Results 271 to 280 of about 10,478,036 (300)
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O-Glycosylation of the Mucin Type
Biological Chemistry, 2001While only about ten percent of the databank entries are defined as glycoproteins, it has been estimated recently that more than half of all proteins are glycoproteins. Mucin-type O-glycosylation is a widespread post-translational modification of proteins found in the entire animal kingdom, but also in higher plants.
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2009 Fifth International Conference on Intelligent Information Hiding and Multimedia Signal Processing, 2009
O-glycosylation of the mammalian protein is studied. It is serine or threonine specific, though any consensus sequence is still unknown. We have been applied support vector machines (SVM) for the prediction of O-glycosylation sites from various kinds of protein information, aiming to investigate a glycosylation condition and elucidate the mechanisms ...
Yukiko Nakajima +3 more
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O-glycosylation of the mammalian protein is studied. It is serine or threonine specific, though any consensus sequence is still unknown. We have been applied support vector machines (SVM) for the prediction of O-glycosylation sites from various kinds of protein information, aiming to investigate a glycosylation condition and elucidate the mechanisms ...
Yukiko Nakajima +3 more
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Regulation of Notch Function by O-Glycosylation
2018The Notch receptor initiates a unique intercellular signaling pathway that is evolutionarily conserved across all metazoans and contributes to the development and maintenance of numerous tissues. Consequently, many diseases result from aberrant Notch signaling.
Beth M, Harvey, Robert S, Haltiwanger
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Use of O‐Glycosylation in Total Synthesis
ChemInform, 2005AbstractFor Abstract see ChemInform Abstract in Full Text.
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Structural Insight into the Stabilizing Effect of O-Glycosylation
Biochemistry, 2017Protein glycosylation has been shown to have a variety of site-specific and glycan-specific effects, but so far, the molecular logic that leads to such observations has been elusive. Understanding the structural changes that occur and being able to correlate those with the physical properties of the glycopeptide are valuable steps toward being able to ...
Patrick K. Chaffey +9 more
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Methods in Enzymology: O‐Glycosylation of Proteins
2005Cell surface and extracellular proteins are O-glycosylated, where the most abundant type of O-glycosylation in proteins is the GalNAc attachment to serine (Ser) or threonine (Thr) in the protein chain by an a-glycosidic linkage. Most eukaryotic nuclear and cytoplasmic proteins modified by a-linked O-GlcNAc to Ser or Thr exhibit reciprocal O-GlcNAc ...
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An O-Glycosylated NeuroexcitatoryConusPeptide
Biochemistry, 1998We purified and characterized a novel peptide from the venom of the fish-hunting cone snail Conus striatus that inhibits voltage-gated K+ channels. The peptide, kappaA-conotoxin SIVA, causes characteristic spastic paralytic symptoms when injected into fish, and in frog nerve-muscle preparations exposed to the toxin, repetitive action potentials are ...
A G, Craig +14 more
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O-Glycosylation in Development of Zebrafish
2014Zebrafish are a useful vertebrate model for the analysis of development and organogenesis. As zebrafish are highly similar to humans at the molecular and developmental levels, they are also regarded as an excellent system for modeling human diseases. Concerning analysis of zebrafish glycosylation, the recent development in live imaging technology by ...
Akira Kurosaka +2 more
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Why are proteins O-glycosylated?
Trends in Biochemical Sciences, 1990The O-linked oligosaccharides of glycoproteins are usually clustered within heavily glycosylated regions of the peptide chain. Steric interactions between carbohydrate and peptide within these clusters induce the peptide core to adopt a stiff and extended conformation and this conformational effect appears to represent a major function of O ...
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Global view of human protein glycosylation pathways and functions
Nature Reviews Molecular Cell Biology, 2020Katrine T Schjoldager +2 more
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