Signalling pathways and molecular interactions of NOD1 and NOD2
Top Cited Papers
Open Access
- 9 December 2005
- journal article
- review article
- Published by Springer Nature in Nature Reviews Immunology
- Vol. 6 (1) , 9-20
- https://doi.org/10.1038/nri1747
Abstract
The NOD (nucleotide-binding oligomerization domain) proteins NOD1 and NOD2 have important roles in innate immunity as sensors of microbial components derived from bacterial peptidoglycan. The importance of these molecules is underscored by the fact that mutations in the gene that encodes NOD2 occur in a subpopulation of patients with Crohn's disease, and NOD1 has also been shown to participate in host defence against infection with Helicobacter pylori. Here, we focus on the molecular interactions between these NOD proteins and other intracellular molecules to elucidate the mechanisms by which NOD1 and NOD2 contribute to the maintenance of mucosal homeostasis and the induction of mucosal inflammation.Keywords
This publication has 97 references indexed in Scilit:
- Membrane recruitment of NOD2 in intestinal epithelial cells is essential for nuclear factor–κB activation in muramyl dipeptide recognitionThe Journal of cell biology, 2005
- Muramyl dipeptide and toll-like receptor sensitivity in NOD2-associated Crohn's diseaseThe Lancet, 2005
- The Crohn's Disease Protein, NOD2, Requires RIP2 in Order to Induce Ubiquitinylation of a Novel Site on NEMOCurrent Biology, 2004
- Toll-like receptor signallingNature Reviews Immunology, 2004
- Heterotypic interactions among NACHT domains: implications for regulation of innate immune responsesBiochemical Journal, 2004
- Interactions between commensal intestinal bacteria and the immune systemNature Reviews Immunology, 2004
- Helicobacter pyloriInfection and the Development of Gastric CancerNew England Journal of Medicine, 2001
- Synergistic Effect of Muramyldipeptide with Lipopolysaccharide or Lipoteichoic Acid To Induce Inflammatory Cytokines in Human Monocytic Cells in CultureInfection and Immunity, 2001
- Expression and Functional Analysis of Apaf-1 IsoformsJournal of Biological Chemistry, 2000
- Isolation of glucosaminyl-β(1–4)-muramic acid and phosphoric acid ester of this disacoharide from acid hydrolysates of peptidoglycan of Bacillus cereus ahu 1356 cell wallsBiochemical and Biophysical Research Communications, 1971