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Two Single-Nucleotide Polymorphisms associated with susceptibility to develop dengue in NOD1 or RIPK2 genes were observed Children from Colombia.
our work indicates that NOD1 plays a previously undetected protective role in larval survival through CD44a-mediated activation of the PI3K-Akt signaling.
Upregulation of miR-495 ameliorates the high glucose-induced inflammatory, cell differentiation and extracellular matrix accumulation of human CFs by modulating both the NF-kappaB and TGF-beta1/Smad signaling pathways through downregulation of NOD1 expression.
Study proposes that NOD1 contributes to inflammation not only by promoting pro-inflammatory processes, but also by suppressing anti-inflammatory pathways.
Overexpression of either NOD1 or NOD2 reduces cell proliferation and increases clonogenic potential in vitro in breast cancer cell lines.
NOD1 (rs6958571) SNP was associated with gram-positive blood stream infection in Caucasian infants and extremely low birth weight infants.
In transgenic mice expressing human NOD1 and deficient for the murine NOD1, we showed enhanced clearance of a lipl21- mutant of Leptospira interrogans compared to the complemented strain, or to what was observed in NOD1KO mice, suggesting that LipL21 facilitates escape from immune surveillance in humans.
The changes in the nucleotide-binding oligomerization domain-like receptors (NLRs) in human corneas with disease expression may reflect different susceptibility to infectious and non-infectious injuries in corneas with various diseases.
A role for NOD1 in HCMV control via RIPK2- IKKalpha-IRF3 signaling, NOD1 polymorphisms predict the risk of infection.
Bronchial epithelial overexpression of TLR4 and NOD1 in severe/very severe stable COPD, associated with increased bronchial inflammation and P. aeruginosa bacterial load, may play a role in the pathogenesis of COPD
study provides structural and dynamic insights into the NOD1-RIP2 oligomer formation, which will be crucial in understanding the molecular basis of NOD1-mediated CARD-CARD interaction in higher and lower eukaryotes
Based on molecular docking studies using PG ligands, we propose few residues - G825, D826 and N850 in hNOD1-LRR and L904, G905, W931, L932 and S933 in hNOD2-LRR, evolutionarily conserved across different host species, which may play a major role in ligand recognition.
Nucleotide-binding oligomerization domain (NOD1) was the most significantly associated gene when analyzing exonic rare variants (RVs) in chromosome 7p to carotid bifurcation intima-media thickness (bIMT).
Fusion of human SGT1 (hSGT1) to NOD1 LRR significantly enhanced the solubility, and the fusion protein was stabilized by coexpression of mouse Hsp90alpha.
the results suggest that the chronic activation of NOD1 and NOD2 receptors might play a role in the development of gastric cancer.
this study reveals that LRRK2 is a new positive regulator of Rip2 and promotes inflammatory cytokine induction through the Nod1/2-Rip2 pathway.
Finally, NOD1 agonist increased the formation of cranial and subintestinal vessel plexus in zebrafish, and this effect was abrogated by concurrent PPARgamma activation. Overall, these findings identify a PPARgamma-miR-125a-NOD1 signaling axis in endothelial cells that is critical in the regulation of inflammation-mediated angiogenesis.
NOD1/2 gene variants are not linked with T2DM and IR.
findings show that NOD1, a PRR 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 receptors, acting through distinct pathways.
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