Titlebook: Ganglioside Biochemistry; Cheorl-Ho Kim Book 2020 Springer Nature Singapore Pte Ltd. 2020 Glycans.Sialic acid.sugar code.Tumor associated

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书目名称Ganglioside Biochemistry影响因子(影响力)




书目名称Ganglioside Biochemistry影响因子(影响力)学科排名




书目名称Ganglioside Biochemistry网络公开度




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书目名称Ganglioside Biochemistry被引频次




书目名称Ganglioside Biochemistry被引频次学科排名




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书目名称Ganglioside Biochemistry年度引用学科排名




书目名称Ganglioside Biochemistry读者反馈




书目名称Ganglioside Biochemistry读者反馈学科排名

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Book 2020eceives detailed attention. The significance of sialic acids in regulation ofthe complement system is explained, and the closing chapter focuses especially on the role of sialyl T antigen in cancer.  The book will be of value for all who are interested in functional glycobiology and glycomic studies

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https://doi.org/10.1007/978-3-642-91761-5istic events are also observed in so-called pretranslational modification such as alternative splicing to allow diverse mRNA variants in spliced mRNA levels. Therefore, the diverse reality is globally created from pretranslational alternative splicing as well as PTM including phosphorylation and gly

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https://doi.org/10.1007/978-3-662-34141-4 as a metastatic gastric cancer in humans [1]. In fact, some relationship between the ABO blood groups and stomach cancers were found in an earlier document [2]. Blood group lipoids have been found from human gastric mucosa and gastric cancer [3]. Linking clue of incidence between the secretor facto

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Glycosylation,istic events are also observed in so-called pretranslational modification such as alternative splicing to allow diverse mRNA variants in spliced mRNA levels. Therefore, the diverse reality is globally created from pretranslational alternative splicing as well as PTM including phosphorylation and gly

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N-Glycan and O-Glycan Glycosylation in Eukaryotes,teins and the rest 4% is cytoplasmic and nuclear proteins [1]. In contrast, O-glycosylated proteins occupy at least approximately 12% level from all glycosylated proteins in human. The glycoproteins both with N- and O-glycosylations are estimated to hold at least 10% of all glycosylated proteins [2]

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Sialyltransferase, Sialylation, and Sulfoylation,rmation, tumor metastasis, and inflammation. The sialyl-carbohydrates are key molecules in cellular recognition and cell–pathogen interaction. To synthesize the sialyl-glycoconjugates, sialyltransferases (STs) transfer SA residues from donor substrates to acceptors (Fig. 3.1). The naturally occurrin

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