Results 301 to 310 of about 347,689 (338)
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Glycosyl sulfates as glycosyl donors
Tetrahedron Letters, 1994Abstract Glycosyl sulfates are easily synthesised from tetrabenzyl pyranoses; their reaction with various acceptors promoted by Lewis acids affords glycosides and disaccharides as α,β mixtures.
CIPOLLA, LAURA FRANCESCA +4 more
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Glycosyl Sulfoxides in Glycosylation Reactions
Topics in Current Chemistry, 2018Carbohydrate chemistry has benefited a lot from the intrinsic reactivity of sulfoxide since it was introduced in glycosylation reactions by Kahne in 1989. Since then, extensive studies have been explored by employing sulfoxide as glycosyl donors and activation reagents in construction of glycosidic bonds.
Jing Zeng +5 more
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Glycosyl trichloroacetylcarbamate: a new glycosyl donor for O-glycosylation
Carbohydrate Research, 2005Glycosyl trichloroacetylcarbamates, readily obtained by reacting 1-hydroxy sugars with trichloroacetylisocyanate, have been found as excellent glycosyl donors, and the corresponding O-glycosides are formed in good to excellent yields with a fairly good degree of selectivity.
K, Jayakanthan, Yashwant D, Vankar
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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
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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
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Journal of the American Chemical Society, 2008
The glycosylation state of individual antibodies was imaged using an atomic force microscope with a probe modified with lectins and an image acquisition system that permits simultaneous acquisition of sample topography data along with a map of lectin binding sites.
Hongda, Wang +5 more
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The glycosylation state of individual antibodies was imaged using an atomic force microscope with a probe modified with lectins and an image acquisition system that permits simultaneous acquisition of sample topography data along with a map of lectin binding sites.
Hongda, Wang +5 more
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Carbohydrate Research, 2013
Synthesis of glycosyl hydroperoxides derived from 2,3,4,6-tetra-O-benzyl-d-glucopyranose and 2,3,4,6-di-O-isopropylidene-d-mannofuranose was performed via a Schmidt's imidate intermediate with hydrogen peroxide in an ethyl ether solution in the presence of an acid catalyst.
Barbara, Szechner +2 more
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Synthesis of glycosyl hydroperoxides derived from 2,3,4,6-tetra-O-benzyl-d-glucopyranose and 2,3,4,6-di-O-isopropylidene-d-mannofuranose was performed via a Schmidt's imidate intermediate with hydrogen peroxide in an ethyl ether solution in the presence of an acid catalyst.
Barbara, Szechner +2 more
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Current Opinion in Biotechnology, 1993
The majority of candidate recombinant therapeutics are glycoproteins. Four aspects of glycobiology are requisite if the full potential of such reagents is to be realised: an understanding of glycan biosynthesis and its regulation, rapid and sensitive oligosaccharide analytical techniques, determination of structure-function relationships in protein ...
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The majority of candidate recombinant therapeutics are glycoproteins. Four aspects of glycobiology are requisite if the full potential of such reagents is to be realised: an understanding of glycan biosynthesis and its regulation, rapid and sensitive oligosaccharide analytical techniques, determination of structure-function relationships in protein ...
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Current Opinion in Cell Biology, 1992
Protein glycosylation is more abundant and structurally diverse than all other types of post-translational modifications combined. Protein-bound saccharides range from dynamic monosaccharides on nuclear and cytoplasmic proteins, to enormously complex 'recognition' molecules on extracellular N- or O-linked glycoproteins or proteoglycans.
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Protein glycosylation is more abundant and structurally diverse than all other types of post-translational modifications combined. Protein-bound saccharides range from dynamic monosaccharides on nuclear and cytoplasmic proteins, to enormously complex 'recognition' molecules on extracellular N- or O-linked glycoproteins or proteoglycans.
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PROTEOMICS, 2001
With the advances of molecular biology and with improved analytical techniques a significant change of perception has taken place regarding prokaryotic glycoproteins. Glycosylation of proteins from prokaryotes is no longer considered a specific feature of certain organisms but has been demonstrated for many archaea and bacteria.
C, Schäffer, M, Graninger, P, Messner
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With the advances of molecular biology and with improved analytical techniques a significant change of perception has taken place regarding prokaryotic glycoproteins. Glycosylation of proteins from prokaryotes is no longer considered a specific feature of certain organisms but has been demonstrated for many archaea and bacteria.
C, Schäffer, M, Graninger, P, Messner
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