Intracellular functions of N-linked glycans.

By Ari Helenius, and Markus Aebi. Science, 2001

2,297 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology, Organic Chemistry

View Paper: https://www.semanticscholar.org/paper/7c627bc792c82e63e320ef7b889105a04505521b

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Citations in the corpus

TLR9 signals after translocating from the ER to CpG DNA in the lysosome (2004, background): “Whereas PGNase F cleaves all ER- and Golgi-derived carbohydrate modifications, Endo H loses its ability to cleave carbohydrate species once they have been modified by Golgi-localized enzyme”
How proteins move lipids and lipids move proteins (2001, background): “Diacylglycerol (DAG) activates protein kinases C and inositol-1,4,5-trisphosphate (Ins(1,4,5)P 3 ) opens Ca channels in the ER (BOX 2).”
A comprehensive classification system for lipids11 The evaluation of this manuscript was handled by the former Editor-in-Chief Trudy Forte. Published, JLR Papers in Press, February 16, 2005. DOI 10.1194/jlr.E400004-JLR200 (2005, background): “Polyprenol phosphate sugars and polyprenol diphosphate sugars function in extracytoplasmic glycosylation reactions (41), in extracellular polysaccharide biosynthesis [for instance, peptidoglycan polymerization in bacteria (42)], and in eukaryotic protein N-glycosylation (43, 44).”
Sorting of lysosomal proteins. (2009, background): “The glycans play a pivotal role in protein folding, oligomerization, quality control, sorting, and transport (for review see [2,3]).”
Quality control in the endoplasmic reticulum protein factory (2003, background): “The glycans add hydrophobicity to the folding peptide but also act as substrates for the lectin chaperones calnexin and calreticulin, whose role in glycoprotein folding has been extensively reviewe”
Association of Piriformospora indica with Arabidopsis thaliana roots represents a novel system to study beneficial plant–microbe interactions and involves early plant protein modifications in the endoplasmic reticulum and at the plasma membrane (2004, background): “In concert with glucosidase I, the enzyme catalyses the fist steps in N-linked glycan trimming and processing which occur in the ER. The role of glycans in the early secretory pathway is related to protein folding, quality control and protein sorting (reviewed in Helenius and Aebi 2001 ).”
Glycosylation and stabilization of programmed death ligand-1 suppresses T-cell activity (2016, positive): “…complex that transfers a preformed glycan composed of oligosaccharides to an asparagine (Asn) side-chain acceptor located within the NXT motif (-Asn-X-Ser/Thr-) 10,11 and can be classiﬁed into high-mannose, hybrid and complex types based on the saccharide composition and branching features.”
Identification and Quantification of Protein Glycosylation (2012, background): “N-glycosylation occurs solely on proteins that shuttle via the secretory pathway [7].”
Protein quality control in the early secretory pathway (2008, background): “As anticipated above, mannose trimming allows discrimination between unfolded and terminally misfolded glycoproteins (Helenius and Aebi, 2001); the latter are recognized by the concerted action of a1/a2”