Results 211 to 220 of about 155,076 (257)

Genetic Divergence of H1N1pdm09 in Saudi Arabia: Unveiling a Novel N-Glycosylation Site and Its Role in Vaccine Mismatch. [PDF]

open access: yesVaccines (Basel)
Abdulgader SA   +11 more
europepmc   +1 more source

N-Glycosylation

2021
N-glycosylation is a highly conserved glycan modification, and more than 7000 proteins are N-glycosylated in humans. N-glycosylation has many biological functions such as protein folding, trafficking, and signal transduction. Thus, glycan modification to proteins is profoundly involved in numerous physiological and pathological processes.
Tetsuya, Hirata, Yasuhiko, Kizuka
openaire   +2 more sources

Function of N-glycosylation in plants

Plant Science, 2018
Protein N-glycosylation is one of the major post-translational modifications in eukaryotic cells. In lower unicellular eukaryotes, the known functions of N-glycans are predominantly in protein folding and quality control within the lumen of the endoplasmic reticulum (ER).
Yukihiro, Nagashima   +2 more
openaire   +2 more sources

Facile synthesis of N-glycosyl amides using a N-glycosyl-2,4-dinitrobenzenesulfonamide and thioacids

Carbohydrate Research, 2009
N-Glucosyl-2,4-dinitrobenzenesulfonamide was prepared from N-acetyl-d-glucosamine and 2,4-dinitrobenzenesulfonyl chloride. Amidation of several thioacids using the N-glucosylsulfonamide donor proceeded smoothly to give the desired N-glucosylamides in good to high yields.
Rommel S, Talan   +2 more
openaire   +2 more sources

Stereochemistry of the N-glycosylation sites in glycoproteins

Protein Engineering Design and Selection, 1995
The stereochemical features displayed by the N-glycosidic linkage in crystalline N-linked glycoproteins are analyzed. From the statistical analysis of 44 different glycosylation sites belonging to 26 glycoproteins of the Brookhaven Protein Data Bank, a mean standard geometry for the GlcNAc moiety, along with a rationalization of its conformational ...
Imberty, A., Perez, Sarah
openaire   +3 more sources

The humanization of N-glycosylation pathways in yeast

Nature Reviews Microbiology, 2005
Yeast and other fungal protein-expression hosts have been extensively used to produce industrial enzymes, and are often the expression system of choice when manufacturing costs are of primary concern. However, for the production of therapeutic glycoproteins intended for use in humans, yeast have been less useful owing to their inability to modify ...
Stefan, Wildt, Tilllman U, Gerngross
openaire   +2 more sources

N‐Glycosylation

ChemInform, 2003
AbstractFor Abstract see ChemInform Abstract in Full Text.
openaire   +1 more source

The N-glycosylation pattern of Caenorhabditis elegans

Carbohydrate Research, 2008
Determining the exact nature of N-glycosylation in Caenorhabditis elegans, a nematode worm and genetic model organism, has proved to have been an unexpected challenge in recent years; a wide range of modifications of its N-linked oligosaccharides have been proposed on the basis of structural and genomic analysis. Particularly mass spectrometric studies
Katharina, Paschinger   +3 more
openaire   +2 more sources

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