Relevant bibliographies by topics / O-fucosylation

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  2. Dissertations / Theses
  3. Book chapters

Academic literature on the topic 'O-fucosylation'

Author: Grafiati
Published: 4 June 2021
Last updated: 16 February 2022

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Journal articles on the topic "O-fucosylation"

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Holdener, Bernadette C., and Robert S. Haltiwanger. "Protein O-fucosylation: structure and function." Current Opinion in Structural Biology 56 (June 2019): 78–86. http://dx.doi.org/10.1016/j.sbi.2018.12.005.

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Ricketts, Lindsay M., Malgosia Dlugosz, Kelvin B. Luther, Robert S. Haltiwanger, and Elaine M. Majerus. "O-Fucosylation Is Required for ADAMTS13 Secretion." Journal of Biological Chemistry 282, no. 23 (2007): 17014–23. http://dx.doi.org/10.1074/jbc.m700317200.

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Verbij, Fabian C., Eva Stokhuijzen, Paul H. P. Kaijen, Floris van Alphen, Alexander B. Meijer, and Jan Voorberg. "Identification of glycans on plasma-derived ADAMTS13." Blood 128, no. 21 (2016): e51-e58. http://dx.doi.org/10.1182/blood-2016-06-720912.

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Key Points ADAMTS13 contains complex type N-linked glycans, which contain terminal mannose, sialic acids, and fucose residues. TSP1 repeats are modified by O-fucosylation and C-mannosylation; O-fucosylation was also observed in the disintegrin domain.
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Keeley, Tyler S., Shengyu Yang, and Eric Lau. "The Diverse Contributions of Fucose Linkages in Cancer." Cancers 11, no. 9 (2019): 1241. http://dx.doi.org/10.3390/cancers11091241.

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Fucosylation is a post-translational modification of glycans, proteins, and lipids that is responsible for many biological processes. Fucose conjugation via α(1,2), α(1,3), α(1,4), α(1,6), and O’- linkages to glycans, and variations in fucosylation linkages, has important implications for cancer biology. This review focuses on the roles that fucosylation plays in cancer, specifically through modulation of cell surface proteins and signaling pathways. How L-fucose and serum fucosylation patterns might be used for future clinical diagnostic, prognostic, and therapeutic approaches will be discuss
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Zhang, Ao, Steven J. Berardinelli, Christina Leonhard-Melief, et al. "O-Fucosylation of ADAMTSL2 is required for secretion and is impacted by geleophysic dysplasia-causing mutations." Journal of Biological Chemistry 295, no. 46 (2020): 15742–53. http://dx.doi.org/10.1074/jbc.ra120.014557.

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ADAMTSL2 mutations cause an autosomal recessive connective tissue disorder, geleophysic dysplasia 1 (GPHYSD1), which is characterized by short stature, small hands and feet, and cardiac defects. ADAMTSL2 is a matricellular protein previously shown to interact with latent transforming growth factor-β binding protein 1 and influence assembly of fibrillin 1 microfibrils. ADAMTSL2 contains seven thrombospondin type-1 repeats (TSRs), six of which contain the consensus sequence for O-fucosylation by protein O-fucosyltransferase 2 (POFUT2). O-fucose–modified TSRs are subsequently elongated to a gluco
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Lira-Navarrete, Erandi, Jessika Valero-González, Raquel Villanueva, et al. "Structural Insights into the Mechanism of Protein O-Fucosylation." PLoS ONE 6, no. 9 (2011): e25365. http://dx.doi.org/10.1371/journal.pone.0025365.

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Luo, Yi, and Robert S. Haltiwanger. "O-Fucosylation of Notch Occurs in the Endoplasmic Reticulum." Journal of Biological Chemistry 280, no. 12 (2005): 11289–94. http://dx.doi.org/10.1074/jbc.m414574200.

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Niwa, Yuki, Takehiro Suzuki, Naoshi Dohmae, and Siro Simizu. "O-fucosylation of CCN1 is required for its secretion." FEBS Letters 589, no. 21 (2015): 3287–93. http://dx.doi.org/10.1016/j.febslet.2015.09.012.

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Verbij, Fabian, Eva Stokhuijzen, Floris van Alphen, Paul Kaijen, Alexander Meijer, and Jan Voorberg. "Analysis of the Glycan Composition on Plasma Derived ADAMTS13 Employing Tandem Mass Spectrometry." Blood 126, no. 23 (2015): 1069. http://dx.doi.org/10.1182/blood.v126.23.1069.1069.

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Abstract Acquired thrombotic thrombocytopenic purpura (TTP) is a life-threatening disorder that results from the development of auto-antibodies against ADAMTS13 disrupting the binding of ADAMTS13 to von Willebrand factor and thereby preventing the proteinase activity and/or increasing the clearance from the circulation. Previous research from our department identified 9 O-linked glycosylation, 6 O-fucosylation and 2 C-mannosylation sites on plasma derived ADAMTS13. One of the N-linked glycosylation sites (N1354) is close to one of the previously identified peptides preferentially presented on
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Pennarubia, Florian, Emilie Pinault, Bilal Al Jaam, et al. "Mouse WIF1 Is Only Modified with O-Fucose in Its EGF-like Domain III Despite Two Evolutionarily Conserved Consensus Sites." Biomolecules 10, no. 9 (2020): 1250. http://dx.doi.org/10.3390/biom10091250.

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The Wnt Inhibitory Factor 1 (Wif1), known to inhibit Wnt signaling pathways, is composed of a WIF domain and five EGF-like domains (EGF-LDs) involved in protein interactions. Despite the presence of a potential O-fucosylation site in its EGF-LDs III and V, the O-fucose sites occupancy has never been demonstrated for WIF1. In this study, a phylogenetic analysis on the distribution, conservation and evolution of Wif1 proteins was performed, as well as biochemical approaches focusing on O-fucosylation sites occupancy of recombinant mouse WIF1. In the monophyletic group of gnathostomes, we showed
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Dissertations / Theses on the topic "O-fucosylation"

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Pennarubia, Florian. "Analyses biochimiques et fonctionnelles de protéines cibles de POFUT1." Thesis, Limoges, 2018. http://www.theses.fr/2018LIMO0075.

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La O-fucosylation, catalysée par Pofut1, est une glycosylation rare qui consiste en l’ajout d’un fucose O-lié sur la sérine ou la thréonine d’une séquence consensus (C2X4(S/T)C3), portée par un domaine EGF-like (ELD) d’une glycoprotéine membranaire ou sécrétée. Notre analyse de la lignée murine Pofut1cax/cax, hypomorphe pour le gène Pofut1, a révélé une hypertrophie musculaire post-natale associée à une diminution du pool de cellules satellites. Ce phénotype est en partie associé à un défaut d’interaction entre les récepteurs NOTCH hypo-O-fucosylés des myoblastes dérivés de cellulessatellites
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Audfray, Aymeric. "La protéine-O-fucosyltransférase 1 (Pofut1) : caractérisation fonctionnelle et régulation de la voie de signalisation de Notch au cours de la myogenèse." Limoges, 2008. https://aurore.unilim.fr/theses/nxfile/default/9265bb72-4572-4eac-8191-98d5650a5fea/blobholder:0/2008LIMO4051.pdf.

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La myogenèse du muscle squelettique est un processus complexe dont certaines étapes sont régulées par la voie de signalisation de Notch. Chez les Mammifères, la présence de O‑fucosylglycannes sur la partie extracellulaire des récepteurs Notch influence l’activation de la voie de signalisation. Leur synthèse débute par l’action de la O‑fucosyltransférase Pofut1. Au cours de ce travail de thèse, nous avons mis en évidence, par mutagenèse dirigée, l’implication du site conservé de N‑glycosylation N65 pour l’intégrité structurale de Pofut1. Ceci constitue un nouvel exemple de l’influence de la N‑g
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Loriol, Céline. "Les O-fucosyltransférases : caractérisation des enzymes bovines et étude préliminaire du rôle de Pofut1 murine dans la différenciation de la cellule musculaire." Limoges, 2006. http://aurore.unilim.fr/theses/nxfile/default/1c0efd0e-f3ae-4389-9e61-7d992890c88d/blobholder:0/2006LIMO0055.pdf.

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La O-fucosylation est l’ajout d’un fucose sur un résidu sérine ou thréonine compris dans deux types de domaines peptidiques, les EGF et les TSR. Cette modification post-traductionnelle dépend de deux enzymes, Pofut1 pour les EGF et Pofut2 pour les TSR. Nous avons étudié l’évolution des gènes Pofut1 et Pofut2, et avons démontré que ces gènes présents en un seul exemplaire, existaient déjà chez l'ancêtre des Bilatériens voire des Métazoaires, probablement sous forme morcelée. Une situation originale existe pour Pofut2, retrouvé chez un groupe de Protozoaires, les Apicomplexés. La structure des d
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Der, Vartanian Audrey. "Rôle(s) de la protéine O-fucosyltransférase 1 au cours de la différenciation myogénique." Thesis, Limoges, 2015. http://www.theses.fr/2015LIMO0048.

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Au cours de la myogenèse post-natale, la voie de signalisation de Notch participe au développement et à la régénération du muscle squelettique chez les mammifères. Elle permet le maintien de l'état prolifératif des myoblastes, contrôle la quiescence des cellules satellites in vivo et préserve une sous-population de cellules de réserve indifférenciées in vitro. L' activation de la voie et l'interaction du récepteur Notch avec ses ligands est dépendante de leur entité glucidique, notamment de leurs O-fucosylglycannes. La synthèse de ces derniers est initiée par la protéine O-fucosyltransférase 1
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Heu, Katy. "Caractérisation de la lignée murine hypomorphe Pofut1cax : un modèle d’étude in vivo du rôle de la O-fucosylation de Notch au cours de la myogenèse." Limoges, 2013. http://www.theses.fr/2013LIMO4033.

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La protéine O-fucosyltransférase 1 (POFUT1) greffe des résidus O-fucose sur des domaines EGF-like retrouvés sur diverses protéines dont les récepteurs Notch et leurs ligands. En plus de son rôle d’O-fucosyltransférase, POFUT1 possède aussi un rôle de chaperonne pour le récepteur Notch. La présence de résidus O-fucose ainsi que leur allongement par la -1,3-GlcNAc-transférase (lunatic fringe) influence la liaison de Notch avec ses ligands. La voie de signalisation Notch est connue pour son rôle dans divers processus biologiques. Dans le développement du muscle squelettique, la voie de signalisa
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6

Sui, Ning. "DELLA is O-Fucosylated by SPINDLY." Diss., 2016. http://hdl.handle.net/10161/13413.

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<p>Plant growth and development are strictly regulated by internal hormonal signaling networks, which integrate and coordinate to promote plants’ adaptation and survival in the changing environment. Among the diverse hormones, gibberellins (GAs) are the phytohormones that regulate various processes, from seed germination to fruit development. The conserved plant-specific GRAS family protein DELLAs, key repressors in the GA signaling pathway, serve as the central coordinator of multiple signaling networks through physical interactions with many key transcription factors/regulators in other pat
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Book chapters on the topic "O-fucosylation"

1

Berardinelli, Steven John, and Robert S. Haltiwanger. "Analyzing the Effects of O-Fucosylation on Secretion of ADAMTS Proteins Using Cell-Based Assays." In Methods in Molecular Biology. Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9698-8_3.

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Yamakawa, Tomoko, Tomonori Ayukawa, and Kenji Matsuno. "Metabolism and Transportation Pathways Of GDP-Fucose that are Required for the O-Fucosylation Of Notch." In Advances in Experimental Medicine and Biology. Springer US, 2012. http://dx.doi.org/10.1007/978-1-4614-0899-4_3.

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Luo, Y., K. B. Luther, and R. S. Haltiwanger. "O-Fucosylation of Glycoproteins." In Comprehensive Glycoscience. Elsevier, 2007. http://dx.doi.org/10.1016/b978-044451967-2/00089-1.

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Luther, Kelvin B., and Robert S. Haltiwanger. "O-Fucosylation of Proteins." In Reference Module in Chemistry, Molecular Sciences and Chemical Engineering. Elsevier, 2020. http://dx.doi.org/10.1016/b978-0-12-819475-1.00051-1.

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Leonhard-Melief, Christina, and Robert S. Haltiwanger. "O-Fucosylation of Thrombospondin Type 1 Repeats." In Methods in Enzymology. Elsevier, 2010. http://dx.doi.org/10.1016/s0076-6879(10)80018-7.

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