Relevant bibliographies by topics / Enzymatic glycosylation

Academic literature on the topic 'Enzymatic glycosylation'

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Published: 9 March 2023
Last updated: 10 March 2023

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Journal articles on the topic "Enzymatic glycosylation"

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Kennedy, L., and T. J. Lyons. "Non-enzymatic glycosylation." British Medical Bulletin 45, no. 1 (1989): 174–90. http://dx.doi.org/10.1093/oxfordjournals.bmb.a072310.

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Chang, Cheng-Wei Tom. "Predictable Enzymatic Glycosylation." Chemistry & Biology 16, no. 6 (June 2009): 579–80. http://dx.doi.org/10.1016/j.chembiol.2009.06.001.

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Rivas, Francisco, Andres Parra, Antonio Martinez, and Andres Garcia-Granados. "Enzymatic glycosylation of terpenoids." Phytochemistry Reviews 12, no. 2 (April 26, 2013): 327–39. http://dx.doi.org/10.1007/s11101-013-9301-9.

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WEIGNEROVÁ, Lenka, Jaroslav SPÍZEK, Lucie NAJMANOVÁ, and Vladimír KREN. "Enzymatic Glycosylation of Lincomycin." Bioscience, Biotechnology, and Biochemistry 65, no. 8 (January 2001): 1897–99. http://dx.doi.org/10.1271/bbb.65.1897.

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Jeong, Hee Yong, Ji Youn Lee, and Tai Hyun Park. "Specificity of enzymatic in vitro glycosylation by PNGase F: a comparison of enzymatic and non-enzymatic glycosylation." Enzyme and Microbial Technology 35, no. 6-7 (December 2004): 587–91. http://dx.doi.org/10.1016/j.enzmictec.2004.08.010.

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Bojarová, Pavla, Ruben R. Rosencrantz, Lothar Elling, and Vladimír Křen. "Enzymatic glycosylation of multivalent scaffolds." Chemical Society Reviews 42, no. 11 (2013): 4774. http://dx.doi.org/10.1039/c2cs35395d.

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Council, Claire E., Kelly J. Kilpin, Jessica S. Gusthart, Sarah A. Allman, Bruno Linclau, and Seung Seo Lee. "Enzymatic glycosylation involving fluorinated carbohydrates." Organic & Biomolecular Chemistry 18, no. 18 (2020): 3423–51. http://dx.doi.org/10.1039/d0ob00436g.

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This contribution reviews the enzymatic synthesis, including optimisation efforts, of fluorinated carbohydrates involving fluorinated donors and/or acceptors, as well as the enzymatic activation of the fluorinated donors.
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Schultz, Michael, and Horst Kunz. "Enzymatic glycosylation of o-glycopeptides." Tetrahedron Letters 33, no. 37 (September 1992): 5319–22. http://dx.doi.org/10.1016/s0040-4039(00)79082-4.

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Zhou, Maoquan, and Jon S. Thorson. "Asymmetric Enzymatic Glycosylation of Mitoxantrone." Organic Letters 13, no. 10 (May 20, 2011): 2786–88. http://dx.doi.org/10.1021/ol200977u.

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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 "Enzymatic glycosylation"

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Taylor, Thomas Alex. "Investigations into novel enzymatic glycosylation methods." Thesis, University of Oxford, 2015. https://ora.ox.ac.uk/objects/uuid:3bfd1078-79d8-4c68-83a0-0bb5343583eb.

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Glycosylation is one of the most prevalent post-translational modifications found on human proteins. There is a great interest in developing new methodologies for the synthesis of glycoproteins, both to elucidate the functions of glycans on proteins and to exploit the beneficial properties they can confer on biotherapeutics. Here, research was carried out investigating enzymatic techniques to achieve the formation of homogenous glycoproteins. EndoS was the first enzyme investigated. EndoS natural activity is for the hydrolysis of glycans specifically from IgG, yet there has been research into its use for the opposite reaction and for glycan extension reactions. Here, a number of EndoS mutants were formed and investigated for this reaction, with a number of novel constructs giving a moderate yield of the glycosylated product. Structural investigations of EndoS were also conducted. In addition, research was conducted into the use of PglB in vitro for the direct glycosylation of an asparagine reside on a peptide with GlcNAc. Studies here demonstrate that it is possible to use far simpler glycan donor substrates with PglB. Additional studies showed that it was possible to conduct further enzymatic glycosylation reactions with GalT and EndoA after the initial PglB reaction. Further research was undertaken with EndoA, with it being desired to investigate whether it could catalyse the formation of a thioglycosidic linkage between two glycans, with the thiol bearing glycan acceptor to be attached to a peptide using PglB. After the successful synthesis of all the substrates, disappointingly, neither of the two enzymatic reactions were successful. Finally, the use of a glycal donor in an EndoA catalysed glycosylation was investigated. Unfortunately, no consumption of the glycan was observed in this reaction.
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Lyons, T. J. "Non-enzymatic glycosylation of collagen : In vivo and in vitro studies." Thesis, Queen's University Belfast, 1985. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.372984.

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Guedes, Sofia de Morais Correia Pereira. "Study of oxidation and non-enzymatic glycosylation posttranslational modifications using a proteomic approach." Doctoral thesis, Uniiversidade de Aveiro, 2011. http://hdl.handle.net/10773/7034.

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Doutoramento em Bioquímica
A glicosilação não-enzimática e o stress oxidativo representam dois processos importantes visto desempenharem um papel importante no que respeita às complicações de vários processos patofisiológicos. No presente, a associação entre a glicosilação não-enzimática e a oxidação de proteínas é reconhecida como sendo um dos principais responsáveis pela acumulação de proteínas não-funcionais que, por sua vez, promove uma contínua sensibilização para um aumento do stress oxidativo ao nível celular. Embora esteja disponível bastante informação no que respeita aos dois processos e suas consequências ao nível estrutural e funcional, permanecem questões por esclarecer acerca do que se desenvolve ao nível molecular. Com o objectivo de contribuir para uma melhor compreensão da relação entre a glicosilação não-enzimática e a oxidação, proteínas modelo (albumina, insulina e histonas H2B e H1) foram submetidas a sistemas in vitro de glicosilação não-enzimática e oxidação em condições controladas e durante um período de tempo específico. A identificação dos locais de glicosilação e oxidação foi realizada através de uma abordagem proteómica, na qual após digestão enzimática se procedeu à análise por cromatografia líquida acoplada a espectrometria de massa tandem (MALDI-TOF/TOF). Esta abordagem permitiu a obtenção de elevadas taxas de cobertura das sequências proteicas, permitindo a identificação dos locais preferenciais de glicosilação e oxidação nas diferentes proteínas estudadas. Como esperado, os resíduos de lisina foram os preferencialmente glicosilados. No que respeita à oxidação, além das modificações envolvendo hidroxilações e adições de oxigénio, foram identificadas deamidações, carbamilações e conversões oxidativas específicas de vários aminoácidos. No geral, os resíduos mais afectados pela oxidação foram os resíduos de cisteína, metionina, triptofano, tirosina, prolina, lisina e fenilalanina. Ao longo do período de tempo estudado, os resultados indicaram que a oxidação teve início em zonas expostas da proteína e/ou localizadas na vizinhança de resíduos de cisteína e metionina, ao invés de exibir um comportamente aleatório, ocorrendo de uma forma nãolinear por sua vez dependente da estabilidade conformacional da proteína. O estudo ao longo do tempo mostrou igualmente que, no caso das proteínas préglicosiladas, a oxidação das mesmas ocorreu de forma mais rápida e acentuada, sugerindo que as alterações estruturais induzidas pela glicosilação promovem um estado pro-oxidativo. No caso das proteínas pré-glicosiladas e oxidadas, foi identificado um maior número de modificações oxidativas assim como de resíduos modificados na vizinhança de resíduos glicosilados. Com esta abordagem é realizada uma importante contribuição na investigação das consequências do dano ‘glico-oxidativo’ em proteínas ao nível molecular através da combinação da espectrometria de massa e da bioinformática.
Glycation and oxidative stress are two important processes known to play a key role in complications of many pathophysiological processes. It is nowadays acknowledged the association between glycation and oxidation events as a major responsible for the accumulation of non-functional damaged proteins that in turn promote continuous sensitization to further oxidative stress at the cellular level. Despite the large amount of information concerning both events and their consequences at structural and functional levels, questions remain to answer on what happens at the protein molecular level. With the aim of contributing to better understand the interrelationship between glycation and oxidation, model proteins (BSA, insulin and histones H2B and H1) were submitted to in vitro systems of glycation and oxidation under controlled conditions and through a specific period of time. Identification of glycation and oxidation sites was performed through a proteomics approach. Protein samples were enzimatically digested and further analyzed by nano-liquid chromatography coupled to MALDI-TOF/TOF mass spectrometry. This approach allowed obtaining high protein coverage rates, enabling the identification of the most susceptible sites of glycation and oxidation in the different studied proteins. As expected, lysine residues were preferentially glycated and with respect to oxidation, besides protein hydroxyl derivatives and oxygen additions, modifications such as deamidations, carbamylations and specific amino acid oxidative conversions were detected. In general, the main affected amino acids by oxidative damage were cysteine, methionine, tryptophan, tyrosine, proline, lysine and phenylalanine. The time-course study of the oxidative damage indicated the oxidative attack, rather than occurring randomly, initiates at surface-exposed regions and/or near cysteine and methionine residues and occurs in a non-linear way depending on the conformational stability of the protein. Time-course analysis also showed a more pronounced and earlier occurrence of the oxidative damage in the case of preglycated proteins, suggesting that structural changes caused by glycation induce a pro-oxidant state. This increased oxidative damage included not only a greater number of oxidative modifications, but also of oxidized residues, occurring in the vicinity of the glycated residues. Through this kind of approach, an important contribution is made in the investigation of the consequences of protein ‘glycoxidative’ damage at a molecular level through the profit combination of mass spectrometry and bioinformatics.
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Lam, Chi-wai, and 林智威. "Potential role of non-enzymatic glycation and glycoxidation of low density lipoprotein in diabetic atherosclerosis." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2002. http://hub.hku.hk/bib/B3122751X.

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Li, Yuyuan. "Study on the nonenzymatic glycation of nuleosides/nucleotides and proteins with sugars : an in vitro investigation of advanced glycation endproducts (AGES) formation /." View online ; access limited to URI, 2008. http://0-digitalcommons.uri.edu.helin.uri.edu/dissertations/AAI3328724.

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Höök, Peter. "A novel single skeletal muscle cell in vitro motility assay : effects of aging and non-enzymatic glycosylation on myosin function /." Stockholm, 2001. http://diss.kib.ki.se/2001/91-628-4688-4/.

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Fitchette, Anne-Catherine. "Immunolocalisation de la xylosylation et le la fucosylation des glycannes complexes dans l'appareil de Golgi des cellules de sycomore (Acer pseudoplatanus L. )." Rouen, 1993. http://www.theses.fr/1993ROUES003.

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Les glycanes complexes portés par les glycoprotéines végétales diffèrent de ceux rencontrés chez les mammifères par l'absence d'acide sialique et par la présence d'un résidu fucose α1,3 lié au GlcNAc de la partie réductrice de l'unité chitobiose et d'un xylose lié en β1,2 au β-mannose. La séquence des évènements de maturation des glycanes n'est pas aussi bien connue dans la cellule végétale que pour la cellule animale. Dans cette étude, nous nous sommes principalement intéressés aux xylosyl- et fucosyl-transférases spécifiques aux plantes et intervenant dans la glycosylation tardive. Nous avons préparé des anticorps dirigés contre les glycanes végétaux contenant des résidus xylose ou fucose. Par immunodétection à l'aide de ces anticorps, nous avons visualisé la distribution subcellulaire des glycoprotéines portant ces glycanes complexes dans les cellules de sycomore. De plus, cette approche immunocytochimique a permis une localisation indirecte des xylosyl- et fucosyl-transférases en détectant les glycanes produits par ces enzymes dans les empilements golgiens des cellules de sycomore. Nos résultats indiquent que les glycanes complexes N-liés aux glycoprotéines vacuolaires ou pariétales sont xylosylés principalement dans le Golgi médian, alors que leur fucosylation est un évènement tardif intervenant dans le Golgi trans
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SINGH, MEENAKSHI. "Synthesis of Group B Streptococcus tipe II (GBSII) Oligosaccharide of Vaccine Development." Doctoral thesis, Università degli Studi di Milano, 2019. http://hdl.handle.net/2434/680023.

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Carbohydrates are among the most abundant molecules found on the cell surfaces of bacteria, parasites, and viruses. Apart from the conventional roles of carbohydrates as energy sources and structural polymers, carbohydrates are also associated with cancer metastasis, protein stabilization, pathogen infection and the immune response. Cells of our body have sensors made out of carbohydrates on outer surface of plasma membrane and acts as sensors and can detect many kinds of stimuli, and can signal the immune system to respond. Carbohydrate-protein molecular recognition processes have pivotal roles in infections and in immune response to pathogens. To date, several vaccines based on isolated capsular polysaccharides (CPSs) are marketed against infectious diseases. However, the use of isolated capsular polysaccharide poses several limitations, as natural sources are generally limited and the isolation is very challenging. Additionally, the isolated polysaccharides are heterogeneous and often contains impurities. Furthermore, limited protection of certain CPS antigens impairs the efficiency of vaccines. To overcome limitations associated with isolated polysaccharides, synthetic oligosaccharides present an effective alternative with great potential to understand glycan immunology and rationally design effective antigens. Consequently, characterization and reconstruction of carbohydrate epitopes with authentic composition has become one of the major target in glycoscience. To this end, strategies are needed to facilitate the streamlined design and generation of these antigens. This thesis concerns the development of an effective synthetic strategy to obtain Group B Streptococcus (GBS) type II oligosaccharide for vaccine development. GBS, a Gram-positive bacterium, inhabits the intestinal and genitourinary tract of 10‐30% of humans. GBS is one of the primary causes of bacterial infections among neonates and pregnant women, resulting in many severe diseases such as sepsis, meningitis, abortion, and so on. Type II GBS is one of the predominant GBS serotypes and is associated with about 15% of the invasive infections in adults and infants; therefore, represents an important human pathogen. The development of effective preventive vaccine against GBS is much needed to help pregnant women protect their newborns. This thesis describes the effective synthetic strategy to synthesize GBS type II oligosaccharide to be applied for vaccine development. Herein, we present a new and convenient synthesis of the repeating unit of GBS type II capsular polysaccharide. The structure of GBS type II was elucidated in 1983 and the repeating unit of GBS type II is a heptasaccharide composed of α-Neu5Ac (2-3)-ß-D-Gal-(1-4)- ß-D-GlcNAc-(1-3)-[-ß-D-Gal-(1-6)]-ß-D-Gal-(1-4)-ß-D-Gal-(1-3)-ß-D-Glc. The presented synthetic strategy is based on the five subcomponents derived from the retro synthetic analysis. Suitably protected lactosamine and lactose derivatives are pivotal building blocks in our synthesis and both disaccharide fragments have been achieved from the cheap and readily available lactose. Having started from two disaccharides saves the efforts of glycosylation and reduces the number of synthetic steps. The building blocks have been obtained in good overall yield following the optimized synthetic approach. The synthesis of backbone linear chain trisaccharide [ß-D-Gal-(1-4)-ß-D-Gal-(1-3)-ß-D-Glc] and pentasaccharide [ß-D-Gal-(1-4)-ß-D-GlcNAc-(1-3)-ß-D-Gal-(1-4)-ß-D-Gal-(1-3)-ß-D-Glc] has been achieved in excellent yield (~80% yield). The final steps of the synthesis comprise- the incorporation of ß-D-Gal unit into the linear chain pentasaccharide (currently ongoing) followed by the enzymatic introduction of sialic acid (NeuNAc unit) and subsequent deprotection to yield the repeating unit of GBS type II capsular polysaccharide. To conclude, in this thesis we present an efficient and easy handling synthetic approach to the heptasaccharide repeating unit of GBS type II. Readily available and cheap dairy side-product lactose has been used as a key structure in the presented scheme, allowing the efficient synthesis of the pentasaccharide backbone of the target compound. The synthetic GBS II fragments will be used for glycan array and structural studies and immunochemical characterization with specific monoclonal antibodies. This thesis comprises of four main chapters and the experimental section containing the methods and synthetic procedures for the discussed schemes. Chapter one is a general introduction and deals with the necessity and the social importance of the described project. Chapter two of the thesis outlines the scientific background and pathogenesis of GBS, carbohydrates and their biological importance, and general introduction of vaccines and how the carbohydrates can be used as a suitable vaccine candidate. Chapter two establishes the importance of synthetic carbohydrates and how the synthetic carbohydrates can be used to develop suitable effective vaccines against GBS diseases. Chapter three of the thesis contains the general introduction and structural features of GBS II CPS and the retrosynthetic analysis of GBS II CPS to identify the building blocks for the synthesis of GBS CPS II. Chapter four of the thesis summarizes the synthetic strategies and results to achieve the building blocks described in chapter three and the recombination of fragments to achieve the final molecule GBS II CPS repeating unit. The last part of the thesis will consists of the experimental methods and synthetic procedures to achieve the proposed molecule along with the characterization data.
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Alsamad, Fatima. "Développement d’une méthode de détection et de quantification des produits de glycation avancée par spectroscopie de diffusion Raman. Towards Normalization Selection of Raman Data in the Context of Protein Glycation: Application of Validity Indices to PCA Processed Spectra In depth investigation of collagen non-enzymatic glycation by Raman spectroscopy Surface Enhanced Raman Spectroscopy for Quantitative Analysis: Results of a Large-Scale European Multi-Instrument Interlaboratory Study." Thesis, Reims, 2020. http://www.theses.fr/2020REIMP202.

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Dans un contexte de vieillissement de la population et d’accroissement des maladies chroniques liées à l’âge, l’étude de la glycation non-enzymatique des protéines constitue un axe de recherche d’actualité. En effet, les produits de glycation avancée (AGE) jouent un rôle important dans la complication des maladies liées à l’âge comme le diabète. La compréhension des mécanismes de glycation est complexe du fait de la variété importante d’AGE formés. L’objectif de cette thèse est d’étudier in vitro la glycation des protéines, le collagène de type I en particulier, au moyen de cette technique de microscopie photonique. Deux AGE, la carboxyméthyllysine et la pentosidine, ont été ciblés. L’exploitation des spectres Raman a nécessité des adaptations chimiométriques originales. En effet, une approche couplant l’analyse en composantes principales aux indices de validité a été développée pour déterminer le type de normalisation à appliquer aux données spectrales. De plus, la régression Lasso a été utilisée pour identifier des marqueurs Raman associés au processus de glycation. Ces investigations ont été menées en réalisant des réactions de glycation sous diverses conditions expérimentales et en considérant les dosages en AGE par chromatographie liquide couplée à la spectrométrie de masse en tandem comme références. Ces travaux permettent de positionner l’apport et les limitations analytiques de la microspectroscopie Raman dans l’étude moléculaire de la glycation non-enzymatique des protéines
In the context of an aging population and an increase in age-related chronic diseases, the study of protein non-enzymatic glycation constitutes a topical research axis. Indeed, the advanced glycation products (AGE) play an important role in the complication of age-related diseases such as diabetes. Understanding the mechanisms of glycation is complex due to the large variety of AGE formed. The objective of this work is to study protein glycation in vitro, especially type I collagen, using this biophotonic technique. Two AGE, carboxymethyllysine and pentosidine, were targeted. The exploitation of Raman spectra required original chemometric adaptation. Indeed, an approach coupling principal component analysis to validity indices has been developed to determine the type of normalization to apply to spectral data. Additionally, Lasso regression was used to identify Raman markers associated with glycation process. These investigations were carried out by performing chemical reactions to induce glycation under various experimental conditions and by considering the AGE assays by liquid chromatography coupled to tandem mass spectrometry as references. This work makes it possible to position the contribution and the analytical limitations of Raman microspectroscopy in the molecular study of the non-enzymatic glycation of proteins
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Reaver, Nathan George Frederick. "Development and Characterization of Aptamers for the use in Surface Plasmon Resonance Sensors for the Detection of Glycated Blood Proteins." University of Toledo / OhioLINK, 2013. http://rave.ohiolink.edu/etdc/view?acc_num=toledo1373319138.

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Books on the topic "Enzymatic glycosylation"

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Lyons, Timothy James. Non-enzymatic glycosylation of collagen: In vivo and in vitro studies. 1985.

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Book chapters on the topic "Enzymatic glycosylation"

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Shoda, Shin-ichiro. "Enzymatic Glycosylation." In Glycoscience: Chemistry and Chemical Biology I–III, 1465–96. Berlin, Heidelberg: Springer Berlin Heidelberg, 2001. http://dx.doi.org/10.1007/978-3-642-56874-9_34.

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Shoda, Shin-ichiro. "Enzymatic Glycosylation." In Glycoscience, 1465–96. Berlin, Heidelberg: Springer Berlin Heidelberg, 2001. http://dx.doi.org/10.1007/978-3-662-11893-1_10.

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Divakar, Soundar. "Enzymatic Glycosylation of Alcohols." In Enzymatic Transformation, 123–35. India: Springer India, 2012. http://dx.doi.org/10.1007/978-81-322-0873-0_7.

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Divakar, Soundar. "Glycosylation of Some Selected Phenols and Vitamins." In Enzymatic Transformation, 137–214. India: Springer India, 2012. http://dx.doi.org/10.1007/978-81-322-0873-0_8.

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Divakar, Soundar. "Glycosylation of Phenols and Vitamins: An Overview." In Enzymatic Transformation, 215–24. India: Springer India, 2012. http://dx.doi.org/10.1007/978-81-322-0873-0_9.

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Blixt, Ola, and Nahid Razi. "Enzymatic Glycosylation by Transferases." In Glycoscience, 1361–85. Berlin, Heidelberg: Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/978-3-540-30429-6_32.

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Schultz, Michael, and Horst Kunz. "Enzymatic glycosylation of O-glycopeptides." In Peptides, 645–46. Dordrecht: Springer Netherlands, 1992. http://dx.doi.org/10.1007/978-94-011-2264-1_259.

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Thimm, Julian, and Joachim Thiem. "Enzymatic Glycosylation by Glycohydrolases and Glycosynthases." In Glycoscience, 1387–409. Berlin, Heidelberg: Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/978-3-540-30429-6_33.

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Zimowski, Jan. "Enzymatic Glycosylation of Tomatidine in Tomato Plants." In Advances in Experimental Medicine and Biology, 71–80. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4899-1367-8_7.

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Suzuki, Yukio, and Kei Uchida. "Enzymatic Glycosylation of Aglycones of Pharmacological Significance." In Carbohydrate Biotechnology Protocols, 297–312. Totowa, NJ: Humana Press, 1999. http://dx.doi.org/10.1007/978-1-59259-261-6_24.

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Conference papers on the topic "Enzymatic glycosylation"

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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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Herderich, M., S. Diem, and B. Gutsche. "Novel Forms of Tryptophan Glycoconjugates: Chemical Versus Enzymatic Glycosylation." In The 4th International Electronic Conference on Synthetic Organic Chemistry. Basel, Switzerland: MDPI, 2000. http://dx.doi.org/10.3390/ecsoc-4-01924.

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Shoda, Shin-ichiro, Yoshinori Misawa, Koushin Ushizaki, Hideyuki Kuwata, Michinari Kohri, Masaya Fujita, and Takeshi Watanabe. "SUGAR OXAZALINES: A NOVEL GLYCOSYL DONOR FOR ENZYMATIC GLYCOSYLATION CATALYZED BY CHITINASE." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.635.

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Collen, D. "SYNERGISM, MUTANTS AND HYBRIDS OF TISSUE-TYPE PLASMINOGEN ACTIVATO(t-PA) AND SINGLE CHAIN UROKINASE-TYPE PLASMINOGEN ACTIVATOR(scu-PA):POTENTIAL FORTHROMBOLYTIC THERAPY." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643725.

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With the development and clinical investigation of the fibrin-specific thrombolytic agents t-PA and scu-PA, many questions relating to their optimal use remain to be answered. It is, however, becoming apparent that these agents, in addition to several advantages,suffer some shortcomings, e.g. their therapeutic dose is large and their fibrin-specificity is limited.Therefore,the quest for better thrombolytic agents remains open.We will report results of four main lines of research which we are pursuing to obtain better agents or regimens for fibrin-specific thrombolytic therapy.1. Synergism between t-PA and scu-PA. t—PA and scu—PA in molar ratios between 4:1 and 1:4 show no synergism for thrombolysis of a plasma clot immersed in plasma in vitro(Thromb. Haemost. 56, 35, 1986) but display significant in vivo synergismin a rabbit model (Circulation 74, 838, 19867and in man (Am. Heart J. 112, 1083,1986).Recently we have confirmed synergism for thrombolysis between t-PA and scu-PA in a coronary thrombosis model in the dog(Zuskind et al., unpubl.) and in the baboon (Collen et al., unpubl.). Sequential infusion of t-PA followed by scu-PA butnot of scu-PA followed by t-PA is syneristic(Collen et al., this meeting).2. Mutants of t-PA. In collaboration with Larssen et al.,deletion mutants of t-PA, obtained by in vitro mutagenesis are characterized with respect to pharmacokinetics and thrombolytic properties.Mutants lacking the finger—like domain and/or the growth factor domainand/or one or all of the glycosylation sites have a much slower clearance (Larssenet al., this meeting) but unaltered specific thrombolytic properties and fibrin-specificity (Collen et al., this meeting).3. Mutants of scu-PA. A truncated form of scu-PA, lacking the 143 NH2~terminal amino acids was shown to be pharmacologically and thrombolytically indistinguishable from intact scu—PA (Stump et al.).Mutants of scu—PA in which Lys 158 is replaced,whereby they can no longer be converted to urokinase, still haveintrinsic plasminogen activating properties and act synergistically with t-PA on thrombolysis in vivo (Nelles et al., this meeting).4. Hybrids of t-PA and scu-PA. In collaboration with Pierard et al. (this meeting) hybrids of NH2~terminal regions of t-PA and COOH-terminal regions of u-PA were constructed which, after translation in transient expression systems, showed apparent specific activities comparable to that of natural two-chain u-PA. One hybrid, composed of the finger domain of t-PA and the B-chain of u-PA, was scaled up, purified and characterized (Gheysen et al., this meeting). This hybrid had theenzymatic properties typical of single chain u-PA, but had not acquired the fibrinaffinity of t-PA.Based on the finding that the isolated A-chain of t-PA retains the intact fibrin-affinity of the native molecule (Holvoet et al.,Eur.J. Biochem. 158, 173, 1986) andthat a low Mr form of scu-PA retains the functional properties of the intact moleule (J. Biol. Chem. 261, 17120, 1986), we have constructed and expressed a hybrid consisting of the NH -terminal region of t-PA (amino acids 1 to 263) and the COOH-terminal region of scu-PA (amino acids 144to 411) (Lijnen et al., this meeting). This hybrid has both fibrin affinity of t-PA (although less pronounced) and the enzymatic properties of scu-PA. The activation of plasminogen by the hybrid is apparently stimulated by fibrin.We believe that continued research along these lines will yield thrombolytic agents or therapeutic schemes, which may be superior to t-PA and/or scu-PA in terms of specific thrombolytic activity and fibrin-specificity.
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