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Triple-negative and HER2-overexpressing breast cancer cell sialylation impacts tumor microenvironment T-lymphocyte subset recruitment: a possible mechanism of tumor escape.

Cancer management and research

Garbar C, Mascaux C, Merrouche Y, Bensussan A.
PMID: 29765252
Cancer Manag Res. 2018 May 04;10:1051-1059. doi: 10.2147/CMAR.S162932. eCollection 2018.

INTRODUCTION: Breast cancers develop different patterns of sialylation to modulate their tumor-infiltrating lymphocyte (TIL) environment. We studied the relationship between α-2,6 sialyltransferases and the TIL in different breast cancer molecular subgroups.MATERIALS AND METHODS: Immunohistochemical preparations were made from 39...

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Garbar C, Mascaux C, Merrouche Y, et al. Triple-negative and HER2-overexpressing breast cancer cell sialylation impacts tumor microenvironment T-lymphocyte subset recruitment: a possible mechanism of tumor escape. Cancer Manag Res. 2018;10:1051-1059doi: 10.2147/CMAR.S162932.
Garbar, C., Mascaux, C., Merrouche, Y., & Bensussan, A. (2018). Triple-negative and HER2-overexpressing breast cancer cell sialylation impacts tumor microenvironment T-lymphocyte subset recruitment: a possible mechanism of tumor escape. Cancer management and research, 101051-1059. https://doi.org/10.2147/CMAR.S162932
Garbar, Christian, et al. "Triple-negative and HER2-overexpressing breast cancer cell sialylation impacts tumor microenvironment T-lymphocyte subset recruitment: a possible mechanism of tumor escape." Cancer management and research vol. 10 (2018): 1051-1059. doi: https://doi.org/10.2147/CMAR.S162932
Garbar C, Mascaux C, Merrouche Y, Bensussan A. Triple-negative and HER2-overexpressing breast cancer cell sialylation impacts tumor microenvironment T-lymphocyte subset recruitment: a possible mechanism of tumor escape. Cancer Manag Res. 2018 May 04;10:1051-1059. doi: 10.2147/CMAR.S162932. eCollection 2018. PMID: 29765252; PMCID: PMC5942397.
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A Cartography of Siglecs and Sialyltransferases in Gynecologic Malignancies: Is There a Road Towards a Sweet Future?.

Frontiers in oncology

Haas Q, Simillion C, von Gunten S.
PMID: 29594046
Front Oncol. 2018 Mar 13;8:68. doi: 10.3389/fonc.2018.00068. eCollection 2018.

Altered surface glycosylation is a key feature of cancers, including gynecologic malignancies. Hypersialylation, the overexpression of sialic acid, is known to promote tumor progression and to dampen antitumor responses by mechanisms that also involve sialic acid binding immunoglobulin-like lectins...

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Haas Q, Simillion C, von Gunten S. A Cartography of Siglecs and Sialyltransferases in Gynecologic Malignancies: Is There a Road Towards a Sweet Future?. Front Oncol. 2018;8:68doi: 10.3389/fonc.2018.00068.
Haas, Q., Simillion, C., & von Gunten, S. (2018). A Cartography of Siglecs and Sialyltransferases in Gynecologic Malignancies: Is There a Road Towards a Sweet Future?. Frontiers in oncology, 868. https://doi.org/10.3389/fonc.2018.00068
Haas, Quentin, et al. "A Cartography of Siglecs and Sialyltransferases in Gynecologic Malignancies: Is There a Road Towards a Sweet Future?." Frontiers in oncology vol. 8 (2018): 68. doi: https://doi.org/10.3389/fonc.2018.00068
Haas Q, Simillion C, von Gunten S. A Cartography of Siglecs and Sialyltransferases in Gynecologic Malignancies: Is There a Road Towards a Sweet Future?. Front Oncol. 2018 Mar 13;8:68. doi: 10.3389/fonc.2018.00068. eCollection 2018. PMID: 29594046; PMCID: PMC5859025.
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α2,6-Sialylation mediates hepatocellular carcinoma growth in vitro and in vivo by targeting the Wnt/β-catenin pathway.

Oncogenesis

Zhao Y, Wei A, Zhang H, Chen X, Wang L, Zhang H, Yu X, Yuan Q, Zhang J, Wang S.
PMID: 28553930
Oncogenesis. 2017 May 29;6(5):e343. doi: 10.1038/oncsis.2017.40.

Abnormal sialylation due to overexpression of sialyltransferases has been associated with tumorigenesis and tumor progression. Although ST6Gal-I influences cancer persistence and progression by affecting various receptors, the underlying mechanisms and mediators remain largely obscure, especially in hepatocellular carcinoma (HCC)....

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Zhao Y, Wei A, Zhang H, et al. α2,6-Sialylation mediates hepatocellular carcinoma growth in vitro and in vivo by targeting the Wnt/β-catenin pathway. Oncogenesis. 2017;6(5):e343doi: 10.1038/oncsis.2017.40.
Zhao, Y., Wei, A., Zhang, H., Chen, X., Wang, L., Zhang, H., Yu, X., Yuan, Q., Zhang, J., & Wang, S. (2017). α2,6-Sialylation mediates hepatocellular carcinoma growth in vitro and in vivo by targeting the Wnt/β-catenin pathway. Oncogenesis, 6(5), e343. https://doi.org/10.1038/oncsis.2017.40
Zhao, Y, et al. "α2,6-Sialylation mediates hepatocellular carcinoma growth in vitro and in vivo by targeting the Wnt/β-catenin pathway." Oncogenesis vol. 6,5 (2017): e343. doi: https://doi.org/10.1038/oncsis.2017.40
Zhao Y, Wei A, Zhang H, Chen X, Wang L, Zhang H, Yu X, Yuan Q, Zhang J, Wang S. α2,6-Sialylation mediates hepatocellular carcinoma growth in vitro and in vivo by targeting the Wnt/β-catenin pathway. Oncogenesis. 2017 May 29;6(5):e343. doi: 10.1038/oncsis.2017.40. PMID: 28553930; PMCID: PMC5523073.
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Engineering of CHO cells for the production of vertebrate recombinant sialyltransferases.

PeerJ

Houeix B, Cairns MT.
PMID: 30775162
PeerJ. 2019 Feb 11;7:e5788. doi: 10.7717/peerj.5788. eCollection 2019.

BACKGROUND: Sialyltransferases (SIATs) are a family of enzymes that transfer sialic acid (Sia) to glycan chains on glycoproteins, glycolipids, and oligosaccharides. They play key roles in determining cell-cell and cell-matrix interactions and are important in neuronal development, immune regulation,...

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Houeix B, Cairns MT. Engineering of CHO cells for the production of vertebrate recombinant sialyltransferases. PeerJ. 2019;7:e5788doi: 10.7717/peerj.5788.
Houeix, B., & Cairns, M. T. (2019). Engineering of CHO cells for the production of vertebrate recombinant sialyltransferases. PeerJ, 7e5788. https://doi.org/10.7717/peerj.5788
Houeix, Benoit, and Cairns, Michael T. "Engineering of CHO cells for the production of vertebrate recombinant sialyltransferases." PeerJ vol. 7 (2019): e5788. doi: https://doi.org/10.7717/peerj.5788
Houeix B, Cairns MT. Engineering of CHO cells for the production of vertebrate recombinant sialyltransferases. PeerJ. 2019 Feb 11;7:e5788. doi: 10.7717/peerj.5788. eCollection 2019. PMID: 30775162; PMCID: PMC6375257.
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ST3Gal IV Mediates the Growth and Proliferation of Cervical Cancer Cells .

Frontiers in oncology

Wu Y, Chen X, Dong W, Xu Z, Jian Y, Xu C, Zhang L, Wei A, Yu X, Wang S, Wang Y, Liu G, Sun X, Wang S.
PMID: 33598419
Front Oncol. 2021 Feb 01;10:540332. doi: 10.3389/fonc.2020.540332. eCollection 2020.

ST3Gal IV is one of the principal sialyltransferases responsible for the biosynthesis of α2, 3-sialic acid to the termini

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Wu Y, Chen X, Dong W, et al. ST3Gal IV Mediates the Growth and Proliferation of Cervical Cancer Cells . Front Oncol. 2021;10:540332doi: 10.3389/fonc.2020.540332.
Wu, Y., Chen, X., Dong, W., Xu, Z., Jian, Y., Xu, C., Zhang, L., Wei, A., Yu, X., Wang, S., Wang, Y., Liu, G., Sun, X., & Wang, S. (2020). ST3Gal IV Mediates the Growth and Proliferation of Cervical Cancer Cells . Frontiers in oncology, 10540332. https://doi.org/10.3389/fonc.2020.540332
Wu, Yinshuang, et al. "ST3Gal IV Mediates the Growth and Proliferation of Cervical Cancer Cells ." Frontiers in oncology vol. 10 (2020): 540332. doi: https://doi.org/10.3389/fonc.2020.540332
Wu Y, Chen X, Dong W, Xu Z, Jian Y, Xu C, Zhang L, Wei A, Yu X, Wang S, Wang Y, Liu G, Sun X, Wang S. ST3Gal IV Mediates the Growth and Proliferation of Cervical Cancer Cells . Front Oncol. 2021 Feb 01;10:540332. doi: 10.3389/fonc.2020.540332. eCollection 2020. PMID: 33598419; PMCID: PMC7882721.
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Glycation Interferes with the Expression of Sialyltransferases in Meningiomas.

Cells

Selke P, Bork K, Zhang T, Wuhrer M, Strauss C, Horstkorte R, Scheer M.
PMID: 34943806
Cells. 2021 Nov 25;10(12). doi: 10.3390/cells10123298.

Meningiomas are the most common non-malignant intracranial tumors and prefer, like most tumors, anaerobic glycolysis for energy production (Warburg effect). This anaerobic glycolysis leads to an increased synthesis of the metabolite methylglyoxal (MGO) or glyoxal (GO), which is known...

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Selke P, Bork K, Zhang T, et al. Glycation Interferes with the Expression of Sialyltransferases in Meningiomas. Cells. 2021;10(12)doi: 10.3390/cells10123298.
Selke, P., Bork, K., Zhang, T., Wuhrer, M., Strauss, C., Horstkorte, R., & Scheer, M. (2021). Glycation Interferes with the Expression of Sialyltransferases in Meningiomas. Cells, 10(12), . https://doi.org/10.3390/cells10123298
Selke, Philipp, et al. "Glycation Interferes with the Expression of Sialyltransferases in Meningiomas." Cells vol. 10,12 (2021). doi: https://doi.org/10.3390/cells10123298
Selke P, Bork K, Zhang T, Wuhrer M, Strauss C, Horstkorte R, Scheer M. Glycation Interferes with the Expression of Sialyltransferases in Meningiomas. Cells. 2021 Nov 25;10(12). doi: 10.3390/cells10123298. PMID: 34943806; PMCID: PMC8699175.
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Cell Line-, Protein-, and Sialoglycosite-Specific Control of Flux-Based Sialylation in Human Breast Cells: Implications for Cancer Progression.

Frontiers in chemistry

Saeui CT, Cho KC, Dharmarha V, Nairn AV, Galizzi M, Shah SR, Gowda P, Park M, Austin M, Clarke A, Cai E, Buettner MJ, Ariss R, Moremen KW, Zhang H, Yarema KJ.
PMID: 32117864
Front Chem. 2020 Feb 05;8:13. doi: 10.3389/fchem.2020.00013. eCollection 2020.

Sialylation, a post-translational modification that impacts the structure, activity, and longevity of glycoproteins has been thought to be controlled primarily by the expression of sialyltransferases (STs). In this report we explore the complementary impact of metabolic flux on sialylation...

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Saeui CT, Cho KC, Dharmarha V, et al. Cell Line-, Protein-, and Sialoglycosite-Specific Control of Flux-Based Sialylation in Human Breast Cells: Implications for Cancer Progression. Front Chem. 2020;8:13doi: 10.3389/fchem.2020.00013.
Saeui, C. T., Cho, K. C., Dharmarha, V., Nairn, A. V., Galizzi, M., Shah, S. R., Gowda, P., Park, M., Austin, M., Clarke, A., Cai, E., Buettner, M. J., Ariss, R., Moremen, K. W., Zhang, H., & Yarema, K. J. (2020). Cell Line-, Protein-, and Sialoglycosite-Specific Control of Flux-Based Sialylation in Human Breast Cells: Implications for Cancer Progression. Frontiers in chemistry, 813. https://doi.org/10.3389/fchem.2020.00013
Saeui, Christopher T, et al. "Cell Line-, Protein-, and Sialoglycosite-Specific Control of Flux-Based Sialylation in Human Breast Cells: Implications for Cancer Progression." Frontiers in chemistry vol. 8 (2020): 13. doi: https://doi.org/10.3389/fchem.2020.00013
Saeui CT, Cho KC, Dharmarha V, Nairn AV, Galizzi M, Shah SR, Gowda P, Park M, Austin M, Clarke A, Cai E, Buettner MJ, Ariss R, Moremen KW, Zhang H, Yarema KJ. Cell Line-, Protein-, and Sialoglycosite-Specific Control of Flux-Based Sialylation in Human Breast Cells: Implications for Cancer Progression. Front Chem. 2020 Feb 05;8:13. doi: 10.3389/fchem.2020.00013. eCollection 2020. PMID: 32117864; PMCID: PMC7013041.
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From Substrate to Transition State Analogues: The First Potent Inhibitor of Sialyltransferases.

Angewandte Chemie (International ed. in English)

Schröder PN, Giannis A.
PMID: 29711575
Angew Chem Int Ed Engl. 1999 May 17;38(10):1379-1380. doi: 10.1002/(SICI)1521-3773(19990517)38:10<1379::AID-ANIE1379>3.0.CO;2-M.

No abstract available.

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Schröder PN, Giannis A. From Substrate to Transition State Analogues: The First Potent Inhibitor of Sialyltransferases. Angew Chem Int Ed Engl. 1999;38(10):1379-1380doi: 10.1002/(SICI)1521-3773(19990517)38:10<1379::AID-ANIE1379>3.0.CO;2-M.
Schröder, P. N., & Giannis, A. (1999). From Substrate to Transition State Analogues: The First Potent Inhibitor of Sialyltransferases. Angewandte Chemie (International ed. in English), 38(10), 1379-1380. https://doi.org/10.1002/(SICI)1521-3773(19990517)38:10<1379::AID-ANIE1379>3.0.CO;2-M
Schröder, Peer Nils, and Giannis, Athanassios. "From Substrate to Transition State Analogues: The First Potent Inhibitor of Sialyltransferases." Angewandte Chemie (International ed. in English) vol. 38,10 (1999): 1379-1380. doi: https://doi.org/10.1002/(SICI)1521-3773(19990517)38:10<1379::AID-ANIE1379>3.0.CO;2-M
Schröder PN, Giannis A. From Substrate to Transition State Analogues: The First Potent Inhibitor of Sialyltransferases. Angew Chem Int Ed Engl. 1999 May 17;38(10):1379-1380. doi: 10.1002/(SICI)1521-3773(19990517)38:10<1379::AID-ANIE1379>3.0.CO;2-M. PMID: 29711575.
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Expression of α2,6-sialic acid-containing and Lewis-active glycolipids in several types of human ovarian carcinomas.

Oncology letters

Tanaka K, Mikami M, Aoki D, Kiguchi K, Ishiwata I, Iwamori M.
PMID: 22870113
Oncol Lett. 2010 Nov;1(6):1061-1066. doi: 10.3892/ol.2010.171. Epub 2010 Sep 09.

To identify glycolipid antigens associated with histologically defined types of ovarian carcinomas, we determined the amounts of α2,6-sialyl and Lewis-active glycolipids, the specific activities of the α2,3- and α2,6-sialyltransferases, and the gene expression of sugar transferases in mucinous and...

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Tanaka K, Mikami M, Aoki D, et al. Expression of α2,6-sialic acid-containing and Lewis-active glycolipids in several types of human ovarian carcinomas. Oncol Lett. 2010;1(6):1061-1066doi: 10.3892/ol.2010.171.
Tanaka, K., Mikami, M., Aoki, D., Kiguchi, K., Ishiwata, I., & Iwamori, M. (2010). Expression of α2,6-sialic acid-containing and Lewis-active glycolipids in several types of human ovarian carcinomas. Oncology letters, 1(6), 1061-1066. https://doi.org/10.3892/ol.2010.171
Tanaka, Kyoko, et al. "Expression of α2,6-sialic acid-containing and Lewis-active glycolipids in several types of human ovarian carcinomas." Oncology letters vol. 1,6 (2010): 1061-1066. doi: https://doi.org/10.3892/ol.2010.171
Tanaka K, Mikami M, Aoki D, Kiguchi K, Ishiwata I, Iwamori M. Expression of α2,6-sialic acid-containing and Lewis-active glycolipids in several types of human ovarian carcinomas. Oncol Lett. 2010 Nov;1(6):1061-1066. doi: 10.3892/ol.2010.171. Epub 2010 Sep 09. PMID: 22870113; PMCID: PMC3412467.
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Chemoenzymatic Syntheses of Tumor-Associated Carbohydrate Antigen Globo-H and Stage-Specific Embryonic Antigen 4.

Advanced synthesis & catalysis

Wang Z, Gilbert M, Eguchi H, Yu H, Cheng J, Muthana S, Zhou L, Wang PG, Chen X, Huang X.
PMID: 20305750
Adv Synth Catal. 2008 Aug 04;350(11):1717-1728. doi: 10.1002/adsc.200800129.

Gangliosides have attracted much attention due to their important biological properties. Herein, we report the first chemoenzymatic syntheses of two globo series of ganglioside oligosaccharides, Globo-H 1 and stage-specific embryonic antigen-4 (SSEA-4) 2. The common precursor SSEA-3 pentasaccharide for...

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Wang Z, Gilbert M, Eguchi H, et al. Chemoenzymatic Syntheses of Tumor-Associated Carbohydrate Antigen Globo-H and Stage-Specific Embryonic Antigen 4. Adv Synth Catal. 2008;350(11):1717-1728doi: 10.1002/adsc.200800129.
Wang, Z., Gilbert, M., Eguchi, H., Yu, H., Cheng, J., Muthana, S., Zhou, L., Wang, P. G., Chen, X., & Huang, X. (2008). Chemoenzymatic Syntheses of Tumor-Associated Carbohydrate Antigen Globo-H and Stage-Specific Embryonic Antigen 4. Advanced synthesis & catalysis, 350(11), 1717-1728. https://doi.org/10.1002/adsc.200800129
Wang, Zhen, et al. "Chemoenzymatic Syntheses of Tumor-Associated Carbohydrate Antigen Globo-H and Stage-Specific Embryonic Antigen 4." Advanced synthesis & catalysis vol. 350,11 (2008): 1717-1728. doi: https://doi.org/10.1002/adsc.200800129
Wang Z, Gilbert M, Eguchi H, Yu H, Cheng J, Muthana S, Zhou L, Wang PG, Chen X, Huang X. Chemoenzymatic Syntheses of Tumor-Associated Carbohydrate Antigen Globo-H and Stage-Specific Embryonic Antigen 4. Adv Synth Catal. 2008 Aug 04;350(11):1717-1728. doi: 10.1002/adsc.200800129. PMID: 20305750; PMCID: PMC2842016.
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Identification of sialyltransferases of Streptococcus agalactiae.

Journal of bioscience and bioengineering

Watanabe M, Miyake K, Yamamoto S, Kataoka Y, Koizumi S, Endo T, Ozaki A, Iijima S.
PMID: 16233258
J Biosci Bioeng. 2002;93(6):610-3.

Group B streptococci, Streptococcus agalactiae, produce high-molecular-weight polysaccharides containing N-acetylneuraminic acid. Although the type-specific capsular polysaccharide (CP) synthesis (cps) genes of several S. agalactiae strains have been extensively analyzed, to date, no sialyltransferase activity has been detected from any...

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Watanabe M, Miyake K, Yamamoto S, et al. Identification of sialyltransferases of Streptococcus agalactiae. J Biosci Bioeng. 2002;93(6):610-3
Watanabe, M., Miyake, K., Yamamoto, S., Kataoka, Y., Koizumi, S., Endo, T., Ozaki, A., & Iijima, S. (2002). Identification of sialyltransferases of Streptococcus agalactiae. Journal of bioscience and bioengineering, 93(6), 610-3.
Watanabe, Masaki, et al. "Identification of sialyltransferases of Streptococcus agalactiae." Journal of bioscience and bioengineering vol. 93,6 (2002): 610-3.
Watanabe M, Miyake K, Yamamoto S, Kataoka Y, Koizumi S, Endo T, Ozaki A, Iijima S. Identification of sialyltransferases of Streptococcus agalactiae. J Biosci Bioeng. 2002;93(6):610-3. PMID: 16233258.
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Investigation of glycan evolution based on a comprehensive analysis of glycosyltransferases using phylogenetic profiling.

Biophysics and physicobiology

Tomono T, Kojima H, Fukuchi S, Tohsato Y, Ito M.
PMID: 27493855
Biophys Physicobiol. 2015 Nov 12;12:57-68. doi: 10.2142/biophysico.12.0_57. eCollection 2015.

Glycans play important roles in such cell-cell interactions as signaling and adhesion, including processes involved in pathogenic infections, cancers, and neurological diseases. Glycans are biosynthesized by multiple glycosyltransferases (GTs), which function sequentially. Excluding mucin-type O-glycosylation, the non-reducing terminus of...

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Tomono T, Kojima H, Fukuchi S, et al. Investigation of glycan evolution based on a comprehensive analysis of glycosyltransferases using phylogenetic profiling. Biophys Physicobiol. 2015;12:57-68doi: 10.2142/biophysico.12.0_57.
Tomono, T., Kojima, H., Fukuchi, S., Tohsato, Y., & Ito, M. (2015). Investigation of glycan evolution based on a comprehensive analysis of glycosyltransferases using phylogenetic profiling. Biophysics and physicobiology, 1257-68. https://doi.org/10.2142/biophysico.12.0_57
Tomono, Takayoshi, et al. "Investigation of glycan evolution based on a comprehensive analysis of glycosyltransferases using phylogenetic profiling." Biophysics and physicobiology vol. 12 (2015): 57-68. doi: https://doi.org/10.2142/biophysico.12.0_57
Tomono T, Kojima H, Fukuchi S, Tohsato Y, Ito M. Investigation of glycan evolution based on a comprehensive analysis of glycosyltransferases using phylogenetic profiling. Biophys Physicobiol. 2015 Nov 12;12:57-68. doi: 10.2142/biophysico.12.0_57. eCollection 2015. PMID: 27493855; PMCID: PMC4736839.
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Showing 1 to 12 of 34 entries