title: Chemical assembly of N-glycoproteins: a refined toolbox to address a ubiquitous posttranslational modification.
abstract: Incremental developments in the chemistry of peptides, proteins and carbohydrates have enabled researchers to assemble entire glycoproteins with high precision. Based on sophisticated ligation chemistries pure glycoproteins bearing a single glycosylation pattern have become available. The impact of N-glycosylation on the function of glycoproteins is generally recognized but not well understood. Based on the recent advances in the synthesis of glycoproteins by chemical methods researchers can finally start to elucidate the various roles of carbohydrates in complex biomolecules in detail.
authors: Bioorganische Chemie, Gebäude NWI, Universität Bayreuth, 95440 Bayreuth, Germany. carlo.unverzagt@uni-bayreuth.de
authors: Carlo
authors: C
authors: Unverzagt
authors: Yasuhiro
authors: Y
authors: Kajihara
mesh_terms: D000117:Acetylglucosamine / Q000737:chemistry / Q000378:metabolism; D002241:Carbohydrates / Q000096:biosynthesis / Q000737:chemistry; D006023:Glycoproteins / Q000096:biosynthesis / Q000737:chemistry*; D006031:Glycosylation; D010447:Peptide Hydrolases / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D012260:Ribonucleases / Q000378:metabolism
chemical_list: D002241:Carbohydrates; D006023:Glycoproteins; D012260:Ribonucleases; C029600:ribonuclease B; D010447:Peptide Hydrolases; D000117:Acetylglucosamine