Literatura académica sobre el tema "IgG N-glycosylation"
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Artículos de revistas sobre el tema "IgG N-glycosylation"
Kao, Chih-Chin, San-Yuan Wang, Yung-Kun Chuang, Wei-Yuan Lee, Wei-Chiao Chang, Mai-Szu Wu, Tai-Chih Kuo y I.-Lin Tsai. "Clinical Mass Spectrometry Discovered Human IgG Sialylation as a Potential Biosignature for Kidney Function". Journal of Personalized Medicine 11, n.º 8 (31 de julio de 2021): 761. http://dx.doi.org/10.3390/jpm11080761.
Texto completoPfeifle, R., J. Kittler, M. Wuhrer, G. Schett y G. Krönke. "AB0016 THE IMPACT OF IL-17A THERAPY ON IGG SIALYLATION IN HUMANS". Annals of the Rheumatic Diseases 80, Suppl 1 (19 de mayo de 2021): 1042.1–1043. http://dx.doi.org/10.1136/annrheumdis-2021-eular.1087.
Texto completoKozłowska, Kamila, Magdalena Rydlewska, Marta Ząbczyńska y Ewa Pocheć. "IgG glycosylation in autoimmune diseases". Postępy Higieny i Medycyny Doświadczalnej 72 (12 de noviembre de 2018): 975–90. http://dx.doi.org/10.5604/01.3001.0012.7351.
Texto completoHahm, Lee y Ahn. "Investigation of Site-Specific Differences in Glycan Microheterogeneity by N-Glycopeptide Mapping of VEGFR-IgG Fusion Protein". Molecules 24, n.º 21 (30 de octubre de 2019): 3924. http://dx.doi.org/10.3390/molecules24213924.
Texto completoShadrina, Alexandra S., Alexander S. Zlobin, Olga O. Zaytseva, Lucija Klarić, Sodbo Z. Sharapov, Eugene D Pakhomov, Marcus Perola et al. "Multivariate genome-wide analysis of immunoglobulin G N-glycosylation identifies new loci pleiotropic with immune function". Human Molecular Genetics 30, n.º 13 (12 de marzo de 2021): 1259–70. http://dx.doi.org/10.1093/hmg/ddab072.
Texto completoMajewska, Natalia I., Max L. Tejada, Michael J. Betenbaugh y Nitin Agarwal. "N-Glycosylation of IgG and IgG-Like Recombinant Therapeutic Proteins: Why Is It Important and How Can We Control It?" Annual Review of Chemical and Biomolecular Engineering 11, n.º 1 (7 de junio de 2020): 311–38. http://dx.doi.org/10.1146/annurev-chembioeng-102419-010001.
Texto completoSu, Zhipeng, Qing Xie, Yanping Wang y Yunsen Li. "Abberant Immunoglobulin G Glycosylation in Rheumatoid Arthritis by LTQ-ESI-MS". International Journal of Molecular Sciences 21, n.º 6 (17 de marzo de 2020): 2045. http://dx.doi.org/10.3390/ijms21062045.
Texto completoChinello, Clizia, Noortje de Haan, Giulia Capitoli, Barbara Trezzi, Antonella Radice, Lisa Pagani, Lucrezia Criscuolo et al. "Definition of IgG Subclass-Specific Glycopatterns in Idiopathic Membranous Nephropathy: Aberrant IgG Glycoforms in Blood". International Journal of Molecular Sciences 23, n.º 9 (23 de abril de 2022): 4664. http://dx.doi.org/10.3390/ijms23094664.
Texto completoGreto, Valentina L., Ana Cvetko, Tamara Štambuk, Niall J. Dempster, Domagoj Kifer, Helena Deriš, Ana Cindrić et al. "Extensive weight loss reduces glycan age by altering IgG N-glycosylation". International Journal of Obesity 45, n.º 7 (3 de mayo de 2021): 1521–31. http://dx.doi.org/10.1038/s41366-021-00816-3.
Texto completoŠtambuk, Jerko, Frano Vučković, Siniša Habazin, Maja Hanić, Mislav Novokmet, Susanna Nikolaus, Florian Tran et al. "Distinct Longitudinal Changes in Immunoglobulin G N-Glycosylation Associate with Therapy Response in Chronic Inflammatory Diseases". International Journal of Molecular Sciences 23, n.º 15 (30 de julio de 2022): 8473. http://dx.doi.org/10.3390/ijms23158473.
Texto completoTesis sobre el tema "IgG N-glycosylation"
Klarić, Lucija. "Genetic analysis of IgG N-glycosylation in health and disease". Thesis, University of Edinburgh, 2018. http://hdl.handle.net/1842/31097.
Texto completoKawaguchi, Nobuko. "Serum immunoglobulin G Fc region N-glycosylation profiling by matrix-assisted laser desorption/ionization mass spectrometry can distinguish breast cancer patients from cancer-free controls". Kyoto University, 2016. http://hdl.handle.net/2433/216178.
Texto completoKyoto University (京都大学)
0048
新制・課程博士
博士(医学)
甲第19924号
医博第4144号
新制||医||1017(附属図書館)
33010
京都大学大学院医学研究科医学専攻
(主査)教授 武藤 学, 教授 野田 亮, 教授 小川 修
学位規則第4条第1項該当
Luz, Johanna Da. "Aspects of N-glycosylation in human IgE /". Stockholm : [Karolinska institutets bibl.], 2002. http://diss.kib.ki.se/2002/91-7349-130-6.
Texto completoDi, Patria Laura. "N-glycosylation as a regulatory process in the IGF-1 system: from mechanisms to clinical implications". Doctoral thesis, Urbino, 2020. http://hdl.handle.net/11576/2681298.
Texto completoSAPORITI, SIMONA. "IN SILICO INVESTIGATIONS OF N-GLYCOSYLATION ROLE IN MODULATING IGG1 CONFORMATIONAL BEHAVIOR AND FC EFFECTOR FUNCTIONS". Doctoral thesis, Università degli Studi di Milano, 2020. http://hdl.handle.net/2434/796070.
Texto completoCabanes-Macheteau, Marion. "N-glycosylation d'un anticorps recombinant produit dans du tabac transgénique". Rouen, 1998. http://www.theses.fr/1998ROUES071.
Texto completoGavériaux, Claire. "Etude de l'interaction entre l'immunoglobuline e et son recepteur de forte affinite : mise au point d'un nouvel essai immunoenzymatique sur cellules, le celisa, importance de la n-glycosylation et de l'activation de la proteine kinase c dans l'expresion fonctionnelle de ce recepteur". Université Louis Pasteur (Strasbourg) (1971-2008), 1988. http://www.theses.fr/1988STR13014.
Texto completoRaymond, Céline. "Production d'IgG sialylées en CHO et impact sur leurs fonctions effectrices". Thèse, 2015. http://hdl.handle.net/1866/15979.
Texto completoOnly a fraction of the N-glycans present on the Fc fragment of the human IgGs is sialylated. However, a new interest for sialylation has risen since two major articles were published, one showing that sialylation reduces the capacity of the antibody to trigger antibody-dependent cell cytotoxicity (ADCC), whereas the other showed that the IgGs carrying α2,6-sialic acids on their Fc N-glycans were responsible for the anti-inflammatory activity of intravenous immunoglobulins (IVIGs) injected at high doses. Therapeutic monoclonal antibodies (mAbs) are in majority recombinant IgGs produced in mammalian cell culture. Since the end of the nineties, mAbs have become a major class of pharmaceutical products, and their success is still growing. The control of Fc N-glycosylation is a key parameter for the improvement of the therapeutic efficacy of mAbs. Sialylated IgGs are found only as traces in the classic CHO cell culture processes. In this study, we developed a method for the production of IgGs with a human-like sialylation in CHO cells. We focused on a production strategy relying on the transient co-expression of an IgG1 with the β1,4-galactosyltransferase I (β4GTI) and the β-galactoside-α2,6-sialyltransferase I (ST6GalI). We showed that this method allowed the enrichment of the IgG1 glycoprofile in the fucosylated di-galactosylated mono-α2,6-sialylated glycane G2FS(6)1, which is the main sialylated glycan found in human IgGs. We then adapted this method to the production of highly galactosylated or highly sialylated IgGs with and without core-fucosylation. The analysis of the glycosylation profiles obtained using the various enzyme combinations co-expressed with the native IgG1 or the mutant IgG1 F243A allowed us to discuss the influence of the under-galactosylation found in IgGs produced in CHO cells versus the Fc structural constraints on the limitation of IgG sialylation in CHO cells. We used the IgG1 glycovariants produced with our method to assess the impact of Fc α2,6-sialylation on the interaction of the IgG with the receptor FcγRIIIa, which is the main receptor mediating the ADCC response. We showed that the presence of α2,6-sialylation in the Fc increased the stability of the IgG-FcγRIIIa complex. This benefit however did not translate into an improved ADCC capacity. Finally, we initiated the development of a stable expression platform for the production of sialylated IgGs at yields relevant for the industry. We obtained a cell line capable of producing IgGs enriched in G2FS(6)1 at 400 mg/L. This may eventually represent a novel approach to manufacture a recombinant IVIG surrogate. With this work, we contributed to a better understanding of the impact of sialylation on the effector functions of IgGs. We also improved our understanding of the techniques allowing for the modification and control of the glycosylation profile of IgGs in cell culture.
Capítulos de libros sobre el tema "IgG N-glycosylation"
Cajic, Samanta, René Hennig, Robert Burock y Erdmann Rapp. "Capillary (Gel) Electrophoresis-Based Methods for Immunoglobulin (G) Glycosylation Analysis". En Experientia Supplementum, 137–72. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-76912-3_4.
Texto completoStockmann, Henning, Karen P. Coss, M. Estela Rubio-Gozalbo, Ina Knerr, Maria Fitzgibbon, Ashwini Maratha, James Wilson, Pauline Rudd y Eileen P. Treacy. "IgG N-Glycosylation Galactose Incorporation Ratios for the Monitoring of Classical Galactosaemia". En JIMD Reports, 47–53. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/8904_2015_490.
Texto completoChakrabarti, Atis, Jukka Kervinen, Egbert Müller, Toru Tanaka y Kazuaki Muranaka. "Analytical Characterization of Monoclonal Antibodies with Novel Fc Receptor-Based Chromatography Technique". En Monoclonal Antibodies [Working Title]. IntechOpen, 2020. http://dx.doi.org/10.5772/intechopen.95356.
Texto completoChakrabarti, Atis, Jukka Kervinen, Egbert Müller, Toru Tanaka y Kazuaki Muranaka. "Analytical Characterization of Monoclonal Antibodies with Novel Fc Receptor-Based Chromatography Technique". En Monoclonal Antibodies [Working Title]. IntechOpen, 2020. http://dx.doi.org/10.5772/intechopen.95356.
Texto completoActas de conferencias sobre el tema "IgG N-glycosylation"
Lloyd, Katy A., Johanna Steen, Phillip J. Titcombe, Daniel L. Mueller, Lars Klareskog, Vivianne Malmström y Caroline Grönwall. "08.19 Variable domain n-linked glycosylation is a key feature of monoclonal acpa-igg". En 37th European Workshop for Rheumatology Research 2–4 March 2017 Athens, Greece. BMJ Publishing Group Ltd and European League Against Rheumatism, 2017. http://dx.doi.org/10.1136/annrheumdis-2016-211055.19.
Texto completo"A study of causal relationships between human IgG N-glycosylation traits and twelve associated diseases". En Bioinformatics of Genome Regulation and Structure/ Systems Biology. institute of cytology and genetics siberian branch of the russian academy of science, Novosibirsk State University, 2020. http://dx.doi.org/10.18699/bgrs/sb-2020-085.
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