Found 2 structures.
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1. Compound ID: 832
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b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-+
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b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-D-GlcNAc |
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Structure type: oligomer
Trivial name: antigen type I
Contained glycoepitopes: IEDB_130646,IEDB_130655,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_150939,IEDB_151531,IEDB_153529,IEDB_153531,IEDB_153557,IEDB_158533,IEDB_158548,IEDB_158550,IEDB_190606,SB_165,SB_166,SB_173,SB_187,SB_195,SB_30,SB_7,SB_88
The structure is contained in the following publication(s):
- Article ID: 230
Feizi T "Progress in deciphering the information content of the 'glycome' - a crescendo in the closing years of the millennium" -
Glycoconjugate Journal 17(7-9) (2000) 553-565
The closing years of the second millennium have been uplifting for carbohydrate biology. Optimism that oligosaccharide sequences are bearers of crucial biological information has been borne out by the constellation of efforts of carbohydrate chemists, biochemists, immunochemists, and cell- and molecular biologists. The direct involvement of specific oligosaccharide sequences in protein targeting and folding, and in mechanisms of infection, inflammation and immunity is now unquestioned. With the emergence of families of proteins with carbohydrate-binding activities, assignments of information content for defined oligosaccharide sequences will become more common, but the pinpointing and elucidation of the bioactive domains on oligosaccharides will continue to pose challenges even to the most experienced carbohydrate biologists. The neoglycolipid technology incorporates some of the key requirements for this challenge: namely the resolution of complex glycan mixtures, and ligand binding coupled with sequence determination by mass spectrometry.
monoclonal antibodies, mass spectrometry, blood group antigen, carbohydrate ligands, differentiation antigens, embryonic development, galectins, inflammation, leukocyte adhesion, neoglycolipids, oligosaccharide ligands, oligosaccharid probes, selectins
NCBI PubMed ID: 11421348Journal NLM ID: 8603310Publisher: Kluwer Academic Publishers
Correspondence: t.feizi@ic.ac.uk
Institutions: The Glycosciences Laboratory, Imperial College School of Medicine, Harrow, United Kingdom
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2. Compound ID: 15304
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b-D-Galp-(1-4)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-6)-+
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b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-+ |
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b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-+ | |
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b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-3)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-D-GlcpNAc |
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Structure type: oligomer
Trivial name: VSG complex N-glycan
Compound class: N-glycan
Contained glycoepitopes: IEDB_123886,IEDB_130646,IEDB_130655,IEDB_130697,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_137776,IEDB_140108,IEDB_140122,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_144983,IEDB_150939,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_153529,IEDB_153531,IEDB_153557,IEDB_158533,IEDB_158548,IEDB_158550,IEDB_190606,IEDB_423128,IEDB_540672,IEDB_548907,IEDB_983930,SB_165,SB_166,SB_173,SB_187,SB_195,SB_197,SB_198,SB_30,SB_33,SB_44,SB_67,SB_7,SB_72,SB_73,SB_74,SB_85,SB_88
The structure is contained in the following publication(s):
- Article ID: 5943
Heng J, Naderer T, Ralph SA, McConville MJ "Glycosylated compounds of parasitic protozoa" -
Book: Microbial Glycobiology (series: Structures, Relevance and Applications) (2010) 203-231
This chapter describes the range of glycan structures and pathways that are found in different parasitic protozoa. All parasitic protists express a range of glycoconjugates that form protective protein-rich or carbohydrate-rich surface coats. Protein-rich coats are typically found on developmental stages that inhabit nonhydrolytic niches, such as the bloodstream and nonacidified intracellular vacuoles. These coats are commonly dominated by a limited repertoire of antigenically diverse proteins that are commonly, but not always, glycosylphosphatidylinositol- (GPI-) anchored and modified with N- or O-glycans. Carbohydrate-rich coats are commonly found on developmental stages that dwell within hydrolytic environments, such as vertebrate and arthropod digestive tracts and lysosomal vacuoles. These coats are dominated by GPI-anchored glycoproteins that are heavily modified with N-glycans, O-glycans, or phosphoglycans. Free GPI glycolipids (not attached to protein) can also be abundant or dominant components of these coats. Some parasitic protists can also form highly resistant cyst stages encased within polysaccharide-rich cell walls. Considerable progress has been made in defining the structures of the surface and intracellular glycans of the parasitic protists, their biosynthesis and the role that individual components play in parasite infectivity.
O-glycosylation, Glycosylphosphatidylinositol, N-glycosylation, protozoan parasites, Phosphoglycosylation
Publication DOI: 10.1016/B978-0-12-374546-0.00012-2Publisher: Amsterdam: Elsevier
Correspondence: malcolmm@unimelb.edu.au
Editors: Moran A
Institutions: Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Australia
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