1266:. The first consideration for this method is the choice of host, as there are many different factors that can influence the success of glycoprotein recombination such as cost, the host environment, the efficacy of the process, and other considerations. Some examples of host cells include E. coli, yeast, plant cells, insect cells, and mammalian cells. Of these options, mammalian cells are the most common because their use does not face the same challenges that other host cells do such as different glycan structures, shorter half life, and potential unwanted immune responses in humans. Of mammalian cells, the most common cell line used for recombinant glycoprotein production is the
462:
760:
antibodies to recognise the HIV glycans and almost all so-called 'broadly neutralising antibodies (bnAbs) recognise some glycans. This is possible mainly because the unusually high density of glycans hinders normal glycan maturation and they are therefore trapped in the premature, high-mannose, state. This provides a window for immune recognition. In addition, as these glycans are much less variable than the underlying protein, they have emerged as promising targets for vaccine design.
301:
133:-linked glycoproteins. These two types of glycoproteins are distinguished by structural differences that give them their names. Glycoproteins vary greatly in composition, making many different compounds such as antibodies or hormones. Due to the wide array of functions within the body, interest in glycoprotein synthesis for medical use has increased. There are now several methods to synthesize glycoproteins, including recombination and glycosylation of proteins.
118:, is dispensable for isolated cells (as evidenced by survival with glycosides inhibitors) but can lead to human disease (congenital disorders of glycosylation) and can be lethal in animal models. It is therefore likely that the fine processing of glycans is important for endogenous functionality, such as cell trafficking, but that this is likely to have been secondary to its role in host-pathogen interactions. A famous example of this latter effect is the
1255:
3340:
37:
767:
cell, causing a decrease in drug effectiveness. Therefore, being able to inhibit this behavior would decrease P-glycoprotein interference in drug delivery, making this an important topic in drug discovery. For example, P-Glycoprotein causes a decrease in anti-cancer drug accumulation within tumor cells, limiting the effectiveness of chemotherapies used to treat cancer.
110:
glycosylation can be structurally essential. For example, inhibition of asparagine-linked, i.e. N-linked, glycosylation can prevent proper glycoprotein folding and full inhibition can be toxic to an individual cell. In contrast, perturbation of glycan processing (enzymatic removal/addition of carbohydrate residues to the glycan), which occurs in both the
1291:. These two methods are examples of natural linkage. However, there are also methods of unnatural linkages. Some methods include ligation and a reaction between a serine-derived sulfamidate and thiohexoses in water. Once this linkage is complete, the amino acid sequence can be expanded upon using solid-phase peptide synthesis.
825:
A glycoprotein is a compound containing carbohydrate (or glycan) covalently linked to protein. The carbohydrate may be in the form of a monosaccharide, disaccharide(s). oligosaccharide(s), polysaccharide(s), or their derivatives (e.g. sulfo- or phospho-substituted). One, a few, or many carbohydrate
766:
are critical for antitumor research due to its ability block the effects of antitumor drugs. P-glycoprotein, or multidrug transporter (MDR1), is a type of ABC transporter that transports compounds out of cells. This transportation of compounds out of cells includes drugs made to be delivered to the
594:
The unique interaction between the oligosaccharide chains have different applications. First, it aids in quality control by identifying misfolded proteins. The oligosaccharide chains also change the solubility and polarity of the proteins that they are bonded to. For example, if the oligosaccharide
1278:
The formation of the link between the glycan and the protein is key element of the synthesis of glycoproteins. The most common method of glycosylation of N-linked glycoproteins is through the reaction between a protected glycan and a protected
Asparagine. Similarly, an O-linked glycoprotein can be
1230:
The glycosylation of proteins has an array of different applications from influencing cell to cell communication to changing the thermal stability and the folding of proteins. Due to the unique abilities of glycoproteins, they can be used in many therapies. By understanding glycoproteins and their
1179:, protein-carbohydrate ratio, aggregation state, size, and sometimes branching of a glycan chain. In conjunction with composition-gradient analysis, analyzes self- and hetero-association to determine binding affinity and stoichiometry with proteins or carbohydrates in solution without labeling.
109:
and nucleus can be modified through the reversible addition of a single GlcNAc residue that is considered reciprocal to phosphorylation and the functions of these are likely to be an additional regulatory mechanism that controls phosphorylation-based signalling. In contrast, classical secretory
759:
The viral spike of the human immunodeficiency virus is heavily glycosylated. Approximately half the mass of the spike is glycosylation and the glycans act to limit antibody recognition as the glycans are assembled by the host cell and so are largely 'self'. Over time, some patients can evolve
585:
is the study of the carbohydrate components of cells. Though not exclusive to glycoproteins, it can reveal more information about different glycoproteins and their structure. One of the purposes of this field of study is to determine which proteins are glycosylated and where in the amino acid
595:
chains are negatively charged, with enough density around the protein, they can repulse proteolytic enzymes away from the bonded protein. The diversity in interactions lends itself to different types of glycoproteins with different structures and functions.
1242:, meaning it happens after the production of the protein. Glycosylation is a process that roughly half of all human proteins undergo and heavily influences the properties and functions of the protein. Within the cell, glycosylation occurs in the
574:, or on the outer surface of the plasma membrane, and make up a large portion of the proteins secreted by eukaryotic cells. They are very broad in their applications and can function as a variety of chemicals from antibodies to hormones.
105:, where they play a role in cell–cell interactions. It is important to distinguish endoplasmic reticulum-based glycosylation of the secretory system from reversible cytosolic-nuclear glycosylation. Glycoproteins of the
570:
Glycoprotein size and composition can vary largely, with carbohydrate composition ranges from 1% to 70% of the total mass of the glycoprotein. Within the cell, they appear in the blood, the
1702:
Stepper J, Shastri S, Loo TS, Preston JC, Novak P, Man P, et al. (February 2011). "Cysteine S-glycosylation, a new post-translational modification found in glycopeptide bacteriocins".
602:, which are secreted in the mucus of the respiratory and digestive tracts. The sugars when attached to mucins give them considerable water-holding capacity and also make them resistant to
2345:
586:
sequence the glycosylation occurs. Historically, mass spectrometry has been used to identify the structure of glycoproteins and characterize the carbohydrate chains attached.
2994:
287:, also known as non-enzymatic glycosylation, sugars are covalently bonded to a protein or lipid molecule, without the controlling action of an enzyme, but through a
247:
229:
211:
101:
In proteins that have segments extending extracellularly, the extracellular segments are also often glycosylated. Glycoproteins are also often important
1767:
3166:
2987:
1088:
Resultant shifts in electrophoretic migration help distinguish among proteins with N-glycan, O-glycan, or GPI linkages and also between high
3144:
3133:
833:
in which the carbohydrate units are polysaccharides that contain amino sugars. Such polysaccharides are also known as glycosaminoglycans.
1653:"Three Decades of Research on O-GlcNAcylation - A Major Nutrient Sensor That Regulates Signaling, Transcription and Cellular Metabolism"
2369:
2353:
1270:
line. However, as technologies develop, the most promising cell lines for recombinant glycoprotein production are human cell lines.
3183:
2980:
1155:, composition, sequence, and sometimes branching of a glycan chain. It can also be used for site-specific glycosylation profiling.
2437:
2317:
1573:
1503:
1175:
In conjunction with size-exclusion chromatography, UV/Vis absorption and differential refractometry, provides information on
3207:
3159:
2814:
2305:
1930:"Glycan clustering stabilizes the mannose patch of HIV-1 and preserves vulnerability to broadly neutralizing antibodies"
2261:
Maverakis E, Kim K, Shimoda M, Gershwin ME, Patel F, Wilken R, Raychaudhuri S, Ruhaak LR, Lebrilla CB (February 2015).
1189:
Measures the mechanisms underlying the biomolecular interactions, including reaction rates, affinities and associated
2854:
2704:
1184:
634:
3365:
3217:
3152:
1239:
1108:
87:
2972:
749:
3174:
2415:
1170:
908:
797:
782:
1840:"Complete purification and characterization of the taste-modifying protein, miraculin, from miracle fruit"
1764:
3239:
2951:
2430:
2381:
792:
1987:"Composition and Antigenic Effects of Individual Glycan Sites of a Trimeric HIV-1 Envelope Glycoprotein"
3330:
3202:
3179:
2941:
1267:
1048:
102:
3175:
3038:
2904:
2864:
269:
1165:
To identify specific sugars, their sequence, linkages, and the anomeric nature of glycosidic chain.
2844:
2819:
2338:
1928:
Pritchard LK, Spencer DI, Royle L, Bonomelli C, Seabright GE, Behrens AJ, et al. (June 2015).
1121:
1031:
A variety of methods used in detection, purification, and structural analysis of glycoproteins are
3088:
3007:
1985:
Behrens AJ, Vasiljevic S, Pritchard LK, Harvey DJ, Andev RS, Krumm SA, et al. (March 2016).
1879:
Pritchard LK, Vasiljevic S, Ozorowski G, Seabright GE, Cupo A, Ringe R, et al. (June 2015).
972:
529:
412:
3360:
3255:
2879:
2423:
2263:"Glycans in the immune system and The Altered Glycan Theory of Autoimmunity: a critical review"
2171:"Glycans in the immune system and The Altered Glycan Theory of Autoimmunity: a critical review"
181:
163:
119:
83:
3306:
1787:
Dell A, Morris HR (March 2001). "Glycoprotein structure determination by mass spectrometry".
1243:
1190:
1104:
737:
656:
521:
384:
111:
2169:
Maverakis E, Kim K, Shimoda M, Gershwin ME, Patel F, Wilken R, et al. (February 2015).
649:
H antigen of the ABO blood compatibility antigens. Other examples of glycoproteins include:
1941:
1796:
1306:
571:
8:
3124:
2884:
2809:
2696:
2673:
2637:
2609:
2334:
787:
399:
1945:
1800:
3272:
3059:
2834:
2287:
2262:
2195:
2170:
2140:"Nomenclature of glycoproteins, glycopeptides and peptidoglycans, Recommendations 1985"
2121:
2064:
2040:"Targeting host-derived glycans on enveloped viruses for antibody-based vaccine design"
2039:
2011:
1986:
1962:
1929:
1905:
1880:
1820:
1727:
1679:
1652:
1262:
There are several techniques for the assembly of glycoproteins. One technique utilizes
1232:
947:
897:
1856:
1839:
1616:
Gamblin DP, Scanlan EM, Davis BG (January 2009). "Glycoprotein synthesis: an update".
158:
There are several types of glycosylation, although the first two are the most common.
3317:
3289:
3277:
3222:
3076:
2909:
2738:
2392:
2313:
2292:
2238:
2200:
2113:
2069:
2016:
1967:
1910:
1861:
1812:
1719:
1684:
1633:
1579:
1569:
1509:
1499:
1451:
1410:
1213:
1146:
1063:
802:
690:
686:
509:
288:
95:
2139:
2125:
1824:
1731:
693:. They may also help components of the tissue bind to inorganic substances, such as
3187:
3081:
2824:
2641:
2594:
2282:
2274:
2230:
2190:
2182:
2103:
2059:
2051:
2006:
1998:
1957:
1949:
1900:
1892:
1851:
1804:
1711:
1674:
1664:
1625:
1441:
1400:
1301:
1160:
610:
218:
1715:
3028:
2781:
2753:
2669:
2404:
2055:
2002:
1896:
1771:
1446:
1429:
1366:
1263:
1075:
1054:
999:
513:
477:
461:
450:
417:
115:
67:
1126:
Resultant shifts in electrophoretic migration help distinguish and characterize
3344:
3234:
3064:
2931:
2450:
2278:
2186:
1341:
1176:
1152:
1113:
To purify glycoproteins or glycopeptides that bind the particular lectin used.
1079:
807:
763:
671:
204:
3002:
1881:"Structural Constraints Determine the Glycosylation of HIV-1 Envelope Trimers"
1583:
1513:
3354:
3311:
3230:
3054:
2936:
2924:
2604:
1669:
1083:
883:
828:
614:
517:
481:
222:
200:
91:
71:
20:
2445:
1808:
1069:
Leads to detection of a radioactive sugar after electrophoretic separation.
3266:
2849:
2761:
2628:
2458:
2296:
2242:
2204:
2117:
2108:
2091:
2073:
2035:
2020:
1971:
1914:
1816:
1723:
1688:
1637:
1455:
1414:
1346:
1321:
989:
815:
725:
137:
79:
28:
24:
1865:
1141:
Identifies sugars that the glycoprotein contains and their stoichiometry.
3260:
3098:
3070:
2961:
2956:
2946:
2919:
2889:
2874:
2743:
2599:
2589:
2466:
1198:
920:
879:
664:
603:
532:(Neu5Ac). These glycans link themselves to specific areas of the protein
525:
422:
374:
277:
1238:
The process of glycosylation (binding a carbohydrate to a protein) is a
638:(or MHC), which are expressed on the surface of cells and interact with
3284:
3093:
3003:
2789:
1953:
1351:
1311:
1209:
1136:
1011:
1007:
552:
533:
389:
300:
273:
265:
240:
174:
125:
Though there are different types of glycoproteins, the most common are
75:
52:
2234:
2090:
Ambudkar SV, Kimchi-Sarfaty C, Sauna ZE, Gottesman MM (October 2003).
1629:
1405:
1388:
813:
689:. These help bind together the fibers, cells, and ground substance of
663:
that is required for normal platelet aggregation and adherence to the
2899:
2894:
2869:
2859:
2771:
1878:
1336:
1288:
1254:
1127:
745:
which alters human tongue receptors to recognize sour foods as sweet.
732:
721:
717:
582:
564:
505:
343:
284:
235:, sugars are attached directly to carbon, such as in the addition of
192:
140:
2089:
653:
gonadotropins (luteinizing hormone and follicle-stimulating hormone)
559:-linked glycoprotein has the sugar is bonded to an oxygen atom of a
551:-linked glycoprotein has glycan bonds to the nitrogen containing an
308:
Monosaccharides commonly found in eukaryotic glycoproteins include:
3339:
2718:
2713:
2708:
2686:
2681:
2659:
2654:
2614:
1280:
1018:
985:
964:
893:
859:
660:
622:
453:, improve proteins' stability and are involved in cell signalling.
258:
196:
144:
3114:
2766:
2649:
2446:
2306:"Carbohydrates Can Be Attached to Proteins to Form Glycoproteins"
1361:
1316:
1097:
1089:
924:
775:
694:
626:
501:
489:
438:
356:
328:
236:
106:
63:
1984:
3014:
2839:
2558:
2518:
1430:"Glycobiology in the cytosol: the bitter side of a sweet world"
1356:
1284:
1118:
1101:
960:
939:
675:
639:
560:
497:
493:
485:
484:
to a protein. There are 10 common monosaccharides in mammalian
476:
The critical structural element of all glycoproteins is having
433:
369:
333:
254:
188:
36:
1927:
1258:
Depiction of differences in glycans amongst different animals.
2733:
2728:
2573:
2568:
2563:
2553:
2548:
2543:
2523:
2508:
2503:
2488:
2475:
1326:
1130:, i.e. variants of a glycoprotein differing in carbohydrate.
942:), virus–cell, bacterium–cell, and hormone–cell interactions
935:
869:
742:
709:
679:
599:
170:
2046:. Viral pathogenesis • Preventive and therapeutic vaccines.
3033:
2914:
2829:
2723:
2538:
2533:
2528:
2513:
2498:
2493:
2483:
2260:
2168:
1331:
705:
698:
2346:"Biological Importance of the glycosylation of a protein"
1563:
1496:
2221:
Davis BG (February 2002). "Synthesis of glycoproteins".
1701:
1489:
1487:
1485:
1483:
1481:
1479:
1477:
1475:
1473:
1471:
1469:
1467:
1465:
1493:
1434:
Biochimica et
Biophysica Acta (BBA) - General Subjects
3328:
2370:"Carbohydrate Chemistry and Glycobiology: A Web Tour"
977:
Various proteins involved in hormone and drug action
1749:
1564:
Nelson DL, Cox MM, Hoskins AA, Lehninger AL (2013).
1462:
756:
parasite to escape the immune response of the host.
645:
sialyl Lewis X antigen on the surface of leukocytes.
169:, sugars are attached to nitrogen, typically on the
1615:
1062:Incubation of cultured cells with glycoproteins as
1035:Some important methods used to study glycoproteins
1017:Specific glycoproteins on the surface membranes of
2405:"Structure of Glycoprotein and Carbohydrate Chain"
2303:
1837:
598:One example of glycoproteins found in the body is
539:The two most common linkages in glycoproteins are
312:The principal sugars found in human glycoproteins
1559:
1557:
1555:
1553:
1551:
1549:
1547:
1545:
1543:
55:residues (Asn-x-Ser/Thr motifs) in glycoproteins.
3352:
2380:(5512): 2263–2502. 23 March 2001. Archived from
2164:
2162:
2160:
2085:
2083:
1831:
1541:
1539:
1537:
1535:
1533:
1531:
1529:
1527:
1525:
1523:
625:(immunoglobulins), which interact directly with
1427:
1386:
2409:Home Page for Learning Environmental Chemistry
1611:
1609:
1607:
1605:
1603:
1601:
1599:
1597:
1595:
1593:
934:Various proteins involved in cell–cell (e.g.,
613:recognition. Examples of glycoproteins in the
187:, sugars are attached to oxygen, typically on
3160:
2988:
2431:
2216:
2214:
2157:
2080:
2033:
1520:
1231:synthesis, they can be made to treat cancer,
1002:and its analogs, key proteins in development
304:Eight sugars commonly found in glycoproteins.
2092:"P-glycoprotein: from genomics to mechanism"
1782:
1780:
3134:N-acetylglucosamine-1-phosphate transferase
1590:
1389:"N-glycan processing in ER quality control"
555:amino acid within the protein sequence. An
3167:
3153:
2995:
2981:
2438:
2424:
2211:
1786:
1750:Murray RC, Granner DK, Rodwell VW (2006).
1053:Detects glycoproteins as pink bands after
952:Certain plasma proteins of coldwater fish
16:Protein with oligosaccharide modifications
2337:at the U.S. National Library of Medicine
2286:
2194:
2107:
2063:
2010:
1961:
1904:
1855:
1777:
1678:
1668:
1445:
1404:
911:(HCG), thyroid-stimulating hormone (TSH)
685:structural glycoproteins, which occur in
153:
2312:(5th ed.). New York: W.H. Freeman.
1838:Theerasilp S, Kurihara Y (August 1988).
1745:
1743:
1741:
1387:Ruddock LW, Molinari M (November 2006).
1253:
821:Quoting from recommendations for IUPAC:
716:Soluble glycoproteins often show a high
642:as part of the adaptive immune response.
460:
299:
136:Glycosylation is also known to occur on
35:
2744:Structural maintenance of chromosomes 3
2304:Berg JM, Tymoczko JL, Stryer L (2002).
1428:Funakoshi Y, Suzuki T (February 2009).
1373:
843:Some functions served by glycoproteins
3353:
1568:(Sixth ed.). Macmillan Learning.
1494:Picanco e Castro V, Swiech SH (2018).
1219:Determination of amino acid sequence.
1135:Compositional analysis following acid
814:Distinction between glycoproteins and
3148:
2976:
2419:
2220:
1738:
1204:To determine linkage between sugars.
957:Interact with specific carbohydrates
199:or non-canonical amino acids such as
3240:Pseudo-Hurler polydystrophy (ML III)
3208:Congenital disorder of glycosylation
1650:
1566:Lehninger Principles of Biochemistry
967:(cell adhesion lectins), antibodies
257:is attached to the sulfur atom of a
1844:The Journal of Biological Chemistry
982:Affect folding of certain proteins
735:, is a glycoprotein extracted from
13:
2253:
295:
14:
3377:
2855:Cholesterylester transfer protein
2705:Chondroitin sulfate proteoglycans
2328:
1752:Harper's Illustrated Biochemistry
1279:formed through the addition of a
931:Cell attachment-recognition site
449:The sugar group(s) can assist in
3338:
2352:. 15 August 2015. Archived from
1273:
1249:
1185:Dual Polarisation Interferometry
778:that are glycoproteins include:
635:major histocompatibility complex
609:Glycoproteins are important for
82:is attached to the protein in a
3218:Post-translational modification
2132:
2027:
1978:
1921:
1872:
1240:post-translational modification
866:Lubricant and protective agent
831:are a subclass of glycoproteins
280:, serving as a membrane anchor.
96:Secreted extracellular proteins
43:-linked protein glycosylation (
1758:
1695:
1644:
1421:
1380:
1235:, high cholesterol, and more.
1109:lectin affinity chromatography
750:Variable surface glycoproteins
712:) are HIV viral coat proteins.
272:glycolipid is attached to the
88:posttranslational modification
1:
2393:"Glycan Recognizing Proteins"
1857:10.1016/S0021-9258(18)37991-2
1754:(27th ed.). McGraw–Hill.
1716:10.1016/j.febslet.2011.01.023
2056:10.1016/j.coviro.2015.02.002
2003:10.1016/j.celrep.2016.02.058
1897:10.1016/j.celrep.2015.05.017
1447:10.1016/j.bbagen.2008.09.009
1225:
1171:Multi-angle light scattering
909:Human chorionic gonadotropin
837:
798:Human chorionic gonadotropin
783:Follicle-stimulating hormone
752:allow the sleeping sickness
577:
456:
7:
2952:Tumor necrosis factor alpha
2044:Current Opinion in Virology
1651:Hart GW (27 October 2014).
1294:
1074:Treatment with appropriate
1026:
793:Thyroid-stimulating hormone
770:
589:
567:amino acid in the protein.
90:. This process is known as
10:
3382:
3203:Dolichol kinase deficiency
3176:Lysosomal storage diseases
2942:Thyroxine-binding proteins
2279:10.1016/j.jaut.2014.12.002
2187:10.1016/j.jaut.2014.12.002
1657:Frontiers in Endocrinology
1049:Periodic acid-Schiff stain
996:Regulation of development
547:-linked glycoproteins. An
103:integral membrane proteins
18:
3298:
3248:
3216:
3195:
3123:
3107:
3047:
3039:Oligosaccharyltransferase
3021:
2905:Serum amyloid P component
2865:Colony-stimulating factor
2802:
2780:
2752:
2695:
2668:
2636:
2627:
2582:
2474:
2465:
217:, sugars are attached to
2845:B-cell activating factor
2820:Alpha 1-antichymotrypsin
2339:Medical Subject Headings
1670:10.3389/fendo.2014.00183
1151:Provides information on
1122:affinity electrophoresis
919:Various, e.g., alkaline
708:) and glycoprotein-120 (
143:proteins in the form of
98:are often glycosylated.
19:Not to be confused with
3184:carbohydrate metabolism
3089:Aspartylglucosaminidase
3008:carbohydrate metabolism
2267:Journal of Autoimmunity
2175:Journal of Autoimmunity
1809:10.1126/science.1058890
1770:27 October 2012 at the
1393:Journal of Cell Science
1283:donor with a protected
1092:and complex N-glycans.
678:, and is important for
659:, an integrin found on
530:N-acetylneuraminic acid
413:N-Acetylneuraminic acid
3366:Carbohydrate chemistry
3256:Aspartylglucosaminuria
3235:I-cell disease (ML II)
2880:Membrane glycoproteins
2386:Special Web Supplement
2109:10.1038/sj.onc.1206948
1259:
1191:conformational changes
835:
826:units may be present.
674:, which surrounds the
606:by digestive enzymes.
473:
305:
154:Types of glycosylation
120:ABO blood group system
56:
3307:solute carrier family
1934:Nature Communications
1765:Glycan classification
1268:Chinese hamster ovary
1257:
1244:endoplasmic reticulum
1105:column chromatography
890:Immunologic molecule
823:
738:Synsepalum dulcificum
657:glycoprotein IIb/IIIa
522:N-acetylgalactosamine
472:-linked glycoproteins
464:
418:Aminononulosonic acid
385:N-Acetylgalactosamine
303:
112:endoplasmic reticulum
39:
1399:(Pt 21): 4373–4380.
1374:Notes and references
1307:Female sperm storage
856:Structural molecule
808:Erythropoietin (EPO)
572:extracellular matrix
2885:Myelin protein zero
2810:Activin and inhibin
2610:Phytohaemagglutinin
2384:on 9 January 2008.
2356:on 30 November 2020
1946:2015NatCo...6.7479P
1850:(23): 11536–11539.
1801:2001Sci...291.2351D
1795:(5512): 2351–2356.
1201:(linkage) analysis
1036:
876:Transport molecule
844:
788:Luteinizing hormone
400:N-Acetylglucosamine
313:
3273:Alpha-mannosidosis
3060:Beta-galactosidase
2835:Asialoglycoprotein
1954:10.1038/ncomms8479
1260:
1034:
948:Antifreeze protein
898:histocompatibility
842:
720:, for example, in
670:components of the
621:molecules such as
474:
311:
306:
57:
47:-glycosylation of
3326:
3325:
3318:Galactosialidosis
3290:Schindler disease
3278:Beta-mannosidosis
3223:lysosomal enzymes
3142:
3141:
3077:alpha-Mannosidase
2970:
2969:
2910:Sialoglycoprotein
2798:
2797:
2739:Platelet factor 4
2623:
2622:
2319:978-0-7167-4684-3
2235:10.1021/cr0004310
2102:(47): 7468–7485.
1997:(11): 2695–2706.
1891:(10): 1604–1613.
1630:10.1021/cr078291i
1575:978-1-319-38149-3
1505:978-1-4939-7312-5
1406:10.1242/jcs.03225
1223:
1222:
1147:Mass spectrometry
1064:radioactive decay
1024:
1023:
803:Alpha-fetoprotein
704:Glycoprotein-41 (
691:connective tissue
687:connective tissue
682:-egg interaction.
632:molecules of the
510:acetylglucosamine
447:
446:
289:Maillard reaction
78:side-chains. The
3373:
3343:
3342:
3334:
3188:Glycoproteinoses
3169:
3162:
3155:
3146:
3145:
3082:beta-mannosidase
2997:
2990:
2983:
2974:
2973:
2825:Apolipoprotein H
2634:
2633:
2595:Intrinsic factor
2472:
2471:
2440:
2433:
2426:
2417:
2416:
2412:
2400:
2388:
2365:
2363:
2361:
2323:
2300:
2290:
2247:
2246:
2223:Chemical Reviews
2218:
2209:
2208:
2198:
2166:
2155:
2154:
2152:
2150:
2136:
2130:
2129:
2111:
2087:
2078:
2077:
2067:
2031:
2025:
2024:
2014:
1982:
1976:
1975:
1965:
1925:
1919:
1918:
1908:
1876:
1870:
1869:
1859:
1835:
1829:
1828:
1784:
1775:
1762:
1756:
1755:
1747:
1736:
1735:
1699:
1693:
1692:
1682:
1672:
1648:
1642:
1641:
1618:Chemical Reviews
1613:
1588:
1587:
1561:
1518:
1517:
1491:
1460:
1459:
1449:
1425:
1419:
1418:
1408:
1384:
1161:NMR spectroscopy
1037:
1033:
845:
841:
611:white blood cell
478:oligosaccharides
314:
310:
3381:
3380:
3376:
3375:
3374:
3372:
3371:
3370:
3351:
3350:
3349:
3337:
3329:
3327:
3322:
3294:
3244:
3220:
3212:
3191:
3173:
3143:
3138:
3119:
3103:
3043:
3029:Dolichol kinase
3017:
3001:
2971:
2966:
2794:
2776:
2748:
2691:
2664:
2619:
2578:
2461:
2444:
2403:
2391:
2368:
2359:
2357:
2344:
2331:
2326:
2320:
2256:
2254:Further reading
2251:
2250:
2219:
2212:
2167:
2158:
2148:
2146:
2138:
2137:
2133:
2088:
2081:
2032:
2028:
1983:
1979:
1926:
1922:
1877:
1873:
1836:
1832:
1785:
1778:
1772:Wayback Machine
1763:
1759:
1748:
1739:
1700:
1696:
1649:
1645:
1614:
1591:
1576:
1562:
1521:
1506:
1492:
1463:
1426:
1422:
1385:
1381:
1376:
1371:
1367:Monosaccharides
1297:
1276:
1252:
1233:Crohn's Disease
1228:
1055:electrophoretic
1029:
894:Immunoglobulins
840:
819:
773:
764:P-glycoproteins
592:
580:
514:glucuronic acid
459:
451:protein folding
420:
298:
296:Monosaccharides
156:
116:Golgi apparatus
84:cotranslational
70:(sugar) chains
68:oligosaccharide
32:
17:
12:
11:
5:
3379:
3369:
3368:
3363:
3348:
3347:
3324:
3323:
3321:
3320:
3315:
3302:
3300:
3296:
3295:
3293:
3292:
3287:
3282:
3281:
3280:
3275:
3263:
3258:
3252:
3250:
3246:
3245:
3243:
3242:
3237:
3227:
3225:
3214:
3213:
3211:
3210:
3205:
3199:
3197:
3193:
3192:
3172:
3171:
3164:
3157:
3149:
3140:
3139:
3137:
3136:
3130:
3128:
3121:
3120:
3118:
3117:
3111:
3109:
3105:
3104:
3102:
3101:
3096:
3091:
3086:
3085:
3084:
3079:
3067:
3065:Hexosaminidase
3062:
3057:
3051:
3049:
3045:
3044:
3042:
3041:
3036:
3031:
3025:
3023:
3019:
3018:
3000:
2999:
2992:
2985:
2977:
2968:
2967:
2965:
2964:
2959:
2954:
2949:
2944:
2939:
2934:
2932:Thrombopoietin
2929:
2928:
2927:
2922:
2917:
2907:
2902:
2897:
2892:
2887:
2882:
2877:
2872:
2867:
2862:
2857:
2852:
2847:
2842:
2837:
2832:
2827:
2822:
2817:
2812:
2806:
2804:
2800:
2799:
2796:
2795:
2793:
2792:
2786:
2784:
2778:
2777:
2775:
2774:
2769:
2764:
2758:
2756:
2750:
2749:
2747:
2746:
2741:
2736:
2731:
2726:
2721:
2716:
2711:
2701:
2699:
2693:
2692:
2690:
2689:
2684:
2678:
2676:
2666:
2665:
2663:
2662:
2657:
2652:
2646:
2644:
2631:
2625:
2624:
2621:
2620:
2618:
2617:
2612:
2607:
2602:
2597:
2592:
2586:
2584:
2580:
2579:
2577:
2576:
2571:
2566:
2561:
2556:
2551:
2546:
2541:
2536:
2531:
2526:
2521:
2516:
2511:
2506:
2501:
2496:
2491:
2486:
2480:
2478:
2469:
2463:
2462:
2451:glycoconjugate
2443:
2442:
2435:
2428:
2420:
2414:
2413:
2401:
2389:
2366:
2342:
2330:
2329:External links
2327:
2325:
2324:
2318:
2301:
2257:
2255:
2252:
2249:
2248:
2229:(2): 579–602.
2210:
2156:
2144:www.qmul.ac.uk
2131:
2079:
2038:(April 2015).
2026:
1977:
1920:
1871:
1830:
1776:
1757:
1737:
1710:(4): 645–650.
1694:
1643:
1624:(1): 131–163.
1589:
1574:
1519:
1504:
1461:
1420:
1378:
1377:
1375:
1372:
1370:
1369:
1364:
1359:
1354:
1349:
1344:
1342:P-glycoprotein
1339:
1334:
1329:
1324:
1319:
1314:
1309:
1304:
1298:
1296:
1293:
1275:
1272:
1251:
1248:
1227:
1224:
1221:
1220:
1217:
1206:
1205:
1202:
1195:
1194:
1187:
1181:
1180:
1177:molecular mass
1173:
1167:
1166:
1163:
1157:
1156:
1153:molecular mass
1149:
1143:
1142:
1139:
1132:
1131:
1124:
1115:
1114:
1111:
1094:
1093:
1086:
1084:phospholipases
1080:exoglycosidase
1071:
1070:
1067:
1059:
1058:
1051:
1045:
1044:
1041:
1028:
1025:
1022:
1021:
1015:
1004:
1003:
997:
993:
992:
983:
979:
978:
975:
969:
968:
958:
954:
953:
950:
944:
943:
932:
928:
927:
917:
913:
912:
906:
902:
901:
891:
887:
886:
877:
873:
872:
867:
863:
862:
857:
853:
852:
851:Glycoproteins
849:
839:
836:
818:
812:
811:
810:
805:
800:
795:
790:
785:
772:
769:
747:
746:
714:
713:
702:
683:
672:zona pellucida
668:
654:
647:
646:
643:
630:
591:
588:
579:
576:
458:
455:
445:
444:
441:
436:
430:
429:
426:
415:
409:
408:
405:
402:
396:
395:
392:
387:
381:
380:
377:
372:
366:
365:
362:
359:
353:
352:
349:
346:
340:
339:
336:
331:
325:
324:
321:
318:
297:
294:
293:
292:
281:
262:
251:-glycosylation
244:
233:-glycosylation
226:
215:-glycosylation
208:
205:hydroxyproline
195:, but also on
185:-glycosylation
178:
173:side-chain of
167:-glycosylation
155:
152:
66:which contain
15:
9:
6:
4:
3:
2:
3378:
3367:
3364:
3362:
3361:Glycoproteins
3359:
3358:
3356:
3346:
3341:
3336:
3335:
3332:
3319:
3316:
3313:
3312:Salla disease
3309:
3308:
3304:
3303:
3301:
3297:
3291:
3288:
3286:
3283:
3279:
3276:
3274:
3271:
3270:
3269:
3268:
3264:
3262:
3259:
3257:
3254:
3253:
3251:
3247:
3241:
3238:
3236:
3232:
3231:Mucolipidosis
3229:
3228:
3226:
3224:
3219:
3215:
3209:
3206:
3204:
3201:
3200:
3198:
3194:
3189:
3185:
3181:
3180:Inborn errors
3177:
3170:
3165:
3163:
3158:
3156:
3151:
3150:
3147:
3135:
3132:
3131:
3129:
3126:
3122:
3116:
3113:
3112:
3110:
3106:
3100:
3097:
3095:
3092:
3090:
3087:
3083:
3080:
3078:
3075:
3074:
3073:
3072:
3068:
3066:
3063:
3061:
3058:
3056:
3055:Neuraminidase
3053:
3052:
3050:
3046:
3040:
3037:
3035:
3032:
3030:
3027:
3026:
3024:
3020:
3016:
3013:
3009:
3005:
2998:
2993:
2991:
2986:
2984:
2979:
2978:
2975:
2963:
2960:
2958:
2955:
2953:
2950:
2948:
2945:
2943:
2940:
2938:
2937:Thyroglobulin
2935:
2933:
2930:
2926:
2925:Glycophorin C
2923:
2921:
2918:
2916:
2913:
2912:
2911:
2908:
2906:
2903:
2901:
2898:
2896:
2893:
2891:
2888:
2886:
2883:
2881:
2878:
2876:
2873:
2871:
2868:
2866:
2863:
2861:
2858:
2856:
2853:
2851:
2848:
2846:
2843:
2841:
2838:
2836:
2833:
2831:
2828:
2826:
2823:
2821:
2818:
2816:
2813:
2811:
2808:
2807:
2805:
2801:
2791:
2788:
2787:
2785:
2783:
2779:
2773:
2770:
2768:
2765:
2763:
2760:
2759:
2757:
2755:
2751:
2745:
2742:
2740:
2737:
2735:
2732:
2730:
2727:
2725:
2722:
2720:
2717:
2715:
2712:
2710:
2706:
2703:
2702:
2700:
2698:
2694:
2688:
2685:
2683:
2680:
2679:
2677:
2675:
2671:
2667:
2661:
2658:
2656:
2653:
2651:
2648:
2647:
2645:
2643:
2639:
2635:
2632:
2630:
2629:Proteoglycans
2626:
2616:
2613:
2611:
2608:
2606:
2605:Peptidoglycan
2603:
2601:
2598:
2596:
2593:
2591:
2588:
2587:
2585:
2581:
2575:
2572:
2570:
2567:
2565:
2562:
2560:
2557:
2555:
2552:
2550:
2547:
2545:
2542:
2540:
2537:
2535:
2532:
2530:
2527:
2525:
2522:
2520:
2517:
2515:
2512:
2510:
2507:
2505:
2502:
2500:
2497:
2495:
2492:
2490:
2487:
2485:
2482:
2481:
2479:
2477:
2473:
2470:
2468:
2464:
2460:
2459:glycopeptides
2456:
2455:glycoproteins
2452:
2448:
2441:
2436:
2434:
2429:
2427:
2422:
2421:
2418:
2410:
2406:
2402:
2398:
2394:
2390:
2387:
2383:
2379:
2375:
2371:
2367:
2355:
2351:
2347:
2343:
2340:
2336:
2335:Glycoproteins
2333:
2332:
2321:
2315:
2311:
2307:
2302:
2298:
2294:
2289:
2284:
2280:
2276:
2272:
2268:
2264:
2259:
2258:
2244:
2240:
2236:
2232:
2228:
2224:
2217:
2215:
2206:
2202:
2197:
2192:
2188:
2184:
2180:
2176:
2172:
2165:
2163:
2161:
2145:
2141:
2135:
2127:
2123:
2119:
2115:
2110:
2105:
2101:
2097:
2093:
2086:
2084:
2075:
2071:
2066:
2061:
2057:
2053:
2049:
2045:
2041:
2037:
2030:
2022:
2018:
2013:
2008:
2004:
2000:
1996:
1992:
1988:
1981:
1973:
1969:
1964:
1959:
1955:
1951:
1947:
1943:
1939:
1935:
1931:
1924:
1916:
1912:
1907:
1902:
1898:
1894:
1890:
1886:
1882:
1875:
1867:
1863:
1858:
1853:
1849:
1845:
1841:
1834:
1826:
1822:
1818:
1814:
1810:
1806:
1802:
1798:
1794:
1790:
1783:
1781:
1773:
1769:
1766:
1761:
1753:
1746:
1744:
1742:
1733:
1729:
1725:
1721:
1717:
1713:
1709:
1705:
1698:
1690:
1686:
1681:
1676:
1671:
1666:
1662:
1658:
1654:
1647:
1639:
1635:
1631:
1627:
1623:
1619:
1612:
1610:
1608:
1606:
1604:
1602:
1600:
1598:
1596:
1594:
1585:
1581:
1577:
1571:
1567:
1560:
1558:
1556:
1554:
1552:
1550:
1548:
1546:
1544:
1542:
1540:
1538:
1536:
1534:
1532:
1530:
1528:
1526:
1524:
1515:
1511:
1507:
1501:
1497:
1490:
1488:
1486:
1484:
1482:
1480:
1478:
1476:
1474:
1472:
1470:
1468:
1466:
1457:
1453:
1448:
1443:
1439:
1435:
1431:
1424:
1416:
1412:
1407:
1402:
1398:
1394:
1390:
1383:
1379:
1368:
1365:
1363:
1360:
1358:
1355:
1353:
1350:
1348:
1345:
1343:
1340:
1338:
1335:
1333:
1330:
1328:
1325:
1323:
1320:
1318:
1315:
1313:
1310:
1308:
1305:
1303:
1300:
1299:
1292:
1290:
1286:
1282:
1274:Glycosylation
1271:
1269:
1265:
1264:recombination
1256:
1250:Recombination
1247:
1245:
1241:
1236:
1234:
1218:
1215:
1211:
1208:
1207:
1203:
1200:
1197:
1196:
1192:
1188:
1186:
1183:
1182:
1178:
1174:
1172:
1169:
1168:
1164:
1162:
1159:
1158:
1154:
1150:
1148:
1145:
1144:
1140:
1138:
1134:
1133:
1129:
1125:
1123:
1120:
1117:
1116:
1112:
1110:
1106:
1103:
1099:
1096:
1095:
1091:
1087:
1085:
1081:
1077:
1073:
1072:
1068:
1065:
1061:
1060:
1056:
1052:
1050:
1047:
1046:
1042:
1039:
1038:
1032:
1020:
1016:
1013:
1009:
1006:
1005:
1001:
998:
995:
994:
991:
987:
984:
981:
980:
976:
974:
971:
970:
966:
962:
959:
956:
955:
951:
949:
946:
945:
941:
937:
933:
930:
929:
926:
922:
918:
915:
914:
910:
907:
904:
903:
899:
895:
892:
889:
888:
885:
884:ceruloplasmin
881:
878:
875:
874:
871:
868:
865:
864:
861:
858:
855:
854:
850:
847:
846:
834:
832:
830:
829:Proteoglycans
822:
817:
816:proteoglycans
809:
806:
804:
801:
799:
796:
794:
791:
789:
786:
784:
781:
780:
779:
777:
768:
765:
761:
757:
755:
751:
744:
740:
739:
734:
731:
730:
729:
727:
723:
719:
711:
707:
703:
700:
696:
692:
688:
684:
681:
677:
673:
669:
666:
662:
658:
655:
652:
651:
650:
644:
641:
637:
636:
631:
628:
624:
620:
619:
618:
616:
615:immune system
612:
607:
605:
601:
596:
587:
584:
575:
573:
568:
566:
562:
558:
554:
550:
546:
542:
537:
535:
531:
527:
523:
519:
518:iduronic acid
515:
511:
507:
503:
499:
495:
491:
487:
483:
479:
471:
467:
463:
454:
452:
442:
440:
437:
435:
432:
431:
427:
424:
419:
416:
414:
411:
410:
406:
403:
401:
398:
397:
393:
391:
388:
386:
383:
382:
378:
376:
373:
371:
368:
367:
363:
360:
358:
355:
354:
350:
347:
345:
344:β-D-Galactose
342:
341:
337:
335:
332:
330:
327:
326:
323:Abbreviation
322:
319:
316:
315:
309:
302:
290:
286:
282:
279:
275:
271:
267:
263:
260:
256:
252:
250:
245:
242:
238:
234:
232:
227:
224:
223:phosphoserine
220:
216:
214:
209:
206:
202:
201:hydroxylysine
198:
194:
190:
186:
184:
179:
176:
172:
168:
166:
161:
160:
159:
151:
149:
147:
142:
139:
134:
132:
128:
123:
121:
117:
113:
108:
104:
99:
97:
93:
92:glycosylation
89:
85:
81:
77:
73:
69:
65:
61:
60:Glycoproteins
54:
51:-glycans) at
50:
46:
42:
38:
34:
30:
26:
22:
21:peptidoglycan
3305:
3267:mannosidosis
3265:
3069:
3012:glycoprotein
3011:
2850:4-1BB ligand
2762:Fibromodulin
2467:Mucoproteins
2454:
2408:
2396:
2385:
2382:the original
2377:
2373:
2358:. Retrieved
2354:the original
2350:BiochemPages
2349:
2310:Biochemistry
2309:
2270:
2266:
2226:
2222:
2178:
2174:
2147:. Retrieved
2143:
2134:
2099:
2095:
2047:
2043:
2029:
1994:
1991:Cell Reports
1990:
1980:
1937:
1933:
1923:
1888:
1885:Cell Reports
1884:
1874:
1847:
1843:
1833:
1792:
1788:
1760:
1751:
1707:
1704:FEBS Letters
1703:
1697:
1660:
1656:
1646:
1621:
1617:
1565:
1498:. Springer.
1495:
1440:(2): 81–94.
1437:
1433:
1423:
1396:
1392:
1382:
1347:Proteoglycan
1322:Glycopeptide
1277:
1261:
1237:
1229:
1057:separation.
1030:
990:calreticulin
827:
824:
820:
774:
762:
758:
753:
748:
736:
726:blood plasma
715:
648:
633:
608:
597:
593:
581:
569:
556:
548:
544:
543:-linked and
540:
538:
475:
469:
468:-linked and
465:
448:
404:Aminohexose
307:
248:
230:
212:
182:
164:
157:
145:
135:
130:
129:-linked and
126:
124:
100:
80:carbohydrate
74:attached to
59:
58:
48:
44:
40:
33:
29:glycopeptide
25:proteoglycan
3261:Fucosidosis
3071:mannosidase
2962:Vitronectin
2957:Uteroglobin
2947:Transcortin
2920:Glycophorin
2890:Osteonectin
2875:Lactoferrin
2600:Orosomucoid
2590:Haptoglobin
2181:(6): 1–13.
2034:Crispin M,
1216:sequencing
1199:Methylation
921:phosphatase
880:Transferrin
754:Trypanosoma
665:endothelium
604:proteolysis
526:sialic acid
488:including:
423:Sialic acid
390:Aminohexose
375:Deoxyhexose
357:β-D-Mannose
329:β-D-Glucose
278:polypeptide
141:cytoplasmic
3355:Categories
3285:Sialidosis
3249:Catabolism
3094:Fucosidase
3048:Catabolism
3004:Metabolism
2790:Syndecan 1
1584:1249676451
1514:1005519572
1352:Ribophorin
1312:Glycocalyx
1210:Amino acid
1137:hydrolysis
1128:glycoforms
1012:thrombosis
1008:Hemostasis
623:antibodies
553:asparagine
534:amino acid
524:(GalNAc),
512:(GlcNAc),
482:covalently
370:α-L-Fucose
274:C-terminus
266:glypiation
241:tryptophan
219:phosphorus
175:asparagine
76:amino acid
72:covalently
3196:Anabolism
3108:Transport
3022:Anabolism
2900:Protein S
2895:Protein C
2870:Hemopexin
2860:Clusterin
2772:Keratocan
2360:18 August
2050:: 63–69.
2036:Doores KJ
1337:Miraculin
1289:Threonine
1226:Synthesis
1019:platelets
965:selectins
900:antigens
860:Collagens
848:Function
838:Functions
733:Miraculin
722:egg white
718:viscosity
661:platelets
583:Glycomics
578:Glycomics
565:threonine
508:(Gal), N-
506:galactose
457:Structure
285:glycation
253:, a beta-
193:threonine
2719:Brevican
2714:Neurocan
2709:Aggrecan
2687:Perlecan
2682:Testican
2660:Versican
2655:Biglycan
2615:Ovomucin
2397:bioWORLD
2297:25578468
2273:: 1–13.
2243:11841255
2205:25578468
2149:16 March
2126:11259597
2118:14576852
2096:Oncogene
2074:25747313
2021:26972002
1972:26105115
1940:: 7479.
1915:26051934
1825:23936441
1817:11269315
1768:Archived
1732:29992601
1724:21251913
1689:25386167
1638:19093879
1456:18952151
1415:17074831
1295:See also
1281:glycosyl
1027:Analysis
986:Calnexin
973:Receptor
905:Hormone
776:Hormones
771:Hormones
627:antigens
590:Examples
528:, and 5-
520:(IdoA),
516:(GlcA),
261:residue.
259:cysteine
197:tyrosine
64:proteins
3345:Biology
3127:tagging
3115:SLC17A5
3015:enzymes
3010:·
2767:Lumican
2650:Decorin
2447:Protein
2374:Science
2288:4340844
2196:4340844
2065:4827424
2012:4805854
1963:4500839
1942:Bibcode
1906:4555872
1866:3403544
1797:Bibcode
1789:Science
1680:4209869
1663:: 183.
1362:Protein
1317:Glycome
1098:Agarose
1090:mannose
1040:Method
961:Lectins
925:patatin
916:Enzyme
695:calcium
640:T cells
536:chain.
504:(Man),
502:mannose
500:(Xyl),
496:(Fuc),
492:(Glc),
490:glucose
486:glycans
480:bonded
439:Pentose
428:NeuNAc
407:GlcNAc
394:GalNAc
361:Hexose
348:Hexose
237:mannose
148:-GlcNAc
107:cytosol
3331:Portal
2840:Avidin
2519:MUC5AC
2341:(MeSH)
2316:
2295:
2285:
2241:
2203:
2193:
2124:
2116:
2072:
2062:
2019:
2009:
1970:
1960:
1913:
1903:
1864:
1823:
1815:
1730:
1722:
1687:
1677:
1636:
1582:
1572:
1512:
1502:
1454:
1413:
1357:Glycan
1285:Serine
1119:Lectin
1102:lectin
1066:bands
940:oocyte
870:Mucins
676:oocyte
600:mucins
561:serine
498:xylose
494:fucose
434:Xylose
334:Hexose
317:Sugar
255:GlcNAc
189:serine
138:nucleo
3299:Other
2803:Other
2734:CSPG5
2729:CSPG4
2583:Other
2574:MUC20
2569:MUC19
2564:MUC17
2559:MUC16
2554:MUC15
2549:MUC13
2544:MUC12
2524:MUC5B
2509:MUC3B
2504:MUC3A
2489:CD164
2476:Mucin
2122:S2CID
1821:S2CID
1774:SIGMA
1728:S2CID
1327:Gp120
1076:endo-
1010:(and
1000:Notch
936:sperm
743:berry
710:gp120
680:sperm
617:are:
320:Type
276:of a
221:on a
171:amide
27:, or
3099:NAGA
3034:GCS1
2915:CD43
2830:CD70
2815:ADAM
2724:CD44
2539:MUC8
2534:MUC7
2529:MUC6
2514:MUC4
2499:MUC2
2494:MUC1
2484:CD43
2457:and
2362:2015
2314:ISBN
2293:PMID
2239:PMID
2201:PMID
2151:2021
2114:PMID
2070:PMID
2017:PMID
1968:PMID
1911:PMID
1862:PMID
1813:PMID
1720:PMID
1685:PMID
1634:PMID
1580:OCLC
1570:ISBN
1510:OCLC
1500:ISBN
1452:PMID
1438:1790
1411:PMID
1332:Gp41
1302:Ero1
1214:cDNA
1043:Use
724:and
706:gp41
699:bone
443:Xyl
379:Fuc
364:Man
351:Gal
338:Glc
268:, a
203:and
114:and
62:are
3221:of
3182:of
3125:M6P
2378:291
2283:PMC
2275:doi
2231:doi
2227:102
2191:PMC
2183:doi
2104:doi
2060:PMC
2052:doi
2007:PMC
1999:doi
1958:PMC
1950:doi
1901:PMC
1893:doi
1852:doi
1848:263
1805:doi
1793:291
1712:doi
1708:585
1675:PMC
1665:doi
1626:doi
1622:109
1442:doi
1401:doi
1397:119
1287:or
1212:or
1082:or
1078:or
697:in
563:or
283:In
270:GPI
264:In
246:In
239:to
228:In
210:In
191:or
180:In
162:In
86:or
53:Asn
3357::
3233::
3178::
3006::
2782:HS
2754:KS
2707::
2697:CS
2674:CS
2670:HS
2642:DS
2638:CS
2453::
2449:,
2407:.
2395:.
2376:.
2372:.
2348:.
2308:.
2291:.
2281:.
2271:57
2269:.
2265:.
2237:.
2225:.
2213:^
2199:.
2189:.
2179:57
2177:.
2173:.
2159:^
2142:.
2120:.
2112:.
2100:22
2098:.
2094:.
2082:^
2068:.
2058:.
2048:11
2042:.
2015:.
2005:.
1995:14
1993:.
1989:.
1966:.
1956:.
1948:.
1936:.
1932:.
1909:.
1899:.
1889:11
1887:.
1883:.
1860:.
1846:.
1842:.
1819:.
1811:.
1803:.
1791:.
1779:^
1740:^
1726:.
1718:.
1706:.
1683:.
1673:.
1659:.
1655:.
1632:.
1620:.
1592:^
1578:.
1522:^
1508:.
1464:^
1450:.
1436:.
1432:.
1409:.
1395:.
1391:.
1246:.
1193:.
1107:,
1014:)
988:,
963:,
923:,
896:,
882:,
741:a
728:.
425:)
150:.
122:.
94:.
23:,
3333::
3314:)
3310:(
3190:)
3186:(
3168:e
3161:t
3154:v
2996:e
2989:t
2982:v
2672:/
2640:/
2439:e
2432:t
2425:v
2411:.
2399:.
2364:.
2322:.
2299:.
2277::
2245:.
2233::
2207:.
2185::
2153:.
2128:.
2106::
2076:.
2054::
2023:.
2001::
1974:.
1952::
1944::
1938:6
1917:.
1895::
1868:.
1854::
1827:.
1807::
1799::
1734:.
1714::
1691:.
1667::
1661:5
1640:.
1628::
1586:.
1516:.
1458:.
1444::
1417:.
1403::
1100:-
938:–
701:.
667:.
629:.
557:O
549:N
545:O
541:N
470:O
466:N
421:(
291:.
249:S
243:.
231:C
225:.
213:P
207:.
183:O
177:.
165:N
146:O
131:O
127:N
49:N
45:N
41:N
31:.
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