A5057835124- Glycosylation and Glycoproteins Research
- Carbohydrate Chemistry and Synthesis
- Galectins and Cancer Biology
- Intraperitoneal and Appendiceal Malignancies
- Cancer, Lipids, and Metabolism
- RNA modifications and cancer
- Ovarian cancer diagnosis and treatment
- Neuroendocrine Tumor Research Advances
- Sperm and Testicular Function
- Microbial Metabolic Engineering and Bioproduction
- Lipid Membrane Structure and Behavior
- Lysosomal Storage Disorders Research
- Immunotherapy and Immune Responses
- Lipid metabolism and biosynthesis
- RNA Interference and Gene Delivery
- Monoclonal and Polyclonal Antibodies Research
- Ubiquitin and proteasome pathways
- Metabolism, Diabetes, and Cancer
- Multiple Sclerosis Research Studies
Unité de Glycobiologie Structurale et Fonctionnelle
2015-2021
Institut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement
2020
Centre National de la Recherche Scientifique
2015-2019
Université de Lille
2014-2019
University of Siena
1990
The post-translational modification of proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) is regulated a unique couple enzymes. O-GlcNAc transferase (OGT) transfers the GlcNAc residue from UDP-GlcNAc, final product hexosamine biosynthetic pathway (HBP), whereas O-GlcNAcase (OGA) removes it. This study and others show that OGT O-GlcNAcylation levels are increased in cancer cell lines. In context we studied effect silencing colon lines HT29 HCT116 primary line CCD841CoN. Herein report...
Glycosylation is a group of post-translational modifications that displays large variety structures and are implicated in plethora biological processes. Therefore, studying glycosylation requires different technical approaches reliable tools, lectins being part them. Here, we describe the use recombinant mushroom lectin PVL to discriminate O-GlcNAcylation, modification consisting attachment single N-acetylglucosamine residue proteins confined within cytosolic, nuclear mitochondrial...