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Glycan

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390:, bind to the three glucose residues present on the core N-linked glycan. These chaperone proteins then serve to aid in the folding of the protein that the glycan is attached to. Following proper folding, the three glucose residues are removed, and the glycan moves on to further processing reactions. If the protein fails to fold properly, the three glucose residues are reattached, allowing the protein to re-associate with the chaperones. This cycle may repeat several times until a protein reaches its proper conformation. If a protein repeatedly fails to properly fold, it is excreted from the endoplasmic reticulum and degraded by cytoplasmic proteases. 492:-linked glycans is N-acetyl-galactosamine. After this, several different pathways are possible. A Core 1 structure is generated by the addition of galactose. A Core 2 structure is generated by the addition of N-acetyl-glucosamine to the N-acetyl-galactosamine of the Core 1 structure. Core 3 structures are generated by the addition of a single N-acetyl-glucosamine to the original N-acetyl-galactosamine. Core 4 structures are generated by the addition of a second N-acetyl-glucosamine to the Core 3 structure. Other core structures are possible, though less common. 329:, a lipid, on the external side of the endoplasmic reticulum membrane. Five mannose residues are then added to this structure. At this point, the partially finished core glycan is flipped across the endoplasmic reticulum membrane, so that it is now located within the reticular lumen. Assembly then continues within the endoplasmic reticulum, with the addition of four more mannose residues. Finally, three glucose residues are added to this structure. Following full assembly, the glycan is transferred en bloc by the 32: 809:
predetermined precursor ion in the first quadrupole, a fragmented in the collision quadrupole, and a predetermined fragment ion in the third quadrupole. It is a non-scanning technique, wherein each transition is detected individually and the detection of multiple transitions occurs concurrently in duty cycles. This technique is being used to characterize the immune glycome.
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Within the immune system the N-linked glycans on an immune cell's surface will help dictate that migration pattern of the cell, e.g. immune cells that migrate to the skin have specific glycosylations that favor homing to that site. The glycosylation patterns on the various immunoglobulins including
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Once transferred to the nascent peptide chain, N-linked glycans, in general, undergo extensive processing reactions, whereby the three glucose residues are removed, as well as several mannose residues, depending on the N-linked glycan in question. The removal of the glucose residues is dependent on
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calls for a new focus on glycoscience, a field that explores the structures and functions of glycans and promises great advances in areas as diverse as medicine, energy generation, and materials science. Until now, glycans have received little attention from the research community due to a lack of
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from glycoproteins are analyzed routinely by high-performance-liquid-chromatography (reversed phase, normal phase and ion exchange HPLC) after tagging the reducing end of the sugars with a fluorescent compound (reductive labeling). A large variety of different labels were introduced in the recent
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Bermingham, ML; Colombo, M; McGurnaghan, SJ; Blackbourn, LAK; Vučković, F; Pučić Baković, M; Trbojević-Akmačić, I; Lauc, G; Agakov, F; Agakova, AS; Hayward, C; Klarić, L; Palmer, CNA; Petrie, JR; Chalmers, J; Collier, A; Green, F; Lindsay, RS; Macrury, S; McKnight, JA; Patrick, AW; Thekkepat, S;
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In recent years, high performance liquid chromatography online coupled to mass spectrometry became very popular. By choosing porous graphitic carbon as a stationary phase for liquid chromatography, even non derivatized glycans can be analyzed. Detection is here done by mass spectrometry, but in
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Although MRM has been used extensively in metabolomics and proteomics, its high sensitivity and linear response over a wide dynamic range make it especially suited for glycan biomarker research and discovery. MRM is performed on a triple quadrupole (QqQ) instrument, which is set to detect a
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residues in the peptide may be temporarily blocked from forming disulfide bonds with other cysteine residues, due to the size of a nearby glycan. Therefore, the presence of a N-linked glycan allows the cell to control which cysteine residues will form disulfide bonds.
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residue serves as a signal that the protein to which this glycan is attached should be moved to the lysosome. This recognition and trafficking of lysosomal enzymes by the presence of mannose-6-phosphate is accomplished by two proteins: CI-MPR (cation-independent
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years, where 2-aminobenzamide (AB), anthranilic acid (AA), 2-aminopyridin (PA), 2-aminoacridone (AMAC) and 3-(acetylamino)-6-aminoacridine (AA-Ac) are just a few of them. Different labels have to be used for different ESI modes and MS systems used.
501: : Core 1 and Core 2 generation. White square = N-acetyl-galactosamine; black circle = galactose; Black square = N-acetyl-glucosamine. Note: There is a mistake in this diagram. The bottom square should always be white in each image, not black. 417:
and other immune receptors. Glycans may also be involved in "self" and "non self" discrimination, which may be relevant to the pathophysiology of various autoimmune diseases; including rheumatoid arthritis and type 1 diabetes.
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Harvey DJ, Bateman RH, Bordoli RS, Tyldesley R (2000). "Ionisation and fragmentation of complex glycans with a quadrupole time-of-flight mass spectrometer fitted with a matrix-assisted laser desorption/ionisation ion source".
370:. Processing and modification of N-linked glycans within the Golgi does not follow a linear pathway. As a result, many different variations of N-linked glycan structure are possible, depending on enzyme activity in the Golgi. 988:
The focus of the NCFG is the development in the glycosciences, with an emphasis on exploring the molecular mechanisms of glycan recognition by proteins important in human biology and disease. They have a number of
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Pabst M, Bondili JS, Stadlmann J, Mach L, Altmann F (July 2007). "Mass plus retention time equals structure: a strategy for the analysis of N-glycans by carbon LC-ESI-MS and its application to fibrin N-glycans".
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units to the various core structures. These are formed by the repetitive addition of galactose and N-acetyl-glucosamine units. Polylactosamine chains on O-linked glycans are often capped by the addition of a
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tools to probe their often complex structures and properties. The report presents a roadmap for transforming glycoscience from a field dominated by specialists to a widely studied and integrated discipline.
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Nakagawa, S; Hato, M; Takegawa, Y; Deguchi, K; Ito, H; Takahata, M; Iwasaki, N; Minami, A; Nishimura, S-I (2007). "Detection of altered N-glycan profiles in whole serum from rheumatoid arthritis patients".
579:, have been found to be important in developing normal intestinal microflora. Certain strains of intestinal bacteria bind specifically to mucin, allowing them to colonize the intestine. 218:
Glycans can be found attached to proteins as in glycoproteins and proteoglycans. In general, they are found on the exterior surface of cells. O- and N-linked glycans are very common in
1782:"Selected reaction monitoring to differentiate and relatively quantitate isomers of sulfated and unsulfated core 1 O-glycans from salivary MUC7 protein in rheumatoid arthritis" 1530:
Pabst M, Kolarich D, Pöltl G, et al. (January 2009). "Comparison of fluorescent labels for oligosaccharides and introduction of a new postlabeling purification method".
553:, on blood vessel endothelial cells, can be induced by a number of factors. One such factor is the response of the endothelial cell to certain bacterial molecules, such as 925:
and other carbohydrate-binding proteins have revealed a wide variety of the structural basis for glycome function. The purity of test samples have been obtained through
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Schulz, BL; Packer NH, NH; Karlsson, NG (Dec 2002). "Small-scale analysis of O-linked oligosaccharides from glycoproteins and mucins separated by gel electrophoresis".
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N-linked glycans also play an important role in cell-cell interactions. For example, tumour cells make N-linked glycans that are abnormal. These are recognized by the
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Aizpurua-Olaizola, O.; Toraño, J. Sastre; Falcon-Perez, J.M.; Williams, C.; Reichardt, N.; Boons, G.-J. (2018). "Mass spectrometry for glycan biomarker discovery".
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Hase S, Ikenaka T, Matsushima Y (November 1978). "Structure analyses of oligosaccharides by tagging of the reducing end sugars with a fluorescent compound".
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to a nascent peptide chain, within the reticular lumen. This core structure of N-linked glycans, thus, consists of 14 residues (3 glucose, 9 mannose, and 2
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and make them available to the scientific community free of charge. The data generated by these resources are captured in databases accessible through the
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without prefractionation, although a discrimination between isobaric glycan structures is more challenging or even not always possible. Anyway, direct
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for complete structural analysis of complex glycans is a difficult and complex field. However, the structure of the binding site of numerous
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Lectin and antibody arrays provide high-throughput screening of many samples containing glycans. This method uses either naturally occurring
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Metabolic labeling of glycans can be used as a way to detect glycan structures. A well-known strategy involves the use of
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Maverakis E, Kim K, Shimoda M, Gershwin M, Patel F, Wilken R, Raychaudhuri S, Ruhaak LR, Lebrilla CB (2015).
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are usually analysed without any tags, due to the chemical release conditions preventing them to be labeled.
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IgE, IgM, IgD, IgE, IgA, and IgG bestow them with unique effector functions by altering their affinities for
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residue at either -1 or +3 relative to the serine or threonine is favourable for O-linked glycosylation.
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Varki, Ajit; Cummings, Richard; Esko, Jeffrey; Freeze, Hudson; Hart, Gerald; Marth, Jamey, eds. (1999).
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Flowers, Sarah A.; Ali, Liaqat; Lane, Catherine S.; Olin, Magnus; Karlsson, Niclas G. (2013-04-01).
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enzymes is also accomplished by N-linked glycans. The modification of an N-linked glycan with a
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linked glycosidically". However, in practice the term glycan may also be used to refer to the
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Attachment sides can be analysed by tandem MS experiments (side-specific glycan analysis).
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High-resolution mass spectrometry (MS) and high-performance liquid chromatography (HPLC)
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N-linked glycans are extremely important in proper protein folding in eukaryotic cells.
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Dwek, Raymond A. (1996). "Glycobiology: Toward Understanding the Function of Sugars".
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N-linked glycans also contribute to protein folding by steric effects. For example,
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Useful for complex glycan mixtures (generation of a further analysis dimension).
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The following are examples of the commonly used techniques in glycan analysis:
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10.1002/1097-0231(20001130)14:22<2135::AID-RCM143>3.0.CO;2-#
1108: 994: 1439: 868: 766: 758: 684: 676: 664: 477: 295: 265: 1717: 1681: 1300: 1283: 1258: 1157: 1065:, a web resource maintained through a partnership between the CFG and 815::Advantages and disadvantages of mass spectrometry in glycan analysis 1062: 922: 918: 607: 520: 461: 291: 257: 185: 177: 20: 260:. The sequon is an Asn-X-Ser or Asn-X-Thr sequence, where X is any 1893: 985: 895: 793: 785: 777: 576: 402: 307: 137: 510:
A common structural theme in O-linked glycans is the addition of
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proper protein folding. These processing reactions occur in the
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https://www.ncbi.nlm.nih.gov/books/bv.fcgi?rid=glyco.figgrp.562
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https://www.ncbi.nlm.nih.gov/books/bv.fcgi?rid=glyco.figgrp.561
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https://www.ncbi.nlm.nih.gov/books/bv.fcgi?rid=glyco.figgrp.469
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as synonyms meaning "compounds consisting of a large number of
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of these cells into the surrounding tissue during infection.
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residue is also added, to the next to penultimate residue, a
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In eukaryotes, N-linked glycans are derived from a core 14-
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of monosaccharide residues, and can be linear or branched.
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residue of a peptide chain in the Golgi apparatus. Unlike
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Wada Y, Azadi P, Costello CE, et al. (April 2007).
1284:"N-Glycan Profile and Kidney Disease in Type 1 Diabetes" 1028: 460:-linked glycans are assembled one sugar at a time on a 835:
Applicable for small sample amounts (lower fmol range)
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The first monosaccharide attached in the synthesis of
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SLex is also important to proper immune response. P-
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Transforming Glycoscience: A Roadmap for the Future
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Transforming Glycoscience: A Roadmap for the Future
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Transforming Glycoscience: A Roadmap for the Future
817: 56:. Unsourced material may be challenged and removed. 409:as a sign that the cell in question is cancerous. 222:but may also be found, although less commonly, in 1363:"U.S. National Research Council Report-in-Brief, 1311:20.500.11820/413dce5a-e852-4787-aac9-62c2c6d4389f 1181: 1179: 1177: 1175: 986:National Center for Functional Glycomics (NCFG) 898:-labeled sugars which can be reacted using the 382:proteins in the endoplasmic reticulum, such as 776:(HPLC) instruments can be further analyzed by 1874: 1282:Gornik, O; McKeigue, PM; Colhoun, HM (2018). 915:nuclear magnetic resonance (NMR) spectroscopy 8: 1739:Ruhaak LR, Deelder AM, Wuhrer M (May 2009). 1086:. This site provides information about the 844:Glycan sequencing by tandem MS experiments. 519:residue (similar to neuraminic acid). If a 1959: 1881: 1867: 1859: 890:Metabolic and covalent labeling of glycans 2127: 1815: 1797: 1756: 1600: 1582: 1471: 1438: 1309: 1299: 1257: 1211: 1090:'s reports and workshops on glycoscience. 252:to the nitrogen (N) in the side chain of 116:Learn how and when to remove this message 1334:"U.S. National Research Council Report, 878:Glycan arrays, like that offered by the 176:is a glycan (or, to be more specific, a 2102:Emanual Maverakis; et al. (2015). 1100: 655:Another type of cellular glycan is the 357:Processing, modification, and diversity 1046:, NIH funded glycoinformatics resource 774:high-performance liquid chromatography 746:The most commonly applied methods are 507: : Core 3 and Core 4 generation. 164:, even if the carbohydrate is only an 939:PAGE (polyacrylamide electrophoresis) 854:Need of a proper experimental design. 248:N-Linked glycans are attached in the 188:is a glycan composed of β-1,4-linked 7: 168:. Glycans usually consist solely of 54:adding citations to reliable sources 1786:Molecular & Cellular Proteomics 1419:TrAC Trends in Analytical Chemistry 1051:Consortium for Functional Glycomics 880:Consortium for Functional Glycomics 472:-linked glycans, there is no known 804:Multiple reaction monitoring (MRM) 268:and the glycan may be composed of 14: 1039:Swiss Institute of Bioinformatics 476:yet. However, the placement of a 172:of monosaccharides. For example, 687:residue to a protein (forming a 30: 1023:Carbohydrate Structure Database 663:, and include polymers such as 575:-linked glycans, in particular 41:needs additional citations for 1088:U.S. National Research Council 1084:U.S. National Research Council 1057:that work together to develop 796:-MS, electrospray ionisation ( 734:Tools used for glycan research 705:U.S. National Research Council 1: 1509:10.1016/S0006-291X(78)80037-0 1497:Biochem. Biophys. Res. Commun 1250:10.1016/j.jchromb.2007.03.003 1006:, Glycan structure repository 999:protocols for glycan analysis 991:resources for glycan analysis 542:blood antigen determination. 421:The targeting of degradative 298:, and other monosaccharides. 196:-glucosamine. Glycans can be 1063:Functional Glycomics Gateway 1031:, Australian glycan database 527:(SLex) structure is formed. 432:mannose-6-phosphate receptor 1627:Rapid Commun. Mass Spectrom 1055:participating investigators 800:) is more frequently used. 214:Glycan-protein interactions 180:) composed of β-1,4-linked 2191: 2120:10.1016/j.jaut.2014.12.002 1841:Essentials of Glycobiology 1431:10.1016/j.trac.2017.12.015 1393:Essentials of Glycobiology 1204:10.1016/j.jaut.2014.12.002 772:Fractionated glycans from 648: 444: 236: 211: 18: 16:Class of organic compounds 1758:10.1007/s00216-009-2664-5 1584:10.3389/fchem.2022.999770 1113:IUPAC Gold Book - Glycans 1025:, Russian glycan database 943:capillary electrophoresis 729:glycophosphatidylinositol 610:involved in formation of 565:and helps to mediate the 334:oligosaccharyltransferase 325:residues are attached to 1544:10.1016/j.ab.2008.09.041 1019:, German glycan database 947:affinity electrophoresis 531:Functions and importance 374:Functions and importance 19:Not to be confused with 2108:Journal of Autoimmunity 2084:Sphingosine-1-phosphate 1910:metabolic intermediates 1799:10.1074/mcp.M113.028878 1121:10.1351/goldbook.G02645 1067:Nature Publishing Group 931:affinity chromatography 906:Tools for glycoproteins 703:A 2012 report from the 2170:Carbohydrate chemistry 1571:Frontiers in Chemistry 1059:resources and services 447:O-linked glycosylation 327:dolichol monophosphate 310:unit assembled in the 239:N-linked glycosylation 2007:Globotriaosylceramide 1473:10.1093/glycob/cwl086 1037:, glycan database by 995:training in glycomics 933:etc.) and analytical 911:X-ray crystallography 873:monoclonal antibodies 639:plasminogen activator 340:-acetylglucosamine). 316:endoplasmic reticulum 250:endoplasmic reticulum 170:O-glycosidic linkages 606:Mucin, a protein in 551:Weibel-Palade bodies 407:Natural Killer cells 273:-acetylgalactosamine 208:Glycans and proteins 50:improve this article 1639:2000RCMS...14.2135H 974:Glycosyltransferase 964:Glycoside hydrolase 900:Staudinger ligation 851:Destructive method. 427:mannose-6-phosphate 331:glycosyltransferase 2045:Galactocerebroside 1931:Galactocerebroside 1906:glycosphingolipids 1078:2014-10-20 at the 1015:2021-02-11 at the 712:Glycans and lipids 657:glycosaminoglycans 645:Glycosaminoglycans 474:consensus sequence 323:-acetylglucosamine 288:-acetylglucosamine 2092: 2091: 2072: 2071: 1851:978-0-87969-559-0 1745:Anal Bioanal Chem 1718:10.1021/ac070363i 1682:10.1021/ac025890a 1301:10.2337/dc17-1042 1158:10.1021/cr940283b 1130:978-0-9678550-9-7 860: 859: 782:mass spectrometry 651:Glycosaminoglycan 349:Dark squares are 195: 183: 126: 125: 118: 100: 2182: 2155:Oligosaccharides 2141: 2131: 2026:Glucocerebroside 1960: 1943:Lactosylceramide 1936:Glucocerebroside 1883: 1876: 1869: 1860: 1855: 1830: 1829: 1819: 1801: 1777: 1771: 1770: 1760: 1736: 1730: 1729: 1700: 1694: 1693: 1665: 1659: 1658: 1621: 1615: 1614: 1604: 1586: 1562: 1556: 1555: 1527: 1521: 1520: 1492: 1486: 1485: 1475: 1451: 1445: 1444: 1442: 1414: 1408: 1407: 1388: 1382: 1381: 1379: 1378: 1369:. Archived from 1359: 1353: 1352: 1350: 1349: 1340:. Archived from 1330: 1324: 1323: 1313: 1303: 1278: 1272: 1271: 1261: 1244:(1–2): 133–137. 1238:J. Chromatogr. B 1232: 1226: 1225: 1215: 1183: 1170: 1169: 1141: 1135: 1134: 1105: 1010:Glycosciences.DE 818: 538:is important in 193: 181: 121: 114: 110: 107: 101: 99: 58: 34: 26: 2190: 2189: 2185: 2184: 2183: 2181: 2180: 2179: 2145: 2144: 2101: 2098: 2093: 2088: 2068: 2049: 2030: 2011: 1992: 1955: 1947: 1912: 1890:Glycoconjugates 1887: 1852: 1837: 1834: 1833: 1779: 1778: 1774: 1738: 1737: 1733: 1702: 1701: 1697: 1676:(23): 6088–97. 1667: 1666: 1662: 1633:(22): 2135–42. 1623: 1622: 1618: 1564: 1563: 1559: 1529: 1528: 1524: 1494: 1493: 1489: 1453: 1452: 1448: 1416: 1415: 1411: 1404: 1403:978-087969770-9 1390: 1389: 1385: 1376: 1374: 1361: 1360: 1356: 1347: 1345: 1332: 1331: 1327: 1280: 1279: 1275: 1234: 1233: 1229: 1185: 1184: 1173: 1143: 1142: 1138: 1131: 1107: 1106: 1102: 1097: 1080:Wayback Machine 1017:Wayback Machine 982: 955: 935:electrophoresis 908: 892: 865: 806: 744: 736: 725: 714: 701: 669:heparan sulfate 653: 647: 597:, a protein in 533: 512:polylactosamine 486: 456:In eukaryotes, 454: 449: 443: 441:-Linked glycans 376: 368:neuraminic acid 364:Golgi apparatus 359: 304: 281:neuraminic acid 246: 241: 235: 233:-Linked glycans 216: 210: 166:oligosaccharide 142:monosaccharides 136:are defined by 134:polysaccharides 122: 111: 105: 102: 59: 57: 47: 35: 24: 17: 12: 11: 5: 2188: 2186: 2178: 2177: 2172: 2167: 2162: 2157: 2147: 2146: 2143: 2142: 2097: 2096:External links 2094: 2090: 2089: 2087: 2086: 2080: 2078: 2074: 2073: 2070: 2069: 2067: 2066: 2060: 2058: 2051: 2050: 2048: 2047: 2041: 2039: 2032: 2031: 2029: 2028: 2022: 2020: 2013: 2012: 2010: 2009: 2003: 2001: 1994: 1993: 1991: 1990: 1985: 1980: 1975: 1969: 1967: 1957: 1949: 1948: 1946: 1945: 1940: 1939: 1938: 1933: 1922: 1920: 1914: 1913: 1888: 1886: 1885: 1878: 1871: 1863: 1857: 1856: 1850: 1832: 1831: 1792:(4): 921–931. 1772: 1731: 1712:(13): 5051–7. 1695: 1660: 1616: 1557: 1522: 1487: 1446: 1409: 1402: 1383: 1354: 1325: 1273: 1227: 1171: 1152:(2): 683–720. 1136: 1129: 1099: 1098: 1096: 1093: 1092: 1091: 1070: 1047: 1041: 1032: 1026: 1020: 1007: 1001: 981: 978: 977: 976: 971: 966: 961: 954: 951: 927:chromatography 907: 904: 891: 888: 871:or artificial 864: 861: 858: 857: 856: 855: 852: 847: 846: 845: 842: 839: 836: 830: 829: 824: 805: 802: 743: 740: 735: 732: 724: 721: 713: 710: 700: 697: 649:Main article: 646: 643: 642: 641: 635: 630: 625: 623:Thrombospondin 620: 614: 604: 602:cell membranes 536:Sialyl lewis x 532: 529: 525:Sialyl-Lewis X 485: 482: 453: 450: 445:Main article: 442: 436: 375: 372: 358: 355: 303: 300: 245: 242: 237:Main article: 234: 228: 209: 206: 202:heteropolymers 184:-glucose, and 150:glycoconjugate 124: 123: 38: 36: 29: 15: 13: 10: 9: 6: 4: 3: 2: 2187: 2176: 2173: 2171: 2168: 2166: 2165:Carbohydrates 2163: 2161: 2160:Glycoproteins 2158: 2156: 2153: 2152: 2150: 2139: 2135: 2130: 2125: 2121: 2117: 2113: 2109: 2105: 2100: 2099: 2095: 2085: 2082: 2081: 2079: 2075: 2065: 2062: 2061: 2059: 2057: 2052: 2046: 2043: 2042: 2040: 2038: 2033: 2027: 2024: 2023: 2021: 2019: 2018:sphingomyelin 2014: 2008: 2005: 2004: 2002: 2000: 1995: 1989: 1986: 1984: 1981: 1979: 1976: 1974: 1971: 1970: 1968: 1966: 1961: 1958: 1954: 1950: 1944: 1941: 1937: 1934: 1932: 1929: 1928: 1927: 1924: 1923: 1921: 1919: 1915: 1911: 1907: 1903: 1902:sphingolipids 1899: 1895: 1891: 1884: 1879: 1877: 1872: 1870: 1865: 1864: 1861: 1853: 1847: 1843: 1842: 1836: 1835: 1827: 1823: 1818: 1813: 1809: 1805: 1800: 1795: 1791: 1787: 1783: 1776: 1773: 1768: 1764: 1759: 1754: 1751:(1): 163–74. 1750: 1746: 1742: 1735: 1732: 1727: 1723: 1719: 1715: 1711: 1707: 1699: 1696: 1691: 1687: 1683: 1679: 1675: 1671: 1664: 1661: 1656: 1652: 1648: 1644: 1640: 1636: 1632: 1628: 1620: 1617: 1612: 1608: 1603: 1598: 1594: 1590: 1585: 1580: 1576: 1572: 1568: 1561: 1558: 1553: 1549: 1545: 1541: 1538:(2): 263–73. 1537: 1533: 1532:Anal. Biochem 1526: 1523: 1518: 1514: 1510: 1506: 1503:(1): 257–63. 1502: 1498: 1491: 1488: 1483: 1479: 1474: 1469: 1466:(4): 411–22. 1465: 1461: 1457: 1450: 1447: 1441: 1436: 1432: 1428: 1424: 1420: 1413: 1410: 1405: 1399: 1395: 1394: 1387: 1384: 1373:on 2015-09-23 1372: 1368: 1366: 1358: 1355: 1344:on 2014-10-20 1343: 1339: 1337: 1329: 1326: 1321: 1317: 1312: 1307: 1302: 1297: 1293: 1289: 1288:Diabetes Care 1285: 1277: 1274: 1269: 1265: 1260: 1255: 1251: 1247: 1243: 1239: 1231: 1228: 1223: 1219: 1214: 1209: 1205: 1201: 1197: 1193: 1189: 1182: 1180: 1178: 1176: 1172: 1167: 1163: 1159: 1155: 1151: 1147: 1140: 1137: 1132: 1126: 1122: 1118: 1114: 1110: 1104: 1101: 1094: 1089: 1085: 1081: 1077: 1074: 1071: 1068: 1064: 1060: 1056: 1052: 1048: 1045: 1042: 1040: 1036: 1033: 1030: 1027: 1024: 1021: 1018: 1014: 1011: 1008: 1005: 1002: 1000: 996: 992: 987: 984: 983: 979: 975: 972: 970: 969:Glycosylation 967: 965: 962: 960: 957: 956: 952: 950: 948: 944: 940: 936: 932: 928: 924: 920: 916: 912: 905: 903: 901: 897: 889: 887: 885: 884:Z Biotech LLC 881: 876: 874: 870: 862: 853: 850: 849: 848: 843: 840: 837: 834: 833: 832: 831: 828: 827:Disadvantages 825: 823: 820: 819: 816: 814: 810: 803: 801: 799: 795: 789: 787: 783: 779: 775: 770: 768: 763: 760: 755: 753: 749: 741: 739: 733: 731: 730: 722: 720: 719: 711: 709: 706: 698: 696: 694: 690: 686: 682: 678: 674: 670: 666: 662: 658: 652: 644: 640: 637:Urinary type 636: 634: 631: 629: 626: 624: 621: 618: 615: 613: 612:dental plaque 609: 605: 603: 600: 596: 593: 592: 591: 589: 588:glycoproteins 585: 580: 578: 574: 570: 568: 567:extravasation 564: 560: 556: 555:peptidoglycan 552: 549:release from 548: 543: 541: 537: 530: 528: 526: 522: 518: 513: 508: 506: 502: 500: 496: 493: 491: 483: 481: 479: 475: 471: 467: 463: 459: 451: 448: 440: 437: 435: 433: 428: 424: 419: 416: 410: 408: 404: 399: 396: 391: 389: 385: 381: 373: 371: 369: 365: 356: 354: 352: 347: 346: 341: 339: 335: 332: 328: 324: 322: 318:. First, two 317: 313: 309: 301: 299: 297: 293: 289: 287: 282: 278: 274: 272: 267: 263: 259: 256:(Asn) in the 255: 251: 243: 240: 232: 229: 227: 225: 221: 215: 207: 205: 203: 199: 191: 187: 179: 175: 171: 167: 163: 159: 155: 151: 148:portion of a 147: 143: 139: 135: 131: 120: 117: 109: 98: 95: 91: 88: 84: 81: 77: 74: 70: 67: â€“  66: 62: 61:Find sources: 55: 51: 45: 44: 39:This article 37: 33: 28: 27: 22: 2111: 2107: 1840: 1789: 1785: 1775: 1748: 1744: 1734: 1709: 1705: 1698: 1673: 1669: 1663: 1630: 1626: 1619: 1574: 1570: 1560: 1535: 1531: 1525: 1500: 1496: 1490: 1463: 1460:Glycobiology 1459: 1449: 1422: 1418: 1412: 1392: 1386: 1375:. Retrieved 1371:the original 1364: 1357: 1346:. Retrieved 1342:the original 1335: 1328: 1294:(1): 79–87. 1291: 1287: 1276: 1241: 1237: 1230: 1195: 1191: 1149: 1145: 1139: 1112: 1103: 1035:GlycoSuiteDB 909: 893: 877: 866: 826: 821: 812: 811: 807: 790: 771: 764: 756: 745: 737: 726: 715: 702: 699:Glycoscience 693:proteoglycan 689:glycoprotein 661:uronic acids 654: 583: 582:Examples of 581: 572: 571: 544: 534: 509: 503: 497: 494: 489: 487: 469: 457: 455: 452:Introduction 438: 420: 411: 405:receptor on 400: 392: 388:calreticulin 377: 360: 350: 348: 342: 337: 320: 305: 285: 270: 247: 244:Introduction 230: 217: 189: 162:proteoglycan 154:glycoprotein 152:, such as a 146:carbohydrate 129: 127: 112: 103: 93: 86: 79: 72: 60: 48:Please help 43:verification 40: 2056:sphingosine 1965:ganglioside 1953:Ganglioside 1926:Cerebroside 1898:glycolipids 1854:. NBK20709. 1440:1874/364403 1198:(6): 1–13. 1192:J Autoimmun 993:as well as 792:instead of 723:GPI-Anchors 718:glycolipids 673:chondroitin 599:erythrocyte 595:Glycophorin 563:bloodstream 559:neutrophils 517:sialic acid 224:prokaryotes 2149:Categories 1706:Anal. Chem 1670:Anal. Chem 1577:: 999770. 1377:2012-10-03 1348:2012-10-03 1259:2115/28276 1095:References 822:Advantages 628:Factor VII 262:amino acid 254:asparagine 220:eukaryotes 212:See also: 158:glycolipid 128:The terms 76:newspapers 2175:Glycomics 2037:sulfatide 1999:globoside 1808:1535-9484 1593:2296-2646 1146:Chem. Rev 1109:"Glycans" 1029:UniCarbKB 1004:GlyTouCan 980:Resources 959:Glycoside 949:, etc.). 633:Factor IX 466:threonine 423:lysosomal 380:Chaperone 312:cytoplasm 277:galactose 174:cellulose 2138:25578468 2114:: 1–13. 2064:Ceramide 1918:Ceramide 1826:23457413 1767:19247642 1726:17539604 1690:12498206 1655:11114021 1611:36262345 1552:18940176 1482:17223647 1425:: 7–14. 1320:29146600 1268:17392038 1222:25578468 1166:11848770 1115:. 2009. 1076:Archived 1013:Archived 953:See also 681:dermatan 586:-linked 547:selectin 495:Images: 484:Assembly 395:cysteine 384:calnexin 302:Assembly 192:-acetyl- 106:May 2012 65:"Glycan" 2129:4340844 1956:pathway 1817:3617339 1635:Bibcode 1602:9574008 1213:4340844 1082:by the 923:enzymes 919:lectins 869:lectins 813:Table 1 767:glycans 759:glycans 685:xylosyl 677:keratan 665:heparin 561:in the 478:proline 343:Image: 296:mannose 266:proline 264:except 160:, or a 130:glycans 90:scholar 2136:  2126:  1908:, and 1896:, and 1894:lipids 1848:  1824:  1814:  1806:  1765:  1724:  1688:  1653:  1609:  1599:  1591:  1550:  1517:743278 1515:  1480:  1400:  1318:  1266:  1220:  1210:  1164:  1127:  1044:GlyGen 863:Arrays 608:saliva 521:fucose 462:serine 292:fucose 258:sequon 186:chitin 178:glucan 92:  85:  78:  71:  63:  21:Glucan 2077:Other 2035:From 2016:From 1997:From 1963:From 896:azide 794:MALDI 786:MALDI 778:MALDI 617:Notch 590:are: 577:mucin 403:CD337 308:sugar 198:homo- 138:IUPAC 97:JSTOR 83:books 2134:PMID 1904:and 1846:ISBN 1822:PMID 1804:ISSN 1763:PMID 1722:PMID 1686:PMID 1651:PMID 1607:PMID 1589:ISSN 1548:PMID 1513:PMID 1478:PMID 1398:ISBN 1316:PMID 1264:PMID 1218:PMID 1162:PMID 1125:ISBN 1049:The 997:and 913:and 882:and 752:HPLC 750:and 727:See 716:See 679:and 386:and 314:and 132:and 69:news 2124:PMC 2116:doi 2054:To 1988:GD2 1983:GM3 1978:GM2 1973:GM1 1812:PMC 1794:doi 1753:doi 1749:394 1714:doi 1678:doi 1643:doi 1597:PMC 1579:doi 1540:doi 1536:384 1505:doi 1468:doi 1435:hdl 1427:doi 1423:100 1306:hdl 1296:doi 1254:hdl 1246:doi 1242:853 1208:PMC 1200:doi 1154:doi 1117:doi 798:ESI 695:). 691:or 540:ABO 464:or 200:or 52:by 2151:: 2132:. 2122:. 2112:57 2110:. 2106:. 1900:: 1892:, 1820:. 1810:. 1802:. 1790:12 1788:. 1784:. 1761:. 1747:. 1743:. 1720:. 1710:79 1708:. 1684:. 1674:74 1672:. 1649:. 1641:. 1631:14 1629:. 1605:. 1595:. 1587:. 1575:10 1573:. 1569:. 1546:. 1534:. 1511:. 1501:85 1499:. 1476:. 1464:17 1462:. 1458:. 1433:. 1421:. 1314:. 1304:. 1292:41 1290:. 1286:. 1262:. 1252:. 1240:. 1216:. 1206:. 1196:57 1194:. 1190:. 1174:^ 1160:. 1150:96 1148:. 1123:. 1111:. 945:, 941:, 921:, 765:O- 757:N- 748:MS 675:, 671:, 667:, 415:Fc 294:, 290:, 283:, 279:, 275:, 226:. 156:, 2140:. 2118:: 1882:e 1875:t 1868:v 1828:. 1796:: 1769:. 1755:: 1728:. 1716:: 1692:. 1680:: 1657:. 1645:: 1637:: 1613:. 1581:: 1554:. 1542:: 1519:. 1507:: 1484:. 1470:: 1443:. 1437:: 1429:: 1406:. 1380:. 1367:" 1351:. 1338:" 1322:. 1308:: 1298:: 1270:. 1256:: 1248:: 1224:. 1202:: 1168:. 1156:: 1133:. 1119:: 1069:. 937:( 929:( 584:O 573:O 490:O 470:N 458:O 439:O 351:N 338:N 321:N 286:N 271:N 231:N 194:D 190:N 182:D 119:) 113:( 108:) 104:( 94:· 87:· 80:· 73:· 46:. 23:.

Index

Glucan

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polysaccharides
IUPAC
monosaccharides
carbohydrate
glycoconjugate
glycoprotein
glycolipid
proteoglycan
oligosaccharide
O-glycosidic linkages
cellulose
glucan
chitin
homo-
heteropolymers
Glycan-protein interactions
eukaryotes
prokaryotes

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