Results 261 to 270 of about 191,408 (290)
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Glycosylation Analysis for Congenital Disorders of Glycosylation
Current Protocols in Human Genetics, 2015AbstractCongenital disorders of glycosylation (CDG) are a group of diseases with highly variable phenotypes and inconsistent clinical features. Since the first description of a CDG in 1980, approximately 100 disorders have been identified. Most of these are defects in protein glycosylation, although an increasing number are defects of glycolipid or ...
Xueli, Li +3 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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Glycosylation of alcohols using glycosyl boranophosphates as glycosyl donors
Tetrahedron Letters, 2013Abstract A novel glycosylation that uses glycosyl boranophosphate triesters as glycosyl donors and trityl cation (Tr+) as an activator was developed. Two types of reactions were studied: (1) the boranophosphate triester was activated with TrNTf2 to react with an alcohol and (2) O-trityl ethers worked as both glycosyl acceptors and Tr+ sources.
Shiro Tatsumi +3 more
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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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N-Glycosyl Amides as Glycosyl Donors in Stereoselective Glycosylation Reactions
Synthesis, 2004AbstractFor Abstract see ChemInform Abstract in Full Text.
Norbert Pleuss, Horst Kunz
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The Journal of Organic Chemistry, 2016
Nucleoside O-glycosylation represents an archetypal problem in chemical selectivity, inasmuch as the nucleobase (an undesired site of reaction) is usually more nucleophilic than the hydroxyl (the desired site of reaction). Optimized reaction conditions have been developed for the efficient O-glycosylation of nucleoside hydroxyls. Both thioglycoside and
Yonglian, Zhang, Spencer, Knapp
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Nucleoside O-glycosylation represents an archetypal problem in chemical selectivity, inasmuch as the nucleobase (an undesired site of reaction) is usually more nucleophilic than the hydroxyl (the desired site of reaction). Optimized reaction conditions have been developed for the efficient O-glycosylation of nucleoside hydroxyls. Both thioglycoside and
Yonglian, Zhang, Spencer, Knapp
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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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2021
Human lifespan has increased significantly in the last 200 years, emphasizing our need to age healthily. Insights into molecular mechanisms of aging might allow us to slow down its rate or even revert it. Similar to aging, glycosylation is regulated by an intricate interplay of genetic and environmental factors.
Ana, Cindrić +3 more
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Human lifespan has increased significantly in the last 200 years, emphasizing our need to age healthily. Insights into molecular mechanisms of aging might allow us to slow down its rate or even revert it. Similar to aging, glycosylation is regulated by an intricate interplay of genetic and environmental factors.
Ana, Cindrić +3 more
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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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Glycosylation with sulfoxide-based glycosyl donors
Chemical CommunicationsThis feature article elucidates the development and notable progress of glycosyl sulfoxide-based glycosylation reactions, with a specific emphasis on cases where sulfinyl groups are situated either directly at the anomeric position or more distally.
Pinru Wu +3 more
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