Relevant bibliographies by topics / Glycosylation

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Glycosylation'

Author: Grafiati
Published: 4 June 2021
Last updated: 28 September 2024

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Journal articles on the topic "Glycosylation"

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Mendez-Yañez, Angela, Patricio Ramos, and Luis Morales-Quintana. "Role of Glycoproteins during Fruit Ripening and Seed Development." Cells 10, no. 8 (August 15, 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 provide valuable information and discuss the available literature focused on three principal topics: (I) glycosylations as a key posttranslational modification in development in plants, (II) experimental and bioinformatics tools to analyze glycosylations, and (III) a literature review related to glycosylations in fruit ripening. Based on these three topics, we propose that it is necessary to increase the number of studies related to posttranslational modifications, specifically protein glycosylation because the specific role of glycosylation in the posttranslational process and how this process affects normal fruit development and ripening remain unclear to date.
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Mal, Dipakranjan, and Soumen Chakraborty. "C-Glycosylation of Substituted β-Naphthols with Trichloroacet­imidate Glycosyl Donors." Synthesis 50, no. 07 (January 3, 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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Demeter, Fruzsina, Tímea Balogh, Tse-Kai Fu, Margaret Dah-Tsyr Chang, Yuan-Chuan Lee, Anikó Borbás, and Mihály Herczeg. "Preparation of α-l-Rhamnobiosides by Open and Conventional Glycosylations for Studies of the rHPL Lectin." Synlett 30, no. 19 (October 10, 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, which are often useful for lectin binding studies, open glycosylation reactions of propargyl and phenylthio rhamnosides were investigated as a rapid route to the α-(1,3)-linked rhamnobioside binding motif. The efficacy of open glycosylations proved to be highly dependent on both the type of donor and the solvent applied. Using a trichloroacetimidate donor in 1,4-dioxane, the open glycosylation reactions proceeded with high regioselectivity and in good yields. Conventional glycosylations, on the other hand, afforded the α-(1,2)- and α-(1,3)-linked rhamnobioside derivatives with slightly higher yields via three-step longer syntheses.
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Pasing, Yvonne, Albert Sickmann, and Urs Lewandrowski. "N-glycoproteomics: mass spectrometry-based glycosylation site annotation." Biological Chemistry 393, no. 4 (April 1, 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-glycopeptides, including benefits and challenges of analysis.
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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 (September 25, 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 glycosides have been developed to meet the requirement of latent-active reactivities under appropriate glycosylation conditions. Radical halogenation provides a newer route of activation of allyl glycosides to an activated allylic glycoside. Such an allylic halide activation subjects the glycoside reactive under acid catalysis, leading to the conversion to a glycosyl cation and subsequent glycosylation with a number of acceptors. The complete anomeric selectivity favoring the 1,2-trans-anomeric glycosides points to the possibility of a preferred conformation of the glycosyl cation. This article discusses about advancements in the selectivity of glycosylations, followed by delineating the allylic halogenation of allyl glycoside as a glycosylation method and demonstrates synthesis of a repertoire of di- and trisaccharides, including xylosides, with varied protecting groups.
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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 the same glycosyl donors. These studies indicate that subtle steric and electronic effects need to be considered in order to fine-tune C-glycosylations when using highly functionalized glycosyl donors.
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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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FeCl3 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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Deng, Li-Fan, Yingwei Wang, Shiyang Xu, Ao Shen, Hangping Zhu, Siyu Zhang, Xia Zhang, and Dawen Niu. "Palladium catalysis enables cross-coupling–like S N 2-glycosylation of phenols." Science 382, no. 6673 (November 24, 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 addition intermediate diverges from an arylating agent (Csp 2 electrophile) to a glycosylating agent (Csp 3 electrophile). This method inherits many merits of cross-coupling reactions, including operational simplicity and functional group tolerance. It preserves the S N 2 mechanism for various substrates and is amenable to late-stage glycosylation of commercial drugs and natural products.
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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 the glycoside product. As donor activation and glycosylation are carried out in two distinct steps, unique chemoselectivities can be obtained. Successful glycosylation can be performed independent of anomeric reactivities of the building blocks. In addition, one-pot protocols have been developed that have enabled multiple-step glycosylations in the same reaction flask without the need for intermediate purification. Complex glycans containing both 1,2-cis and 1,2-trans linkages, branched oligosaccharides, uronic acids, sialic acids, modifications such as sulfate esters and deoxy glycosides have been successfully synthesized. The preactivation-based chemoselective glycosylation is a powerful strategy for oligosaccharide assembly complementing the more traditional premixed method.
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Mestrom, Przypis, Kowalczykiewicz, Pollender, Kumpf, Marsden, Bento, et al. "Leloir Glycosyltransferases in Applied Biocatalysis: A Multidisciplinary Approach." International Journal of Molecular Sciences 20, no. 21 (October 23, 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 inaccessible synthetic routes. The development of nucleotide recycling cascades has allowed for the efficient production and reuse of nucleotide sugar donors in robust one-pot multi-enzyme glycosylation cascades. In this way, large glycans and glycoconjugates with complex stereochemistry can be constructed. With recent advances, LeLoir glycosyltransferases are close to being applied industrially in multi-enzyme, programmable cascade glycosylations.
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Dissertations / Theses on the topic "Glycosylation"

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Seward, Christopher M. P. "Stereoselective glycosylation chemistry." Thesis, University of Oxford, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.270281.

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Rising, Thomas W. D. F. "Glycosylation using endohexosaminidases." Thesis, University of Oxford, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.436989.

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Yassine, Hanane. "Caractérisation d’endocan murin : dualité fonctionnelle pro- ou anti-tumorale de l’endocan selon son statut de glycosylation. Etude des mécanismes d’action anti-tumorale." Thesis, Lille 2, 2014. http://www.theses.fr/2014LIL2S029/document.

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Une tumeur nécessite un approvisionnement en oxygène et en nutriments pour sa croissance mais aussi pour la dissémination à distance vers d’autres organes. L’angiogenèse tumorale est le phénomène exploité par la tumeur pour accomplir ses besoins. Les «Tip cells » situées à l’extrémité des capillaires en bourgeonnement initient et guident la croissance des néovaisseaux. Ces cellules sont considérées actuellement comme une cible thérapeutique pertinente pour les médicaments anti-angiogéniques. De nombreuses études ont permis d’identifier un cluster de marqueurs moléculaires exprimés de manière privilégiée au niveau des « Tip cells ». Un de ces marqueurs appelé endocan, a été identifié au laboratoire, et a fait objet du travail réalisé pendant la thèse. Endocan est un protéoglycane circulant surexprimé dans de nombreux cancers humains dont l’expression est fréquemment associée à un mauvais pronostic. Par son glycane, endocan intervient dans la croissance tumorale en augmentant l’effet des facteurs de croissance, mais aussi la migration des cellules endothéliales. Mon travail de thèse s’est orienté sur la caractérisation biochimique et fonctionnelle d’endocan murin afin d’avoir un modèle animal utile pour une meilleure compréhension de l’activité pro-tumorale d’endocan humain. Les travaux présentés dans ce manuscrit montrent qu’endocan murin est un protéoglycane de type chondroitine sulfate, mais partiellement glycosylé. Ce déficit de glycosylation est gouverné par des domaines peptiques distants codés par l’exon 1 et l’exon 2 et qui distinguent l’endocan murin de son homologue humain. Dans un modèle de xénogreffe tumorale chez la souris SCID, nous avons démontré qu’endocan murin ne présente aucun pouvoir pro-tumoral. Contrairement à l’endocan humain, il ralentit la vitesse de croissance tumorale. Cette propriété anti-tumorale est liée à la présence d’une forme non glycosylée. Nous avons pu montrer à travers plusieurs modèles de xénogreffes tumorales que cette propriété de freinage de la croissance tumorale s’étend aussi au core protéique d’endocan humain. De plus, nous avons pu démonter qu’une administration systémique d’endocan non glycosylé est significativement associée à un ralentissement de la croissance tumorale. Ceci établit la relation de causalité entre le polypeptide d’endocan et la propriété anti-tumorale observée dans les différents modèles animaux. Le polypeptide d’endocan ne modifie pas in vitro la prolifération ni la viabilité des cellules HT-29 ce qui laisse penser à un mécanisme d’action indirect. Sur le plan pathologique, nous avons montré que les formes non glycosylée d’endocan humain et murin sont associées à une réaction inflammatoire stromale constituée d’une infiltration pan-leucocytaire. La déplétion des leucocytes CD122+ (essentiellement les cellules NK murines) abolit partiellement l’effet anti-tumoral induit par l’endocan non glycosylé. Nos résultats ajoutent endocan au concert des molécules endothéliales tumorales qui participent au contrôle de la réaction inflammatoire stromale
Solid tumor requires a supply of oxygen and nutrients for growth but also for metastasizing to another organ. Tumor angiogenesis is the phenomenon exploited by tumor to fulfill these needs. The"Tip cells" located at the end of sprouting capillaries initiate and guide the growth of neovessels. These cells are currently considered as an important therapeutic target for anti-angiogenic drugs. Many studies have identified a cluster of molecular markers selectively expressed by the \\\\\\\\\\\\\\\\\\\\\\\\\\\\\\\"Tip cells.\\\\\\\\\\\\\\\\\\\\\\\\\\\\\\\" One of these markers called “endocan”, has represented the subject of the thesis work.Endocan is a circulating proteoglycan overexpressed in many human carcinomas, and expression is often associated with poor prognosis. It is suspected to play an important role in tumor development. Through its glycan chain, endocan modulates the effect of growth factors, and also the migration of endothelial cells. My thesis work has focused on the biochemical and functional characterization of mouse endocan in order to obtain a useful animal model for better understanding of the pro tumoral activity of human endocan. The work presented in this manuscript shows that mouse endocan is a chondroitin sulfate proteoglycan but much less glycanated than human endocan. Our data indicate that combinatorial distant domains from the O-glycanation site, located within exons 1 and 2 determine the glycanation pattern of endocan. In SCID mouse model of tumor xenograft we demonstrated that mouse endocan does not exhibit a pro tumoral activity. In opposite to the human homologue, overexpression of mouse endocan in HT-29 cells delayed the tumor appearance and reduced the tumor growth rate. This tumor growth inhibition was mostly supported by non glycanated mouse endocan. Unexpectedly, human non glycanated endocan overexpressed in HT-29, A549, or K1000 cells also delayed the tumor appearance and reduced the tumor growth. Moreover, systemic delivery of human non glycanated endocan also reproduced HT-29 tumor delay. In vitro, endocan polypeptide did not affect HT-29 cell proliferation, nor cell viability.Interestingly, a stromal inflammatory reaction was observed only in tumors overexpressing endocan polypeptide. In addition, depletion of CD122+ cells was able to delete partially the tumor delaying effect of endocan polypeptide. These results reveal a novel pathway for endocan in the control of tumor growth, which involves innate immune cells
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Rivinoja, A. (Antti). "Golgi pH and glycosylation." Doctoral thesis, University of Oulu, 2009. http://urn.fi/urn:isbn:9789514292699.

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Abstract Glycans, as a part of glycoproteins, glycolipids and other glycoconjugates, are involved in many vital intra- and inter-cellular tasks, such as protein folding and sorting, protein quality control, vesicular trafficking, cell signalling, immunological defence, cell motility and adhesion. Therefore, their correct construction is crucial for the normal functioning of eukaryotic cells and organisms they form. Most cellular glycans are constructed in the Golgi, and abnormalities in their structure may derive, for instance, from alkalinization of the Golgi lumen. In this work we show that Golgi pH is generally higher and more variable in abnormally glycosylating, i.e. strongly T-antigen (Gal-β1,3-GalNAc-ser/thr) expressing cancer cells, than in non-T-antigen expressing cells. We also confirmed that the Golgi pH alterations detected in cancer cells have the potential to induce glycosylation changes. A mere 0.2 pH unit increase in Golgi pH is able to induce T-antigen expression and inhibit terminal N-glycosylation in normally glycosylating cells. The mechanism of inhibition involves mislocalization of the corresponding glycosyltransferases. We also studied potential factors that can promote Golgi pH misregulation in health and disease, and found that cultured cancer cells, despite variation and elevation in Golgi pH, are fully capable of acidifying the Golgi lumen under the normal Golgi pH. Moreover, we introduce a Golgi localized Cl-/HCO3- exchanger, AE2a, that participates in Golgi pH regulation by altering luminal bicarbonate concentration and thus also buffering capacity. Participation of AE2a in Golgi pH regulation is especially intriguing, because it also provides a novel mechanism for expelling protons from the Golgi lumen.
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Anttonen, Katri Pauliina. "Protein glycosylation in actinomycetes." Thesis, University of Aberdeen, 2010. http://digitool.abdn.ac.uk:80/webclient/DeliveryManager?pid=92515.

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The aims of this project were to study the glycoproteome in two mycobacteria; M. marinum and M. smegmatis, and to assess the role of protein glycosylation by knocking out the Pmt homologues.  Due to technical difficulties in the construction of knock out strains in mycobacteria, the aims were changed to further elucidate the protein O-glycosylation pathway identified in S. coelicolor.  Reverse transcriptase PCR was used to show that pmt, ppm1 and the putative ppm2 (SCO1014) are expressed throughout the complex life cycle of S. coelicolor.  The putative ppm2- strain AV301, which can not be complemented with a wild type copy of SCO1014, was shown to harbour a point mutation in ppm1.  In Western blots, soluble Ppm1 localised to both the cytosolic and membrane fractions whereas Ppm2 was only seen in the membrane fraction.  Two bands at different molecular masses for Ppm2 were seen suggesting that this enzyme might be processed in Streptomyces.  Using the bacterial two hybrid system, it was shown that unlike in mycobacteria, Ppm1 does  not interact with Ppm2 in vivo.  Furthermore, unlike the yeast Pmt enzymes, Streptomyces Pmt does not dimerise in vivo, suggesting that bacterial Pmt homologues might have an alternative mode of action from the eukaryote enzymes.  To study the role of GDP-Mannose (GDP-Man) in protein glycosylation, three putative GDP-Man synthases were identified and disrupted; disruption in SCO1388 caused no obvious phenotypes whereas the SCO3039 and SCO4238 disruption strains had an earlier onset of pigment production as a sign of stress.  In attempts to disrupt all three GDP-Man synthases, it was discovered that the disruption of both SCO3039 and SCO4238 was lethal.
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Green, L. "Studies in glycosylation methodology." Thesis, University of Cambridge, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.599657.

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This thesis is divided into two sections. The first section covers techniques, strategies and mechanisms of oligosaccharide formation, illustrated with both literature and the author's results, highlighting the many subtleties involved in performing a glycosylation. These include attempts at trans-glycoside formation on a polymer support without the use of an acetyl directing group and the curious failure of an acetyl group to direct a glycosylation in the synthesis of a lactosamine derivative. The second section describes studies towards the development of stereocontrolled glycosylation protocol, based upon a intramolecular aglycon delivery strategy. Various tethers ranging from anomeric carbonates to anomeric phosphoranes were tried to realise this strategy but a solution remained elusive.
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Karg, Saskia Ruth. "N-glycosylation engineering in tobacco /." Zürich : ETH, 2008. http://e-collection.ethbib.ethz.ch/show?type=diss&nr=17989.

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Kameh, Homa. "Aberrant glycosylation in HEMPAS patients." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1997. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp01/MQ28786.pdf.

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Harthill, Jean Elizabeth. "N-glycosylation of horseradish peroxidase." Thesis, University of Oxford, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.292612.

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Kaloo, Sara. "Glycosylation of Carbohydrates by Glycosyltranferases." Thesis, University of Manchester, 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.508556.

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Books on the topic "Glycosylation"

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Davey, Gavin P., ed. Glycosylation. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-1685-7.

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1948-, Al-Rubeai Mohamed, ed. Glycosylation. Dordrecht: Kluwer Academic, 2002.

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Pezer, Marija, ed. Antibody Glycosylation. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-76912-3.

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Bill, Roslyn M., Leigh Revers, and Iain B. H. Wilson. Protein Glycosylation. Boston, MA: Springer US, 1998. http://dx.doi.org/10.1007/978-1-4615-4939-0.

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Bill, Roslyn M. Protein glycosylation. Boston: Kluwer Academic Publishers, 1998.

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Beck, Alain, ed. Glycosylation Engineering of Biopharmaceuticals. Totowa, NJ: Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-327-5.

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Cohen, Margo Panush. Diabetes and Protein Glycosylation. New York, NY: Springer New York, 1986. http://dx.doi.org/10.1007/978-1-4612-4938-2.

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Kameh, Homa. Aberrant glycosylation in HEMPAS patients. Ottawa: National Library of Canada = Bibliothèque nationale du Canada, 1999.

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Brooks, Susan A. Glycosylation in diverse cell systems: Challenges and new frontiers in experimental biology. London: Society for Experimental Biology, 2011.

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Winstel, Volker. Role of wall teichoic acid glycosylation. [S.l: s.n.], 2013.

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Book chapters on the topic "Glycosylation"

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Shenoy, Anjali, and Adam W. Barb. "Recent Advances Toward Engineering Glycoproteins Using Modified Yeast Display Platforms." In Glycosylation, 185–205. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1685-7_9.

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Mariethoz, Julien, Davide Alocci, Niclas G. Karlsson, Nicolle H. Packer, and Frédérique Lisacek. "An Interactive View of Glycosylation." In Glycosylation, 41–65. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1685-7_3.

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Kiely, Leonie J., and Rita M. Hickey. "Characterization and Analysis of Food-Sourced Carbohydrates." In Glycosylation, 67–95. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1685-7_4.

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Mota, Letícia Martins, Venkata S. Tayi, and Michael Butler. "Cell Free Remodeling of Glycosylation of Antibodies." In Glycosylation, 117–46. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1685-7_6.

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Walsh, Ian, Sophie Zhao, Katherine Wongtrakul-Kish, Matthew Choo, Shi Jie Tay, Christopher H. Taron, Pauline M. Rudd, and Terry Nguyen-Khuong. "Glycoinformatics Tools for Comprehensive Characterization of Glycans Enzymatically Released from Proteins." In Glycosylation, 3–23. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1685-7_1.

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Campbell, Matthew P., Sophie Zhao, Jodie L. Abrahams, Terry Nguyen-Khuong, and Pauline M. Rudd. "GlycoStore: A Platform for H/UPLC and Capillary Electrophoresis Glycan Data." In Glycosylation, 25–40. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1685-7_2.

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McDonald, Andrew G., and Gavin P. Davey. "O-Glycologue: A Formal-Language-Based Generator of O-Glycosylation Networks." In Glycosylation, 223–36. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1685-7_11.

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Gardner, Richard A., Paulina A. Urbanowicz, and Daniel I. R. Spencer. "N-glycan Characterization by Liquid Chromatography Coupled with Fluorimetry and Mass Spectrometry." In Glycosylation, 267–80. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1685-7_13.

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O’Farrell, Laura K., Alexander D. Fraser, and Gavin P. Davey. "Monitoring the Sialome on Human." In Glycosylation, 323–29. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1685-7_17.

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Hayes, Jerrard M., Darren M. O’Hara, and Gavin P. Davey. "Metabolic Labeling of Primary Using Carbohydrate Click Chemistry." In Glycosylation, 315–22. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1685-7_16.

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Conference papers on the topic "Glycosylation"

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AEBI, MARKUS. "N-LINKED PROTEIN GLYCOSYLATION." In 23rd International Solvay Conference on Chemistry. WORLD SCIENTIFIC, 2014. http://dx.doi.org/10.1142/9789814603836_0023.

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Herrmann, M. "SP0137 From glycosylation to inflammation." In Annual European Congress of Rheumatology, 14–17 June, 2017. BMJ Publishing Group Ltd and European League Against Rheumatism, 2017. http://dx.doi.org/10.1136/annrheumdis-2017-eular.7291.

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Davis, Benjamin G., and Sarah J. Ward. "GLYCOSYLATION VIA INTRAMOLECULAR TRANSFER (G.I.T.)." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.409.

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Hart, Joanne B., Andrew Falshaw, Erzsebet Farkas, Lars Kroger, Joachim Thiem, and Anna Win. "ENZYMATIC GLYCOSYLATION OF INOSITOL SUGARS." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.736.

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Beletić, Anđelo, Ivana Duvnjak Orešković, Tea Pribić, Jasminka Krištić, and Gordan Lauc. "Glycosylation Research in Bovines-the Significance and Recent Updates." In Socratic lectures 10. University of Lubljana Press, 2024. http://dx.doi.org/10.55295/psl.2024.i10.

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Glycosylation is an enzymatic process of attaching carbohydrate chains, glycans, to bi-omolecules, thereby influencing their biological features. Understanding the glycosyla-tion patterns and mechanisms in bovines (Bos taurus) has the potential to bring im-provements in various fields, aspects such as reproduction, herd health management, and the quality and safety of milk and meat products. The article, starting with a glimpse into glycobiology, will continue with overviewing the previous 5-year achievements of glycosylation in bovines, collated during a recent PubMed search. Hereafter, more details about the four studies will follow as the selected examples and go along with the concluding remarks and general future research directions. Keywords: data mining, glycosylation, bovines
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Kaufman, Randal J., David G. Bole, and Andrew J. Dorner. "THE INFLUENCE OF N-LINKED GLYCOSYLATION AND BINDING PROTEIN (BiP) ASSOCIATION IN THE SECRETION EFFICIENCY OF COMPLEX GLYCOPROTEINS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644016.

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We have studied the role of Binding Protein (BiP) or glucose regulated protein, GRP 78) in the processing and secretion of factor VIII (fVIII), von Willebrand factor (vWF), and tissue plasminogen activator(tPA) expressed in Chinese hamster ovary cell lines.fVIII is a 300 kDa protein which has a heavily glycosylated internal domain containing 20 clustered potential N-linked glycosylation sites.A significant proportion of the expressed fVIII is bound to BiP in the endoplasmic reticulum (ER) in a stable complex andnever secreted. Deletion of the heavily glycosylatedregion results in a lesser degree of association with BiP and increased secretion. Tunicamycin treatmentof cells producing the deleted form of fVIII resultsin stable association of the unglycosylated fVIII with BiP and inhibition of efficient secretion. vWF contains 17 potential N-linked glycosylation sites which are scattered throughout the molecule. vWF is transiently associated with BiP in the ER, demonstrating that CHO cells are competent to saecrete a complex glycoprotein. tPA, which contains 3 utilized N-linked glycosylation sites, exhibits low level association with BiP and is efficiently secreted. Disruptionof normal N-linked glycosylation of tPA, by site directed mutagenesis of the 3 Asn residues to Gin residues or by tunicamycin treatment of the tPA expressing CHO cells, results in reduced levels of secretion and increased association with BiP. This effect is enhanced by high levels of expression. The findings suggest that occupancy of glycosylation sites may effect protein folding and alter secretion efficiency by influencing the extent and stability of association with BiP.
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Fairweather, Jon K., Erich J. Molitor, Michael West, and Rick A. Wolf. "A STUDY OF MICROWAVE ASSISTED GLYCOSYLATION." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.626.

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Liu, Liming, Yuhan Nan, Jing Wang, Jingjing Zhang, Jinglin Zhou, and Haiyan Wu. "PLS-based process analysis for glycosylation reaction." In 2016 12th World Congress on Intelligent Control and Automation (WCICA). IEEE, 2016. http://dx.doi.org/10.1109/wcica.2016.7578264.

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Ross, M. Elizabeth. "Brain Features Distinguishing Congenital Disorders of Glycosylation." In Congenital Dystrophies - Neuromuscular Disorders Precision Medicine: Genomics to Care and Cure. Hamad bin Khalifa University Press (HBKU Press), 2020. http://dx.doi.org/10.5339/qproc.2020.nmd.9.

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Nakajima, Yukiko, Kazutoshi Sakakibara, Masahiro Ito, and Ikuko Nishikawa. "Prediction of the O-glycosylation by Support Vector Machines and Characteristics of the Crowded and Isolated O-glycosylation Sites." In 2009 Fifth International Conference on Intelligent Information Hiding and Multimedia Signal Processing (IIH-MSP). IEEE, 2009. http://dx.doi.org/10.1109/iih-msp.2009.154.

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Reports on the topic "Glycosylation"

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Tsekovska, Rositsa, Roumyana Mironova, and Ivan Ivanov. Protein Glycosylation in Bacteria. "Prof. Marin Drinov" Publishing House of Bulgarian Academy of Sciences, April 2021. http://dx.doi.org/10.7546/crabs.2021.04.01.

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Eichler, Jerry. Protein Glycosylation in Archaea: A Post-Translational Modification to Enhance Extremophilic Protein Stability. Fort Belvoir, VA: Defense Technical Information Center, January 2010. http://dx.doi.org/10.21236/ada515568.

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De Leoz, Maria Lorna A., David L. Duewer, and Stephen E. Stein. NIST interlaboratory study on the glycosylation of NISTmAb, a monoclonal antibody reference material, June 2015 to February 2016. Gaithersburg, MD: National Institute of Standards and Technology, July 2017. http://dx.doi.org/10.6028/nist.ir.8186.

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Liu, Xinyu, Wei Zhang, Mi-Mi Sun, and Qing-Hua Shang. Diagnostic value of Serum Mac-2 Binding Protein Glycosylation Isomer in liver fibrosis: A systematic review and meta-analysis. INPLASY - International Platform of Registered Systematic Review and Meta-analysis Protocols, October 2023. http://dx.doi.org/10.37766/inplasy2023.10.0086.

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Eyal, Yoram, Gloria Moore, and Efraim Lewinsohn. Study and Manipulation of the Flavanoid Biosynthetic Pathway in Citrus for Flavor Engineering and Seedless Fruit. United States Department of Agriculture, October 2003. http://dx.doi.org/10.32747/2003.7570547.bard.

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The proposal was aimed to identify and functionally characterize key genes/enzymes in the citrus flavanone neohesperidoside biosynthetic pathway and to use them as tools for metabolic engineering to decrease bitterness levels in grapefruit. The proposed section on fruit seediness was dropped as suggested by the reviewers of the proposal. Citrus flavor and aroma is composed of complex combinations of soluble and volatile compounds. The former includes mainly sugars, acids and flavanones, a subgroup of flavonoids that includes bitter compounds responsible for the bitter flavor of grapefruit and pummelo. Bitter species contain mostly bitter flavanone neohesperidosides, while non-bitter species contain mostly tasteless flavanone rutinosides. Both flavanone versions are diglycosides consisting of a rhamnose-glucose oligosaccharide a-linked at position 7 to the flavanone skeleton. However, in the bitter neohesperidosides the rhamnose is attached at position 2 of the glucose moiety, while in the tasteless rutinosides the rhamnose is attached at position 6 of the glucose moiety. Thus, the position of the rhamnose moiety, determined by the specificity of the last enzymes in the pathway- rhamnosyltransferase (1,2 or 1,6 specificity), is the determinant of the bitter flavor. Flavanones, like all flavonoids are synthesized via one of the branches of the phenylpropanoid pathway; the first committed step is catalyzed by the enzyme Chalcone synthase (CHS) followed by Chalcone isomerase (CHI). During the course of the work a key gene/enzyme in the biosynthesis of the bitter flavanones, a 1,2 rhamnosyltransferase (1,2RT), was functionally characterized using a transgenic cell-culture biotransformation system, confirming that this gene is a prime candidate for metabolic engineering of the pathway. This is the first direct functional evidence for the activity of a plant recombinant rhamnosyltransferase, the first confirmed rhamnosyltransferase gene with 1,2 specificity and the second confirmed rhamnosyltransferase gene altogether in plants. Additional genes of the flavanone pathway that were isolated during this work and are potential tools for metabolic engineering include (I) A putative 1,6 rhamnosyltransferase (1,6RT) from oranges, that is presumed to catalyze the biosynthesis of the tasteless flavanones. This gene is a prime candidate for use in future metabolic engineering for decreased bitterness and is currently being functionally characterized using the biotransformation system developed for characterizing rhamnosyltransferases. (2) A putative 7-0-glucosyltransferase presumed to catalyze the first glycosylation step of the flavanone aglycones. Silencing of gene expression in grapefruit was attempted using three genes: (1) The "upstream" flavonoid biosynthesis genes CHS and CHI, by antisense and co-suppression; and (2) The "downstream" 1,2R T, by an RNAi approach. CHS and CHI silencing resulted in some plants with a dramatically decreased level of the bitter flavanone neohesperidoside naringin in leaves. We have yet to study the long-term effect of silencing these genes on tree physiology, and on the actual bitterness of fruit. The effect of 1,2RT silencing on naringin content in grapefruit has yet to be examined, but a slow growth phenotype for these plants was noted. We speculate that silencing of the final glycosylation step of the flavanones delays their evacuation to the vacuole, resulting in accumulation of flavanones in the cytoplasm, causing inhibitory effects on plant growth. This speculation is yet to be established at the product level. Future metabolic engineering experiments are planned with 1,6RT following functional characterization.
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Glycosylation Helps Cellulase Enzymes Bind to Plant Cell Walls (Fact Sheet). Office of Scientific and Technical Information (OSTI), June 2012. http://dx.doi.org/10.2172/1044446.

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