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  • 1
    Keywords: Pharmaceutical technology ; Biochemistry ; Medicine ; Medical genetics ; Pharmaceutical Sciences/Technology ; Medical Biochemistry ; Molecular Medicine ; Gene Function ; Springer eBooks
    Description / Table of Contents: Introducion -- Part. 1. Future technological advances to elucidate the structures and functions of glycans -- Chapter 1. Structural analysis of glycans (analytical and detection methods) -- Chapter 2. Structural biology of glycans -- Chapter 3. Chemical and enzymatic synthesis and production of glycans -- Chapter 4. Technologies to elucidate functions of glycans -- Part 2. Glycans and biopharmaceuticals -- Chapter 1. Antibody pharmaceuticals -- Chapter 2. Standard glycan library -- Chapter 3. Mass production in silk worm and yeast -- Chapter 4. Glycoengineering -- Chapter 5. Glycomimetics -- Chapter 6. Glycan vaccine -- Part 3. Sugar chains (Glycans) involved in medical science and medical care -- Chapter 1. Glycan function in development and evolution -- Chapter 2. Glycans in nervous system -- Chapter 3. Glycans in osseous tissue and articulation -- Chapter 4. Glycans in infection and immunity -- Chapter 5. Next generation medical care -- Chapter 6. Life-style related disease and aging -- Chapter 7. Congenital disorders of glycosylation (CDG), neuromuscular related diseases -- Chapter 8. Glycan biomarkers for cancer and various disease -- Part 4. Food implicated in glycans and its function -- Part 5. Glycan-related materials and their use for biomaterials -- Part 6. Educational materials and training for glycosciences
    Abstract: This book presents the state of the art in glycoscience and proposes a road map for the coming decade, focusing on the potential of glycoscience research to shed light on important basic science issues and give rise to exciting new applications, especially in the field of diagnosis and therapeutics. Individual sections offer in-depth coverage of various topics relating to glycans and biopharmaceuticals, glycans in medical science and medicine, glycan technologies, glycans in food and nutrients, and glycan-related materials and their uses. In addition, the book presents an exemplary training course on glycomics and highlights educational and analytical web resources, and also includes glossaries and boxes summarizing key facts to ensure ease of understanding for non-expert readers and students. Written by more than 150 active participants in the Japan Consortium for Glycobiology and Glycotechnology (JCGG), whose goal is to promote the development of interdisciplinary glycoscience and establish a global network in the field, it is a valuable resource for students, postdocs, and researchers in the life sciences as well as for stakeholders and professionals in government, funding agencies and industry
    Pages: XV, 405 p. 133 illus., 104 illus. in color. : online resource.
    Edition: 1st ed. 2019.
    ISBN: 9789811358562
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  • 2
    Keywords: Biochemistry ; Cytology ; Oncology ; Biochemistry, general ; Cell Biology ; Cancer Research ; Springer Nature Living Reference
    Description / Table of Contents: A. Analytical and Structural Approach - Technical Description for Analyzing Glycan Structures (Reviewed by Yoshiki Yamaguchi): Overview -- EMARS -- Development of glycan array -- Development of glycan array -- Development of glycan array -- Development of glycan array -- Automated programmable one-pot synthesis of glycans -- Lectin array -- Lectin-glycan interaction based on glycan array data -- Glycoform-specific protein staining by lectin and antibody -- Glycosaminoglycans analysis -- Mass analysis -- Mass analysis -- IGOT-lectin capture -- Membrane electrophoresis -- HPLC nucleotide-sugar analysis -- Capillary electrophoresis -- HPLC PA-sugar -- Congenital disorders of glycosylation, analytical aspect -- Quality control of pharmaceutical products and biosimilars -- NMR -- NMR -- STD-NMR -- Conformational analysis of glycans and glycoproteins -- Glycolipid LC-MS -- MALDI-MS -- MALDI-MS -- Sulfoglycolipids -- GAG array -- X-ray -- REMD simulation -- MD simulation and computational screening -- B. Glycoinformatics - New Approach for Informatics and Databases for Glycoscience (Reviewed by Kiyoko F. Aoki-Kinoshita): Informatics overview -- MIRAGE project -- RINGS -- JCGGDB -- UniCarb-DB -- CIRES -- GLYCOSCIENCES.de -- CSDB, Plant and Bacterial Carbohydrate Structure Database -- MonosaccharideDB -- GlycomeDB -- GlycoEpitope -- SugarBindDB -- GLYCAM -- CAZy -- 3D Lectines -- C. Chemoenzymatic Synthesis of Glycans - Chemical and Enzymatic Methods of Glycan Synthesis (Reviewed by Yasuhiro Kajihara and Peter Seeberger): Overview -- Chemical synthesis of glycans -- Chemical synthesis of glycans -- Chemical synthesis of glycans -- Synthesis of homogeneous glycoproteins -- Synthesis of homogeneous glycoproteins -- Synthesis of homogeneous glycoproteins -- Synthesis of homogeneous glycoproteins -- Synthesis of homogeneous glycoproteins -- Glycopeptide/glycoprotein synthesis -- Gangliosides synthesis -- Specific Glycosylation -- Furanoside chemistry -- Glycoside synthesis -- Carbohydrate Library Synthesis -- Development of sugar array -- Development of sugar array -- Development of sugar array -- Automated synthesis -- Automation in glycan synthesis -- GPI chemical synthesis -- Oligosialic acid synthesis -- Synthesis of sulfated glycans -- Synthesis of sulfated glycans -- Synthetic antitumor vaccines -- Synthetic carbohydrate antigens for HIV Vaccine Design -- Chemical approach in biology and disease -- Glycoenzyme inhibitors -- Glycoenzyme inhibitors -- Glycoenzymes in glycan analysis and synthesis -- Endo-enzymes -- Oxazoline derivatives -- Large-scale enzymatic synthesis of glycans with cofactor regeneration -- Large-scale enzymatic synthesis of glycans -- Chemoenzymatic synthesis -- Chemoenzymatic synthesis of heparins -- Chemoenzymatic synthesis of glycoproteins -- Multivalent glycan synthesis -- Biosynthesis of A and B blood group -- Glycosyltransferase structures -- Structural biology of oligosaccharyltransferase (OST) -- Chemoenzymatic synthesis of oligosaccharides and cancer and bacterial vaccines -- Neoglycoprotein and oligosaccharide synthesis -- Chemoenzymatic synthesis of glycoconjugates -- Synthesis of O-glycosylated proteins -- D. Imaging of Glycans - New Techniques for Imaging Glycans (Reviewed by Yasuhiro Kajihara and Chi-Huey Wong): Molecular probes for glycosylation: overview Imaging by Click Chemistry -- Imaging by Click Chemistry -- Imaging by Click Chemistry -- Chemical tools to detect Helicobacter pylori -- Enzymatic imaging -- PET imaging -- Glycoprotein imaging -- E. Neuroglycobiology - The Role of Glycans in Neurobiology and Neuroscience (Reviewed by Kenji Kadomatsu): Neuroglycobiology overview -- Neurochemistry and developmental neurobiology -- Glycans in neurobiology -- Glycosaminoglycans (GAGs) -- GAGs -- Polysialic acid -- Polysialic acid -- Glycolipids sialidase -- HNK-1 -- Ganglioside -- Single molecule imaging -- Glycolipid -- Heparan sulfate proteoglycans (HSPG) -- HSPG -- N-glycans and glial cells
    Abstract: The aim of the book is to provide a succinct overview of the current status of glycoscience from both basic biological and medical points of view and to propose future directions, in order to facilitate further integrations of glycoscience with other fields in biological and medical studies. Glycans (carbohydrate oligomers) are the so-called “building blocks” of carbohydrates, nucleic acids, proteins and lipids and play major roles in many biological phenomena as well as in various pathophysiological processes. However, this area of glycoscience has been neglected from the research community because glycan structures are very complex and functionally diverse and as compared to proteins and nucleic acids simple tools for the amplification, sequencing and auto-synthesis of glycans are not available. Many scientists in other fields of research have now realized that glycosylation, i.e. the addition of glycans to a protein backbone, is the most abundant post translational modification reactions and is an important field of research and sometimes they require a glycobiology and/or glycochemistry approach to be used. It is still difficult, however, for non-expert researchers to use these techniques. This book will provide numerous but simple overviews of current topics and protocols for the experiments. The book is aimed at university students and above, including non-experts in the field of glycoscience
    Pages: Approx. 1200 p. 540 illus., 240 illus. in color. : online resource.
    ISBN: 9784431548362
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  • 3
    Keywords: Life sciences ; Oncology ; Biochemistry ; Cytology ; Life sciences ; Biochemistry, general ; Cell Biology ; Cancer Research ; Springer eBooks
    Description / Table of Contents: A. Analytical and Structural Approach - Technical Description for Analyzing Glycan Structures (Reviewed by Yoshiki Yamaguchi): Overview -- EMARS -- Development of glycan array -- Development of glycan array -- Development of glycan array -- Development of glycan array -- Automated programmable one-pot synthesis of glycans -- Lectin array -- Lectin-glycan interaction based on glycan array data -- Glycoform-specific protein staining by lectin and antibody -- Glycosaminoglycans analysis -- Mass analysis -- Mass analysis -- IGOT-lectin capture -- Membrane electrophoresis -- HPLC nucleotide-sugar analysis -- Capillary electrophoresis -- HPLC PA-sugar -- Congenital disorders of glycosylation, analytical aspect -- Quality control of pharmaceutical products and biosimilars -- NMR -- NMR -- STD-NMR -- Conformational analysis of glycans and glycoproteins -- Glycolipid LC-MS -- MALDI-MS -- MALDI-MS -- Sulfoglycolipids -- GAG array -- X-ray -- REMD simulation -- MD simulation and computational screening -- B. Glycoinformatics - New Approach for Informatics and Databases for Glycoscience (Reviewed by Kiyoko F. Aoki-Kinoshita): Informatics overview -- MIRAGE project -- RINGS -- JCGGDB -- UniCarb-DB -- CIRES -- GLYCOSCIENCES.de -- CSDB, Plant and Bacterial Carbohydrate Structure Database -- MonosaccharideDB -- Glycome DB -- GlycoEpitope -- Sugar Bind DB -- GLYCAM -- CAZy -- 3D Lectines -- C. Chemoenzymatic Synthesis of Glycans - Chemical and Enzymatic Methods of Glycan Synthesis (Reviewed by Yasuhiro Kajihara and Peter Seeberger): Overview -- Chemical synthesis of glycans -- Chemical synthesis of glycans -- Chemical synthesis of glycans -- Synthesis of homogeneous glycoproteins -- Synthesis of homogeneous glycoproteins -- Synthesis of homogeneous glycoproteins -- Synthesis of homogeneous glycoproteins -- Synthesis of homogeneous glycoproteins -- Glycopeptide/glycoprotein synthesis -- Gangliosides synthesis -- Specific Glycosylation -- Furanoside chemistry -- Glycoside synthesis -- Carbohydrate Library Synthesis -- Development of sugar array -- Development of sugar array -- Development of sugar array -- Automated synthesis -- Automation in glycan synthesis -- GPI chemical synthesis -- Oligosialic acid synthesis -- Synthesis of sulfated glycans -- Synthesis of sulfated glycans -- Synthetic antitumor vaccines -- Synthetic carbohydrate antigens for HIV Vaccine Design -- Chemical approach in biology and disease -- Glycoenzyme inhibitors -- Glycoenzyme inhibitors -- Glycoenzymes in glycan analysis and synthesis -- Endo-enzymes -- Oxazoline derivatives -- Large-scale enzymatic synthesis of glycans with cofactor regeneration -- Large-scale enzymatic synthesis of glycans -- Chemoenzymatic synthesis -- Chemoenzymatic synthesis of heparins -- Chemoenzymatic synthesis of glycoproteins -- Multivalent glycan synthesis -- Biosynthesis of A and B blood group -- Glycosyltransferase structures -- Structural biology of oligosaccharyltransferase (OST) -- Chemoenzymatic synthesis of oligosaccharides and cancer and bacterial vaccines -- Neoglycoprotein and oligosaccharide synthesis -- Chemoenzymatic synthesis of glycoconjugates -- Synthesis of O-glycosylated proteins -- D. Imaging of Glycans - New Techniques for Imaging Glycans (Reviewed by Yasuhiro Kajihara and Chi-Huey Wong): Molecular probes for glycosylation: overview Imaging by Click Chemistry -- Imaging by Click Chemistry -- Imaging by Click Chemistry -- Chemical tools to detect Helicobacter pylori -- Enzymatic imaging -- PET imaging -- Glycoprotein imaging -- E. Neuroglycobiology - The Role of Glycans in Neurobiology and Neuroscience (Reviewed by Kenji Kadomatsu): Neuroglycobiology overview -- Neurochemistry and developmental neurobiology -- Glycans in neurobiology -- Glycosaminoglycans (GAGs) -- GAGs -- Polysialic acid -- Polysialic acid -- Glycolipids sialidase -- HNK-1 -- Ganglioside -- Single molecule imaging -- Glycolipid -- Heparan sulfate proteoglycans (HSPG) -- HSPG -- N-glycans and glial cells
    Abstract: The aim of the book is to provide a succinct overview of the current status of glycoscience from both basic biological and medical points of view and to propose future directions, in order to facilitate further integrations of glycoscience with other fields in biological and medical studies. Glycans (carbohydrate oligomers) are the so-called “building blocks” of carbohydrates, nucleic acids, proteins and lipids and play major roles in many biological phenomena as well as in various pathophysiological processes. However, this area of glycoscience has been neglected from the research community because glycan structures are very complex and functionally diverse and as compared to proteins and nucleic acids simple tools for the amplification, sequencing and auto-synthesis of glycans are not available. Many scientists in other fields of research have now realized that glycosylation, i.e. the addition of glycans to a protein backbone, is the most abundant post translational modification reactions and is an important field of research and sometimes they require a glycobiology and/or glycochemistry approach to be used. It is still difficult, however, for non-expert researchers to use these techniques. This book provides numerous but simple overviews of current topics and protocols for the experiments. The book is aimed at university students and above, including non-experts in the field of glycoscience
    Pages: LXII, 1568 p. 333 illus., 233 illus. in color. eReference. : online resource.
    ISBN: 9784431548416
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  • 4
    Keywords: Life sciences ; Oncology ; Immunology ; Biochemistry ; Life sciences ; Biochemistry, general ; Cancer Research ; Immunology ; Springer eBooks
    Description / Table of Contents: 1 N-Glycans and Quality Control of Proteins -- 2 Glycan-Mediated Protein Transport from the Endoplasmic Reticulum -- 3 Gangliosides and T-Cell Immunity -- 4 Gangliosides Regulate Tumor Properties: With Focus on the Suppression of Metastasis-Associated ppGalNAc-T13 with GM1 -- 5 Role of Glycans in Viral Infection -- 6 Discovery and Applications of a Novel Human Pluripotent Stem Cell-Specific Lectin Probe rBC2LCN -- 7 Glycan Structure and Neural Plasticity -- 8 The Involvement of Midkine, a Heparin-Binding Growth Factor, in Cancer Development -- 9 Tumor-Associated Glycans and Their Functional Roles in the Multistep Process of Human Cancer Progression -- 10 Mammalian Sialidase and Tumor Development -- 11 Roles of Glycans in Immune Evasion from NK Immunity -- 12 Glycomic Analysis of Cancer -- 13 Glyco-Predisposing Factor of Diabetes -- 14 Macrophages Govern Ganglioside GM3 Expression in Adipocytes to Regulate Adipogenesis and Insulin Signaling in Homeostatic and Pathogenic Conditions -- 15 O-Mannosyl Glycan and Muscular Dystrophy -- 16 Glycans and Chronic Obstructive Pulmonary Disease (COPD) -- 17 α1,6-Fucosyltransferase Knockout Mice and Schizophrenia-Like Phenotype
    Abstract: This book presents the latest breakthrough results in glycobiology regarding the roles of glycans in relation to quality control and transport of protein, the immune system, viral infection, stem cells, the neural system, and various diseases such as cancer, diabetes, chronic obstructive pulmonary disease, muscular dystrophy, and schizophrenia. Although glycoscience has long been regarded as a very specialized field with no simple analytical method, the recent explosive progress in research continues to provide limitless evidence that glycan chains are the key component in various biological phenomena. Cell surface glycans, for example, change with developmental stages or environmental conditions and thus represent a “face” of the cell that is utilized for identification of iPS and ES cells and as biomarkers in diagnosis or detection of cancer. This book comprises 17 chapters, each of which poses outstanding “glyco-related” questions enabling non-specialists to have a clearer idea about what the future direction for further investigation of glycans in their own research fields will be. Also including basic information to understand the nature of glycans, this title serves as an excellent “textbook” for researchers in diverse research fields who are not familiar with, but nevertheless interested in, glycan chains or sugar chains
    Pages: VIII, 288 p. 87 illus., 41 illus. in color. : online resource.
    ISBN: 9784431553816
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  • 5
    Keywords: Life sciences ; Immunology ; Toxicology ; Chemistry, Organic ; Biochemistry ; Cytology ; Life sciences ; Biochemistry, general ; Cell Biology ; Organic Chemistry ; Immunology ; Pharmacology/Toxicology ; Springer eBooks
    Description / Table of Contents: Part 1 Glucosyltransferases -- 1 Beta-1,3-glucosyltransferase (B3GALTL) -- 2 Protein O-glucosyltransferases rumi (RUMI) -- 3 UDP-glucose:ceramide glucosyltransferase (UGCG) -- 4 UDP-glucose:glycoprotein glucosyltransferase 1,2 (UGGT1,2) -- Part 2 Galactosyltransferases -- 5 Alpha 1,3-galactosyltransferase 2, pseudogene (A3GALT2P) -- 6 Core 1 beta 3Galactosyltransferase (C1GalT1, T-synthase) and its Specific Molecular Chaperone Cosmc (C1GalT1C1) -- 7 Glycoprotein alpha 1,3-galactosyltransferase 1, pseudogene (GGTA1P) -- 8 UDP-Gal:betaGal beta 1,3-galactosyltransferase polypeptide 6 (B3GALT6) -- 9 UDP-Gal:betaGlcNAc beta 1,3-galactosyltransferase, polypeptide 1,2 (B3GALT1,2) -- 10 UDP-Gal:betaGlcNAc beta 1,3-galactosyltransferase, polypeptide 4 (B3GALT4) -- 11 UDP-Gal:betaGlcNAc beta 1,3-galactosyltransferase, polypeptide 5 (B3GALT5) -- 12 UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase, polypeptide 1 (B4GALT1) -- 13 UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase, polypeptide 2-6; xylosylprotein beta 1,4-galactosyltransferase, polypeptide 7 (galactosyltransferase I) (B4GALT2-7) -- 14 UDP-Gal:ceramide galactosyltransferase (UGT8) -- 15 UDP-Gal:lactosylceramide alpha 1,4-galactosyltransferase (A4GALT) -- Part 3 Mannosyltransferases -- 16 Protein O-mannosyl-transferase 1,2 (POMT1,2) -- Part 4 N-Acetylglucosaminyltransferases -- 17 Alpha-1,4-N-acetylglucosaminyltransferase (A4GNT) -- 18 Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 3 (GCNT3) -- 19 Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltrasnsferase 1 (GCNT1) (C2GnT-L)and Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltrasnsferase 3 (GCNT4) (C2GnT-T) -- 20 Fringe (UDP-GlcNAc: O-fucosylpeptide ß1,3 N-acetylglucosaminyltransferase) -- 21 Mannosyl (alpha-1,3-)-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (MGAT1) -- 22 Mannosyl (alpha-1,3-)-glycoprotein beta-1,4-N-acetylglucosaminyltransferase, isozyme A,B (MGAT4A,B) -- 23 Mannosyl (alpha-1,3[6?]-)-glycoprotein beta-1,4-N-acetylglucosaminyltransferase, isozyme C (putative) (MGAT4C) -- 24 Mannosyl (alpha-1,6-)-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (MGAT2) -- 25 Mannosyl (alpha-1,6-)-glycoprotein beta-1,6-N-acetyl-glucosaminyltransferase, isozyme B (MGAT5B) -- 26 Mannosyl (alpha-1,6-)-glycoprotein beta-1,6-N-acetyl-glucosaminyltransferase (MGAT5) -- 27 Mannosyl (beta-1,4-)-glycoprotein beta-1,4-N- acetylglucosaminyltransferase (MGAT3); β1,4-N- Acetylglucosaminyltransferase III (GnT-III, GlcNAc-T III) -- 28 N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase (GCNT2) (IGnT) -- 29 O-linked N-acetylglucosamine (GlcNAc) transferase (UDP-N-acetylglucosamine:polypeptide-N-acetylglucosaminyl transferase) (OGT) -- 30 Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1 (POMGNT1) -- 31 UDP-GlcNAc: beta-Gal beta1,3-N-acetylglucosaminyltransferase 6 (B3GNT6) (Core 3 synthase, C3GnT) -- 32 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 1 (B3GNT1), i-enzyme (iGnT) -- 33 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 (B3GNT2) -- 34 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 3 (B3GNT3) -- 35 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 5 (B3GNT5, Lc3Cer synthase) -- 36 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 7 (B3GNT7) -- 37 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 8 (B3GNT8) -- Part 5 N-Acetylgalactosaminyltransferases -- 38 Beta-1,4 N-acetylgalactosaminyltransferase 1,2 (B4GALNT1,2) -- 39 Beta1,3-N-Acetylgalactosaminyltransferase 2 (B3GALNT2) -- 40 Beta1,4-N-acetylgalactosaminyltransferase-3 (B4GALNT3) and beta1,4-N-acetylgalactosaminyltransferase-4 (B4GALNT4) -- 41 Globoside alpha-1,3-N-acetylgalactosaminyltransferase 1 (GBGT1) -- 42 Histo-blood Group A and B Transferases, Their Gene Structures, and Common O Group Gene Structures -- 43 Histo-blood Group A Variants, O Variants, and Their Alleles -- 44 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 4 (B3GNT4) -- 45 UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferases (ppGalNAc-Ts) -- Part 6 Fucosyltransferases -- 46 Fucosyltransferase 3. GDP-fucose lactosamine α1,3/4-fucosyltransferase. Lea and Leb histo-blood groups (FUT3, Lewis enzyme) -- 47 Fucosyltransferase 4. GDP-fucose lactosamine α1,3-fucosyltransferase. Myeloid specific (FUT4) -- 48 Fucosyltransferase 5. GDP-fucose lactosamine α3/4-fucosyltransferase (FUT5) -- 49 Fucosyltransferase 6. GDP-fucose lactosamine α3-fucosyltransferase (FUT6) -- 50 Fucosyltransferase 7. GDP-fucose lactosamine α1,3-fucosyltransferase. Sialyl-Lex specific (FUT7) -- 51 Fucosyltransferase 8. GDP-fucose N-glycan core α6-fucosyltransferase (FUT8) -- 52 Fucosyltransferase 9. GDP-fucose lactosamine α1,3-fucosyltransferase. Lex specific (FUT9) -- 53 Fucosyltransferases 1, 2. GDP-fucose galactoside α2-fucosyltransferases. FUT1 or H blood group, FUT2 or ABH secretor status and Sec1 (FUT1, FUT2, Sec1) -- 54 Fucosyltransferases 10, 11. GDP-fucose N-glycan core α1,3-fucosyltransferases (FUT10, FUT11) -- 55 Fucosyltransferases 12, 13: Protein O-fucosyltransferases 1 and 2 (POFUT1, POFUT2) -- Part 7 Sialyltransferases -- 56 ST3 beta-galactoside alpha-2,3-sialyltransferase 1 (ST3GAL1) -- 57 ST3 beta-galactoside alpha-2,3-sialyltransferase 2 (ST3GAL2) -- 58 ST3 beta-galactoside alpha-2,3-sialyltransferase 3 (ST3GAL3) -- 59 ST3 beta-galactoside alpha-2,3-sialyltransferase 4 (ST3GAL4) -- 60 ST3 beta-galactoside alpha-2,3-sialyltransferase 5 (ST3GAL5) -- 61 ST3 beta-galactoside alpha-2,3-sialyltransferase 6 (ST3GAL6) -- 62 ST6 beta-galactoside alpha-2,6-sialyltranferase 1 (ST6GAL1) -- 63 ST6 beta-galactoside alpha-2,6-sialyltranferase 2 (ST6GAL2) -- 64 ST6 N-acetylgalactosaminide alpha-2,6-sialyltransferase 1 (ST6GALNAC1) -- 65 ST6 N-acetylgalactosaminide alpha-2,6-sialyltransferase 2 (ST6GALNAC2) -- 66 ST6 N-acetylgalactosaminide alpha-2,6-sialyltransferase 3 (ST6GALNAC3) -- 67 ST6 N-acetylgalactosaminide alpha-2,6-sialyltransferase 4 (ST6GALNAC4) -- 68 ST6 N-acetylgalactosaminide alpha-2,6-sialyltransferase 5,6 (ST6GALNAC5,6) -- 69 ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 1 (ST8SIA1) -- 70 ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 2 (ST8SIA2) -- 71 ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 3 (ST8SIA3) -- 72 ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 4 (ST8SIA4) -- 73 ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 5 (ST8SIA5) -- 74 ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 6 (ST8SIA6) -- Part 8 Glucuronyltransferases -- 75 Beta-1,3-glucuronyltransferase 1 (glucuronosyltransferase P); beta-1,3-glucuronyltransferase 2 (B3GAT1,2) -- 76 Beta-1,3-glucuronyltransferase 3 (glucuronosyltransferase I) (B3GAT3) -- Part 9 GAG polymerase and related enzymes -- 77 Chondroitin polymerizing factor, chondroitin polymerizing factor 2, chondroitin sulfate synthase 1,3 (CHPF, CHPF2, CHSY1, CHSY3) -- 78 Chondroitin sulfate N-acetylgalactosaminyltransferase 1,2 (CSGALNACT1,2) -- 79 Dermatan sulfate epimerases (DSE, DSEL) -- 80 Exostoses (multiple)-like 1-3 (EXTL1-3) -- 81 Exostosin 1,2(EXT1,2) -- 82 Heparin-heparansulfate related GlcA C5-epimerase -- 83 Hyaluronan synthase 1-3 (HAS1-3) -- 84 Xylosyltransferase I,II (XYLT1,2) -- Part 10 Sulfotransferases -- 85 Carbohydrate sulfotransferase 10 (CHST10) -- 86 Carbohydrate (chondroitin 4) sulfotransferase 11-13 (CHST11-13) -- 87 Carbohydrate (chondroitin 6) sulfotransferase 3; carbohydrate (N-acetylglucosamine 6-O) sulfotransferase 7 (CHST3,7) -- 88 Carbohydrate (keratan sulfate Gal-6) sulfotransferase 1 (CHST1) -- 89 Carbohydrate (N-acetylgalactosamine 4-0) sulfotransferase 14 (CHST14) -- 90 Carbohydrate (N-acetylgalactosamine 4-sulfate 6-O) sulfotransferase 15 (CHST15) -- 91 Carbohydrate (N-acetylglucosamine 6-O) sulfotransferase 4 (CHST4) -- 92 Carbohydrate (N-acetylglucosamine 6-O) sulfotransferase 5 and 6 (CHST5,6) -- 93 Carbohydrate (N-acetylglucosamine-6-O) sulfotransferase 2(CHST2) -- 94 Galactose-3-O-sulfotransferase 1-4 (GAL3ST1-4) -- 95 Heparan sulfate 2-O-sulfotransferase (HS2ST) -- 96 Heparan sulfate (glucosamine) 3-O-sulfotransferase 1-6 (HS3ST1-6) -- 97 Heparan-sulfate 6-O-sulfotransferase 1-3 (HS6ST1-3) -- 98 N-Acetylgalactosamine-4-sulfotransferase-1 (GalNAc-4-ST1, CHST8) and N-Acetylgalactosamine-4-sulfotransferase-2 (GalNAc-4-ST2, CHST9) -- 99 N-deacetylase/N-sulfotransferase (heparan glucosaminyl) 1 (NDST1) -- 100 N-deacetylase/N-sulfotransferase (heparan glucosaminyl) 2 (NDST2) -- 101 N-deacetylase/N-sulfotransferase (heparan glucosaminyl) 3,4 (NDST3,4) -- 102 Uronyl-2-sulfotransferase (UST) -- Part 11 Glycosyltransferase-like proteins (inplicated in alpha-dystrogly) -- 103 Fukutin and fukutin-related protein (FKRP) -- 104 Like-glycosyltransferase; glycosyltransferase-like 1B (LARGE, GYLTL1B) -- Part 12 GPI anchor biosynthesis -- 105 Glycosylp
    Abstract: This handbook, now in a new, second edition, is an essential resource for scientists with an interest in the role of glycosyltransferases and related genes involved in the biosynthesis of glycoproteins, glycolipids, and proteoglycans. The first edition of the Handbook of Glycosyltransferases and Related Genes, published in 2002, contained descriptions of more than 100 mammalian genes by over 100 scientists who originally isolated and/or cloned these genes. Since then, there has been a growing body of evidence concerning the roles of glycosyltransferases, and additional glycosyltransferases have been identified. Now more than 200 glycosyltransferases have been isolated from mammalian tissue, corresponding to approximately 1–2% of the total human genome. Some have been found to be involved in development and reproduction, signal transduction, cell death, higher nervous functioning, immunity, and other important biological processes. Glycosyltransferases have also been implicated in the development of lifestyle diseases such as diabetes, cancer, chronic obstructive lung disease (COPD), neuromuscular diseases, and infectious diseases. A functional glycomics approach using gene targeting in mice and analytical methods utilizing glycan arrays, lectin arrays, HPLC, and mass spectrometry identified the target glycoprotein(s) on which glycans are attached by the catalytic reaction of glycosyltransferases. Most of the target proteins have been shown to be cell surface membrane proteins such as growth factor receptors and transporters. The three-dimensional structures of some glycosyltransferases have also been characterized, making it possible to classify them into retaining and inverting enzymes. Such structural information is also included in this invaluable new edition
    Pages: XXXVIII, 1707 p. 205 illus., 75 illus. in color. eReference. : online resource.
    Edition: 2nd ed. 2014.
    ISBN: 9784431542407
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  • 6
    ISSN: 1432-2307
    Keywords: Carcinoma of the esophagus ; Apudoma ; Oat cell carcinoma ; Amyloid ; Argyrophil cells
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary In a series of 79 cases of primary esophageal carcinoma resected at The Center for Adult Diseases, Osaka, there were six tumors with specific histopathologic features valid for the diagnosis of argyrophil cell carcinoma. Of the 6 tumors, 3 were studied electron microscopically and assay for ACTH content was performed on 4 tumors. Clinically, the ages of the 6 patients ranged from 56 to 71 years; two were women and four men. Four of the 6 patients died with widespread tumor recurrences within 9 months of operation. Microscopically, the 6 tumors were composed largely or almost entirely of small, spindle-shaped cells resembling those of oat cell carcinoma of the lung, and were characterized by the arrangement of tumor cells in solid sheets or anastomosing cords, the presence of argyrophil tumor cells, and the deposits of amyloid. Electron microscopically, the three tumors contained neurosecretory-type granules. Using bioassay or radioimmunoassay ACTH activity in the tumor tissues was detected in 3 out of the 4 tumors determined. From the light and electron microscopic characteristics and the assay evidence, it seems reasonable to conclude that the 6 tumors are endocrine polypeptide producing tumors (apudomas) that arise from argyrophil cells normally found among the basal cells of the esophageal mucosa, and that they represent a distinct histopathologic entity clearly distinguishable from other types of esophageal carcinomas.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 1573-2568
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary A case of diffuse leiomyomatosis of the esophagus which was successfully resected is presented. The patient was a 44-year-old man who had an abnormal filling defect, which was incidentally discovered during esophagography, and was observed for two years. Although he remained asymptomatic, an operation was performed because of increase in the tumor's size. The lesion consisted of many confluent myomatous nodules throughout the thoracic portion of the esophagus, mostly seen in the circular layer of the muscularis, and some in the muscularis mucosa. Histologically, these nodules were leiomyomas. This is a very rare condition, and only a dozen similar cases have been reported so far. A brief discussion is made on the definition of diffuse leiomyomatosis of the esophagus.
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 1436-2813
    Keywords: CAD ; double cancers ; concomitant surgery ; CABG
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Concomitant surgical procedures for coronary artery disease and double cancers are reported. A 61-year-old man with severe triple-vessel coronary disease was found to have early gastric cancer and advanced rectal cancer. We successfully performed a concomitant coronary artery bypass graft using an extracorporeal ultrafiltration membrane and curative surgery for both cancers. Concomitant surgery thus appears to be a benefical and safe approach for the treatment of critical coronary artery disease and intraperitoneal double cancers in carefully selected patients.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    BBA - Protein Structure 251 (1971), S. 164-171 
    ISSN: 0005-2795
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology
    Type of Medium: Electronic Resource
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