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NOD1/2 gene variants are not linked with T2DM and IR.
findings show that NOD1, a PRR (show PVRL1 Proteins) that normally senses bacterial peptidoglycans, is activated by HCV viral polymerase, probably through an interaction with dsRNA, suggesting that NOD1 acts as an RNA ligand recognition receptor.
Brain pericytes can sense Gram-negative bacterial products by both NOD1 and TLR4 (show TLR4 Proteins) receptors, acting through distinct pathways.
NOD1 And NOD2 polymorphisms were associated with increased susceptibility to Guillain-Barre syndrome in a Northern Indian population.
over-expression of NOD1 and NOD2 may be involved in the pathogenesis of Vogt-Koyanagi-Harada (VKH) Syndrome syndrome.
Porphyromonas gingivalis induced NOD1 overexpression in endothelial cells and that NOD1 played an important role in the process of VCAM-1 (show VCAM1 Proteins) and ICAM-1 (show ICAM1 Proteins) expression in endothelial cells infected with Porphyromonas gingivalis through the NF-kappaB (show NFKB1 Proteins) signaling pathway.
findings illuminated a role for NOD1 signaling in attenuating H. pylori-induced Cdx2 (show CDX2 Proteins) expression in gastric epithelial cells
NOD1/CARD4 gene may influence the diagnosis and treatment of lung cancer
NOD1 and NOD2, two members of the NOD-like receptor family of pattern recognition receptors, are important mediators of ER-stress-induced inflammation in mouse and human cells
NOD1 signaling results in the induction of the cellular degradation pathway of autophagy and the development of pro-inflammatory responses that activate the adaptive immune system.
this paper shows that deletion of NOD1 aggravated bone resorption induced by Gram-negative bacteria, accompanied by an increase in the numbers of osteoclasts
Sertoli cells have a functional NALP3 (show NLRP3 Proteins) inflammasome that modulates NOD1 and pro-IL-1beta (show IL1B Proteins) expression, while NOD2 inversely promoted IL-1beta (show IL1B Proteins) expression.
The results indicate that Nod1 cooperates with Nod2 or TLRs to produce cytokines in macrophages in response to M. tuberculosis infection.
NOD1 and NOD2, play a collaborative role in T cell activation by alloantigen and that their blockade in vitro can inhibit T cell responses.
NOD1 activation induces cardiac dysfunction associated with excitation-contraction coupling impairment through NF-kappaB (show NFKB1 Proteins) activation.
Activation of NOD1 by DAP (show DAP Proteins) contributes to reperfusion injury via multiple signaling pathways.
Nod1 levels (and Nod2) in osteoclastogenesis are influenced by MyD88 (show MYD88 Proteins) signaling.
Data show that NOD1 or NOD2 synergizes with TLR4 (show TLR4 Proteins) in exacerbating the immune, sickness and brain responses to immune stimulation. Interactions of NLRs and TLRs at the immune cell level extend to interactions affecting brain function and behavior.
This gene encodes a member of the NOD (nucleotide-binding oligomerization domain) family. This member is a cytosolic protein. It contains an N-terminal caspase recruitment domain (CARD), a centrally located nucleotide-binding domain (NBD), and 10 tandem leucine-rich repeats (LRRs) in its C terminus. The CARD is involved in apoptotic signaling, LRRs participate in protein-protein interactions, and mutations in the NBD may affect the process of oligomerization and subsequent function of the LRR domain. This protein is an intracellular pattern-recognition receptor (PRR) that initiates inflammation in response to a subset of bacteria through the detection of bacterial diaminopimelic acid. Multiple alternatively spliced transcript variants differring in the 5' UTR have been described, but the full-length nature of these variants has not been determined.
NLR family, CARD domain containing 1
, caspase recruitment domain family, member 4
, caspase recruitment domain-containing protein 4
, nucleotide-binding oligomerization domain, leucine rich repeat and CARD domain containing 1
, nucleotide-binding oligomerization domain-containing protein 1
, caspase recruitment domain 4