Handbook of Glycosyltransferases and Related Genes

The so-called postgenomic research era has now been launched, and the field of gly­ cobiology and glycotechnology has become one of the most important areas in life science because glycosylation is the most common post-translational modification reaction of proteins in vivo. On the basis of Swiss-Pr...

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Bibliographic Details
Other Authors: Taniguchi, Naoyuki (Editor), Honke, Koichi (Editor), Fukuda, Minoru (Editor)
Format: eBook
Language:English
Published: Tokyo Springer Japan 2002, 2002
Edition:1st ed. 2002
Subjects:
Online Access:
Collection: Springer Book Archives -2004 - Collection details see MPG.ReNa
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100 1 |a Taniguchi, Naoyuki  |e [editor] 
245 0 0 |a Handbook of Glycosyltransferases and Related Genes  |h Elektronische Ressource  |c edited by Naoyuki Taniguchi, Koichi Honke, Minoru Fukuda 
250 |a 1st ed. 2002 
260 |a Tokyo  |b Springer Japan  |c 2002, 2002 
300 |a XVIII, 670 p  |b online resource 
505 0 |a Map 4 Biosynthetic Pathways of Proteoglycans -- Map 5 Biosynthetic Pathways of GPI-Anchor 
505 0 |a 71. Heparan Sulfate/Heparin N-Deacetylase/N-Sulfotransferase-2 -- 72. Heparan Sulfate/Heparin N-Deacetylase/N-Sulfotransferase-3 and -4 -- 73. ?Gal 3-O-Sulfotransferase-1,-2,-3, and -4 -- 74. UDP-Gal Transporter-1 and -2 -- 75. UDP-GlcNAc Transporter -- 76. CMP-Sialic Acid Transporter -- 77. GPI-GlcNAc Transferase: Complex of PIG-A, PIG-C, PIG-H, hGPIl, and PIG-P -- 78. Dolichol Phosphate-Mannose Synthase (DPMI and DPM2) -- 79. PIG-B, GPI-Man Transferase III, Man-(Ethanolaminephosphate) Man-GlcN-(Acyl)PI Mannosyltransferase -- 80. Dolichol Phosphate GlcNAc-1-P Transferase -- 81. ALG3 Mannosyltransferase -- 82. ALG6 Glucosyltransferase -- 83.Oligosaccharyltransferase Complex, Ribophorin-I, Ribophorin-II, OST48, and DAD1 -- 84. Phosphomannomutase -- 85. Phosphomannose Isomerase -- 86. ?-Mannosidase-II -- 87. ?-Mannosidase-IIx -- 88. Lysosomal Enzyme GlcNAc-1-Phosphotransferase -- GlcNAc-1-Phosphodiester ?-N-Acetylglucosaminidase -- Map 3 Biosynthetic Pathways of Glycosphingolipids --  
505 0 |a 22. Polypeptide N-Acetylgalactosaminyltransferases -- 23. ?4-N-Acetylgalactosaminyltransferase -- 24. Histoblood Group A and B Transferases, Their Gene Structures, and Common O Group Gene Structures -- 25. Histoblood Group A Variants, O Variants, and Their Alleles -- 26. Forssman Glycolipid Synthase -- 27. ?2-Fucosyltransferases (FUT1, FUT2, and Sec1) -- 28. ?3/4-Fucosyltransferase (FUT3, Lewis enzyme) -- 29. ?3-Fucosyltransferase-IV (FUT4) -- 30. ?3-Fucosyltransferase-V (FUT5) -- 31. ?3-Fucosyltransferase-VI (FUT6) -- 32. ?3-Fucosyltransferase-VII (FUT7) -- 33. ?3-Fucosyltransferase-IX (FUT9) -- 34. ?6-Fucosyltransferase (FUT8) -- 35. ST3Gal-I -- 36. ST3Gal-II (SAT-IV) -- 37. ST3Gal-III -- 38. ST3Gal-IV -- 39. ST3Gal-V (GM3 Synthase, SAT-I) -- 40. ST6Gal-I -- 41. ST6GalNAc-I -- 42. ST6GalNAc-II -- 43.ST6GalNAc-III (STY) -- 44. ST6GalNAc-IV -- 45. ST8Sia-I (GD3 Synthase, SAT-II) -- 46. ST8Sia-II (STX) -- 47. ST8Sia-III -- 48. ST8Sia-IV (PST-1) -- 49. ST8Sia-V (SAT-V/SAT-III) --  
505 0 |a Preface -- Contributors -- 1. GlcCer Synthase (UDP-Glucose:Ceramide Glucosyltransferase, UGCG) -- 2. ?4-Galactosyltransferase-I -- 3. ?4-Galactosyltransferase-II, -III, -IV, -V, -VI, and -VII -- 4. ?3-Galactosyltransferase-I, -II, and -III -- 5. ?3-Galactosyltransferase-IV (GM1 Synthase) -- 6. ?3-Galactosyltransferase-V -- 7. ?3-Galactosyltransferase -- 8. GalCer Synthase (Ceramide Galactosyltransferase, CGT) -- 9. N-Acetylglucosaminyltransferase-I -- 10. N-Acetylglucosaminyltransferase-II -- 11. N-Acetylglucosaminyltransferase-III -- 12. N-Acetylglucosaminyltransferase-IV -- 13. N-Acetylglucosaminyltransferase-V -- 14. N-Acetylglucosaminyltransferase-VI -- 15. ?3-N-Acetylglucosaminyltransferase (Fringe) -- 16. ?3-N-Acetylglucosaminyltransferase (iGnT) -- 17. ?6-N-Acetylglucosaminyltransferase (IGnT) -- 18. Core 2 ?6-N-Acetylglucosaminyltransferase-I and -III -- 19. Core 2 ?6-N-Acetylglucosaminyltransferase-II -- 20. ?4-N-Acetylglucosaminyltransferase -- 21. O-GlcNAc Transferase --  
505 0 |a 50. CMP-NeuAc Hydroxylase -- 51. HNK-1 Glucuronyltransferase -- 52. GAG Glucuronyltransferase-I -- 53. UDP-Glucose Dehydrogenase -- 54. ?4-N-Acetylhexosaminyltransferase (EXTL2) -- 55. Hyaluronan Synthase-1, -2, and -3 -- 56. Heparan Sulfate GlcA/GlcNAc Transferase -- D-Glucuronyl C5-Epimerase in Heparin/Heparan Sulfate Biosynthesis -- 58. Chondroitin 6-Sulfotransferase -- 59. Keratan Sulfate Gal-6-Sulfotransferase -- 60. Corneal N-Acetylglucosamine 6-O-Sulfotransferase -- 61. N-Acetylglucosamine 6-O-Sulfotransferase -- 62. Intestinal N-Acetylglucosamine 6-O-Sulfotransferase -- 63. High Endothelial Cell N-Acetylglucosamine 6-O-Sulfotransferase -- 64. Chondroitin 4-Sulfotransferase -- 65. HNK-1 Sulfotransferase -- 66. Galactosaminoglycan Uronyl 2-Sulfotransferase -- 67. Heparan Sulfate 2-Sulfotransferase -- 68. Heparan Sulfate 6-Sulfotransferase -- 69. Heparan Sulfate D-Glucosaminyl 3-O-Sulfotransferase-1,-2,-3, and-4 -- 70. Heparan Sulfate/Heparin N-Deacetylase/N-Sulfotransferase-1 --  
653 |a Enzymology 
653 |a Biochemistry 
700 1 |a Honke, Koichi  |e [editor] 
700 1 |a Fukuda, Minoru  |e [editor] 
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989 |b SBA  |a Springer Book Archives -2004 
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520 |a The so-called postgenomic research era has now been launched, and the field of gly­ cobiology and glycotechnology has become one of the most important areas in life science because glycosylation is the most common post-translational modification reaction of proteins in vivo. On the basis of Swiss-Prot data, over 50% proteins are known to undergo glycosylation, but in fact the actual functions of most of the sugar chains in the glycoconjugates remain unknown. The complex carbohydrate chains of glycoproteins, glycolipids, and proteoglycans represent the secondary gene products formed through the reactions of glycosyl­ transferases. The regulation of the biosynthesis of sugar chains is under the control of the expression of glycosyltransferases, their substrate specificity, and their local­ ization in specific tissue sites. There is a growing body of evidence to suggest that these enzymes play pivotal roles in a variety of important cellular differentiation and developmental events, as well as in disease processes. Over 300 glycosyltransferases appear to exist in mammalian tissues. If the genes that have been purified and cloned from various species such as humans, cattle, pigs, rats and mice are counted as one, approximately 110 glycogenes that encode glycosyltransferases and related genes have been cloned at present, and this number continues to grow each day. However, most of the functions of the glycosyltransferase genes and related genes are unknown. This fact has stimulated numerous new and interesting approaches in molecular biologi­ cal investigations