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Relevant bibliographies by topics / Pichia Pastoris N-Glycosylation

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Journal articles
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Academic literature on the topic 'Pichia Pastoris N-Glycosylation'

Author: Grafiati

Published: 4 June 2021

Last updated: 6 September 2023

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Journal articles on the topic "Pichia Pastoris N-Glycosylation"

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Vervecken, Wouter, Vladimir Kaigorodov, Nico Callewaert, Steven Geysens, Kristof De Vusser, and Roland Contreras. "In Vivo Synthesis of Mammalian-Like, Hybrid-Type N-Glycans in Pichia pastoris." Applied and Environmental Microbiology 70, no. 5 (2004): 2639–46. http://dx.doi.org/10.1128/aem.70.5.2639-2646.2004.

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ABSTRACT The Pichia pastoris N-glycosylation pathway is only partially homologous to the pathway in human cells. In the Golgi apparatus, human cells synthesize complex oligosaccharides, whereas Pichia cells form mannose structures that can contain up to 40 mannose residues. This hypermannosylation of secreted glycoproteins hampers the downstream processing of heterologously expressed glycoproteins and leads to the production of protein-based therapeutic agents that are rapidly cleared from the blood because of the presence of terminal mannose residues. Here, we describe engineering of the P. p

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Bretthauer, Roger K. "Genetic engineering of Pichia pastoris to humanize N-glycosylation of proteins." Trends in Biotechnology 21, no. 11 (2003): 459–62. http://dx.doi.org/10.1016/j.tibtech.2003.09.005.

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Jacobs, Pieter P., Steven Geysens, Wouter Vervecken, Roland Contreras, and Nico Callewaert. "Engineering complex-type N-glycosylation in Pichia pastoris using GlycoSwitch technology." Nature Protocols 4, no. 1 (2008): 58–70. http://dx.doi.org/10.1038/nprot.2008.213.

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Kallas, Åsa M., Kathleen Piens, Stuart E. Denman, et al. "Enzymatic properties of native and deglycosylated hybrid aspen (Populus tremula×tremuloides) xyloglucan endotransglycosylase 16A expressed in Pichia pastoris." Biochemical Journal 390, no. 1 (2005): 105–13. http://dx.doi.org/10.1042/bj20041749.

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The cDNA encoding a xyloglucan endotransglycosylase, PttXET16A, from hybrid aspen (Populus tremula×tremuloides) has been isolated from an expressed sequence tag library and expressed in the methylotrophic yeast Pichia pastoris. Sequence analysis indicated a high degree of similarity with other proteins in the XTH (xyloglucan transglycosylase/hydrolase) gene subfamily of GH16 (glycoside hydrolase family 16). In addition to the conserved GH16 catalytic sequence motif, PttXET16A contains a conserved N-glycosylation site situated proximal to the predicted catalytic residues. MS analysis indicated

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Giersing, Birgitte, Kazutoyo Miura, Richard Shimp, et al. "Posttranslational Modification of Recombinant Plasmodium falciparum Apical Membrane Antigen 1: Impact on Functional Immune Responses to a Malaria Vaccine Candidate." Infection and Immunity 73, no. 7 (2005): 3963–70. http://dx.doi.org/10.1128/iai.73.7.3963-3970.2005.

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ABSTRACT Recombinant apical membrane antigen 1 (AMA1) is a leading vaccine candidate for Plasmodium falciparum malaria, as antibodies against recombinant P. falciparum AMA1 (PfAMA1) interrupt merozoite invasion into erythrocytes. In order to investigate the role of posttranslational modification in modulating the functional immune response to recombinant AMA1, two separate alleles of PfAMA1 (FVO and 3D7), in which native N-glycosylation sites have been mutated, were produced using Escherichia coli and a Pichia pastoris expression system. Recombinant Pichia pastoris AMA1-FVO (PpAMA1-FVO) and Pp

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Kukk, Kaia, Sergo Kasvandik, and Nigulas Samel. "N-glycosylation site occupancy in human prostaglandin H synthases expressed in Pichia pastoris." SpringerPlus 3, no. 1 (2014): 436. http://dx.doi.org/10.1186/2193-1801-3-436.

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Li, Siqiang, Peng Sun, Xin Gong, et al. "Engineering O-glycosylation in modified N-linked oligosaccharide (Man12GlcNAc2∼Man16GlcNAc2) Pichia pastoris strains." RSC Advances 9, no. 15 (2019): 8246–52. http://dx.doi.org/10.1039/c8ra08121b.

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Peng, Huakang, Mengqi Wang, Nan Wang та ін. "Different N-Glycosylation Sites Reduce the Activity of Recombinant DSPAα2". Current Issues in Molecular Biology 44, № 9 (2022): 3930–47. http://dx.doi.org/10.3390/cimb44090270.

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Bat plasminogen activators α2 (DSPAα2) has extremely high medicinal value as a powerful natural thrombolytic protein. However, wild-type DSPAα2 has two N-glycosylation sites (N185 and N398) and its non-human classes of high-mannose-type N-glycans may cause immune responses in vivo. By mutating the N-glycosylation sites, we aimed to study the effect of its N-glycan chain on plasminogen activation, fibrin sensitivity, and to observe the physicochemical properties of DSPAα2. A logical structure design was performed in this study. Four single mutants and one double mutant were constructed and expr

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Han, Minghai, Xinfeng Wang, Guilong Yan, et al. "Modification of recombinant elastase expressed in Pichia pastoris by introduction of N-glycosylation sites." Journal of Biotechnology 171 (February 2014): 3–7. http://dx.doi.org/10.1016/j.jbiotec.2013.11.021.

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Peng, Huakang, Nan Wang, Mengqi Wang та ін. "Comparison of Activity and Safety of DSPAα1 and Its N-Glycosylation Mutants". Life 13, № 4 (2023): 985. http://dx.doi.org/10.3390/life13040985.

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DSPAα1 is a potent rude thrombolytic protein with high medicative value. DSPAα1 has two natural N-glycan sites (N153Q-S154-S155, N398Q-K399-T400) that may lead to immune responses when administered in vivo. We aimed to study the effect of its N-glycosylation sites on DSPAα1 in vitro and in vivo by mutating these N-glycosylation sites. In this experiment, four single mutants and one double mutant were predicted and expressed in Pichia pastoris. When the N398Q-K399-T400 site was mutated, the fibrinolytic activity of the mutant was reduced by 75%. When the N153Q-S154-S155 sites were inactivated a

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Dissertations / Theses on the topic "Pichia Pastoris N-Glycosylation"

1

Kreer, Christoph [Verfasser]. "N-glycosylation of intrinsic and engineered N-X-S/T motifs by Pichia pastoris can be exploited to ligate the mannose receptor but reveals no gain in immunogenicity per se / Christoph Kreer." Bonn : Universitäts- und Landesbibliothek Bonn, 2016. http://d-nb.info/1124540229/34.

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Kallas, Åsa. "Heterologous expression, characterization and applications of carbohydrate active enzymes and binding modules." Doctoral thesis, KTH, Träbioteknik, 2006. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-3950.

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Wood and wood products are of great economical and environmental importance, both in Sweden and globally. Biotechnology can be used both for achieving raw material of improved quality and for industrial processes such as biobleaching. Despite the enormous amount of carbon that is fixed as wood, the knowledge about the enzymes involved in the biosynthesis, re-organization and degradation of plant cell walls is relatively limited. In order to exploit enzymes more efficiently or to develop new biotechnological processes, it is crucial to gain a better understanding of the function and mechanism o

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Degani, G. "MOLECULAR CHARACTERIZATION OF MEMBRANE-BOUND GLYCOPROTEINS INVOLVED IN HUMAN DISEASES AND POTENTIAL TARGETS FOR NEW THERAPIES." Doctoral thesis, Università degli Studi di Milano, 2015. http://hdl.handle.net/2434/274187.

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The present thesis is focused on the molecular characterization of two eukaryotic membrane glycoproteins that are promising candidates for new therapeutic approaches to human diseases. The first glycoprotein is the human Receptor for the Advanced Glycation End products (hRAGE), a member of the immunoglobulin superfamily. RAGE is a type I transmembrane glycoprotein that is beneficial in normal physiological conditions but it is also a key player in the etiology and progression of several chronic pathologies such as neurodegenerative disorders (Alzheimer), atherosclerosis, cancer and complicat

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Manoharan, Simna. "Engineering the N-Glycosylation Pathway in Pichia Pastoris for the Expression of Glycoprotein Hormones." Thesis, 2016. http://etd.iisc.ac.in/handle/2005/3017.

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Proteins, participating in a myriad of biological function, are at the core of all cellular activities occurring within living organisms. Therapeutic proteins, hence constitute a major part of the pharmaceutical industry. The glycoprotein hormones follicle stimulating hormone (FSH), luteinizing hormone (LH), thyroid stimulating hormone (TSH) and human chorionic gonadotropin (CG) regulate various reproductive and metabolic functions in humans and hence have high therapeutic potentials. The increasing demand of recombinant proteins for therapeutic uses drives the development of better expressio

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Manoharan, Simna. "Engineering the N-Glycosylation Pathway in Pichia Pastoris for the Expression of Glycoprotein Hormones." Thesis, 2016. http://hdl.handle.net/2005/3017.

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Proteins, participating in a myriad of biological function, are at the core of all cellular activities occurring within living organisms. Therapeutic proteins, hence constitute a major part of the pharmaceutical industry. The glycoprotein hormones follicle stimulating hormone (FSH), luteinizing hormone (LH), thyroid stimulating hormone (TSH) and human chorionic gonadotropin (CG) regulate various reproductive and metabolic functions in humans and hence have high therapeutic potentials. The increasing demand of recombinant proteins for therapeutic uses drives the development of better expressio

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Barker, Megan. "Structural Investigation of Processing α-Glucosidase I from Saccharomyces cerevisiae". Thesis, 2010. http://hdl.handle.net/1807/32660.

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N-glycosylation is the most common eukaryotic post-translational modification, impacting on protein stability, folding, and protein-protein interactions. More broadly, N-glycans play biological roles in reaction kinetics modulation, intracellular protein trafficking, and cell-cell communications. The machinery responsible for the initial stages of N-glycan assembly and processing is found on the membrane of the endoplasmic reticulum. Following N-glycan transfer to a nascent glycoprotein, the enzyme Processing α-Glucosidase I (GluI) catalyzes the selective removal of the terminal glucose re

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Book chapters on the topic "Pichia Pastoris N-Glycosylation"

1

Laukens, Bram, Charlot De Wachter, and Nico Callewaert. "Engineering the Pichia pastoris N-Glycosylation Pathway Using the GlycoSwitch Technology." In Glyco-Engineering. Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4939-2760-9_8.

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Gong, Bing, Michael Cukan, Richard Fisher, Huijuan Li, Terrance A. Stadheim, and Tillman Gerngross. "Characterization of N-Linked Glycosylation on Recombinant Glycoproteins Produced in Pichia pastoris Using ESI-MS and MALDI-TOF." In Glycomics. Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-022-5_16.

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