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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.
A role for NOD1 in HCMV control via RIPK2 (zeige RIPK2 Proteine)- IKKalpha (zeige CHUK Proteine)-IRF3 (zeige IRF3 Proteine) signaling, NOD1 polymorphisms predict the risk of infection.
Bronchial epithelial overexpression of TLR4 (zeige TLR4 Proteine) and NOD1 in severe/very severe stable COPD (zeige ARCN1 Proteine), associated with increased bronchial inflammation and P. aeruginosa bacterial load, may play a role in the pathogenesis of COPD (zeige ARCN1 Proteine)
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
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 (zeige SUGT1 Proteine) (hSGT1 (zeige ECD Proteine)) to NOD1 LRR significantly enhanced the solubility, and the fusion protein was stabilized by coexpression of mouse Hsp90alpha (zeige HSP90AA2 Proteine).
the results suggest that the chronic activation of NOD1 and NOD2 receptors might play a role in the development of gastric cancer.
the absence of Nod1 does not impair the recruitment of neutrophils in response to P. aeruginosa
These findings reveal macrophage NOD1 as a cell-specific target to combat diet-induced inflammation past the step of macrophage infiltration, leading to insulin (zeige INS Proteine) resistance.
The studies establish chronic pancreatitis as an IL-33 (zeige IL33 Proteine)-dependent inflammation resulting from synergistic interactions between the NOD1 and CCKR signaling pathways.
Results show that the simultaneous absence of Nod1 and Nod2 is associated with accelerated T cell death upon alloantigen encounter, suggesting these proteins might provide new targets to ameliorate T cell responses in a variety of inflammatory states, including those associated with bone marrow or solid organ transplantation.
this study shows that the effect of the gut microbiota on bone is dependent on NOD1 and NOD2 signaling
we propose that NOD1 signaling in mesenchymal stromal cells serves as an important pathway underlying the requirement for microbiota in the maintenance of steady-state hematopoiesis
results suggest a previously unappreciated role for the innate immune receptor Nod1 in suppressing colitis-associated tumorigenesis through a T cell-mediated mechanism
NOD1 activation in cardiac fibroblasts induces myocardial fibrosis in a murine model of type 2 diabetes.
this study reveals that LRRK2 is a new positive regulator of Rip2 and promotes inflammatory cytokine induction through the Nod1/2-Rip2 pathway.
this paper shows that deletion of NOD1 aggravated bone resorption induced by Gram-negative bacteria, accompanied by an increase in the numbers of osteoclasts
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