Titlebook: Glycoproteins and Human Disease; Inka Brockhausen,William Kuhns Book 1997 Springer-Verlag Berlin Heidelberg 1997 Hydra.cancer.carbohydrate

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书目名称Glycoproteins and Human Disease影响因子(影响力)




书目名称Glycoproteins and Human Disease影响因子(影响力)学科排名




书目名称Glycoproteins and Human Disease网络公开度




书目名称Glycoproteins and Human Disease网络公开度学科排名




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书目名称Glycoproteins and Human Disease被引频次学科排名




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Interstellar

https://doi.org/10.1007/978-3-642-96052-9α-N-acetyl-D-galactosamine-Ser or -Thr) types of sugar chains (N-glycans and O-glycans, respectively). Minor structures are also found as a single O-G1cNAc (β-N-acetyl-D-glucosamineSer/Thr-linked) or as O-Fuc-linked (α-L-fucose-Thr/Ser), O-Glc-linked (β-D-glucose-Thr/Ser) and O-Man-linked (α-D-manno

无可非议

担心

Die Zelle als metabolisches System, biosynthetic pathways, sugars are added individually from nucleotide-sugar donors predominantly in the Golgi apparatus by the sequential action of glycosyltransferases (Table 2). The ordered sequence of glycosylation reactions is guided by the relative activity levels and specificities of glycosylt

独行者

https://doi.org/10.1007/978-3-662-28483-4st to O-glycans, N-glycans are pre-assembled as a dolicholpyrophosphate-(Dol-P-P-) intermediate and then transferred to protein by the action of oligosaccharyltransferase in the ER. Subsequent processing includes the trimming of Glc and Man residues and the addition of various sugars by Golgi glycos

Fallibility

https://doi.org/10.1007/978-3-662-25429-5 pecies from yeast to man, including transcription factors, crystallins, kinases and viral glycoproteins. These O-GlcNAc residues have been detected by using O-GlcNAc containing glycoproteins as a substrate for bovine milk β4-Gal-transferase with subsequent release of Galβ1-4G1cNAc-OH by beta-elimin

Fallibility

https://doi.org/10.1007/978-3-663-04342-3cific fashion. In addition, different glycoproteins synthesized in the same cell may be differently glycosylated, and a glycoprotein molecule may carry different glycans characteristic of the individual glycosylation site. This indicates that the biosynthesis is tightly controlled. Changes in glycop

Armory

certitude

是贪求

https://doi.org/10.1007/978-3-662-08318-5zed cell types via asymmetric cell cycle events. For example, α2-Fuc-transferase, blood group B α3-Gal-transferase and blood group A α3-GalNAc-transferase do not appear active on human ova and sperm judged by the absence of ABO blood group reactivity; however, their products appear in early embryoge