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

Deleterious

書目名稱Glycoproteins and Human Disease影響因子(影響力)




書目名稱Glycoproteins and Human Disease影響因子(影響力)學(xué)科排名




書目名稱Glycoproteins and Human Disease網(wǎng)絡(luò)公開度




書目名稱Glycoproteins and Human Disease網(wǎng)絡(luò)公開度學(xué)科排名




書目名稱Glycoproteins and Human Disease被引頻次




書目名稱Glycoproteins and Human Disease被引頻次學(xué)科排名




書目名稱Glycoproteins and Human Disease年度引用




書目名稱Glycoproteins and Human Disease年度引用學(xué)科排名




書目名稱Glycoproteins and Human Disease讀者反饋




書目名稱Glycoproteins and Human Disease讀者反饋學(xué)科排名

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

無可非議

擔(dān)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

獨(dú)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

是貪求

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