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Glycosylation

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AGEs are responsible for many things. These molecules play an important role especially in nutrition, they are responsible for the brownish color and the aromas and flavors of some foods. It is demonstrated that cooking at high temperature results in various food products having high levels of AGEs.
982:, the body of the patient produces antibodies against the enzyme lymphocytes galactosyltransferase which inhibits the glycosylation of IgG. Therefore, the changes in the N-glycosylation produce the immunodeficiency involved in this illness. In this second group we can also find disorders caused by 564:
and Thr) in order for mannosylation to occur. Recently there has been a breakthrough in the technique of predicting whether or not the sequence will have a mannosylation site that provides an accuracy of 93% opposed to the 67% accuracy if we just consider the WXXW motif.
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All these diseases are difficult to diagnose because they do not only affect one organ, they affect many of them and in different ways. As a consequence, they are also hard to treat. However, thanks to the many advances that have been made in
964:-glycosylation, disorders of lipid glycosylation and disorders of other glycosylation pathways and of multiple glycosylation pathways. No effective treatment is known for any of these disorders. 80% of these affect the nervous system. 933:. One of the modulators that intervene in this process is the Fringe, a glycosyltransferase that modifies the O-fucose to activate or deactivate parts of the signalling, acting as a positive or negative regulator, respectively. 551:
and the second carbon of the tryptophan. However, not all the sequences that have this pattern are mannosylated. It has been established that, in fact, only two thirds are and that there is a clear preference for the second
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transmission of viruses. In addition, glycosylation is often used by viruses to shield the underlying viral protein from immune recognition. A significant example is the dense glycan shield of the envelope spike of the
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Overall, glycosylation needs to be understood by the likely evolutionary selection pressures that have shaped it. In one model, diversification can be considered purely as a result of endogenous functionality (such as
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There are three types of glycosylation disorders sorted by the type of alterations that are made to the glycosylation process: congenital alterations, acquired alterations and non-enzymatic acquired alterations.
243:-linked glycans mediate a critical quality control check point in glycoprotein folding in the endoplasmic reticulum. Glycosylation also plays a role in cell-to-cell adhesion (a mechanism employed by cells of the 516:, on the cell-surface laminin receptor alpha dystroglycan. It has been suggested this rare finding may be linked to the fact that alpha dystroglycan is highly conserved from lower vertebrates to mammals. 2404:
Razaghi A, Villacrés C, Jung V, Mashkour N, Butler M, Owens L, Heimann K (October 2017). "Improved therapeutic efficacy of mammalian expressed-recombinant interferon gamma against ovarian cancer cells".
658:-benzylidene) in order to achieve desired regioselectivity. The other challenge of chemical glycosylation is the stereoselectivity that each glycosidic linkage has two stereo-outcomes, α/β or 595:. In 2011, the first crystal structure of a protein containing this type of glycosylation was determined—that of human complement component 8. Currently it is established that 18% of human 220:. This modification serves various functions. For instance, some proteins do not fold correctly unless they are glycosylated. In other cases, proteins are not stable unless they contain 271:
are presented and hence what antibody specificities are exhibited. This immunological role may well have driven the diversification of glycan heterogeneity and creates a barrier to
670:-glycoside is more challenging to synthesis. New methods have been developed based on solvent participation or the formation of bicyclic sulfonium ions as chiral-auxiliary groups. 996:
Non-enzymatic disorders, are also acquired, but they are due to the lack of enzymes that attach oligosaccharides to the protein. In this group the illnesses that stand out are
407:-linked glycosylation is a very prevalent form of glycosylation and is important for the folding of many eukaryotic glycoproteins and for cell–cell and cell– 3246: 2761: 698:
of the protein. In this process the intervention of an enzyme is not needed. It takes place across and close to the water channels and the protruding tubules.
899:. This means it is crucial in embryonic development, to the point that it has been tested on mice that the removal of glycans in Notch proteins can result in 1169:
Jung ST, Kang TH, Kelton W, Georgiou G (December 2011). "Bypassing glycosylation: engineering aglycosylated full-length IgG antibodies for human therapy".
255:, which recognize specific carbohydrate moieties. Glycosylation is an important parameter in the optimization of many glycoprotein-based drugs such as 834:(from Streptococcus pneumoniae): cleaves all non-reducing terminal β-linked N-acetylglucosamine residues from complex carbohydrates and glycoproteins. 3221: 1979:Świa̧tecka, D.; Kostyra, H.; Świa̧tecki, A. (2010). "Impact of glycated pea proteins on the activity of free‐swimming and immobilised bacteria". 1254:
Dalziel M, Crispin M, Scanlan CN, Zitzmann N, Dwek RA (January 2014). "Emerging principles for the therapeutic exploitation of glycosylation".
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Henle, Thomas; Duerasch, Anja; Weiz, Alexander; Ruck, Michael; Moeckel, Ulrike (1 November 2020). "Glycation Reactions of Casein Micelles".
1738:"Mutations in the Trp-Ser-X-Trp-Ser motif of the erythropoietin receptor abolish processing, ligand binding, and activation of the receptor" 83:. Glycans serve a variety of structural and functional roles in membrane and secreted proteins. The majority of proteins synthesized in the 2625: 950: 1469: 2546:-glycosylation sites in human proteins using artificial neural networks that examine the sequence context of Asn-Xaa-Ser/Thr sequons. 918:. The Notch proteins go through these organelles in their maturation process and can be subject to different types of glycosylation: 2523: 2300: 2198: 1111: 756:, heart damage... And, if they are present at a decreased level, skin elasticity is reduced which is an important symptom of aging. 1512:
Yoshida-Moriguchi T, Yu L, Stalnaker SH, Davis S, Kunz S, Madson M, Oldstone MB, Schachter H, Wells L, Campbell KP (January 2010).
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Having elevated levels of AGEs in the body has a direct impact on the development of many diseases. It has a direct implication in
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undergo the process of C-mannosylation. Numerous studies have shown that this process plays an important role in the secretion of
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modification. Aglycosylation is a feature of engineered antibodies to bypass glycosylation. Five classes of glycans are produced:
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attachment to terminal saccharide residues) and that diversity within the multicellular organism is then exploited endogenously.
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are one of the proteins most commonly modified in this way. However, there is another group of proteins that undergo
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which is the most glycated and structurally abundant protein, especially in humans. Also, some studies have shown
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is twofold. Firstly, the highly soluble glycans may have a direct physicochemical stabilisation effect. Secondly,
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Crispin M, Harvey DJ, Bitto D, Bonomelli C, Edgeworth M, Scrivens JH, Huiskonen JT, Bowden TA (March 2014).
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Varki A, Cummings RD, Esko JD, Freeze HH, Stanley P, Bertozzi CR, Hart GW, Etzler ME (2009). Varki A (ed.).
616: 2357:"Mitotic Intragenic Recombination:A Mechanism of Survivalfor Several Congenital Disorders of Glycosylation" 978:. In these cases, the changes in glycosylation are the cause of certain biological events. For example, in 3231: 3179: 3113: 2999: 2994: 2699: 1055: 997: 954: 923: 919: 443: 431:-linked glycans of a protein can modulate a protein's function, in some cases acting as an on/off switch. 399: 121: 76:(also 'non-enzymatic glycation' and 'non-enzymatic glycosylation') may refer to a non-enzymatic reaction. 38: 929:
All of the Notch proteins are modified by an O-fucose, because they share a common trait: O-fucosylation
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residue in the sequence W–X–X–W (W indicates tryptophan; X is any amino acid). A
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Gill, Vidhu; Kumar, Vijay; Singh, Kritanjali; Kumar, Ashok; Kim, Jong-Joo (17 December 2019).
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There are various mechanisms for glycosylation, although most share several common features:
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Covalent attachment and further modification of carbohydrate residues to a substrate molecule
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Lima, M.; Baynes, J.W. (2013). "Glycation". In Lennarz, William J.; Lane, M. Daniel (eds.).
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Ardejani, Maziar S.; Noodleman, Louis; Powers, Evan T.; Kelly, Jeffery W. (15 March 2021).
3040: 2922: 1594: 1299:"Structural plasticity of the Semliki Forest virus glycome upon interspecies transmission" 1021:
It has been reported that mammalian glycosylation can improve the therapeutic efficacy of
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At first, the reaction forms temporary molecules which later undergo different reactions (
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Glycosylation can also module the thermodynamic and kinetic stability of the proteins.
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Ihara, Yoshito. "C-Mannosylation: A Modification on Tryptophan in Cellular Proteins".
177:-linked glycans, a rare form of glycosylation where a sugar is added to a carbon on a 3215: 2676: 2325: 1283: 1204: 1030: 1013:, scientists can now understand better these disorders and have discovered new CDGs. 821: 687: 490: 244: 209: 157: 2603: 2434: 2152: 1818:-Glycosylation as the driving force of progress in synthetic carbohydrate chemistry" 2969: 2939: 2744: 2716: 2461:
platform for prediction of N-, O- and C-glycosites in eukaryotic protein sequences"
1636:"C-mannosylation supports folding and enhances stability of thrombospondin repeats" 1061: 803: 351:, is an enzymatic process. Indeed, glycosylation is thought to be the most complex 290: 236: 201: 49: 531:
The mannose molecule is attached to the C2 of the first tryptophan of the sequence
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of proteins meaning it alters their structure and biological activity. It is the
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have been reported in the literature. Fucose and GlcNAc have been found only in
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is a cell signalling pathway whose role is, among many others, to control the
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Crich D (August 2010). "Mechanism of a chemical glycosylation reaction".
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on the enzymes that control the glycosylation of Notch proteins, such as
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residues. The influence of glycosylation on the folding and stability of
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Posttranslational Modification of Proteins: Expanding Nature's Inventory
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or non-enzymatic glycation. It is a spontaneous reaction and a type of
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Varki A, Cummings R, Esko J, Freeze H, Hart G, Marth J, eds. (1999).
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L. express aglycosylated monoclonal antibody with antitumor activity"
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of a reducing sugar (mainly glucose and fructose) and the amino acid
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is a special form of glycosylation that features the formation of a
2287:. Handbook of Clinical Neurology. Vol. 113. pp. 1737–43. 611:
if they do not undergo C-mannosylation This explains why a type of
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In this second group the main disorders are infectious diseases,
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Phosphoglycans linked through the phosphate of a phosphoserine.
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Some of the specific modulators that control this process are
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AGEs accumulate in long-lived extracellular proteins such as
1354:. Viral pathogenesis • Preventive and therapeutic vaccines. 381:). Therefore, glycosylation is a site-specific modification. 87:
undergo glycosylation. Glycosylation is also present in the
926:(more specifically: O-linked glucose and O-linked fucose). 583:-mannosylation is unusual because the sugar is linked to a 2326:"Alteraciones de la glicosilación en enfermedades humanas" 2283:
Jaeken J (2013). "Congenital disorders of glycosylation".
2067:"НЕФЕРМЕНТАТИВНОЕ ГЛИКИРОВАНИЕ БЕЛКОВ: ОТ ДИАБЕТА ДО РАКА" 1076: – Technology enabling rapid molecule diversification 355:, because of the large number of enzymatic steps involved. 2324:
Jiménez Martínez, María del Carmen (January–March 2002).
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and regulate and modify their receptor mechanisms at the
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in the lumen of the endoplasmic reticulum and widely in
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usually refers to an enzyme-catalysed reaction, whereas
1867:"Mechanism of Glycosylation of Anomeric Sulfonium Ions" 1140:(2nd ed.). Cold Spring Harbor Laboratories Press. 1051:
Pages displaying short descriptions of redirect targets
322:—the types of sugars that are linked to a given protein 2836:(amino acid→pyruvate, acetyl CoA, or TCA intermediate) 879:-linked oligosaccharides unless α1,3-core fucosylated. 650:
Glycosylation can also be effected using the tools of
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Lovelace LL, Cooper CL, Sodetz JM, Lebioda L (2011).
1098:(Second ed.). Academic Press. pp. 405–411. 732:
may trigger spontaneous non-enzymatic glycosylation.
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Additional information on glycosylation and figures
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Supplementary Material of the Book "The Sugar Code"
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Biochemical and Biophysical Research Communications
1070: – Attachment of a sugar to a protein or lipid 1025:. For example, therapeutic efficacy of recombinant 816:): releases only β1,4-linked, nonreducing terminal 2236:"Significance of glycosylation in Notch signaling" 1058: – Reaction of a glycosyl donor and acceptor 903:or malformations of vital organs like the heart. 678:The non-enzymatic glycosylation is also known as 185:is one of the few naturally occurring substances. 127:requires participation of a special lipid called 79:Glycosylation is a form of co-translational and 328:—can be unbranched or branched chains of sugars 1865:Fang T, Gu Y, Huang W, Boons GJ (March 2016). 1230:(2nd ed.). Oxford University Press, USA. 1033:platform, was improved against drug-resistant 607:containing proteins which are retained in the 2619: 1464:. Roberts and Co. Publishers, Englewood, CO. 748:that can lead to many complications such as: 334:—can be short- or long-chain oligosaccharides 164:side-chains, or to oxygens on lipids such as 8: 68:. In biology (but not always in chemistry), 2175:"Roles of glycosylation in Notch signaling" 3101: 3018: 2911: 2904: 2816: 2792: 2683: 2626: 2612: 2604: 2173:Stanley, Pamela; Okajima, Tetsuya (2010). 2121:"Glycosylation regulates Notch signalling" 1916:Journal of Agricultural and Food Chemistry 717:...) and form permanent residues known as 547:is formed between the first carbon of the 2586: 2494: 2484: 2380: 2259: 2082: 2041: 2031: 1890: 1841: 1753: 1712: 1702: 1661: 1651: 1610: 1549: 1436: 1371: 1322: 365:The process is non-templated (unlike DNA 358:The donor molecule is often an activated 305:Glycosylation increases diversity in the 263:system. It is the presence or absence of 2065:Ansari, N.A.; Rasheed, Z. (March 2010). 1871:Journal of the American Chemical Society 415:-linked glycosylation process occurs in 200:Glycosylation is the process by which a 2561:Emanual Maverakis; et al. (2015). 2542:NetNGlyc: The NetNglyc server predicts 2518:. Cold Spring Harbor Laboratory Press. 2179:Current Topics in Developmental Biology 1129: 1127: 1125: 1123: 1086: 2455:Chauhan JS, Rao A, Raghava GP (2013). 2361:The American Journal of Human Genetics 2234:Hideyuki, Takeuchi (17 October 2014). 2125:Nature Reviews. Molecular Cell Biology 1812:Nigudkar SS, Demchenko AV (May 2015). 3247:Congenital disorders of glycosylation 2537:-glycosylation of proteins on the web 2229: 2227: 2225: 2114: 2112: 2110: 1949: 1947: 1945: 1588: 1586: 1584: 951:congenital disorders of glycosylation 759:They are also the precursors of many 627:Formation of GPI anchors (glypiation) 7: 2736:Electron acceptors other than oxygen 1956:Encyclopedia of Biological Chemistry 1249: 1247: 1096:Encyclopedia of Biological Chemistry 861:-glycosylation. This enzyme cleaves 623:if it lacked C-mannosylation sites. 587:rather than a reactive atom such as 1742:The Journal of Biological Chemistry 1346:Crispin M, Doores KJ (April 2015). 994:Non-enzymatic acquired alterations: 869:-linked unsubstituted Galβ1,3GalNAc 259:. Glycosylation also underpins the 2355:S. Kane, Megan (4 February 2016). 2293:10.1016/B978-0-444-59565-2.00044-7 1575:Glycoscience: Biology and Medicine 1491:. Nova Publishers. pp. 45ff. 1104:10.1016/B978-0-12-378630-2.00120-1 556:to be one of the polar ones (Ser, 25: 1634:Aleksandra, Shcherbakova (2019). 267:which dictates which blood group 1954:Baynes, J. W.; Lima, M. (2013). 1488:Biotechnology and Bioengineering 1171:Current Opinion in Biotechnology 137:-linked glycans attached to the 3222:Post-translational modification 2757:Substrate-level phosphorylation 2119:Haines, Nicole (October 2003). 1226:Drickamer K, Taylor ME (2006). 1017:Effects on therapeutic efficacy 820:from complex carbohydrates and 719:Advanced Glycation end-products 684:post-translational modification 353:post-translational modification 81:post-translational modification 884:Regulation of Notch signalling 105:-linked glycans attached to a 1: 3160:Reverse cholesterol transport 2191:10.1016/S0070-2153(10)92004-8 1779:Accounts of Chemical Research 1755:10.1016/S0021-9258(19)49956-0 1047:Advanced glycation endproduct 2812:(protein→peptide→amino acid) 2486:10.1371/journal.pone.0067008 2285:Pediatric Neurology Part III 1593:Julenius, Karin (May 2007). 1364:10.1016/j.coviro.2015.02.002 1303:Journal of Proteome Research 1228:Introduction to Glycobiology 1183:10.1016/j.copbio.2011.03.002 539:sugar is added to the first 278:human immunodeficiency virus 2419:10.1016/j.yexcr.2017.08.014 1352:Current Opinion in Virology 787:or remove some part of the 674:Non-enzymatic glycosylation 652:synthetic organic chemistry 471:Phosphoserine glycosylation 316:—the site of glycan linkage 85:rough endoplasmic reticulum 48:is the reaction in which a 3263: 3197:Phospagen system (ATP-PCr) 2667:Primary nutritional groups 2579:10.1016/j.jaut.2014.12.002 2515:Essentials of Glycobiology 2407:Experimental Cell Research 2373:10.1016/j.ajhg.2015.12.007 2252:10.1016/j.bbrc.2014.05.115 1421:10.1038/s41557-021-00646-w 1137:Essentials of Glycobiology 1011:next-generation sequencing 441: 397: 36: 29: 3059: 3031:Anoxygenic photosynthesis 3021: 2985: 2953:Pentose phosphate pathway 2948: 2931: 2914: 2708:Oxidative phosphorylation 2330:Rev Inst Nal Enf Resp Mex 980:Rheumatoid Arthritis (RA) 3051:Entner-Doudoroff pathway 2713:electron transport chain 2700:Pyruvate decarboxylation 2084:10.18097/pbmc20105602168 2071:Biomeditsinskaya Khimiya 1928:10.1021/acs.jafc.6b00472 854:Streptococcus pneumoniae 845:-Acetylgalactosaminidase 814:Streptococcus pneumoniae 800:Arthrobacter ureafaciens 796:α2-3,6,8,9-Neuraminidase 746:diabetes mellitus type 2 498:Dictyostelium discoideum 30:Not to be confused with 3145:Sphingolipid metabolism 3046:DeLey-Doudoroff pathway 2894:carbohydrate catabolism 2889:Carbohydrate metabolism 2875:Purine nucleotide cycle 2567:Journal of Autoimmunity 1736:Yoshimura (June 1992). 1704:10.1074/jbc.M111.219766 1542:10.1126/science.1180512 1268:10.1126/science.1235681 960:, disorders of protein 947:Congenital alterations: 690:attachment between the 666:. Generally, the α- or 617:erythropoietin receptor 575:-mannosylation, type I 3237:Carbohydrate chemistry 3114:Fatty acid degradation 2834:Amino acid degradation 1213:Biotecnologia Aplicada 1205:"Transgenic plants of 1056:Chemical glycosylation 1027:human interferon gamma 924:O-linked glycosylation 920:N-linked glycosylation 895:process in equivalent 832:-Acetylglucosaminidase 703:Amadori rearrangements 646:Chemical glycosylation 532: 444:O-linked glycosylation 400:N-linked glycosylation 347:Glycosylation, unlike 301:Glycoprotein diversity 249:sugar-binding proteins 39:Chemical glycosylation 3150:Eicosanoid metabolism 3106:Fatty acid metabolism 2870:Pyrimidine metabolism 2729:Anaerobic respiration 1612:10.1093/glycob/cwm050 968:Acquired alterations: 912:endoplasmic reticulum 621:endoplasmic reticulum 609:endoplasmic reticulum 530: 459:, but also occurs in 438:-linked glycosylation 423:, but very rarely in 394:-linked glycosylation 375:endoplasmic reticulum 257:monoclonal antibodies 208:attached to a target 125:-linked glycosylation 64:) in order to form a 3124:Fatty acid synthesis 2829:Amino acid synthesis 1958:. pp. 405–411. 1883:10.1021/jacs.5b08436 972:autoimmune illnesses 908:glycosyltransferases 893:cell differentiation 775:There are different 605:Trombospondin type 1 409:extracellular matrix 265:glycosyltransferases 2688:Aerobic respiration 2533:GlyProt: In-silico 2477:2013PLoSO...867008C 2033:10.3390/biom9120888 1697:(20): 17585–17592. 1653:10.7554/eLife.52978 1534:2010Sci...327...88Y 1413:2021NatCh..13..480A 998:Alzheimer's disease 931:consensus sequences 503:Leishmania mexicana 91:and nucleus as the 3192:Ethanol metabolism 3140:Steroid metabolism 2865:Nucleotide salvage 2797:Protein metabolism 1981:J. Sci. Food Agric 1834:10.1039/c5sc00280j 1485:Flynne WG (2008). 1074:Glycorandomization 851:-glycosidase from 810:β1,4-Galactosidase 711:Maillard reactions 613:cytokine receptors 577:cytokine receptors 533: 320:Glycan composition 129:dolichol phosphate 3227:Organic reactions 3209: 3208: 3205: 3204: 3168: 3167: 3081: 3080: 3077: 3076: 3064:Xylose metabolism 3010: 3009: 2883: 2882: 2860:Purine metabolism 2805:Protein synthesis 2782: 2781: 2704:Citric acid cycle 2662:Metabolic network 2657:Metabolic pathway 1993:10.1002/jsfa.4022 1987:(11): 1837–1845. 1965:978-0-12-378631-9 1922:(14): 2953–2961. 1791:10.1021/ar100035r 1498:978-1-60456-067-1 1315:10.1021/pr401162k 1262:(6166): 1235681. 1237:978-0-19-928278-4 1207:Nicotiana tabacum 1147:978-0-87969-770-9 988:Alagille syndrome 509:Trypanosoma cruzi 62:glycosyl acceptor 16:(Redirected from 3254: 3180:Metal metabolism 3102: 3087:Lipid metabolism 3019: 2912: 2905: 2817: 2793: 2719: 2684: 2628: 2621: 2614: 2605: 2600: 2590: 2529: 2508: 2498: 2488: 2439: 2438: 2401: 2395: 2394: 2384: 2352: 2346: 2345: 2343: 2341: 2321: 2315: 2314: 2280: 2274: 2273: 2263: 2231: 2220: 2219: 2217: 2215: 2170: 2164: 2163: 2161: 2159: 2116: 2105: 2104: 2086: 2062: 2056: 2055: 2045: 2035: 2011: 2005: 2004: 1976: 1970: 1969: 1951: 1940: 1939: 1911: 1905: 1904: 1894: 1862: 1856: 1855: 1845: 1828:(5): 2687–2704. 1822:Chemical Science 1809: 1803: 1802: 1774: 1768: 1767: 1757: 1748:(16): 11619–25. 1733: 1727: 1726: 1716: 1706: 1682: 1676: 1675: 1665: 1655: 1631: 1625: 1624: 1614: 1590: 1579: 1578: 1570: 1564: 1563: 1553: 1509: 1503: 1502: 1482: 1476: 1475: 1460:Walsh C (2006). 1457: 1451: 1450: 1440: 1401:Nature Chemistry 1392: 1386: 1385: 1375: 1343: 1337: 1336: 1326: 1294: 1288: 1287: 1251: 1242: 1241: 1223: 1217: 1216: 1201: 1195: 1194: 1166: 1160: 1159: 1131: 1118: 1117: 1091: 1052: 889:Notch signalling 619:remained in the 506:, and xylose in 411:attachment. The 360:nucleotide sugar 326:Glycan structure 286:cell trafficking 222:oligosaccharides 21: 3262: 3261: 3257: 3256: 3255: 3253: 3252: 3251: 3212: 3211: 3210: 3201: 3185:Iron metabolism 3164: 3128: 3089: 3073: 3055: 3041:Carbon fixation 3006: 2981: 2944: 2927: 2923:Gluconeogenesis 2896: 2891: 2879: 2851: 2844: 2815: 2788: 2778: 2739: 2723: 2711: 2678: 2671: 2645: 2632: 2560: 2526: 2511: 2454: 2448: 2443: 2442: 2403: 2402: 2398: 2354: 2353: 2349: 2339: 2337: 2323: 2322: 2318: 2303: 2282: 2281: 2277: 2233: 2232: 2223: 2213: 2211: 2201: 2172: 2171: 2167: 2157: 2155: 2137:10.1038/nrm1228 2131:(10): 786–797. 2118: 2117: 2108: 2064: 2063: 2059: 2013: 2012: 2008: 1978: 1977: 1973: 1966: 1953: 1952: 1943: 1913: 1912: 1908: 1864: 1863: 1859: 1811: 1810: 1806: 1776: 1775: 1771: 1735: 1734: 1730: 1684: 1683: 1679: 1633: 1632: 1628: 1592: 1591: 1582: 1572: 1571: 1567: 1528:(5961): 88–92. 1511: 1510: 1506: 1499: 1484: 1483: 1479: 1472: 1459: 1458: 1454: 1394: 1393: 1389: 1345: 1344: 1340: 1296: 1295: 1291: 1253: 1252: 1245: 1238: 1225: 1224: 1220: 1203: 1202: 1198: 1168: 1167: 1163: 1148: 1133: 1132: 1121: 1114: 1093: 1092: 1088: 1083: 1050: 1043: 1029:, expressed in 1023:biotherapeutics 1019: 939: 916:Golgi apparatus 910:located in the 901:embryonic death 897:precursor cells 886: 773: 771:Deglycosylation 738: 676: 648: 629: 599:, secreted and 569:Thrombospondins 525: 473: 457:Golgi apparatus 446: 440: 402: 396: 388: 379:Golgi apparatus 377:, cisternae in 341: 314:Glycosidic bond 303: 261:ABO blood group 198: 41: 35: 28: 23: 22: 15: 12: 11: 5: 3260: 3258: 3250: 3249: 3244: 3239: 3234: 3229: 3224: 3214: 3213: 3207: 3206: 3203: 3202: 3200: 3199: 3194: 3189: 3188: 3187: 3176: 3174: 3170: 3169: 3166: 3165: 3163: 3162: 3157: 3152: 3147: 3142: 3136: 3134: 3130: 3129: 3127: 3126: 3121: 3118:Beta oxidation 3110: 3108: 3099: 3083: 3082: 3079: 3078: 3075: 3074: 3072: 3071: 3066: 3060: 3057: 3056: 3054: 3053: 3048: 3043: 3038: 3036:Chemosynthesis 3033: 3028: 3026:Photosynthesis 3022: 3016: 3012: 3011: 3008: 3007: 3005: 3004: 3003: 3002: 2997: 2986: 2983: 2982: 2980: 2979: 2978: 2977: 2975:Leloir pathway 2967: 2966: 2965: 2963:Polyol pathway 2955: 2949: 2946: 2945: 2943: 2942: 2936:Glycogenolysis 2932: 2929: 2928: 2926: 2925: 2915: 2909: 2902: 2885: 2884: 2881: 2880: 2878: 2877: 2872: 2867: 2862: 2856: 2854: 2846: 2845: 2843: 2842: 2837: 2831: 2825: 2823: 2814: 2813: 2807: 2801: 2799: 2790: 2784: 2783: 2780: 2779: 2777: 2776: 2775: 2774: 2769: 2764: 2749: 2747: 2741: 2740: 2738: 2737: 2733: 2731: 2725: 2724: 2722: 2721: 2692: 2690: 2681: 2673: 2672: 2670: 2669: 2664: 2659: 2653: 2651: 2647: 2646: 2633: 2631: 2630: 2623: 2616: 2608: 2602: 2601: 2558: 2553: 2548: 2539: 2530: 2524: 2509: 2447: 2446:External links 2444: 2441: 2440: 2396: 2347: 2316: 2301: 2275: 2221: 2199: 2165: 2106: 2077:(2): 168–178. 2073:(in Russian). 2057: 2006: 1971: 1964: 1941: 1906: 1877:(9): 3002–11. 1857: 1804: 1785:(8): 1144–53. 1769: 1728: 1677: 1626: 1605:(8): 868–876. 1580: 1565: 1504: 1497: 1477: 1471:978-0974707730 1470: 1452: 1407:(5): 480–487. 1387: 1338: 1309:(3): 1702–12. 1289: 1243: 1236: 1218: 1196: 1161: 1146: 1119: 1112: 1085: 1084: 1082: 1079: 1078: 1077: 1071: 1065: 1059: 1053: 1042: 1039: 1035:ovarian cancer 1018: 1015: 1006: 1005: 991: 965: 958:-glycosylation 938: 935: 885: 882: 881: 880: 870: 835: 825: 807: 779:to remove the 772: 769: 737: 734: 692:carbonil group 675: 672: 647: 644: 628: 625: 524: 523:-mannosylation 518: 472: 469: 442:Main article: 439: 433: 398:Main article: 395: 389: 387: 384: 383: 382: 363: 356: 340: 337: 336: 335: 329: 323: 317: 302: 299: 224:linked at the 197: 194: 193: 192: 186: 172: 169: 162:hydroxyproline 132: 66:glycoconjugate 58:glycosyl donor 26: 24: 14: 13: 10: 9: 6: 4: 3: 2: 3259: 3248: 3245: 3243: 3240: 3238: 3235: 3233: 3232:Carbohydrates 3230: 3228: 3225: 3223: 3220: 3219: 3217: 3198: 3195: 3193: 3190: 3186: 3183: 3182: 3181: 3178: 3177: 3175: 3171: 3161: 3158: 3156: 3153: 3151: 3148: 3146: 3143: 3141: 3138: 3137: 3135: 3131: 3125: 3122: 3119: 3115: 3112: 3111: 3109: 3107: 3103: 3100: 3097: 3093: 3088: 3084: 3070: 3069:Radiotrophism 3067: 3065: 3062: 3061: 3058: 3052: 3049: 3047: 3044: 3042: 3039: 3037: 3034: 3032: 3029: 3027: 3024: 3023: 3020: 3017: 3013: 3001: 2998: 2996: 2993: 2992: 2991: 2990:Glycosylation 2988: 2987: 2984: 2976: 2973: 2972: 2971: 2968: 2964: 2961: 2960: 2959: 2956: 2954: 2951: 2950: 2947: 2941: 2937: 2934: 2933: 2930: 2924: 2920: 2917: 2916: 2913: 2910: 2906: 2903: 2900: 2895: 2890: 2886: 2876: 2873: 2871: 2868: 2866: 2863: 2861: 2858: 2857: 2855: 2853: 2847: 2841: 2838: 2835: 2832: 2830: 2827: 2826: 2824: 2822: 2818: 2811: 2808: 2806: 2803: 2802: 2800: 2798: 2794: 2791: 2785: 2773: 2770: 2768: 2765: 2763: 2760: 2759: 2758: 2754: 2751: 2750: 2748: 2746: 2742: 2735: 2734: 2732: 2730: 2726: 2718: 2714: 2709: 2705: 2701: 2697: 2694: 2693: 2691: 2689: 2685: 2682: 2680: 2674: 2668: 2665: 2663: 2660: 2658: 2655: 2654: 2652: 2648: 2644: 2640: 2636: 2629: 2624: 2622: 2617: 2615: 2610: 2609: 2606: 2598: 2594: 2589: 2584: 2580: 2576: 2572: 2568: 2564: 2559: 2557: 2554: 2552: 2549: 2547: 2545: 2540: 2538: 2536: 2531: 2527: 2525:0-87969-559-5 2521: 2517: 2516: 2510: 2506: 2502: 2497: 2492: 2487: 2482: 2478: 2474: 2471:(6): e67008. 2470: 2466: 2462: 2460: 2453: 2450: 2449: 2445: 2436: 2432: 2428: 2424: 2420: 2416: 2412: 2408: 2400: 2397: 2392: 2388: 2383: 2378: 2374: 2370: 2367:(2): 339–46. 2366: 2362: 2358: 2351: 2348: 2335: 2331: 2327: 2320: 2317: 2312: 2308: 2304: 2302:9780444595652 2298: 2294: 2290: 2286: 2279: 2276: 2271: 2267: 2262: 2257: 2253: 2249: 2246:(2): 235–42. 2245: 2241: 2237: 2230: 2228: 2226: 2222: 2210: 2206: 2202: 2200:9780123809148 2196: 2192: 2188: 2184: 2180: 2176: 2169: 2166: 2154: 2150: 2146: 2142: 2138: 2134: 2130: 2126: 2122: 2115: 2113: 2111: 2107: 2102: 2098: 2094: 2090: 2085: 2080: 2076: 2072: 2068: 2061: 2058: 2053: 2049: 2044: 2039: 2034: 2029: 2025: 2021: 2017: 2010: 2007: 2002: 1998: 1994: 1990: 1986: 1982: 1975: 1972: 1967: 1961: 1957: 1950: 1948: 1946: 1942: 1937: 1933: 1929: 1925: 1921: 1917: 1910: 1907: 1902: 1898: 1893: 1888: 1884: 1880: 1876: 1872: 1868: 1861: 1858: 1853: 1849: 1844: 1839: 1835: 1831: 1827: 1823: 1819: 1817: 1808: 1805: 1800: 1796: 1792: 1788: 1784: 1780: 1773: 1770: 1765: 1761: 1756: 1751: 1747: 1743: 1739: 1732: 1729: 1724: 1720: 1715: 1710: 1705: 1700: 1696: 1692: 1688: 1681: 1678: 1673: 1669: 1664: 1659: 1654: 1649: 1645: 1641: 1637: 1630: 1627: 1622: 1618: 1613: 1608: 1604: 1600: 1596: 1589: 1587: 1585: 1581: 1576: 1569: 1566: 1561: 1557: 1552: 1547: 1543: 1539: 1535: 1531: 1527: 1523: 1519: 1517: 1508: 1505: 1500: 1494: 1490: 1489: 1481: 1478: 1473: 1467: 1463: 1456: 1453: 1448: 1444: 1439: 1434: 1430: 1426: 1422: 1418: 1414: 1410: 1406: 1402: 1398: 1391: 1388: 1383: 1379: 1374: 1369: 1365: 1361: 1357: 1353: 1349: 1342: 1339: 1334: 1330: 1325: 1320: 1316: 1312: 1308: 1304: 1300: 1293: 1290: 1285: 1281: 1277: 1273: 1269: 1265: 1261: 1257: 1250: 1248: 1244: 1239: 1233: 1229: 1222: 1219: 1214: 1210: 1208: 1200: 1197: 1192: 1188: 1184: 1180: 1177:(6): 858–67. 1176: 1172: 1165: 1162: 1157: 1153: 1149: 1143: 1139: 1138: 1130: 1128: 1126: 1124: 1120: 1115: 1113:9780123786319 1109: 1105: 1101: 1097: 1090: 1087: 1080: 1075: 1072: 1069: 1066: 1063: 1060: 1057: 1054: 1048: 1045: 1044: 1040: 1038: 1036: 1032: 1028: 1024: 1016: 1014: 1012: 1003: 999: 995: 992: 989: 985: 981: 977: 973: 969: 966: 963: 959: 957: 952: 948: 945: 944: 943: 936: 934: 932: 927: 925: 921: 917: 913: 909: 904: 902: 898: 894: 890: 883: 878: 874: 871: 868: 864: 860: 856: 855: 850: 846: 844: 840: 836: 833: 831: 826: 823: 822:glycoproteins 819: 815: 811: 808: 805: 801: 797: 794: 793: 792: 790: 786: 782: 778: 770: 768: 766: 762: 757: 755: 754:renal failure 751: 747: 742: 735: 733: 731: 727: 722: 720: 716: 715:crosslinkings 712: 708: 704: 699: 697: 693: 689: 685: 681: 673: 671: 669: 665: 661: 657: 653: 645: 643: 641: 637: 633: 626: 624: 622: 618: 614: 610: 606: 602: 601:transmembrane 598: 594: 590: 586: 582: 578: 574: 570: 566: 563: 559: 555: 550: 549:alpha-mannose 546: 542: 538: 529: 522: 519: 517: 515: 511: 510: 505: 504: 500:, mannose in 499: 495: 492: 491:phosphoserine 489: 485: 481: 477: 470: 468: 466: 462: 458: 454: 450: 445: 437: 434: 432: 430: 426: 422: 418: 414: 410: 406: 401: 393: 390: 385: 380: 376: 372: 368: 367:transcription 364: 361: 357: 354: 350: 346: 345: 344: 338: 333: 332:Glycan length 330: 327: 324: 321: 318: 315: 312: 311: 310: 308: 300: 298: 295: 293: 292: 287: 281: 279: 274: 270: 266: 262: 258: 254: 250: 246: 245:immune system 242: 238: 234: 230: 227: 223: 219: 215: 211: 210:macromolecule 207: 203: 195: 190: 187: 184: 180: 176: 173: 170: 167: 163: 159: 158:hydroxylysine 155: 151: 147: 143: 140: 136: 133: 130: 126: 124: 119: 116: 112: 108: 104: 101: 100: 99: 97: 95: 90: 86: 82: 77: 75: 71: 70:glycosylation 67: 63: 59: 55: 51: 47: 46:Glycosylation 43: 40: 33: 19: 3242:Biochemistry 2989: 2970:Galactolysis 2940:Glycogenesis 2745:Fermentation 2717:ATP synthase 2570: 2566: 2543: 2534: 2514: 2468: 2464: 2458: 2413:(1): 20–29. 2410: 2406: 2399: 2364: 2360: 2350: 2338:. Retrieved 2333: 2329: 2319: 2284: 2278: 2243: 2239: 2212:. Retrieved 2182: 2178: 2168: 2156:. Retrieved 2128: 2124: 2074: 2070: 2060: 2023: 2020:Biomolecules 2019: 2009: 1984: 1980: 1974: 1955: 1919: 1915: 1909: 1874: 1870: 1860: 1825: 1821: 1815: 1807: 1782: 1778: 1772: 1745: 1741: 1731: 1694: 1690: 1680: 1643: 1639: 1629: 1602: 1599:Glycobiology 1598: 1574: 1568: 1525: 1521: 1515: 1507: 1487: 1480: 1461: 1455: 1404: 1400: 1390: 1355: 1351: 1341: 1306: 1302: 1292: 1259: 1255: 1227: 1221: 1212: 1206: 1199: 1174: 1170: 1164: 1136: 1095: 1089: 1062:Fucosylation 1037:cell lines. 1031:HEK 293 1020: 1007: 993: 967: 961: 955: 946: 940: 928: 905: 887: 858: 852: 848: 842: 838: 829: 804:sialic acids 774: 758: 743: 739: 736:Role of AGEs 723: 700: 677: 667: 663: 659: 655: 649: 630: 580: 572: 567: 534: 520: 514:Mus musculus 513: 507: 501: 497: 474: 448: 447: 435: 428: 412: 404: 403: 391: 342: 304: 296: 291:Helicobacter 289: 282: 240: 237:glycoprotein 212:, typically 202:carbohydrate 199: 181:side-chain. 174: 134: 122: 102: 93: 78: 69: 50:carbohydrate 45: 44: 42: 18:Glycosylated 3096:lipogenesis 2958:Fructolysis 2772:Lactic acid 2528:. NBK20709. 2185:: 131–164. 2026:(12): 888. 1691:J Biol Chem 857:): removes 709:reactions, 707:Schiff base 640:prenylation 371:translation 369:or protein 231:of certain 118:side-chains 56:'), i.e. a 3216:Categories 2919:Glycolysis 2852:metabolism 2850:Nucleotide 2840:Urea cycle 2821:Amino acid 2810:Catabolism 2753:Glycolysis 2696:Glycolysis 2679:metabolism 2639:catabolism 2635:Metabolism 2340:2 November 2214:2 November 2158:1 November 1081:References 877:asparagine 875:: cleaves 696:side chain 636:GPI anchor 632:Glypiation 554:amino acid 541:tryptophan 453:eukaryotes 417:eukaryotes 339:Mechanisms 233:asparagine 206:covalently 189:Glypiation 179:tryptophan 111:asparagine 37:See also: 3092:lipolysis 2899:anabolism 2643:anabolism 2459:In silico 2093:2310-6905 1429:1755-4349 1284:206548002 1068:Glycation 984:mutations 867:threonine 818:galactose 783:from the 750:cataracts 680:glycation 349:glycation 150:threonine 89:cytoplasm 74:glycation 32:Glycation 3015:Nonhuman 3000:O-linked 2995:N-linked 2787:Specific 2597:25578468 2573:: 1–13. 2505:23840574 2465:PLOS ONE 2435:12800448 2427:28803068 2391:26805780 2311:23622397 2270:24909690 2209:20816394 2153:22917106 2145:14570055 2101:21341505 2052:31861217 2001:20549652 1936:27018258 1901:26878147 1852:26078847 1799:20496888 1723:21454577 1672:31868591 1621:17494086 1560:20044576 1447:33723379 1382:25747313 1358:: 63–9. 1333:24467287 1276:24385630 1191:21420850 1156:20301239 1041:See also 1002:diabetes 949:Over 40 937:Clinical 914:and the 873:PNGase F 785:proteins 761:hormones 726:collagen 721:(AGEs). 688:covalent 597:proteins 589:nitrogen 545:C-C bond 465:bacteria 425:bacteria 307:proteome 273:zoonotic 269:antigens 229:nitrogen 214:proteins 166:ceramide 154:tyrosine 139:hydroxyl 115:arginine 107:nitrogen 3155:Ketosis 2767:Ethanol 2650:General 2588:4340844 2496:3695939 2473:Bibcode 2452:GlycoEP 2382:4746335 2336:: 39–47 2261:4254162 2043:6995512 1892:5078750 1843:4465199 1764:1317872 1714:3093833 1663:6954052 1551:2978000 1530:Bibcode 1522:Science 1438:8102341 1409:Bibcode 1373:4827424 1324:4428802 1256:Science 1215:. 2013. 791:chain. 781:glycans 777:enzymes 767:level. 537:mannose 494:glycans 484:mannose 461:archaea 455:in the 421:archaea 253:lectins 251:called 196:Purpose 96:-GlcNAc 2677:Energy 2595:  2585:  2522:  2503:  2493:  2433:  2425:  2389:  2379:  2309:  2299:  2268:  2258:  2207:  2197:  2151:  2143:  2099:  2091:  2050:  2040:  1999:  1962:  1934:  1899:  1889:  1850:  1840:  1797:  1762:  1721:  1711:  1670:  1660:  1619:  1558:  1548:  1495:  1468:  1445:  1435:  1427:  1380:  1370:  1331:  1321:  1282:  1274:  1234:  1189:  1154:  1144:  1110:  976:cancer 863:serine 812:(from 798:(from 730:lysine 593:oxygen 585:carbon 488:GlcNAc 486:, and 480:fucose 476:Xylose 247:) via 218:lipids 146:serine 142:oxygen 54:glycan 3173:Other 3133:Other 2908:Human 2789:paths 2431:S2CID 2149:S2CID 1640:eLife 1280:S2CID 865:- or 789:sugar 664:trans 386:Types 226:amide 183:Aloin 160:, or 52:(or ' 2897:and 2593:PMID 2520:ISBN 2501:PMID 2423:PMID 2387:PMID 2342:2020 2307:PMID 2297:ISBN 2266:PMID 2216:2020 2205:PMID 2195:ISBN 2160:2020 2141:PMID 2097:PMID 2089:ISSN 2048:PMID 1997:PMID 1960:ISBN 1932:PMID 1897:PMID 1848:PMID 1795:PMID 1760:PMID 1719:PMID 1668:PMID 1617:PMID 1556:PMID 1493:ISBN 1466:ISBN 1443:PMID 1425:ISSN 1378:PMID 1329:PMID 1272:PMID 1232:ISBN 1187:PMID 1152:PMID 1142:ISBN 1108:ISBN 1000:and 922:and 839:endo 463:and 216:and 2921:⇄ 2762:ABE 2583:PMC 2575:doi 2491:PMC 2481:doi 2415:doi 2411:359 2377:PMC 2369:doi 2289:doi 2256:PMC 2248:doi 2244:453 2187:doi 2133:doi 2079:doi 2038:PMC 2028:doi 1989:doi 1924:doi 1887:PMC 1879:doi 1875:138 1838:PMC 1830:doi 1816:cis 1787:doi 1750:doi 1746:267 1709:PMC 1699:doi 1695:286 1658:PMC 1648:doi 1607:doi 1546:PMC 1538:doi 1526:327 1433:PMC 1417:doi 1368:PMC 1360:doi 1319:PMC 1311:doi 1264:doi 1260:343 1179:doi 1100:doi 974:or 841:-α- 765:DNA 668:cis 660:cis 642:.) 591:or 562:Gly 558:Ala 204:is 144:of 113:or 109:of 3218:: 3094:, 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Index

Glycosylated
Glycation
Chemical glycosylation
carbohydrate
glycan
glycosyl donor
glycosyl acceptor
glycoconjugate
glycation
post-translational modification
rough endoplasmic reticulum
cytoplasm
O-GlcNAc
nitrogen
asparagine
arginine
side-chains
N-linked glycosylation
dolichol phosphate
hydroxyl
oxygen
serine
threonine
tyrosine
hydroxylysine
hydroxyproline
ceramide
tryptophan
Aloin
Glypiation

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