Results 211 to 220 of about 155,572 (257)
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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
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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
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N‐Glycosylation

ChemInform, 2003
AbstractFor Abstract see ChemInform Abstract in Full Text.
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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
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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
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N-Glycosylation and Plant Cell Growth

2014
N-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
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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
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Characterization of Protein N‐Glycosylation

2005
Although 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,
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Integrin α5β1 and Its N-Glycosylation

2014
Integrins are transmembrane heterodimeric proteins sensing the cell microenvironment and modulating numerous signaling pathways. Changes in integrin function and expression between normal and tumor cells support involvement of specific integrins in tumor progression and aggressiveness.
Jianguo Gu   +3 more
openaire   +1 more source

N-Glycosylation in Chrysosporium lucknowense enzymes

Carbohydrate Research, 2008
Twenty-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
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