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Journal articles on the topic 'Glycosylation'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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1

Mendez-Yañez, Angela, Patricio Ramos, and Luis Morales-Quintana. "Role of Glycoproteins during Fruit Ripening and Seed Development." Cells 10, no. 8 (2021): 2095. http://dx.doi.org/10.3390/cells10082095.

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Approximately thirty percent of the proteins synthesized in animal or plant cells travel through the secretory pathway. Seventy to eighty percent of those proteins are glycosylated. Thus, glycosylation is an important protein modification that is related to many cellular processes, such as differentiation, recognition, development, signal transduction, and immune response. Additionally, glycosylation affects protein folding, solubility, stability, biogenesis, and activity. Specifically, in plants, glycosylation has recently been related to the fruit ripening process. This review aims to provid

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2

Mal, Dipakranjan, та Soumen Chakraborty. "C-Glycosylation of Substituted β-Naphthols with Trichloroacetimidate Glycosyl Donors". Synthesis 50, № 07 (2018): 1560–68. http://dx.doi.org/10.1055/s-0036-1591746.

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Several glycosyl donors have been systematically investigated for C-glycosylation of substituted β-naphthols to delineate the effect of the substituents. Whereas glycosylations of the parent 2-naphthol are smoothly achievable, those of differently substituted 2-naphthols are cumbersome. Efficiency of the glycosylation depends on the nature of both the glycosyl donors and the substituents of the arene ring. Among various glycosyl donors, trichloroacetimidate glycosyl donors are found to be superior for glycosylation with substituted 2-naphthols.

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3

Demeter, Fruzsina, Tímea Balogh, Tse-Kai Fu та ін. "Preparation of α-l-Rhamnobiosides by Open and Conventional Glycosylations for Studies of the rHPL Lectin". Synlett 30, № 19 (2019): 2185–92. http://dx.doi.org/10.1055/s-0039-1690710.

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To study the effect of oligosaccharides on biological systems (e.g., carbohydrate–lectin interactions), chemical synthesis of the desired carbohydrate derivatives is highly desirable, but it is usually a very complicated task. Most of the stereo- and regioselective glycosylation reactions are carried out by using protected acceptors and donors. At the same time, open glycosylation (use of an unprotected acceptor) may shorten the reaction pathway, if sufficient selectivity can be achieved between the acceptor hydroxyl groups. Toward synthesis of higher oligomers and multivalent derivatives, whi

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4

Pasing, Yvonne, Albert Sickmann, and Urs Lewandrowski. "N-glycoproteomics: mass spectrometry-based glycosylation site annotation." Biological Chemistry 393, no. 4 (2012): 249–58. http://dx.doi.org/10.1515/hsz-2011-0245.

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Abstract Glycosylations are ubiquitous and, in many cases, essential protein modifications. Yet comprehensive and detailed analysis of glycosylations on a proteome-wide scale is a daunting and still unsolved challenge. However, a common workflow has emerged over the last decade for large-scale N-glycosylation site annotation by application of proteomic methodology. Thereby, the qualitative and quantitative assessment of hundreds or thousands of modification sites is enabled. This review presents a short overview about common enrichment techniques and glycosylation site detection for N-glycopep

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5

Brimble, Margaret A., Roger M. Davey, Malcolm D. McLeod, and Maureen Murphy. "C-Glycosylation of Oxygenated Naphthols with 3-Dimethylamino-2,3,6-trideoxy-L-arabino-hexopyranose and 3-Azido-2,3,6-trideoxy-D-arabino-hexopyranose." Australian Journal of Chemistry 56, no. 8 (2003): 787. http://dx.doi.org/10.1071/ch02236.

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In connection with studies directed towards the synthesis of the pyranonaphthoquinone antibiotic medermycin, C-aryl glycosides were prepared by C-glycosylation of naphthols with glycosyl donors. Boron trifluoride diethyl etherate proved to be a suitable Lewis acid to promote the C-glycosylation, and use of the azido glycosyl donor proved more successful than using the dimethylamino glycosyl donor. 5-Hydroxy-1,4-dimethoxynaphthalene underwent facile C-glycosylation with two particular glycosyl donors, whereas 3-bromo-5-hydroxy-1,4-dimethoxynaphthalene was not an effective coupling partner with

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6

Pal, Rita, Anupama Das, and Narayanaswamy Jayaraman. "One-pot oligosaccharide synthesis: latent-active method of glycosylations and radical halogenation activation of allyl glycosides." Pure and Applied Chemistry 91, no. 9 (2019): 1451–70. http://dx.doi.org/10.1515/pac-2019-0306.

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Abstract Chemical glycosylations occupy a central importance to synthesize tailor-made oligo- and polysaccharides of functional importance. Generation of the oxocarbenium ion or the glycosyl cation is the method of choice in order to form the glycosidic bond interconnecting a glycosyl moiety with a glycosyl/aglycosyl moiety. A number of elegant methods have been devised that allow the glycosyl cation formation in a fairly stream-lined manner to a large extent. The latent-active method provides a powerful approach in the protecting group controlled glycosylations. In this context, allyl glycosi

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7

Mukherjee, Mana Mohan, Nabamita Basu, and Rina Ghosh. "Iron(iii) chloride modulated selective 1,2-trans glycosylation based on glycosyl trichloroacetimidate donors and its application in orthogonal glycosylation." RSC Advances 6, no. 107 (2016): 105589–606. http://dx.doi.org/10.1039/c6ra21859h.

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FeCl<sub>3</sub> modulated excellent 1,2-trans selective glycosylations based on trichloroacetimidate glycosyl donors even in the presence of apparently silent C-2 protecting group, along with orthogonal glycosylation reactions are reported.

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8

Deng, Li-Fan, Yingwei Wang, Shiyang Xu, et al. "Palladium catalysis enables cross-coupling–like S _N 2-glycosylation of phenols." Science 382, no. 6673 (2023): 928–35. http://dx.doi.org/10.1126/science.adk1111.

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Despite their importance in life and material sciences, the efficient construction of stereo-defined glycosides remains a challenge. Studies of carbohydrate functions would be advanced if glycosylation methods were as reliable and modular as palladium (Pd)-catalyzed cross-coupling. However, Pd-catalysis excels in forming sp 2 -hybridized carbon centers whereas glycosylation mostly builds sp 3 -hybridized C–O linkages. We report a glycosylation platform through Pd-catalyzed S N 2 displacement from phenols toward bench-stable, aryl-iodide–containing glycosyl sulfides. The key Pd(II) oxidative ad

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9

Yang, Weizhun, Bo Yang, Sherif Ramadan, and Xuefei Huang. "Preactivation-based chemoselective glycosylations: A powerful strategy for oligosaccharide assembly." Beilstein Journal of Organic Chemistry 13 (October 9, 2017): 2094–114. http://dx.doi.org/10.3762/bjoc.13.207.

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Most glycosylation reactions are performed by mixing the glycosyl donor and acceptor together followed by the addition of a promoter. While many oligosaccharides have been synthesized successfully using this premixed strategy, extensive protective group manipulation and aglycon adjustment often need to be performed on oligosaccharide intermediates, which lower the overall synthetic efficiency. Preactivation-based glycosylation refers to strategies where the glycosyl donor is activated by a promoter in the absence of an acceptor. The subsequent acceptor addition then leads to the formation of t

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10

Mestrom, Przypis, Kowalczykiewicz, et al. "Leloir Glycosyltransferases in Applied Biocatalysis: A Multidisciplinary Approach." International Journal of Molecular Sciences 20, no. 21 (2019): 5263. http://dx.doi.org/10.3390/ijms20215263.

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Enzymes are nature’s catalyst of choice for the highly selective and efficient coupling of carbohydrates. Enzymatic sugar coupling is a competitive technology for industrial glycosylation reactions, since chemical synthetic routes require extensive use of laborious protection group manipulations and often lack regio- and stereoselectivity. The application of Leloir glycosyltransferases has received considerable attention in recent years and offers excellent control over the reactivity and selectivity of glycosylation reactions with unprotected carbohydrates, paving the way for previously inacc

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11

Wu, Jun, Nikolaos Kaplaneris, Shaofei Ni, Felix Kaltenhäuser, and Lutz Ackermann. "Late-stage C(sp2)–H and C(sp3)–H glycosylation of C-aryl/alkyl glycopeptides: mechanistic insights and fluorescence labeling." Chemical Science 11, no. 25 (2020): 6521–26. http://dx.doi.org/10.1039/d0sc01260b.

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C–H glycosylations of complex amino acids and peptides were accomplished through the assistance of triazole peptide-isosteres. The palladium-catalyzed glycosylation provided access to complex C-glycosides and fluorescent-labeled glycoamino acids.

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12

Whitfield, Dennis M., Stephen P. Douglas, Ting-Hua Tang, et al. "Differential reactivity of carbohydrate hydroxyls in glycosylations. II. The likely role of intramolecular hydrogen bonding on glycosylation reactions. Galactosylation of nucleoside 5′-hydroxyls for the syntheses of novel potential anticancer agents." Canadian Journal of Chemistry 72, no. 11 (1994): 2225–38. http://dx.doi.org/10.1139/v94-284.

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Contrary to expectations, many primary hydroxy groups are completely unreactive in glycosylation reactions, or give the desired glycosides in very low yields accompanied by products of many side reactions. Hydrogens of such primary hydroxyls are shown to be intramolecularly hydrogen bonded. Intermediates formed by nucleophilic attack by these hydroxyls on activated glycosylating agents may resist hydrogen abstraction. This resistance to proton loss is postulated to be the origin of the observed unreactivity. It is shown that successful glycosylations take place under acidic conditions under wh

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13

Hsu, Mei-Yuan, Sarah Lam, Chia-Hui Wu, Mei-Huei Lin, Su-Ching Lin, and Cheng-Chung Wang. "Direct Dehydrative Glycosylation Catalyzed by Diphenylammonium Triflate." Molecules 25, no. 5 (2020): 1103. http://dx.doi.org/10.3390/molecules25051103.

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Methods for direct dehydrative glycosylations of carbohydrate hemiacetals catalyzed by diphenylammonium triflate under microwave irradiation are described. Both armed and disarmed glycosyl-C1-hemiacetal donors were efficiently glycosylated in moderate to excellent yields without the need for any drying agents and stoichiometric additives. This method has been successfully applied to a solid-phase glycosylation.

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14

Li, Chunbao, Wenjiao Yuan та Yali Liu. "A Rapid and Diastereoselective Synthesis of 2-Deoxy-2-iodo-α-glycosides and its Mechanism for Diastereoselectivity". Synlett 28, № 15 (2017): 1975–78. http://dx.doi.org/10.1055/s-0036-1588440.

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Reductive deiodination of 2-deoxy-2-iodo-glycoside is an efficient and practical approach for the synthesis of 2-deoxyglycosides, which are moieties of bioactive compounds. However, inseparable diastereoisomers are usually formed in the preparation of 2-deoxy-2-iodo-glycosides via glycosylation of glycals with alcohols using current methods. To overcome this problem, a rapid and diastereoselective transformation of glycals and alcohols into 2-deoxy-2-iodo-α-glycosides enabled by I2/PhI(OAc)2 has been developed. 14 glycals, derived from 13 monosaccharides and one disaccharide, diastereoselectiv

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15

Jaeken, Jaak, and Gert Matthijs. "From glycosylation to glycosylation diseases." Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease 1792, no. 9 (2009): 823. http://dx.doi.org/10.1016/j.bbadis.2009.08.003.

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16

Chen, Michael X., Ho-Hsuan Su, Ching-Ya Shiao, et al. "Affinity Purification Coupled to Stable Isotope Dilution LC-MS/MS Analysis to Discover IgG4 Glycosylation Profiles for Autoimmune Pancreatitis." International Journal of Molecular Sciences 22, no. 21 (2021): 11527. http://dx.doi.org/10.3390/ijms222111527.

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Type 1 autoimmune pancreatitis (AIP) is categorized as an IgG4-related disease (IgG4-RD), where a high concentration of plasma IgG4 is one of the common biomarkers among patients. IgG Fc-glycosylation has been reported to be potential biosignatures for diseases. However, human IgG3 and IgG4 Fc-glycopeptides from populations in Asia were found to be isobaric ions when using LC-MS/MS as an analytical tool. In this study, an analytical workflow that coupled affinity purification and stable isotope dilution LC-MS/MS was developed to dissect IgG4 glycosylation profiles for autoimmune pancreatitis.

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17

NISSEN, Nicholas N., Ravi SHANKAR, Richard L. GAMELLI, Ashok SINGH, and Luisa A. DiPIETRO. "Heparin and heparan sulphate protect basic fibroblast growth factor from non-enzymic glycosylation." Biochemical Journal 338, no. 3 (1999): 637–42. http://dx.doi.org/10.1042/bj3380637.

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Non-enzymic glycosylation of basic fibroblast growth factor (bFGF, FGF-2) has recently been demonstrated to decrease the mitogenic activity of intracellular bFGF. Loss of this bioactivity has been implicated in impaired wound healing and microangiopathies of diabetes mellitus. In addition to intracellular localization, bFGF is also widely distributed in the extracellular matrix, primarily bound to heparan sulphate proteoglycans (HSPGs). Nonetheless, it is not clear if non-enzymic glycosylation similarly inactivates matrix-bound bFGF. To investigate this, we measured the effect of non-enzymic g

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18

Lahmann, Martina, and Stefan Oscarson. "Investigation of the reactivity difference between thioglycoside donors with variant aglycon parts." Canadian Journal of Chemistry 80, no. 8 (2002): 889–93. http://dx.doi.org/10.1139/v02-101.

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The reactivity of perbenzoylated thioglycosides with various thiol aglycons has been compared and quantified using competitive glycosylation experiments. Methyl 2,3,4-tri-O-benzyl-α-D-glucopyranoside was employed as acceptor and DMTST as a promoter. The reactivity was found, as expected, to depend on the electron donating properties of the aglycon. Hence, the most reactive donor, the cyclohexyl thioglycoside, was found to be about three times as reactive as the thioethyl glycoside, which in turn was twice as reactive as the thiomethyl donor. The thiophenyl donor was even less reactive, whereas

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19

Bandini, Giulia, Andreia Albuquerque-Wendt, Jan Hegermann, John Samuelson, and Françoise H. Routier. "Protein O- and C-Glycosylation pathways in Toxoplasma gondii and Plasmodium falciparum." Parasitology 146, no. 14 (2019): 1755–66. http://dx.doi.org/10.1017/s0031182019000040.

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AbstractApicomplexan parasites are amongst the most prevalent and morbidity-causing pathogens worldwide. They are responsible for severe diseases in humans and livestock and are thus of great public health and economic importance. Until the sequencing of apicomplexan genomes at the beginning of this century, the occurrence of N- and O-glycoproteins in these parasites was much debated. The synthesis of rudimentary and divergent N-glycans due to lineage-specific gene loss is now well established and has been recently reviewed. Here, we will focus on recent studies that clarified classical O-glyc

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20

HART, G. "Glycosylation." Current Opinion in Cell Biology 4, no. 6 (1992): 1017–23. http://dx.doi.org/10.1016/0955-0674(92)90134-x.

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21

Warren, Charles E. "Glycosylation." Current Opinion in Biotechnology 4, no. 5 (1993): 596–602. http://dx.doi.org/10.1016/0958-1669(93)90083-9.

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22

O'Connell, B. C., and L. A. Tabak. "A Comparison of Serine and Threonine O-Glycosylation by UDP-GaINAc:Polypeptide N-Acetylgalactosaminyltransferase." Journal of Dental Research 72, no. 12 (1993): 1554–58. http://dx.doi.org/10.1177/00220345930720120401.

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O-glycosylated proteins are ubiquitous in eukaryotes and are responsible for a variety of biological functions. O-glycosylation is initiated by the addition of N-acetylgalactosamine to serine or threonine residues, though it is not clear how specific residues are selected for modification. We have compared serine and threonine glycosylation using peptide substrates based on sequences from erythropoietin (EPO) and von Willebrand factor (HVF) that are glycosylated in vivo. UDP-GaINAc :polypeptide N-acetylgalactosaminyltransferase was derived from rat parotid, submandibular, and sublingual glands

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23

Chang, Te-Sheng, Jiumn-Yih Wu, Hsiou-Yu Ding, and Tzi-Yuan Wang. "Enzymatic Glycosylation of Ganoderma Terpenoid via Bacterial Glycosyltransferases and Glycoside Hydrolases." Biomolecules 15, no. 5 (2025): 655. https://doi.org/10.3390/biom15050655.

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Glycosylation is a critical enzymatic modification that involves the attachment of sugar moieties to target compounds, considerably influencing their physicochemical and biological characteristics. This review explored the role of two primary enzyme classes—glycosyltransferases (GTs) and glycoside hydrolases (GHs, glycosidases)—in catalyzing the glycosylation of natural products, with a specific focus on Ganoderma triterpenoids. While GTs typically use activated sugar donors, such as uridine diphosphate glucose, certain GHs can leverage more economical sugar sources, such as sucrose and starch

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24

Balieu, Juliette, Jae-Wan Jung, Philippe Chan, George P. Lomonossoff, Patrice Lerouge, and Muriel Bardor. "Investigation of the N-Glycosylation of the SARS-CoV-2 S Protein Contained in VLPs Produced in Nicotiana benthamiana." Molecules 27, no. 16 (2022): 5119. http://dx.doi.org/10.3390/molecules27165119.

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The emergence of the SARS-CoV-2 coronavirus pandemic in China in late 2019 led to the fast development of efficient therapeutics. Of the major structural proteins encoded by the SARS-CoV-2 genome, the SPIKE (S) protein has attracted considerable research interest because of the central role it plays in virus entry into host cells. Therefore, to date, most immunization strategies aim at inducing neutralizing antibodies against the surface viral S protein. The SARS-CoV-2 S protein is heavily glycosylated with 22 predicted N-glycosylation consensus sites as well as numerous mucin-type O-glycosyla

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25

Ryu, Kyoung-Seok, Jie-Oh Lee, Taek Hun Kwon, et al. "The presence of monoglucosylated N196-glycan is important for the structural stability of storage protein, arylphorin." Biochemical Journal 421, no. 1 (2009): 87–96. http://dx.doi.org/10.1042/bj20082170.

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Although N-glycosylation has been known to increase the stability of glycoproteins, it is difficult to assess the structural importance of glycans in the stabilization of glycoproteins. APA (Antheraea pernyi arylphorin) is an insect hexamerin that has two N-glycosylations at Asn196 and Asn344 respectively. The glycosylation of Asn344 is critical for the folding process; however, glycosylation of Asn196 is not. Interestingly, the N196-glycan (glycosylation of Asn196) remains in an immature form (Glc1Man9GlcNAc2). The mutation of Asn196 to glutamine does not change the ecdysone-binding activity

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26

Downey, A. Michael, and Michal Hocek. "Strategies toward protecting group-free glycosylation through selective activation of the anomeric center." Beilstein Journal of Organic Chemistry 13 (June 27, 2017): 1239–79. http://dx.doi.org/10.3762/bjoc.13.123.

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Glycosylation is an immensely important biological process and one that is highly controlled and very efficient in nature. However, in a chemical laboratory the process is much more challenging and usually requires the extensive use of protecting groups to squelch reactivity at undesired reactive moieties. Nonetheless, by taking advantage of the differential reactivity of the anomeric center, a selective activation at this position is possible. As a result, protecting group-free strategies to effect glycosylations are available thanks to the tremendous efforts of many research groups. In this

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27

Liang, Bing, Menglu Fan, Qi Meng, et al. "Effects of the Glycosylation of the HA Protein of H9N2 Subtype Avian Influenza Virus on the Pathogenicity in Mice and Antigenicity." Transboundary and Emerging Diseases 2024 (May 17, 2024): 1–18. http://dx.doi.org/10.1155/2024/6641285.

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As the H9N2 subtype avian influenza virus (H9N2 AIV) evolves naturally, mutations in the hemagglutinin (HA) protein still occur, which involves some sites with glycosylations. It is widely established that glycosylation of the H9N2 AIV HA protein has a major impact on the antigenicity and pathogenicity of the virus. However, the biological implications of a particular glycosylation modification site (GMS) have not been well investigated. In this study, we generated viruses with different GMSs based on wild-type (WT) viruses. Antigenicity studies revealed that the presence of viruses with a 200

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28

Pasala, Chiranjeevi, Sahil Sharma, Tanaya Roychowdhury, Elisabetta Moroni, Giorgio Colombo, and Gabriela Chiosis. "N-Glycosylation as a Modulator of Protein Conformation and Assembly in Disease." Biomolecules 14, no. 3 (2024): 282. http://dx.doi.org/10.3390/biom14030282.

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Glycosylation, a prevalent post-translational modification, plays a pivotal role in regulating intricate cellular processes by covalently attaching glycans to macromolecules. Dysregulated glycosylation is linked to a spectrum of diseases, encompassing cancer, neurodegenerative disorders, congenital disorders, infections, and inflammation. This review delves into the intricate interplay between glycosylation and protein conformation, with a specific focus on the profound impact of N-glycans on the selection of distinct protein conformations characterized by distinct interactomes—namely, protein

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29

Roy, Avishek, Steve Meregini, Zhenglan Chen, et al. "IgE production and stability regulated by Glycosylation in vivo." Journal of Immunology 210, no. 1_Supplement (2023): 151.19. http://dx.doi.org/10.4049/jimmunol.210.supp.151.19.

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Abstract Rationale: Essential functions of IgE have been attributed to specific glycosylations such as oligomannose (Fcer1a binding) and sialylation (pathogenicity). However, no study has examined how glycosylation affects IgE stability in vivo. Methods: Forward genetic screening for IgE specific phenotypes was performed using N-ethyl-N-nitrosourea (ENU) mutagenized mice. One low IgE phenotype, named benadryl, linked to a mutation in Mpi, which is essential for N-linked glycosylation. Benadrylwas validated by CRISPR knock-in . Immunological studies were performed to determine the causative mec

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Das, Rituparna, and Balaram Mukhopadhyay. "The effect of neighbouring group participation and possible long range remote group participation in O-glycosylation." Beilstein Journal of Organic Chemistry 21 (February 17, 2025): 369–406. https://doi.org/10.3762/bjoc.21.27.

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Stereoselective glycosylations are one of the most challenging tasks of synthetic glycochemists. The protecting building blocks on the glycosides contribute significantly in attaining the required stereochemistry of the resulting glycosides. Strategic installation of suitable protecting groups in the C-2 position, vicinal to the anomeric carbon, renders neighbouring group participation, whereas protecting groups in the distal C-3, C-4, and C-6 positions are often claimed to exhibit remote group participation with the anomeric carbon. Neighbouring group participation and remote group participat

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Dobrica, Mihaela-Olivia, Catalin Lazar, and Norica Branza-Nichita. "N-Glycosylation and N-Glycan Processing in HBV Biology and Pathogenesis." Cells 9, no. 6 (2020): 1404. http://dx.doi.org/10.3390/cells9061404.

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Hepatitis B Virus (HBV) glycobiology has been an area of intensive research in the last decades and continues to be an attractive topic due to the multiple roles that N-glycosylation in particular plays in the virus life-cycle and its interaction with the host that are still being discovered. The three HBV envelope glycoproteins, small (S), medium (M) and large (L) share a very peculiar N-glycosylation pattern, which distinctly regulates their folding, degradation, assembly, intracellular trafficking and antigenic properties. In addition, recent findings indicate important roles of N-linked ol

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Masbuchin, Ainun Nizar, Mohammad Saifur Rohman, and Ping-Yen Liu. "Role of Glycosylation in Vascular Calcification." International Journal of Molecular Sciences 22, no. 18 (2021): 9829. http://dx.doi.org/10.3390/ijms22189829.

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Glycosylation is an important step in post-translational protein modification. Altered glycosylation results in an abnormality that causes diseases such as malignancy and cardiovascular diseases. Recent emerging evidence highlights the importance of glycosylation in vascular calcification. Two major types of glycosylation, N-glycosylation and O-glycosylation, are involved in vascular calcification. Other glycosylation mechanisms, which polymerize the glycosaminoglycan (GAG) chain onto protein, resulting in proteoglycan (PG), also have an impact on vascular calcification. This paper discusses t

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Sasaki, Kaname, and Yusuke Hashimoto. "2,6-Lactones as a New Entry in Stereoselective Glycosylations." Synlett 28, no. 10 (2017): 1121–26. http://dx.doi.org/10.1055/s-0036-1588722.

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The advantages of glycosyl donors bearing a 2,6-lactone moiety in 1,2-cis-β-glycosylation reactions are discussed in the context of recent comprehension on the SN2–SN1 borderline. The 2,6-lactone structure increases the likelihood of the SN2-like reaction, analogous to 4,6-tethered structures or 2-O-electron-deficient substituents, which are known to mound the energetic barrier to SN1 reactions. Furthermore, the glycosyl cation generated from the 2,6-lactone donor seems to direct β-glycosides similar to the torsional and flipped cations generated from 4,6-tethered donors and mannuronate or 3,6

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Whitfield, Dennis M., M. Younus Meah, and Jiří J. Křepinský. "Ultrasonic Agitation Accelerates cis-Glycosylation with Heterogeneous Promoters." Collection of Czechoslovak Chemical Communications 58, no. 1 (1993): 159–72. http://dx.doi.org/10.1135/cccc19930159.

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Ultrasonic agitation increases the yield of glycosylations with donors such as 3,4,6-tri-O-acetyl-2-azido-2-deoxy-α-D-galactopyranosyl chloride using the heterogeneous promoters silver zeolite, cadmium zeolite or a mixture of silver perchlorate and silver carbonate on celite. The stereospecificity of the glycosylation depends on the nature of the alcohol to be glycosylated, the nature of the solid support and the solvent. Glycosylation catalyzed by silver zeolite in toluene solutions of the donor 3,4,6-tri-O-acetyl-2-deoxy-2-phtalimido-β-D-glucopyranosyl bromide, that usually produce trans-β-g

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35

Jia, Xiao G., and Alexei V. Demchenko. "Intramolecular glycosylation." Beilstein Journal of Organic Chemistry 13 (September 29, 2017): 2028–48. http://dx.doi.org/10.3762/bjoc.13.201.

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Carbohydrate oligomers remain challenging targets for chemists due to the requirement for elaborate protecting and leaving group manipulations, functionalization, tedious purification, and sophisticated characterization. Achieving high stereocontrol in glycosylation reactions is arguably the major hurdle that chemists experience. This review article overviews methods for intramolecular glycosylation reactions wherein the facial stereoselectivity is achieved by tethering of the glycosyl donor and acceptor counterparts.

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36

Ernst, J. F., and S. K. H. Prill. "O-Glycosylation." Medical Mycology 39, no. 1 (2001): 67–74. http://dx.doi.org/10.1080/mmy.39.1.67.74.

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37

Stanley, P. "Golgi Glycosylation." Cold Spring Harbor Perspectives in Biology 3, no. 4 (2011): a005199. http://dx.doi.org/10.1101/cshperspect.a005199.

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38

Stanley, Pamela. "Glycosylation engineering." Glycobiology 2, no. 2 (1992): 99–107. http://dx.doi.org/10.1093/glycob/2.2.99.

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Williams, Ruth. "Glycosylation PERKs." Journal of Cell Biology 176, no. 5 (2007): 549b. http://dx.doi.org/10.1083/jcb.1765iti4.

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Ernst, J. F., and S. K. H. Prill. "O -Glycosylation." Medical Mycology 39, no. 1 (2001): 67–74. http://dx.doi.org/10.1080/744118884.

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Wang, Hongda, Linda Obenauer-Kutner, Mei Lin, Yunping Huang, Michael J. Grace, and Stuart M. Lindsay. "Imaging Glycosylation." Journal of the American Chemical Society 130, no. 26 (2008): 8154–55. http://dx.doi.org/10.1021/ja802535p.

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Křen, Vladimír, Petr Halada, and Petr Sedmera. "Agroclavine Glycosylation." Collection of Czechoslovak Chemical Communications 64, no. 1 (1999): 114–18. http://dx.doi.org/10.1135/cccc19990114.

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BORMAN, STU. "GLYCOSYLATION ENGINEERING." Chemical & Engineering News Archive 84, no. 36 (2006): 13–22. http://dx.doi.org/10.1021/cen-v084n036.p013.

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Parslow, G. P., and E. J. Wood. "Protein glycosylation." Biochemical Education 26, no. 2 (1998): 145. http://dx.doi.org/10.1016/s0307-4412(98)00126-5.

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Kennedy, John F., and Charles J. Knill. "Protein Glycosylation." Carbohydrate Polymers 46, no. 4 (2001): 393. http://dx.doi.org/10.1016/s0144-8617(01)00251-x.

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Hennet, Thierry. "Collagen glycosylation." Current Opinion in Structural Biology 56 (June 2019): 131–38. http://dx.doi.org/10.1016/j.sbi.2019.01.015.

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Ploegh, H., and J. J. Neefjes. "Protein glycosylation." Current Opinion in Cell Biology 2, no. 6 (1990): 1125–30. http://dx.doi.org/10.1016/0955-0674(90)90166-c.

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Delente, Jacques J. "Glycosylation revisited." Trends in Biotechnology 3, no. 9 (1985): 218. http://dx.doi.org/10.1016/0167-7799(85)90009-5.

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März, Leopold. "Glycosylation reconfirmed." Trends in Biotechnology 4, no. 4 (1986): 81. http://dx.doi.org/10.1016/0167-7799(86)90199-x.

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West, Christopher M. "Nucleocytoplasmic Glycosylation." Biochimica et Biophysica Acta (BBA) - General Subjects 1800, no. 2 (2010): 47–48. http://dx.doi.org/10.1016/j.bbagen.2009.12.008.

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