Relevant bibliographies by topics / Glycoproteins Biotechnology

Academic literature on the topic 'Glycoproteins Biotechnology'

Author: Grafiati
Published: 10 December 2022
Last updated: 29 January 2023

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Journal articles on the topic "Glycoproteins Biotechnology"

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Zhao, Wenzhu, Ge Xu, Yuejiao Chen, Zhipeng Yu, Jianrong Li, Hanjie Yu, and Xiaojun Liao. "Glycan characterisation and antioxidant activity of a novel N-linked glycoprotein from okra." International Food Research Journal 28, no. 6 (December 1, 2021): 1119–30. http://dx.doi.org/10.47836/ifrj.28.6.03.

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Glycoproteins are present in all living beings, and have many biological functions. The characterisation of glycan structures of plant glycoproteins has become increasingly important in biotechnology and agricultural applications. In the present work, the antioxidant activities of the okra glycoprotein were assessed. The glycan structures of the okra glycoprotein were analysed using lectin microarray combined with matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry. The okra glycoprotein showed relatively strong 2,2-diphenyl-1-picrylhydrazyl-scavenging ability and reducing power. In addition, the glycan structures of the okra glycoprotein mainly contained N-acetylglucosamine, mannose, and galactose. Furthermore, complex-type N-glycans were the major type of glycan structures from the okra glycoprotein. Most of the complex N-glycans of the okra glycoprotein had terminal GalNAc and Gal N-glycan structures; the glycoprotein showed a high level of fucosylated complex-type glycans. Therefore, the okra glycoprotein is a promising antioxidant. Results of the present work might serve as a reference for a better understanding of the structural information and bioactivity of okra glycoprotein.
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Hsieh–Wilson, Linda C. "Tailor-made glycoproteins." Trends in Biotechnology 22, no. 10 (October 2004): 489–91. http://dx.doi.org/10.1016/j.tibtech.2004.08.009.

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Mellors, Alan, and D. Robert Sutherland. "Tools to cleave glycoproteins." Trends in Biotechnology 12, no. 1 (January 1994): 15–18. http://dx.doi.org/10.1016/0167-7799(94)90006-x.

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Lepenies, Bernd, and Peter H. Seeberger. "Simply better glycoproteins." Nature Biotechnology 32, no. 5 (May 2014): 443–45. http://dx.doi.org/10.1038/nbt.2893.

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Goochee, Charles F., Michael J. Gramer, Dana C. Andersen, Jennifer B. Bahr, and James R. Rasmussen. "The Oligosaccharides of Glycoproteins: Bioprocess Factors Affecting Oligosaccharide Structure and their Effect on Glycoprotein Properties." Bio/Technology 9, no. 12 (December 1991): 1347–55. http://dx.doi.org/10.1038/nbt1291-1347.

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Calo, Doron, Yael Eilam, Rachel G. Lichtenstein, and Jerry Eichler. "Towards Glycoengineering in Archaea: Replacement of Haloferax volcanii AglD with Homologous Glycosyltransferases from Other Halophilic Archaea." Applied and Environmental Microbiology 76, no. 17 (July 2, 2010): 5684–92. http://dx.doi.org/10.1128/aem.00681-10.

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ABSTRACT Like eukarya and bacteria, archaea also perform N-glycosylation. However, the N-linked glycans of archaeal glycoproteins present a variety not seen elsewhere. Archaea accordingly rely on N-glycosylation pathways likely involving a broad range of species-specific enzymes. To harness the enormous applied potential of such diversity for the generation of glycoproteins bearing tailored N-linked glycans, the development of an appropriate archaeal glycoengineering platform is required. With a sequenced genome, a relatively well-defined N-glycosylation pathway, and molecular tools for gene manipulation, the haloarchaeon Haloferax volcanii (Hfx. volcanii) represents a promising candidate. Accordingly, cells lacking AglD, a glycosyltransferase involved in adding the final hexose of a pentasaccharide N-linked to the surface (S)-layer glycoprotein, were transformed to express AglD homologues from other haloarchaea. The introduction of nonnative versions of AglD led to the appearance of an S-layer glycoprotein similar to the protein from the native strain. Indeed, mass spectrometry confirmed that AglD and its homologues introduce the final hexose to the N-linked S-layer glycoprotein pentasaccharide. Heterologously expressed haloarchaeal AglD homologues contributed to N-glycosylation in Hfx. volcanii despite an apparent lack of AglD function in those haloarchaea from where the introduced homologues came. For example, although functional in Hfx. volcanii, no transcription of the Halobacterium salinarum aglD homologue, OE1482, was detected in cells of the native host grown under various conditions. Thus, at least one AglD homologue works more readily in Hfx. volcanii than in the native host. These results warrant the continued assessment of Hfx. volcanii as a glycosylation “workshop.”
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Manocha, M. S., D. Xiong, and V. Govindsamy. "Isolation and partial characterization of a complementary protein from the mycoparasite Piptocephalis virginiana that specifically binds to two glycoproteins at the host cell surface." Canadian Journal of Microbiology 43, no. 7 (July 1, 1997): 625–32. http://dx.doi.org/10.1139/m97-089.

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Immunofluorescence microscopy was used to detect in the mycoparasite Piptocephalis virginiana the presence of a complementary glycoprotein that binds specifically to the host cell surface glycoproteins b and c, reported earlier from our laboratory. Germinated spores of P. virginiana treated with cell wall extract of the host Mortierella pusilla, primary antibody prepared against cell wall glycoproteins b and c, and fluorescein isothiocyanate (FITC) – goat anti-rabbit IgG conjugate showed fluorescence. Immunobinding analysis identified from the mycoparasite a protein of 100 kDa that binds with the host glycoproteins b and c, separately as well as collectively. Its purification was achieved by (i) 60% ammonium sulfate precipitation, (ii) heat treatment, (iii) Sephadex G-100 gel filtration, and (iv) preparative polyacrylamide gel electrophoresis (PAGE). The purity was ascertained by sodium dodecyl sulphate (SDS) – PAGE and Western blot analysis. Positive reaction to periodic acid – Schiff s reagent revealed its glycoprotein nature, and mannose was identified as a major sugar component. The specificity of the polyclonal antibody raised against electrophoretically purified complementary protein in rabbit was confirmed by dot immunobinding and Western blot analyses. Immunofluorescence microscopy revealed surface localization of the protein on the germ tubes of P. virginiana. Fluorescence was also observed at the surface of the germinated spores and hyphae of the host M. pusilla, after treatment with complementary protein from P. virginiana, primary antibody prepared against the complementary protein, and FITC – goat anti-rabbit IgG conjugate.Key words: biotrophic mycoparasite, cell surface agglutinin, glycoprotein immunobinding, immunofluorescence, mucoraceous host.
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Shirai, Sahoko, Ryota Uemura, Megumi Maeda, Hiroyuki Kajiura, Ryo Misaki, Kazuhito Fujiyama, and Yoshinobu Kimura. "Direct evidence of cytosolic PNGase activity in Arabidopsis thaliana: in vitro assay system for plant cPNGase activity." Bioscience, Biotechnology, and Biochemistry 85, no. 6 (March 16, 2021): 1460–63. http://dx.doi.org/10.1093/bbb/zbab047.

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ABSTRACT Cytosolic peptide:N-glycanase (cPNGase), which occurs ubiquitously in eukaryotic cells, is involved in the de-N-glycosylation of misfolded glycoproteins in the protein quality control system. In this study, we aimed to provide direct evidence of plant cPNGase activity against a denatured glycoprotein using a crude extract prepared from a mutant line of Arabidopsis thaliana lacking 2 acidic PNGase genes.
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Berman, Phillip W., and Laurence A. Lasky. "Engineering glycoproteins for use as pharmaceuticals." Trends in Biotechnology 3, no. 2 (February 1985): 51–53. http://dx.doi.org/10.1016/0167-7799(85)90059-9.

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Manocha, M. S., and Y. Chen. "Isolation and partial characterization of host cell surface agglutinin and its role in attachment of a biotrophic mycoparasite." Canadian Journal of Microbiology 37, no. 5 (May 1, 1991): 377–83. http://dx.doi.org/10.1139/m91-061.

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Cell surface proteins obtained by alkaline extraction from isolated cell walls of Mortierella pusilla and M. candelabrum, host and nonhost, respectively, of the mycoparasite Piptocephalis virginiana, were tested for their ability to agglutinate mycoparasite spores. The host cell wall protein extract had a high agglutinating activity (788 agglutination units/mg) compared with that of the nonhost extract (21 agglutination units/mg). Sodium dodecyl sulfate – polyacrylamide gel electrophoresis of the crude extract of the host revealed four bands, a, b, c, and d, with respective Mr of 117 000, 100 000, 85 000 and 64 000; these bands except for a faint band c, were absent from the nonhost surface. Deletion of proteins b or c from the crude protein extract of the host significantly reduced its agglutinating activity. Proteins b and c, purified by a series of procedures, were shown to be glycoproteins with glucose and N-acetylglucosamine as major saccharides. The agglutinating activity of a mixture of pure proteins b and c was over 500 times that of either glycoprotein alone, suggesting an involvement of both glycoproteins in the agglutination process. Further characterization showed that the two glycoproteins were heat-resistant with respect to their agglutinin function, which could be totally inhibited by three sugars: arabinose, glucose and N-acetyglucosamine. It is suggested that glycoproteins b and c are the two subunits of a carbohydrate-binding agglutinin present at the host cell surface and involved in agglutination and attachment of the mycoparasite germ tubes. Key words: agglutinin, attachment, cell surface, sugars, glycoproteins, mycoparasitism.
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Dissertations / Theses on the topic "Glycoproteins Biotechnology"

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Andersson, Pontus. "Comparison of Lectins and their suitability in Lectin Affinity Chromatography for isolation of Glycoproteins." Thesis, Uppsala universitet, Institutionen för biologisk grundutbildning, 2020. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-417024.

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Virtually all extracellular proteins in humans are glycoproteins and likewise are many biopharmaceuticals. The glycosylation is directly correlated to biological function and stability of these proteins. The ability to isolate glycoproteins is thus of great importance in many applications. The most common isolation method for glycoproteins is affinity chromatography using lectins, a ubiquitous and versatile group of carbohydrate-binding proteins. The lectin Concanavalin A (ConA) has long been used for this purpose but suffers from undesired leakage into the eluate, causing an inquiry of alternative chromatography ligands or optimization of the ConA resin.In this study, a total of 20 different lectins, including ConA, were evaluated and compared in terms of suitability as ligands in affinity chromatography for glycoprotein isolation. The lectins’ binding to glycoproteins were studied, mainly through microtiter plate binding assays using a monoclonal IgG1 antibody and Conalbumin (Ovotransferrin). Further, sugar-specificities and potential eluting sugars for the lectins were examined through inhibition with eight different carbohydrates. Additionally, the glycoprotein binding and leakage of ConA columns were examined, and a potential leakagereducing treatment of ConA resin evaluated.ConA was found to be superior in binding to the investigated glycoproteins but exhibited a limited binding when immobilized to an agarose resin. This discrepancy is likely a consequence of structurally hidden glycans on the used glycoproteins and requirements of long residence time when used in a chromatographic setting. Binding competition with several sugars were investigated with a similar microtiter plate binding assay. This method displayed potential to predict the behaviour of sugars and their suitability as eluting agents in a chromatography column. The best eluting sugar for ConA was showed to be methylmannoside, ideally in combination with methylglucoside. Lastly, evaluation of ConA columns with a crosslinking glutaraldehyde-treatment showed that the ConA ligand leakage may be significantly reduced, although further studies and optimizations are needed.This study thus presents a repertoire of lectins and their differences in terms of glycoprotein-binding and sugar-specificity, as well as evaluations of ConA columns’ efficiency and potential leakage-prevention.
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PEREIRA, THIAGO M. "Análise das diferenças bioquímicas nos tecidos e lesões tireoidianas por imageamento espectral no infravermelho (FTIR)." reponame:Repositório Institucional do IPEN, 2013. http://repositorio.ipen.br:8080/xmlui/handle/123456789/10567.

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Tese (Doutoramento)
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Instituto de Pesquisas Energeticas e Nucleares - IPEN-CNEN/SP
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Walton, Kelly Louise. "Genetic engineering of the major envelope glycoprotein of a baculovirus." Australasian Digital Theses Program, 2008. http://hdl.handle.net/1959.3/36643.

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Thesis (PhD) - Swinburne University of Technology, 2008.
Submitted for the degree of Doctor of Philosophy, Swinburne University of Technology - 2008. Typescript. Includes bibliographical references (p. 195-208).
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Halle, Briana. "Production of a Cost-Effective, TMV-Based Rabies Vaccine through Recombinant DNA Technology." Scholarship @ Claremont, 2018. http://scholarship.claremont.edu/cmc_theses/1816.

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Infectious diseases remain a significant cause of human deaths, as approximately 15 million deaths were attributed to infectious diseases in 2010 (Dye, 2014). One such disease is rabies, which causes around 59,000 human deaths worldwide annually according to some estimates (Kessels et al., 2017). However, 95% of human deaths attributed to rabies occur in Asia and Africa (Singh et al., 2017). Rabies is preventable, yet it is still a major concern in developing, low-income countries that lack access to the medical care necessary to combat it (Hampson et al., 2015). Alternative techniques for low-cost vaccine production have the potential to resolve this issue. This research investigates the use of recombinant DNA techniques and plant biotechnology to produce a more cost-effective vaccine for rabies. Gene sequences from the rabies glycoprotein were inserted at the end of the coat protein portion of the Tobacco Mosaic Virus (TMV) genome. Plants were then infected with this recombinant virus, with hopes that TMV particles would assemble with proteins produced from the inserted glycoprotein sequence fused to the TMV coat protein. Results thus far suggest some of the sequences could be producing recombinant TMV particles, although issues involving successful extraction and reversion to wild type are still a challenge. Additionally, other research suggests that this is an effective method for vaccine development in general and for rabies.
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Kamdem, Toukam Donatien [Verfasser], Klaus Thomas [Gutachter] Überla, and Albrecht [Gutachter] Bufe. "Targeting antibody responses to the membrane proximal external region of the envelope glycoprotein of human immunodeficiency virus / Donatien Kamdem Toukam ; Gutachter: Klaus Thomas Überla, Albrecht Bufe ; Fakultät für Biologie und Biotechnologie." Bochum : Ruhr-Universität Bochum, 2012. http://d-nb.info/1226426379/34.

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Strycharz, Joseph P. "Polygenic Resistance In The Highly DDT-resistant 91-r Strain Of Drosophila Melanogaster Involves Decreased Penetration, Increased Metabolism And Direct Excretion Of Ddt." 2010. https://scholarworks.umass.edu/theses/424.

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Resistance to dichlorodiphenyltrichloroethane (DDT) in the 91-R strain of Drosophila melanogaster is extremely high compared to the susceptible Canton-S strain (>1500 times). Oxidative detoxification is involved in resistance but is not the only mechanism. Rates of DDT penetration, metabolism, and excretion were determined radiometrically between resistant 91-R and susceptible Canton-S strains. Contact penetration was ~1.5-times slower with 91-R flies compared to Canton-S flies. The 91-R strain had 13-fold more cuticular hydrocarbons, possibly resulting in penetration differences. DDT was metabolized ~33-fold more extensively by 91-R than Canton-S resulting in dichlorodiphenyldichloroethane (DDD), two unidentified metabolites and polar conjugates being formed in significantly greater amounts. 91-R also excreted ~5.0 times more DDT and metabolites than Canton-S. Verapamil pretreatment reduced the LD50 value for 91-R flies topically dosed with DDT by a factor of 10-fold. Thus, it is likely that the increased excretion by 91-R flies is due to the increased expression of ATP-binding cassette (ABC) transporter genes, including MDR50 (CG8525) that had a 36% higher transcript level by quantitative real time PCR than Canton-S flies. In summary, DDT resistance in 91-R is polyfactorial and includes reduced penetration, increased detoxification and direct excretion.
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Books on the topic "Glycoproteins Biotechnology"

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Tang sheng wu xue yu tang sheng wu gong cheng. Beijing: Qing hua da xue chu ban she, 2002.

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International Workshop on Protein Glycosylation (1990 Braunschweig, Germany). Protein glycosylation: Cellular, biotechnological, and analytical aspects. Weinheim, Federal Republic of Germany: VCH, 1991.

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Glycosylation Engineering of Biopharmaceuticals Methods in Molecular Biology. Humana Press Inc., 2013.

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Book chapters on the topic "Glycoproteins Biotechnology"

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Townsend, R. Reid. "Quantitative Monosaccharide Analysis of Glycoproteins." In Chromatography in Biotechnology, 86–101. Washington, DC: American Chemical Society, 1993. http://dx.doi.org/10.1021/bk-1993-0529.ch007.

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Alvarez, María Alejandra. "Expression of the Potentially Immunogenic Truncated Glycoprotein E2 (From Viral Bovine Diarrhoea Virus) in Nicotiana tabacum Chapter 8." In Plant Biotechnology for Health, 133–43. Cham: Springer International Publishing, 2014. http://dx.doi.org/10.1007/978-3-319-05771-2_8.

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Kumar Chatterjee, Swapan, and Snigdha Saha. "Glycan and Its Role in Combating COVID-19." In Biotechnology to Combat COVID-19 [Working Title]. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.97240.

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Newly identified beta-coronavirus i.e. the 2019 novel coronavirus is associated with a contagious transmittable respiratory disease called COVID-19. This disease has been declared as a “pandemic” by the World Health Organization (WHO). The entry of coronavirus in the human respiratory epithelial cells depends upon the interaction between host cell receptor ACE2 and viral S-glycoprotein. However, this type of molecular recognition in between cell surface receptors and envelope glycoproteins are mediated by specific glycan epitopes and attribute to viral entry through membrane fusion. Glycans are essential biomolecules made by all living organisms, have roles in serving structure, energy storage, and system regulatory purposes. The glycan shield plays a crucial role in concealing the surface S protein from molecular recognition. The immunomodulatory properties of Glycan-binding proteins (GBPs) like Lectins, build them as an attractive candidates for vaccine adjuvant. Investigations involving the complement system activation by the lectin pathway in COVID-19 and diseases are in need of the hour. The innate immune response involving complement system could have varied biological effects against an array of microbial infections. The advances in glycoprotein style methods especially immunomodulatory action of some lectins are necessary to boost the effectiveness of treatment of COVID-19 and other pandemics.
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Nilsson, Bo. "Linkage analysis by mass spectrometry of chemically modified oligosaccharides from glycosphingolipids and glycoproteins." In Progress in Biotechnology, 29–47. Elsevier, 1995. http://dx.doi.org/10.1016/s0921-0423(06)80091-2.

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Crispin, M., C. N. Scanlan, and T. A. Bowden. "Structure and Biosynthesis of Glycoprotein Carbohydrates." In Comprehensive Biotechnology, 51–68. Elsevier, 2011. http://dx.doi.org/10.1016/b978-0-444-64046-8.00007-0.

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Crispin, M., C. N. Scanlan, and T. A. Bowden. "Structure and Biosynthesis of Glycoprotein Carbohydrates." In Comprehensive Biotechnology, 73–90. Elsevier, 2011. http://dx.doi.org/10.1016/b978-0-08-088504-9.00009-x.

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De Wachter, Charlot, Linde Van Landuyt, and Nico Callewaert. "Engineering of Yeast Glycoprotein Expression." In Advances in Biochemical Engineering/Biotechnology. Berlin, Heidelberg: Springer Berlin Heidelberg, 2018. http://dx.doi.org/10.1007/10_2018_69.

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Yelverton, Elizabeth, Shirley Norton, John F. Obijeski, and David V. Goeddel. "Rabies Virus Glycoprotein Analogs: Biosynthesis in Escherichia coli." In Biotechnology & Biological Frontiers, 8–20. Routledge, 2019. http://dx.doi.org/10.4324/9780429050329-2.

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"Glycoprotein Targeting and Other Applications of Lectins in Biotechnology." In Advances in Protein and Peptide Sciences, edited by Aabgeena Naeem, M. Saleemuddin, and Rizwan H. Khan, 833–76. BENTHAM SCIENCE PUBLISHERS, 2013. http://dx.doi.org/10.2174/9781608054879113010022.

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Conference papers on the topic "Glycoproteins Biotechnology"

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Wang, Xiaoping, Huanping Lin, Qiaoxia Wang, Yan Gu, and Yi Xu. "Specific Immunity Elicited by Cross-link Complex Alpha-fetoprotein and Glycoprotein 96." In 2012 International Conference on Biomedical Engineering and Biotechnology (iCBEB). IEEE, 2012. http://dx.doi.org/10.1109/icbeb.2012.361.

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Nayel, Omnia, Mohamed Sobhy, Azza Baraka, Mohamed El Samak, and Sherine Abdel Kader. "The Relevance of Platelet Glycoprotein GP IIb/IIIa Polymorphism to Anti-platelets Response in Acute Coronary Syndrome." In Annual International Conference on Advances in Biotechnology. Global Science & Technology Forum (GSTF), 2013. http://dx.doi.org/10.5176/2251-2489_biotech13.34.

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