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Titlebook: Glycosignals in Cancer: Mechanisms of Malignant Phenotypes; Koichi Furukawa,Minoru Fukuda Book 20161st edition Springer Japan 2016 Glycosy

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Roles of Fucosyltransferases in Cancer Phenotypeson and dynamic regulation of growth factor receptor signaling on cell surface, and changes in fucosylation result in differences of biological phenotype in cancer cells. Eleven fucosyltransferases are involved in the synthesis of fucosylated glycans and belong to some family of fucosyltransferases.
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Differential Roles of Mammalian Sialidases in Cancerses of such alteration, our studies have focused on mammalian sialidases, which regulate the cellular sialic acid content by catalyzing the removal of sialic acid residues from glycoproteins and glycolipids. There are four types of mammalian sialidases, designated as NEU1, NEU2, NEU3, and NEU4, encod
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Regulation of Growth Factor Receptors by Glycosphingolipidsuding gangliosides, are involved in crucial biological processes such as cell growth, differentiation, and motility. Certain GSLs have been identified as tumor-associated antigens in various types of cancer cells. Early studies of inhibitory effects of gangliosides on cell growth led to the discover
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Nutrient Regulation of Cancer Cells by O-GlcNAcylationar and cytoplasmic proteins. This modification is regulated by O-GlcNAc transferase (OGT), which attaches O-GlcNAc to proteins and O-GlcNAcase (OGA), which removes O-GlcNAc. O-GlcNAc serves as a nutrient sensor to regulate virtually all cellular processes, as well as playing roles in various disease
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Function of Unique ,-Glycan Structures in Protecting Gastric Mucosa Against , Infection and Gastric ing terminal α1,4-linked .-acetylglucosamine (αGlcNAc). αGlcNAc inhibits growth and motility of ., a microbe causing gastric cancer, by inhibiting biosynthesis of its cell wall component cholesteryl-α-D-glucopyranoside. In addition, αGlcNAc serves as a tumor suppressor for gastric differentiated-typ
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Sialylation and Immune Surveillance of Cancer by Siglecsproteins and lipids. Altered sialylation in cancer can impact at many levels and may result in improved cancer cell survival and spread. Here we focus on sialic acid-dependent interactions of tumour cells with sialic acid-binding Ig-like lectins (siglecs). These proteins are expressed broadly in the
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Expression and Function of Poly-,-Acetyllactosamine Type Glycans in Cancercterization of poly-.-acetyllactosamine is largely dependent on the work by many passionate glycobiologists in the early 1970s. They put great efforts to identify the carbohydrate component of human blood cells. Poly-.-acetyllactosamine chain has various physiological functions by serving as a scaff
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