NOD-like receptor

Nod-like receptorsNOD-like receptors (NLRs)(NOD)-like receptorNB-LRRNLRNLRsNOD domainNOD Like Receptorsnod-like receptor (NLRs) familyNod-like-receptor
The nucleotide-binding oligomerization domain-like receptors, or NOD-like receptors (NLRs), are intracellular sensors of pathogen-associated molecular patterns (PAMPs) that enter the cell via phagocytosis or pores, and damage-associated molecular patterns (DAMPs) that are associated with cell stress.wikipedia
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Macrophage

macrophagesM2 macrophagesTissue macrophages
They are found in lymphocytes, macrophages, dendritic cells and also in non-immune cells, for example in epithelium.

Dendritic cell

dendritic cellsmyeloid dendritic cellsdendritic
They are found in lymphocytes, macrophages, dendritic cells and also in non-immune cells, for example in epithelium.

Epithelium

epithelialepithelial cellsepithelial cell
They are found in lymphocytes, macrophages, dendritic cells and also in non-immune cells, for example in epithelium.

APAF1

Apaf-1activator proteinAPAF
Their homologs have been discovered in many different animal species (APAF1) and also in the plant kingdom (disease-resistance R protein).

R gene

resistance genesdisease-resistance R proteinplant R proteins
Their homologs have been discovered in many different animal species (APAF1) and also in the plant kingdom (disease-resistance R protein).

NACHT domain

NACHTNACHT protein domain
NLRs contain 3 domains – central NACHT (NOD or NBD – nucleotide-binding domain) domain, which is common to all NLRs, most of NLRs have also C-terminal leucine-rich repeat (LRR) and variable N-terminal interaction domain.

Leucine-rich repeat

leucine-rich repeatsLRRleucine rich repeat
NLRs contain 3 domains – central NACHT (NOD or NBD – nucleotide-binding domain) domain, which is common to all NLRs, most of NLRs have also C-terminal leucine-rich repeat (LRR) and variable N-terminal interaction domain.

CARD domain

CARDcaspase recruitment domainCARD motif
N-terminal domain is responsible for homotypic protein-protein interaction and it can consist of caspase recruitment domain (CARD), pyrin domain (PYD), acidic transactivating domain or baculovirus inhibitor repeats (BIRs).

Inhibitor of apoptosis domain

baculoviral IAP repeatBIRBaculovirus Inhibitor of apoptosis protein Repeat
N-terminal domain is responsible for homotypic protein-protein interaction and it can consist of caspase recruitment domain (CARD), pyrin domain (PYD), acidic transactivating domain or baculovirus inhibitor repeats (BIRs).

HUGO Gene Nomenclature Committee

HGNC(HGNC)HUGO
The nomenclature was unified by the HUGO Gene Nomenclature Committee in 2008.

NAIP (gene)

NAIPneuronal apoptosis-inhibitory proteinneuronal apoptosis inhibitory protein

RIPK2

kinase RIP2RIP2 kinase
The recognition of their ligands recruits oligomerization of NACHT domain and CARD-CARD interaction with CARD-containing serine-threonin kinase RIP2 which leads to activation of RIP2.

IκB kinase

IKKIkappaB kinaseIkB kinase
RIP2 mediates the recruitment of kinase TAK1 which phosphorylates and activates IκB kinase.

NF-κB

NF-kBNF-kappaBNFκB
The activation of IκB kinase results in the phosphorylation of inhibitor IκB which releases NF-κB and its nuclear translocation.

Crohn's disease

Crohn’s diseaseCrohn diseaseCrohn
Mutations in NOD2 are associated with Crohn's disease or Blau syndrome.

Blau syndrome

Edward Blau
Mutations in NOD2 are associated with Crohn's disease or Blau syndrome.

Peptidoglycan

mureinpeptidoglycanspeptidoglycan layer
NOD1 and NOD2 recognize peptidoglycan motifs from bacterial cell which consists of N-acetylglucosamine and N-acetylmuramic acid.

N-Acetylglucosamine

N''-acetylglucosamineGlcNAcN-acetyl-D-glucosamine
NOD1 and NOD2 recognize peptidoglycan motifs from bacterial cell which consists of N-acetylglucosamine and N-acetylmuramic acid.