Results 221 to 230 of about 151,535 (246)
Some of the next articles are maybe not open access.
Function of N-glycosylation in plants
Plant Science, 2018Protein 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
N-Glycosylation in Chrysosporium lucknowense enzymes
Carbohydrate Research, 2008Twenty-eight enzymes, encoded by different genes and secreted by different mutant strains of Chrysosporium lucknowense, were subjected to MALDI-TOF MS peptide fingerprinting followed by analysis of the MS data using the GlycoMod tool from the ExPASy proteomic site. Various N-linked glycan structures were discriminated in the C.
Alexander V, Gusakov +2 more
openaire +2 more sources
Facile synthesis of N-glycosyl amides using a N-glycosyl-2,4-dinitrobenzenesulfonamide and thioacids
Carbohydrate Research, 2009N-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
N-Glycosylation and Plant Cell Growth
2014N-linked glycosylation is one of the most prevalent cotranslational protein modifications in plants. It is initiated by a conserved process in the endoplasmic reticulum and subsequently involves a series of different N-glycan maturation steps that take place in the ER and Golgi apparatus.
Christiane, Veit +2 more
openaire +2 more sources
Characterization of Site-Specific N-Glycosylation
2019Even if a consensus sequence has been identified for a posttranslational modification, the presence of such a sequence motif only indicates the possibility, not the certainty that the modification actually occurs. Proteins can be glycosylated on certain amino acid side chains, and these modifications are designated as C-, N-, and O-glycosylation.
Hevér, Helga +2 more
openaire +3 more sources
N-Glycosylation of Plant Recombinant Pharmaceuticals
2009N-glycosylation is a maturation event necessary for the correct function, efficiency, and stability of a high number of biopharmaceuticals. This chapter presented here proposes various methods to determine whether, how, and where a plant pharmaceutical is N-glycosylated.
Bardor, Muriel +6 more
openaire +4 more sources
Heterocyclic N-glycosyl derivatives—XIII
Tetrahedron, 1972Abstract Acid-catalysed reactions of tri-O-acetyl- D -glucal with benzotriazole, 5,6-dimethylbenzotriazole, 5,6-dichlorobenzotriazole and 6-chloropurine have been found to give anomeric mixtures of the corresponding 2′,3′-unsaturated N-glycosyl derivatives with the α-anomers preponderating.
M. Fuertes +5 more
openaire +1 more source
Quantitative Genetics of Human Protein N-Glycosylation
2021Although changes in protein glycosylation are observed in a wide range of diseases and pathological states, the examples of use of glycans as biomarkers and therapeutic targets are limited. This is not in small part because the understanding of human glycome regulation in vivo is incomplete and fragmented.
Jasminka, Krištić +2 more
openaire +2 more sources
Characterization of Protein N‐Glycosylation
2005Although mass spectrometry (MS)-based protein identification is a straightforward task, the characterization of most posttranslational modifications still represents a challenge. N-glycosylation with its well known consensus sequence, common core structure, and "universally" active endoglycosidase seems to belong to the easier category. In this chapter,
openaire +2 more sources

