: |
174 |
Issue: |
5 |
Pages: |
2942-50 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
Toll-like receptor 10 (TLR10) participates in the innate immune response to microbial agents. The human TLR family consist of numerous members, which recognise a wide variety of pathogen-associated molecular patterns. No ligand has yet been reported for TLR10, thus it remains the only orphanfamily member []. It acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. TLR10 has been shown to form homodimers and to interact with TLRs 1 and 2 []. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
Toll-like receptor 9 (TLR9) is a key component of innate and adaptive immunity [, ]. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. TLR9 is activated by unmethylated cytidine-phosphate-guanosine (CpG) dinucleotides, which is more abundant in bacterial genomes or viral DNA compared to the vertebrate genomes [, , , ]. It acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. TLR9 controls lymphocyte response to Helicobacter infection []. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
Interleukin-1 receptor-associated kinase-like 2 (IRAK2) is a critical mediator of TLR/IL1-R signalling [, ]. It is required for production of pro-inflammatory cytokines [, ].All IRAKs are multidomain proteins, consisting of a conserved N-terminal death domain (DD) and a central kinase domain (KD). The DD is a protein interaction motif implicated in binding to the adaptor protein MyD88 []. IRAK2 lacks an active kinase domain, as a critical residue in the kinase domain has changed []. |
|
•
•
•
•
•
|
HT Experiment |
Series Id: |
GSE17344 |
Experiment Type: |
transcription profiling by array |
Study Type: |
WT vs. Mutant |
Source: |
ArrayExpress |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
435
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
457
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1493
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
445
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
419
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Govindaraj RG |
Year: |
2011 |
Journal: |
PLoS One |
Title: |
Comparative analysis of species-specific ligand recognition in Toll-like receptor 8 signaling: a hypothesis. |
Volume: |
6 |
Issue: |
9 |
Pages: |
e25118 |
|
•
•
•
•
•
|
Publication |
First Author: |
Peng G |
Year: |
2005 |
Journal: |
Science |
Title: |
Toll-like receptor 8-mediated reversal of CD4+ regulatory T cell function. |
Volume: |
309 |
Issue: |
5739 |
Pages: |
1380-4 |
|
•
•
•
•
•
|
Publication |
First Author: |
Jurk M |
Year: |
2002 |
Journal: |
Nat Immunol |
Title: |
Human TLR7 or TLR8 independently confer responsiveness to the antiviral compound R-848. |
Volume: |
3 |
Issue: |
6 |
Pages: |
499 |
|
•
•
•
•
•
|
Publication |
First Author: |
Melchjorsen J |
Year: |
2005 |
Journal: |
J Virol |
Title: |
Activation of innate defense against a paramyxovirus is mediated by RIG-I and TLR7 and TLR8 in a cell-type-specific manner. |
Volume: |
79 |
Issue: |
20 |
Pages: |
12944-51 |
|
•
•
•
•
•
|
Publication |
First Author: |
Droemann D |
Year: |
2003 |
Journal: |
Histochem Cell Biol |
Title: |
Toll-like receptor 2 is expressed by alveolar epithelial cells type II and macrophages in the human lung. |
Volume: |
119 |
Issue: |
2 |
Pages: |
103-8 |
|
•
•
•
•
•
|
Publication |
First Author: |
Sheedy FJ |
Year: |
2007 |
Journal: |
J Leukoc Biol |
Title: |
The Troll in Toll: Mal and Tram as bridges for TLR2 and TLR4 signaling. |
Volume: |
82 |
Issue: |
2 |
Pages: |
196-203 |
|
•
•
•
•
•
|
Publication |
First Author: |
Bochud PY |
Year: |
2008 |
Journal: |
J Infect Dis |
Title: |
Toll-like receptor 2 (TLR2) polymorphisms are associated with reversal reaction in leprosy. |
Volume: |
197 |
Issue: |
2 |
Pages: |
253-61 |
|
•
•
•
•
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Publication |
First Author: |
Aliprantis AO |
Year: |
1999 |
Journal: |
Science |
Title: |
Cell activation and apoptosis by bacterial lipoproteins through toll-like receptor-2. |
Volume: |
285 |
Issue: |
5428 |
Pages: |
736-9 |
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Publication |
First Author: |
Takeuchi O |
Year: |
2001 |
Journal: |
Int Immunol |
Title: |
Discrimination of bacterial lipoproteins by Toll-like receptor 6. |
Volume: |
13 |
Issue: |
7 |
Pages: |
933-40 |
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Publication |
First Author: |
Bochud PY |
Year: |
2003 |
Journal: |
J Immunol |
Title: |
Cutting edge: a Toll-like receptor 2 polymorphism that is associated with lepromatous leprosy is unable to mediate mycobacterial signaling. |
Volume: |
170 |
Issue: |
7 |
Pages: |
3451-4 |
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Publication |
First Author: |
Schröder NW |
Year: |
2003 |
Journal: |
J Biol Chem |
Title: |
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. |
Volume: |
278 |
Issue: |
18 |
Pages: |
15587-94 |
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Publication |
First Author: |
Kirschning CJ |
Year: |
2001 |
Journal: |
Int J Med Microbiol |
Title: |
Toll-like receptors: cellular signal transducers for exogenous molecular patterns causing immune responses. |
Volume: |
291 |
Issue: |
4 |
Pages: |
251-60 |
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Publication |
First Author: |
Bulut Y |
Year: |
2001 |
Journal: |
J Immunol |
Title: |
Cooperation of Toll-like receptor 2 and 6 for cellular activation by soluble tuberculosis factor and Borrelia burgdorferi outer surface protein A lipoprotein: role of Toll-interacting protein and IL-1 receptor signaling molecules in Toll-like receptor 2 signaling. |
Volume: |
167 |
Issue: |
2 |
Pages: |
987-94 |
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Publication |
First Author: |
Takeda K |
Year: |
2002 |
Journal: |
J Endotoxin Res |
Title: |
Recognition of lipopeptides by Toll-like receptors. |
Volume: |
8 |
Issue: |
6 |
Pages: |
459-63 |
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Protein Domain |
Type: |
Family |
Description: |
Toll-like receptor 6 (TLR6) participates in the innate immune response to Gram-positive bacteria and fungi. TLRs recognize specific molecular patterns present only in micro-organisms. TLR1 and TLR6 are involved in the discrimination of a subtle difference between triacyl and diacyl lipopeptides through interaction with TLR2 []. Cooperatively with TLR2, TLR6 recognises mycoplasmal macrophage-activating lipopeptide-2 (MALP-2), soluble tuberculosis factor (STF), phenol-soluble modulin (PSM) and Borrelia burgdorferi outer surface protein A lipoprotein (OspA-L) []. TLR6 acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response []. |
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Protein Domain |
Type: |
Family |
Description: |
Toll-like receptor 2 (TLR2) is a member of the Toll-like receptor (TLR) family, which plays a role in activation of innate immunity and pathogen recognition []. It helps mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components, acting via MyD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response [, , , ]. TLR2 in association with TLR1 or TLR6 is essential for recognising bacterial lipoproteins and lipopeptides [, ]. It also promotes apoptosis in response to lipoproteins [].Genetic variations in TLR2 are associated with susceptibility to leprosy, a chronic disease associated with depressed cellular (but not humoral) immunity [, ]. |
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Protein Domain |
Type: |
Family |
Description: |
Toll-like receptor 8 (TLR8) is a key component of innate and adaptive immunity [, , ]. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. It acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response []. TLR8 has been shown to recognise different types of ligands such as viral or bacterial ssRNA, as well as small synthetic molecules. Activation by ligands is species-specific, varying among non-rodents and rodents [, ]. |
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