Relevant bibliographies by topics / Fucosylation

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  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters
  4. Conference papers

Academic literature on the topic 'Fucosylation'

Author: Grafiati
Published: 4 June 2021
Last updated: 14 March 2023

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Journal articles on the topic "Fucosylation"

1

Fujita, Kazutoshi, Koji Hatano, Mamoru Hashimoto, Eisuke Tomiyama, Eiji Miyoshi, Norio Nonomura, and Hirotsugu Uemura. "Fucosylation in Urological Cancers." International Journal of Molecular Sciences 22, no. 24 (December 11, 2021): 13333. http://dx.doi.org/10.3390/ijms222413333.

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Fucosylation is an oligosaccharide modification that plays an important role in immune response and malignancy, and specific fucosyltransferases (FUTs) catalyze the three types of fucosylations: core-type, Lewis type, and H type. FUTs regulate cancer proliferation, invasiveness, and resistance to chemotherapy by modifying the glycosylation of signaling receptors. Oligosaccharides on PD-1/PD-L1 proteins are specifically fucosylated, leading to functional modifications. Expression of FUTs is upregulated in renal cell carcinoma, bladder cancer, and prostate cancer. Aberrant fucosylation in prostate-specific antigen (PSA) could be used as a novel biomarker for prostate cancer. Furthermore, elucidation of the biological function of fucosylation could result in the development of novel therapeutic targets. Further studies are needed in the field of fucosylation glycobiology in urological malignancies.
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Keeley, Tyler S., Shengyu Yang, and Eric Lau. "The Diverse Contributions of Fucose Linkages in Cancer." Cancers 11, no. 9 (August 24, 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 discussed.
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Rydén, Ingvar, Peter Påhlsson, and Stefan Lindgren. "Diagnostic Accuracy of α1-Acid Glycoprotein Fucosylation for Liver Cirrhosis in Patients Undergoing Hepatic Biopsy." Clinical Chemistry 48, no. 12 (December 1, 2002): 2195–201. http://dx.doi.org/10.1093/clinchem/48.12.2195.

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Abstract Background: Increased fucosylation of serum glycoproteins has previously been reported in patients with liver disease. We analyzed α1-acid glycoprotein (AGP) fucosylation in serum samples from patients investigated for suspected liver disease to evaluate its value as a biochemical marker for liver cirrhosis. Methods: We used a novel lectin immunoassay adapted to the AutoDELFIA system to analyze AGP fucosylation in 261 consecutive patients admitted for liver biopsy at Malmö University Hospital in Southern Sweden. The results were compared with histopathologic findings. In addition, AGP fucosylation was compared with other biochemical markers described as useful in the diagnosis of liver cirrhosis. The biochemical markers were compared by ROC curve analysis. Results: AGP fucosylation was significantly (P <0.05) higher in patients with liver cirrhosis (n = 65) than in healthy controls (n = 72), patients with normal histology (n = 29), patients with steatosis only (n = 38), patients with viral or chronic hepatitis without cirrhosis (n = 71), and patients with other liver diseases without histologic signs of cirrhosis (n = 58). By calculating the AGP fucosylation index (AGP-FI = AGP fucosylation/AGP serum concentration), we obtained a high diagnostic accuracy. The areas under the ROC curves for AGP-FI were 0.83 and 0.74 for men and women, respectively, compared with 0.82 for hyaluronic acid and 0.77 for the aspartate aminotransferase/alanine aminotransferase ratio in both men and women. Conclusions: AGP fucosylation appears to be useful in identifying patients with liver cirrhosis among patients investigated for liver disease. The lectin immunoassay showed satisfactory reproducibility and is suitable for routine use in a clinical laboratory.
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Watson, Gregory, Daniel Lester, Hui Ren, Connor M. Forsyth, Elliot Medina, David Gonzalez Perez, Lancia Darville, et al. "Fucosylated Proteome Profiling Identifies a Fucosylated, Non-Ribosomal, Stress-Responsive Species of Ribosomal Protein S3." Cells 10, no. 6 (May 25, 2021): 1310. http://dx.doi.org/10.3390/cells10061310.

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Alterations in genes encoding for proteins that control fucosylation are known to play causative roles in several developmental disorders, such as Dowling-Degos disease 2 and congenital disorder of glycosylation type IIc (CDGIIc). Recent studies have provided evidence that changes in fucosylation can contribute to the development and progression of several different types of cancers. It is therefore important to gain a detailed understanding of how fucosylation is altered in disease states so that interventions may be developed for therapeutic purposes. In this report, we find that fucosylation occurs on many intracellular proteins. This is an interesting finding, as the fucosylation machinery is restricted to the secretory pathway and is thought to predominately affect cell-membrane-bound and secreted proteins. We find that Ribosomal protein S3 (RPS3) is fucosylated in normal tissues and in cancer cells, and that the extent of its fucosylation appears to respond to stress, including MAPK inhibitors, suggesting a new role in posttranslational protein function. Our data identify a new ribosome-independent species of fucosylated RPS3 that interacts with proteins involved in posttranscriptional regulation of RNA, such as Heterogeneous nuclear ribonucleoprotein U (HNRNPU), as well as with a predominance of non-coding RNAs. These data highlight a novel role for RPS3, which, given previously reported oncogenic roles for RPS3, might represent functions that are perturbed in pathologies such as cancer. Together, our findings suggest a previously unrecognized role for fucosylation in directly influencing intracellular protein functions.
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Gong, Huanle, Shoubao Ma, and Depei Wu. "Ex vivo fucosylation promotes the GVL effect of NK cells after Allo-HSCT." Journal of Immunology 202, no. 1_Supplement (May 1, 2019): 69.25. http://dx.doi.org/10.4049/jimmunol.202.supp.69.25.

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Abstract Recent studies demonstrated that ex vivo fucosylation can increase the persistence and anti-GVHD potency of Treg cells. Fucosylation also improves human cord blood engraftment. However, the role of fucosylation in graftversus- leukemia (GVL) effect after allogeneic hematopoietic stem cell transplantation (Allo-HSCT) remains unknown. Here, we established a murine GVL model by intravenously injecting luciferase (lus+)/yfp-expressing B-cell lymphoma (A20) cells and founded that adoptive transfer of fucosylated NK cells markedly prolonged the survival than control NK cells. Ex vivo fucosylation significantly upregulated IFN-γ production in NK cells and enhanced their cytotoxic activity. Flow cytometry analysis revealed that fucosylation promoted the infiltration of NK cells, which may be due to the elevated binding to CD62E. Further studies are needed to confirm the contribution of IFN-γ by using IFN-γ KO mice and investigate the detailed mechanisms of fucosylated NK cells in the regulation of GVL responses.
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Li, Tiezheng, David J. DiLillo, Stylianos Bournazos, John P. Giddens, Jeffrey V. Ravetch, and Lai-Xi Wang. "Modulating IgG effector function by Fc glycan engineering." Proceedings of the National Academy of Sciences 114, no. 13 (March 13, 2017): 3485–90. http://dx.doi.org/10.1073/pnas.1702173114.

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IgG antibodies contain a conserved N-glycosylation site on the Fc domain to which a complex, biantennary glycan is attached. The fine structures of this glycan modulate antibody effector functions by affecting the binding affinity of the Fc to diverse Fc receptor family members. For example, core fucosylation significantly decreases antibody-dependent cellular cytotoxicity (ADCC), whereas terminal α2,6-sialylation plays a critical role in the anti-inflammatory activity of human i.v. immunoglobulin therapy. The effect of specific combinations of sugars in the glycan on ADCC remains to be further addressed, however. Therefore, we synthesized structurally well-defined homogeneous glycoforms of antibodies with different combinations of fucosylation and sialylation and performed side-by-side in vitro FcγR-binding analyses, cell-based ADCC assays, and in vivo IgG-mediated cellular depletion studies. We found that core fucosylation exerted a significant adverse effect on FcγRIIIA binding, in vitro ADCC, and in vivo IgG-mediated cellular depletion, regardless of sialylation status. In contrast, the effect of sialylation on ADCC was dependent on the status of core fucosylation. Sialylation in the context of core fucosylation significantly decreased ADCC in a cell-based assay and suppressed antibody-mediated cell killing in vivo. In contrast, in the absence of fucosylation, sialylation did not adversely impact ADCC.
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Antonarelli, Gabriele, Valentina Pieri, Francesca Maria Porta, Nicola Fusco, Gaetano Finocchiaro, Giuseppe Curigliano, and Carmen Criscitiello. "Targeting Post-Translational Modifications to Improve Combinatorial Therapies in Breast Cancer: The Role of Fucosylation." Cells 12, no. 6 (March 8, 2023): 840. http://dx.doi.org/10.3390/cells12060840.

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Various tumors rely on post-translational modifications (PTMs) to promote invasiveness and angiogenesis and to reprogram cellular energetics to abate anti-cancer immunity. Among PTMs, fucosylation is a particular type of glycosylation that has been linked to different aspects of immune and hormonal physiological functions as well as hijacked by many types of tumors. Multiple tumors, including breast cancer, have been linked to dismal prognoses and increased metastatic potential due to fucosylation of the glycan core, namely core-fucosylation. Pre-clinical studies have examined the molecular mechanisms regulating core-fucosylation in breast cancer models, its negative prognostic value across multiple disease stages, and the activity of in vivo pharmacological inhibition, instructing combinatorial therapies and translation into clinical practice. Throughout this review, we describe the role of fucosylation in solid tumors, with a particular focus on breast cancer, as well as physiologic conditions on the immune system and hormones, providing a view into its potential as a biomarker for predicating or predicting cancer outcomes, as well as a potential clinical actionability as a biomarker.
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Lin, Hongli, Dapeng Wang, Taihua Wu, Cui Dong, Nan Shen, Yuan Sun, Yanling Sun, Hua Xie, Nan Wang, and Lujuan Shan. "Blocking core fucosylation of TGF-β1 receptors downregulates their functions and attenuates the epithelial-mesenchymal transition of renal tubular cells." American Journal of Physiology-Renal Physiology 300, no. 4 (April 2011): F1017—F1025. http://dx.doi.org/10.1152/ajprenal.00426.2010.

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Posttranslational modification of proteins could regulate their multiple biological functions. Transforming growth factor-β receptor I and II (ALK5 and TGF-βRII), which are glycoproteins, play important roles in the renal tubular epithelial-mesenchymal transition (EMT). In the present study, we examined the role of core fucosylation of TGF-βRII and ALK5, which is regulated by α-1,6 fucosyltransferase (Fut8), in the process of EMT of cultured human renal proximal tubular epithelial (HK-2) cells. The typical cell model of EMT induced by TGF-β1 was constructed to address the role of core fucosylation in EMT. Core fucosylation was found to be essential for both TGF-βRII and ALK5 to fulfill their functions, and blocking it with Fut8 small interfering RNA greatly reduced the phosphorylation of Smad2/3 protein, caused the inactivation of TGF-β/Smad2/3 signaling, and resulted in remission of EMT. More importantly, even with high levels of expressions of TGF-β1, TGF-βRII, and ALK5, blocking core fucosylation also could attenuate the EMT of HK-2 cells. Thus blocking core fucosylation of TGF-βRII and ALK5 may attenuate EMT independently of the expression of these proteins. This study may provide new insight into the role of glycosylation in renal interstitial fibrosis. Furthermore, core fucosylation may be a novel potential therapeutic target for treatment of renal tubular EMT.
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MILLS, Philippa, Kevin MILLS, Peter CLAYTON, Andrew JOHNSON, David WHITEHOUSE, and Bryan WINCHESTER. "Congenital disorders of glycosylation type I leads to altered processing of N-linked glycans, as well as underglycosylation." Biochemical Journal 359, no. 2 (October 8, 2001): 249–54. http://dx.doi.org/10.1042/bj3590249.

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The N-linked glycans on transferrin and α1-antitrypsin from patients with congenital disorders of glycosylation type I have increased fucosylation and branching relative to normal controls. The elevated levels of monofucosylated biantennary glycans are probably due to increased α-(1 → 6) fucosylation. The presence of bi- and trifucosylated triantennary and tetra-antennary glycans indicated that peripheral α-(1 → 3), as well as core α-(1 → 6), fucosylation is increased. Altered processing was observed on both the fully and underglycosylated glycoforms.
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Moriwaki, Kenta. "Fucosylation and gastrointestinal cancer." World Journal of Hepatology 2, no. 4 (2010): 151. http://dx.doi.org/10.4254/wjh.v2.i4.151.

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Dissertations / Theses on the topic "Fucosylation"

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Bandini, Giulia. "Studies on fucosylation in Trypanosoma brucei." Thesis, University of Dundee, 2011. https://discovery.dundee.ac.uk/en/studentTheses/c74554c1-f4d3-4bb3-aa31-899fcf507e11.

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The biosynthesis of GDP-Fucose, the activated donor for fucose, has been recently shown to be essential in the parasite Trypanosoma brucei. Fucose is a common sugar modification on eukaryotic glycan structures, but it has not been well described in trypanosomatids. To elucidate the role of fucose in T. brucei we searched for putative fucosyltransferases in this parasite. A single putative T. brucei fucosyltransferase (TbFT) was identified and recombinantly expressed in Escherichia coli. The protein was active and structural characterization of its reaction product identified it as a GDP-Fuc: ß-D-galactose a-1,2-fucosyltransferase with preference for Galß1,3GlcNAc containing structures as glycan acceptors. A procyclic form conditional null mutant for TbFT was generated and this glycosyltransferase shown to be essential for parasite growth in vitro, with the mutant cells displaying a slightly abnormal morphology and an apparent reduction in the surface high molecular weight glycoconjugate complex. Here we also describe the various experimental approaches that were used to try to identify the fucosylated glycocojugates in T. brucei. Lastly, to better understand the biosynthesis of GDP-Mannose, the starting metabolite for the biosynthesis of GDP-Fuc, we biochemically characterized T. brucei phosphomannomutase (TbPMM). Here we show this enzyme could interconvert not only mannose-phosphates, but also glucose-phosphates.
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Keeley, Tyler S. "Investigating the Roles of Fucosylation and Calcium Signaling in Melanoma Invasion." Scholar Commons, 2018. https://scholarcommons.usf.edu/etd/7535.

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Melanoma is the deadliest form of skin cancer. Prognosis for early stage melanoma patients is excellent, and surgery is often curative for these patients. However, once patients have presented with invasive disease, the average 5-year survival rate drops significantly from over 90% to between 10 and 15%. Several therapies have been developed to target a commonly mutated oncogene BRAF, or its downstream effectors. Unfortunately, while these treatments show robust initial response, most patients relapse within a year. Moreover, therapy-resistant tumors are often more invasive and metastatic. Therefore, it is important to investigate the molecular mechanisms underlying melanoma invasion and metastasis, and to prevent melanoma cell dissemination and metastatic progression. Invadopodia are proteolytic membrane protrusions used by metastatic cancer cells to degrade the extracellular matrix and to facilitate cancer cell invasion and metastasis. In my thesis research I have focused on protein fucosylation and store-operated calcium entry, two separate mechanisms involved in invadopodial regulation. Post translational modifications of proteins are essential for their structure and function. Many cell surface proteins require modifications such as glycosylation for protein-protein interactions, cell adhesion, and signal transduction. Fucosylation is a form of glycosylation that adds L-fucose on glycan structures of proteins. There is evidence indicating that fucosylation plays an important but cancer-type and branching dependent role in cancer progression. Emerging evidence indicates that the fucose salvage pathway and protein fucosylation are altered during melanoma progression and metastasis. Here, we report that the fucose salvage pathway inhibits invadopodia formation and extracellular matrix degradation by promoting α(1,2) fucosylation of cell surface proteins. The activation of the fucose salvage pathway decreases invadopodia numbers and inhibits the proteolytic activity of invadopodia in WM793 melanoma cells. Inhibiting fucokinase, one of the critical enzymes in the fucose salvage pathway, in melanoma cells abrogates L-fucose-mediated inhibition of invadopodia, suggesting dependence on the fucose salvage pathway. The inhibition of invadopodia formation by L-Fucose treatment or fucokinase overexpression could be rescued by treatment with α(1,2), but not α(1,3/4) fucosidase, implicating an α(1,2) fucose linkage-dependent inhibitory effect. The ectopic expression of FUT1, an α(1,2) fucosyltransferase, is sufficient to inhibit invadopodia formation and ECM degradation. Our findings indicate that the fucose salvage pathway can inhibit invadopodia formation, and consequently, invasiveness in melanoma via α(1,2) fucosylation. Re-activation of this pathway in melanoma could be useful for preventing melanoma invasion and metastasis. Calcium is a critical second messenger involved in a multitude of biological processes from cell proliferation to muscle contraction. In melanoma, previous studies have found that activation of the store operated calcium entry (SOCE) channel promotes tumor invasion and metastasis, in vitro and in xenograft models. The expression levels of STIM1, an essential component of the store operated calcium channels, has been found to increase with later stages of melanoma. In melanoma cell lines, the over expression of STIM1 enhances invadopodia number whereas STIM1 knockdown inhibits invadopodia formation. Similarly, gelatin degradation activity is enhanced with STIM1 overexpression and abrogated with STIM1 knockdown, implicating STIM1 as an important factor in the regulation of invadopodia formation and melanoma invasion. Though the studies published have shown a significant role of STIM1 in tumor progression, a robust transgenic animal model has not yet been established. Here, we developed a novel transgenic mouse model which, upon 4-hydroxytamoxifen (4OHT) treatment, induces the BRAFV600E mutation and PTEN, STIM1, and STIM2 deletions in melanocytes via an inducible Cre-lox system. Our investigation found that the loss of STIM1 exacerbates tumor growth and results in tumor formation significantly more quickly than STIM1 wild type mice. Whereas PCR analysis of 4OHT-treated skin showed deletion of STIM1 and PTEN, immunohistochemical staining of these genes in tumors did not convincingly demonstrate complete deletion. Therefore, it remains to be determined whether the effects we observed are due to STIM1 and STIM2 loss. These findings need to be corroborated in the future. Our studies focus on two important mechanisms required for melanoma progression and metastasis. We found that α(1,2) fucosylation is able to inhibit invadopodia formation, and melanoma cell invasion. The reestablishment of α(1,2) fucosylation in melanoma could potentially be exploited to inhibit melanoma metastasis. Additionally, early evidence points to STIM1 having a tumor suppressive role in melanoma oncogenesis and tumor growth based on the transgenic mouse model. Although the phenotype is unexpected, further investigation of this model will likely provide important insight for the complicate roles of SOCE in melanoma initiation and progression.
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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 (MDCS) et leurs ligands DSL, ce qui aboutit à une plus faible activation de la signalisation Notch. D’autres protéines potentiellement impliquées dans la myogenèse peuvent également être la cible de POFUT1. C’est notamment le cas de la protéine Wnt inhibitory factor 1 (WIF1), qui dispose de cinq ELDs, dont deux sont potentiellement aptes à recevoir un O-fucose (ELDs III et V). Par une approche phylogénétique, nous avons montré la conservation de ces deux sites de O-fucosylation et de deux sites de N-glycosylation chez la plupart des bilatériens. Nos expériences démontrent l’occupationde tous ces sites, excepté le site de O-fucosylation de l’ELD V, chez la protéine WIF1 murine. La capacité de l’ELD III, produit de manière isolée, à recevoir un fucose O-lié a été démontrée après O-fucosylation in vitro, par l’association de cycloaddition azide-alcyne assistée au cuivre (CuAAC) et de spectrométrie de masse en mode MRM. Cette nouvelle approche expérimentale a par la suite été standardisée et sa sensibilité évaluée en comparant deux autres ELDs (ELDs 12 et 26 de NOTCH1) connus pour être O-fucosylés mais présentant des affinités différentes pour POFUT1. De façonsurprenante, l’ELD V de WIF1 ne peut être O-fucosylé, probablement en raison d’un clash stérique entre cet ELD et POFUT1, prévenant ainsi leur interaction. L’analyse de la protéine WIF1 entière a confirmé les résultats obtenus sur les ELDs isolés et démontre l’occupation des deux sites de N-glycosylation. Enfin, nos résultats montrent également l’importance de ces deux N-glycanes, mais également celle du O-fucose de l’ELD III, pour une sécrétion optimale de la protéine WIF1 murine
The, Pofut1-catalyzed O-fucosylation, is a rare glycosylation which consists of the addition of an O-linked fucose to the serine or threonine of a consensus sequence (C2X4(S/T)C3), carried by an EGF-like domain (ELD) of a membrane or secreted glycoprotein. Our analysis of the murine line Pofut1cax/cax, hypomorphic for the Pofut1 gene, revealed post-natal muscle hypertrophy associated with a decrease in the satellite cell pool. This phenotype was partly associated with a lack of interaction between hypo-O-fucosylated NOTCH receptors of satellite cell-derived myoblasts (SCDM) and their DSL ligands, which resulted in a lower activation of Notch signaling. Other proteins potentially involved in myogenesis may also be the target of POFUT1. This is indeed the case for the protein Wnt inhibitory factor 1 (WIF1), which has five ELDs, whose only two are potentially able to receive an O-fucose (ELDs III and V). Using a phylogenetic approach, we showed in most bilaterians that these two O-fucosylation sites and two N-glycosylation sites were conserved. Our experiments showed theoccupation of all these sites, except for the O-fucosylation site of murine WIF1 protein ELD V. The ability of the ELD III, produced as an isolated protein, to receive O-linked fucose was demonstrated after an in vitro O-fucosylation by combination of copper-catalysed azide-alkyne cycloaddition (CuAAC) and MRM-mass spectrometry. This new experimental approach was then standardized and its sensitivity was evaluated by comparing two other ELDs (NOTCH1 ELDs 12 and 26) known to beO-fucosylated but with different affinities for POFUT1. Surprisingly, WIF1's ELD V could not be O-fucosylated, probably due to a steric clash between this ELD and POFUT1, thus preventing their interaction. The analysis of the full-length WIF1 protein confirmed our results obtained with isolated ELDs and demonstrated the occupation of the two N-glycosylation sites. Finally, our results also showed the importance of these two N-glycans, but also the importance of ELD III’s O-fucose, foroptimal secretion of the murine WIF1 protein
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Javaud, Christophe. "La Fucosylation distale et proximale chez Bos taurus : Structure et expression des gènes FUT4, FUT9 et FUT8." Limoges, 2002. http://www.theses.fr/2002LIMO0057.

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Chez les mammifères, le fucose est greffé à la périphérie des glycannes en position α1,2, α1,3 ou α1,4 lors des dernières étapes de la biosynthèse des oligosaccharides, ou plus préocement en α1,6 sur le premier GlcNAc du groupement chitobiose proximal des N-glycannes exclusivement. Au cours de ce travail, nous avons procédé à une étude approfondie de la fucosylation proximale en clonant le gène FUT8 bovin codant une α6-fucosyltransférase. Ce gène se démarque des autres gènes de fucosyltransférases par sa structure codante multiexonique. De plus, son découpage exon/intron s'avère très différent de celui de l'homme, de la drosophile et du nématode Caenorhabditis elegans. Il existe une excellente corrélation entre l'organisation des exons codant du gène FUT8b et les différents domaines de la protéines. Ces résultats corroborent donc la théorie de la formation ancestrale des gènes par brassage d'exons ("exon shuffling") développée par Gilbert en 1987. Chez Bos taurus, un seul gène codant une α3-fucosyltransférase a été isolé à ce jour. Il s'agit du gène futb (Oulmouden et al. , 1997), orthologue homologue du cluster de gènes humains FUT3-FUT5-FUT6. Alors que l'activité α4-fucosyltransférase responsable de la synthèse des antigènes Le(a) est contrôlée par les produits des gènes FUT3 et FUT5, il a été logiquement postulé que cette activité enzymatique était restreinte aux seules espèces possédant le cluster de gènes Lewis, les hominoi͏̈des (homme et chimpanzé). Après l'identification par Raychoudhury (1997) de l'activité α4-fucosyltransférase chez le rat, et suite aux travaux de Dupuy et al. (2002), montrant que l'α4-fucosylation était en réalité apparue beaucoup plus précocement chez les primates, nous avons entrepris avec succès la recherche d'antigène Le(a) chez le vertébré Bos taurus. Nous avons ensuite isolé deux gènes, bFUT4 et bFUT9 codant des enzymes possédant des aptitudes particulières, contrairement à leurs homologues humaines, pour le transfert du fucose en α1,4. L'α4-fucosylation pourrait donc être plus largement distribuée chez les vertébrés. De plus, par deux mécanismes distincts, chacun de ces gènes est en mesure de coder potentiellement une protéine soluble raccourcie de sa portion transmembranaire, inapte au transfert de fucose, mais dont la fonction de lectine reste à explorer
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Barber, Alistair John. "A behavioural investigation of the function of glycoprotein fucosylation in learning and memory in the day-old domestic chicken." Thesis, Open University, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.236514.

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Joly, Caroline. "Régulation de l'activité α(1,4)fucosyltransférase au cours du développement végétatif et floral du tabac (Nicotiana tabacum cv Xanthi)." Limoges, 2002. http://www.theses.fr/2002LIMO0056.

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Les motifs Lewis(a), générés par les α4-fucosyltransférases, interviennent principalement en tant que signaux de reconnaissance et de communication entre cellules. Néanmoins, les fonctions de l'α4-fucosylation des protéines dans les cellules végétales restent à définir. Nous nous sommes engagés dans l'étude de l'expression de l'activité α(1,4)fucosyltransférase et de la distribution des glycotopes Lewis(a) durant le développement du tabac. Au cours du développement végétatif, l'α4-fucosyltransférase est une enzyme non seulement exprimée de façon ubiquiste mais aussi d'un point de vue spatio-temporel. Nous montrons également que cette activité enzymatique est régulée au cours d'évènements particuliers comme l'élongation cellulaire et la lignification. L'importance de cette régulation est confirmée par l'étude de plants de tabac, exprimant l'α3/4-fucosyltransférase FUT3 humaine. Ces plants présentent un retard de croissance lié à un défaut d'élongation cellulaire. Un phénotype sauvage peut, néanmoins, être rétabli par un apport en gibbérellines. L'étude du développement floral a révélé un profil d'expression de l'activité α(1,4)fucosyltransférase spécifique du grain du pollen. L'α4-fucosyltransférase endogène est régulée comme une protéine "tardive" lors de la microgamétogénèse. De plus, les N-glycoprotéines α4-fucolisées semblent essentielles lors de la germination du grain de pollen et la croissance du tube pollinique. Une dé-régulation de l'activité α(1,4)fucosyltransférase, par surexpression de la FUT3 humaine, induit des altérations structurales et fonctionnelles des grains de pollen. En conclusion, nous montrons que les glycotopes Lewis(a) constituent des facteurs modulant la conformation et/ou de la fonction des glycoprotéines. Ces protéines joueraient, par ailleurs, des rôles clés dans les mécanismes aussi variés que fondamentaux que sont l'élongation cellulaire, la lignification et le développement du grain de pollen
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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‑glycosylation dans le repliement des glycoprotéines. Des analyses combinant l’utilisation de la lignée de cellules myoblastiques C2C12 et le suivi de l’expression des gènes de la myogenèse, constructeurs des O-fucosylglycannes et des acteurs de la voie de Notch, par PCR quantitative en temps réel et à haut débit, nous ont permis de proposer un modèle décrivant le fonctionnement de la voie de signalisation de Notch durant la différenciation myogénique. Ce modèle met en évidence le rôle majeur de plusieurs acteurs de cette voie de signalisation comme Dll1, Notch3, Lfng et Pofut1. Il constitue un point de départ nécessaire aux analyses de la sur- et sous-expression de Pofut1 lors de la différenciation myogénique. Dans cette perspective, nous avons construit une souche de cellules C2C12 surexprimant Pofut1. A terme, les études sur les modifications de l’expression des gènes impliqués dans la biosynthèse des O-fucosylglycannes nous permettront de connaître plus précisément, les mécanismes moléculaires qui orchestrent la voie de signalisation de Notch dans le processus de myogenèse
Skeletal myogenesis is a complex process in which some steps are regulated by Notch signaling pathway. In mammals, the presence of O-fucosylglycans on the extracellular domain of Notch receptors influences the activation of signalling pathway. Pofut1 is an O-fucosyltransferase that initiates O‑fucosylglycans synthesis. During this thesis work, we have identified, by site-directed mutagenesis, the involvement of the conserved N-glycosylation site at position 65, N65, in Pofut1 structural integrity. This is an additional example of the influence of N-glycosylation in glycoprotein folding. Analysis using myogenic C2C12 cell line, and real-time quantitative PCR allowed us to study expression of genes involved in myogenesis, Notch signaling and O-fucosylglycans synthesis. We consequently suggest a model which defines the mechanism of Notch signaling during myogenic differentiation. This model highlights the essential role of several actors of this signalling pathway including Dll1, Notch3, Lfng and Pofut1. It constitutes a necessary starting point for further studies concerning Pofut1 over- and down-expression, during myogenic differentiation. Therefore, we created a C2C12 cell line over-expressing Pofut1. Ultimately, studies on expression modifications of genes implicated in O‑fucosylglycan biosynthesis will enable us to more precisely understand molecular mechanisms that orchestrate Notch signalling in the process of myogenesis
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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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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 deux gènes chez le bovin et leur expression tissulaire ont été établies. Nous trouvons une situation inédite puisqu'il existe pour chacun d’entre eux, cinq variants transcriptionnels dont un seul code l'enzyme active, différemment exprimés selon les tissus bovins. Les enzymes Pofut1 et Pofut2 actives seraient présentes dans tous les tissus analysés, à l’exception notable des muscles squelettiques de l'adulte où des formes atypiques sont présentes. Les autres variants transcriptionnels, la plupart tronqués, auraient un rôle dans la régulation du taux d'expression des gènes. Pofut1 est la première fucosyltransférase à avoir été identifiée comme résidente du réticulum endoplasmique. D'un point de vue fonctionnel, nous avons démontré chez le bovin que cette glycosyltransférase, porteuse de deux N-glycanes vraisemblablement de type oligomannosidique, était correctement repliée et donc douée d'une activité enzymatique, à condition que son premier site de N-glycosylation soit occupé. L’activité des récepteurs Notch et de leurs ligands présents à la surface de nombreuses cellules est modulée par l’état de O-fucosylation de leurs domaines EGF. Etant donné l’implication de ces récepteurs dans la régulation de la myogenèse, la O-fucosylation doit y contribuer tout autant. Ainsi, nous avons débuté une étude des répercussions d’une modulation de l’expression de Pofut1 sur la différenciation de cellules primaires myoblastiques bovines et de cellules murines de la lignée C2C12. Nous montrons que la surexpression transitoire de l’enzyme Pofut1 murine retarde l’expression des facteurs de transcription myogéniques de la famille bHLH: Myf5, MyoD, Myogénine et MRF4. Ces résultats, encore préliminaires, ouvrent de nouvelles et passionnantes perspectives d’analyse de l’influence des O-fucosyltransférases au cours du processus de myogenèse
O-fucosylation is the addition of a fucose on serine or threonine comprised in two types of peptidic domains, EGF and TSR. This post-translational modification depends on two enzymes. Pofut1 is responsible for O-fucosylation of EGF repeats, whereas Pofut2 adds fucose on TSR. We studied the evolution of Pofut1 and Pofut2 genes and demonstrated that these genes, present in a single copy, already existed in the ancestor of Bilaterians, or even Metazoans, probably in polyexonic form. An original situation exists for Pofut2, recovered in a group of Protozoans, the Apicomplexa. Structures of the two bovine genes and their tissular expression have been established. We find an original situation since it exists for each of them, five transcript variants of which only one encodes the active enzyme, differently expressed among bovine tissues. The Pofut1 and Pofut2 active enzymes would be present in all analyzed tissues, except for adult skeletal muscles where atypical forms are present. The other transcript variants, more or less truncated, probably play a role in regulating the expression level of these genes. Pofut1 is the first fucosyltransferase to have been identified as an endoplasmic reticulum resident. Functionally, we demonstrated for the bovine that this glycosyltransferase, bearing two N-glycans probably of oligomannosidic type, was correctly folded and therefore possessed an enzymatic activity, provided its first site of N-glycosylation is occupied. The activity of the Notch receptors and their ligands, present at the surface of numerous cells, is modulated by the state of O-fucosylation of their EGF domains. Considering the implication of these receptors in the regulation of myogenesis, Ofucosylation must contribute all as much there. Thus, we started a study of the repercussions of a modulation of Pofut1 expression on the differentiation of bovine primary muscular cells and murine cells of the C2C12 lineage. We show that the transient surexpression of the murine Pofut1 enzyme delays the expression of myogenic transcription factors belonging to bHLH family: Myf5, MyoD, Myogenine and MRF4. These preliminary results open new and exciting perspectives of analysing the influence of O-fucosyltransferases during the complex process of myogenesis
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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 signalisation Notch est impliquée dans le maintien et l’activation des cellules satellites et l’inhibition de la différenciation des myoblastes. L’inactivation de Pofut1 chez la souris est létale au stade embryonnaire à 9. 5jpc. Chez ces animaux, les anomalies constatées rappellent celles retrouvées chez des mutants d’acteurs de la voie de signalisation Notch (RBPJ et Présénilines). Récemment une mutation spontanée dans le gène murin Pofut1 qui se manifeste par l’insertion d’un élément IAP (intracisternal A particle) de la famille des rétrotransponsons dans l’intron 4 a été aractérisée comme un allèle hypomorphe Pofut1cax (Schuster-Gossler et al. 2009). Ce modèle constitue une nouvelle approche pour étudier le rôle de POFUT1 notamment au cours de la myogenèse. Dans cette perspective, à partir de ce modèle, une analyse morphométrique du muscle squelettique a été réalisée. Cette analyse a permis de mettre en évidence une hypertrophie musculaire à l’âge adulte associée à une diminution du nombre de cellules satellites. L’étude du programme myogénique de cultures primaires de cellules satellites issues de souris cax montre une différenciation précoce. Ces phénotypiques sont similaires à celles obtenues chez des mutants de la voie de signalisation Notch suggérant une régulation de la myogenèse par POFUT1 à travers la modulation de l’interaction du récepteur Notch avec ses ligands
The Notch signaling pathway is an evolutionarily conserved pathway that is critical for tissue morphogenesis during development. Regulation of Notch signaling is involved in somitogenesis, muscle development, and the proliferation and cell fate determination of muscle stem cells. Notch receptors are modified by O-fucosylation of EGF-like repeats by protein O-fucosyltransferase 1 (POFUT1). Fringe enzymes add N-acetylglucosamine to Ofucose and modify Notch signaling by altering the sensitivity of Notch receptors to Notch ligands. Mice embryos lacking Pofut1 die with a phenotype indicative of global inactivation of Notch signaling. To address physiologic functions of O-fucose glycans in myogenesis, we examined mice with hypomorphic allele of Pofut1 (Pofut1cax), a spontaneous mutation in the Pofut1 gene caused by an insertion of an intracisternal A particle retrotransposon in the intron 4 (Schuster-Gossler et al. 2009). Phenotype characterization of this mouse line at the muscle level revealed muscle hypertrophy in adult and a depletion of satellite cells. Isolation and culture of these cells showed early differentiation. Taking together, these results suggest that cax mice phenocopy Notch signaling mutants. The combined data support a key role for Ofucose glycans in Notch regulation of myogenesis through modulation of Notch-ligand interactions
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Book chapters on the topic "Fucosylation"

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Miyoshi, Eiji. "Fucosylation." In Encyclopedia of Cancer, 1–3. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-642-27841-9_2272-2.

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Miyoshi, Eiji. "Fucosylation." In Encyclopedia of Cancer, 1791–93. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-662-46875-3_2272.

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Miyoshi, Eiji. "Fucosylation." In Encyclopedia of Cancer, 1455–57. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-16483-5_2272.

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Miyoshi, Eiji, Katsuhisa Noda, Naoyuki Taniguchi, Yutaka Sasaki, and Norio Hayashi. "Significance of α1-6 Fucosylation in Hepatocellular Carcinoma." In Liver Cirrhosis, 93–104. Tokyo: Springer Japan, 2001. http://dx.doi.org/10.1007/978-4-431-68343-8_12.

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Vestweber, D., K. Lühn, T. Marquardt, and M. Wild. "The Role of Fucosylation in Leukocyte Adhesion Deficiency II." In Leucocyte Trafficking, 53–74. Berlin, Heidelberg: Springer Berlin Heidelberg, 2004. http://dx.doi.org/10.1007/978-3-662-05397-3_4.

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Konno, Yoshinobu, Yuki Kobayashi, Ken Takahashi, Eiji Takahashi, Shinji Sakae, Masako Wakitani, Toshiyuki Suzawa, et al. "Controlling Fucosylation Levels of Antibodies with Osmolality during Cell Culture." In Basic and Applied Aspects, 121–25. Dordrecht: Springer Netherlands, 2010. http://dx.doi.org/10.1007/978-90-481-3892-0_20.

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Wang, Xiangchun, and Naoyuki Taniguchi. "Core Fucosylation of N-linked Glycan for Fine-Tuning TGF-β Receptor Function." In Glycoscience: Biology and Medicine, 1–6. Tokyo: Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-54836-2_56-1.

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Wang, Xiangchun, and Naoyuki Taniguchi. "Core Fucosylation of N-Linked Glycan for Fine-Tuning TGF β Receptor Function." In Glycoscience: Biology and Medicine, 991–97. Tokyo: Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-54841-6_56.

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Konno, Yoshinobu, Yuki Kobayashi, Ken Takahashi, Shinji Sakae, Masako Wakitani, Toshiyuki Suzawa, Keiichi Yano, Masamichi Koike, Kaori Wakamatu, and Shinji Hosoi. "Controlling Fucosylation Levels of Antibodies with Osmolality During Cell Culture in Several Host Cell Lines." In Proceedings of the 21st Annual Meeting of the European Society for Animal Cell Technology (ESACT), Dublin, Ireland, June 7-10, 2009, 585–88. Dordrecht: Springer Netherlands, 2011. http://dx.doi.org/10.1007/978-94-007-0884-6_96.

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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, 25–43. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9698-8_3.

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Conference papers on the topic "Fucosylation"

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Ament, Cindy, Sara Steinmann, Matthias Evert, Kirsten Utpatel, Diego Calvisi, and Katja Evert. "Pathogenetic role of aberrant fucosylation in intrahepatic cholangiocarcinoma." In 38. Jahrestagung der Deutsche Arbeitsgemeinschaft zum Studium der Leber. Georg Thieme Verlag, 2022. http://dx.doi.org/10.1055/s-0041-1740762.

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Keeley, Tyler S., Eric Lau, and Shengyu Yang. "Abstract 895: Fucosylation inhibits invadopodia formation and melanoma invasion." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-895.

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Lester, Daniel K., Pasquale Innamarato, Krithika Kodumudi, Gregory Watson, Matt Mercurio, Shari Pilon-Thomas, Jane Messina, Susan McCarthy, and Eric Lau. "Abstract A73: Fucosylation in CD4+ T cell-mediated melanoma suppression." In Abstracts: AACR Special Conference on Tumor Immunology and Immunotherapy; November 17-20, 2019; Boston, MA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/2326-6074.tumimm19-a73.

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Kerr, SC, PG Woodruff, and JV Fahy. "IL-13 Alters Fucosylation and Sialylation in Airway Epithelial Cells." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a6307.

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Isozaki, Takeo, Shinichiro Nishimi, and Tsuyoshi Kasama. "THU0019 INHIBITION OF FUCOSYLATION IN ENDOTHELIAL CELLS REDUCES RHEUMATOID ARTHRITIS ANGIOGENESIS." In Annual European Congress of Rheumatology, EULAR 2019, Madrid, 12–15 June 2019. BMJ Publishing Group Ltd and European League Against Rheumatism, 2019. http://dx.doi.org/10.1136/annrheumdis-2019-eular.5201.

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Masuzawa, Keita, Hiroyuki Yasuda, Atsushi Matsuda, Hideki Terai, Yuki Sugiura, Junko Hamamoto, Daisuke Arai, et al. "Abstract 365: The role of protein fucosylation in lung cancer progression." In Proceedings: AACR Annual Meeting 2020; April 27-28, 2020 and June 22-24, 2020; Philadelphia, PA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.am2020-365.

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Ales, Evan, Bach-Cuc Nguyen, Winston H. Elliott, Maria A. Kukuruzinska, Catherine E. Costello, Robert Sackstein, and Kevin Brown Chandler. "Abstract 2004: Understanding the role of α1,2-fucosylation in head and neck cancer." In Proceedings: AACR Annual Meeting 2021; April 10-15, 2021 and May 17-21, 2021; Philadelphia, PA. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1538-7445.am2021-2004.

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Snyder, Kara, Hui Ren, Daniel Lester, Bin Fang, John Koomen, and Eric Lau. H. "Abstract P2-04-03: The roles of fucosylation in promoting tumorigenic signaling in breast cancer." In Abstracts: 2019 San Antonio Breast Cancer Symposium; December 10-14, 2019; San Antonio, Texas. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.sabcs19-p2-04-03.

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Okeley, Nicole, Amy Zhang, Stephen Alley, Martha Anderson, Che-Leung Law, and Peter Senter. "Abstract 2945: Antitumor activities of 2-fluorofucose, an orally active agent that inhibits cell-surface fucosylation." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-2945.

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Moriwaki, Kenta, Saori Tsuda, Shinichiro Shinzaki, Yoichi Furukawa, and Eiji Miyoshi. "Abstract 800: Novel GMDS mutation and clinical estimation of fucosylation in several kinds of human cancer." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-800.

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