ArticleGlycobiology2016
Identification and biological consequences of the O-GlcNAc modification of the human innate immune receptor, Nod2.
Article in Glycobiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- ZDHHC5-mediated S-palmitoylation of NOD2 drives neutrophil extracellular trap formation via mitophagy to exacerbate inflammation in COPD.Biomarker research · 2026Article
- The role of O-GlcNAcylation in innate immunity and inflammation.Journal of molecular cell biology · 2023Review
- Multifaceted roles and regulation of nucleotide-binding oligomerization domain containing proteins.Frontiers in immunology · 2023Review
- Palmitoylation restricts SQSTM1/p62-mediated autophagic degradation of NOD2 to modulate inflammation.Cell death and differentiation · 2022Article
- Targeting ProteinCells · 2022Review
- Role and Function of O-GlcNAcylation in Cancer.Cancers · 2021Review
- Understanding the Molecular Drivers of Disease Heterogeneity in Crohn's Disease Using Multi-omic Data Integration and Network Analysis.Inflammatory bowel diseases · 2021Article
- Fluorescent Detection ofBioconjugate chemistry · 2020Article
- When Adherent-invasive E. coli plays with host glycosylation: Does it open new perspectives for therapeutic strategies in Crohn's disease?EBioMedicine · 2020Article
- Enhanced O-linked Glcnacylation in Crohn's disease promotes intestinal inflammation.EBioMedicine · 2020Article
- O-GlcNAcylation in immunity and inflammation: An intricate system (Review).International journal of molecular medicine · 2019Review
- Modulation of the NOD-like receptors NOD1 and NOD2: A chemist's perspective.Bioorganic & medicinal chemistry letters · 2019Review
- Critical observations that shaped our understanding of the function(s) of intracellular glycosylation (O-GlcNAc).FEBS letters · 2018Review
- Too sweet to resist: Control of immune cell function by O-GlcNAcylation.Cellular immunology · 2018Review
- New use for CETSA: monitoring innate immune receptor stability via post-translational modification by OGT.Journal of bioenergetics and biomembranes · 2018Article
- Molecular Recognition of Muramyl Dipeptide Occurs in the Leucine-rich Repeat Domain of Nod2.ACS infectious diseases · 2017Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Nucleotide-binding oligomerization domain 2 (Nod2) is an intracellular receptor that can sense the bacterial peptidoglycan component, muramyl dipeptide. Upon activation, Nod2 induces the production of various inflammatory molecules such as cytokines and chemokines. Genetic linkage analysis identified and revealed three major mutations in Nod2 that are associated with the development of Crohn's disease. The objective of this study is to further characterize this protein by determining whether Nod2 is posttranslationally modified by O-N-acetylglucosamine (O-GlcNAc). O-GlcNAcylation is one type of posttranslational modification in which the O-GlcNAc transferase transfers GlcNAc from UDP-GlcNAc to selected serine and threonine residues of intracellular proteins. We found that wild-type Nod2 and a Nod2 Crohn's-associated variant are O-GlcNAcylated and this modification affects Nod2's ability to signal via the nuclear factor kappa B pathway.
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Registered trials
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