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1,N6-ethenoadenine and other Fluorescent Nucleobase Analogues as Substrates for Purine-Nucleoside Phosphorylases: Spectroscopic and Kinetic Studies.

Current pharmaceutical design

Wierzchowski J, Stachelska-Wierzchowska A, Wielgus-Kutrowska B, Bzowska A.
PMID: 29022509
Curr Pharm Des. 2017 Oct 11; doi: 10.2174/1381612823666171011103551. Epub 2017 Oct 11.

BACKGROUND: Purine-nucleoside phosphorylase (PNP) is known as a tool for the synthesis of various nucleosides and nucleoside analogues. Mechanism, properties, molecular diversity and inhibitors of PNP, particularly these of pharmacological significance, are briefly characterized.METHODS: UV and fluorescence spectroscopy was...

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Wierzchowski J, Stachelska-Wierzchowska A, Wielgus-Kutrowska B, et al. 1,N6-ethenoadenine and other Fluorescent Nucleobase Analogues as Substrates for Purine-Nucleoside Phosphorylases: Spectroscopic and Kinetic Studies. Curr Pharm Des. 2017;doi: 10.2174/1381612823666171011103551.
Wierzchowski, J., Stachelska-Wierzchowska, A., Wielgus-Kutrowska, B., & Bzowska, A. (2017). 1,N6-ethenoadenine and other Fluorescent Nucleobase Analogues as Substrates for Purine-Nucleoside Phosphorylases: Spectroscopic and Kinetic Studies. Current pharmaceutical design, . https://doi.org/10.2174/1381612823666171011103551
Wierzchowski, Jacek, et al. "1,N6-ethenoadenine and other Fluorescent Nucleobase Analogues as Substrates for Purine-Nucleoside Phosphorylases: Spectroscopic and Kinetic Studies." Current pharmaceutical design vol. (2017). doi: https://doi.org/10.2174/1381612823666171011103551
Wierzchowski J, Stachelska-Wierzchowska A, Wielgus-Kutrowska B, Bzowska A. 1,N6-ethenoadenine and other Fluorescent Nucleobase Analogues as Substrates for Purine-Nucleoside Phosphorylases: Spectroscopic and Kinetic Studies. Curr Pharm Des. 2017 Oct 11; doi: 10.2174/1381612823666171011103551. Epub 2017 Oct 11. PMID: 29022509.
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α-1,4-Glucan phosphorylase forms from leaves of spinach (Spinacia oleracea L.) I. In situ localization by indirect immunofluorescence.

Planta

Schächtele C, Steup M.
PMID: 24240359
Planta. 1986 Apr;167(4):444-51. doi: 10.1007/BF00391219.

Antisera were raised against two forms of α-1,4-glucan phosphorylase (EC 2.4.1.1) which had been purified from leaves of Spinacia oleracea L. Immunoglobulin G preparations were isolated from the antisera, and their specificity was ensured by immunoplobulin G preparations were...

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Schächtele C, Steup M. α-1,4-Glucan phosphorylase forms from leaves of spinach (Spinacia oleracea L.) I. In situ localization by indirect immunofluorescence. Planta. 1986;167(4):444-51doi: 10.1007/BF00391219.
Schächtele, C., & Steup, M. (1986). α-1,4-Glucan phosphorylase forms from leaves of spinach (Spinacia oleracea L.) I. In situ localization by indirect immunofluorescence. Planta, 167(4), 444-51. https://doi.org/10.1007/BF00391219
Schächtele, C, and Steup, M. "α-1,4-Glucan phosphorylase forms from leaves of spinach (Spinacia oleracea L.) I. In situ localization by indirect immunofluorescence." Planta vol. 167,4 (1986): 444-51. doi: https://doi.org/10.1007/BF00391219
Schächtele C, Steup M. α-1,4-Glucan phosphorylase forms from leaves of spinach (Spinacia oleracea L.) I. In situ localization by indirect immunofluorescence. Planta. 1986 Apr;167(4):444-51. doi: 10.1007/BF00391219. PMID: 24240359.
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4(5)-Aryl-2-C-glucopyranosyl-imidazoles as New Nanomolar Glucose Analogue Inhibitors of Glycogen Phosphorylase.

ACS medicinal chemistry letters

Bokor É, Kun S, Docsa T, Gergely P, Somsák L.
PMID: 26713107
ACS Med Chem Lett. 2015 Oct 19;6(12):1215-9. doi: 10.1021/acsmedchemlett.5b00361. eCollection 2015 Dec 10.

Inhibition of glycogen phosphorylases may lead to pharmacological treatments of diseases in which glycogen metabolism plays an important role: first of all in diabetes, but also in cardiovascular and tumorous disorders. C-(β-d-Glucopyranosyl) isoxazole, pyrazole, thiazole, and imidazole type compounds...

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Bokor É, Kun S, Docsa T, et al. 4(5)-Aryl-2-C-glucopyranosyl-imidazoles as New Nanomolar Glucose Analogue Inhibitors of Glycogen Phosphorylase. ACS Med Chem Lett. 2015;6(12):1215-9doi: 10.1021/acsmedchemlett.5b00361.
Bokor, �. �., Kun, S., Docsa, T., Gergely, P., & Somsák, L. (2015). 4(5)-Aryl-2-C-glucopyranosyl-imidazoles as New Nanomolar Glucose Analogue Inhibitors of Glycogen Phosphorylase. ACS medicinal chemistry letters, 6(12), 1215-9. https://doi.org/10.1021/acsmedchemlett.5b00361
Bokor, Éva, et al. "4(5)-Aryl-2-C-glucopyranosyl-imidazoles as New Nanomolar Glucose Analogue Inhibitors of Glycogen Phosphorylase." ACS medicinal chemistry letters vol. 6,12 (2015): 1215-9. doi: https://doi.org/10.1021/acsmedchemlett.5b00361
Bokor É, Kun S, Docsa T, Gergely P, Somsák L. 4(5)-Aryl-2-C-glucopyranosyl-imidazoles as New Nanomolar Glucose Analogue Inhibitors of Glycogen Phosphorylase. ACS Med Chem Lett. 2015 Oct 19;6(12):1215-9. doi: 10.1021/acsmedchemlett.5b00361. eCollection 2015 Dec 10. PMID: 26713107; PMCID: PMC4677374.
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Primary structure of sweet potato starch phosphorylase deduced from its cDNA sequence.

Plant physiology

Lin CT, Yeh KW, Lee PD, Su JC.
PMID: 16668119
Plant Physiol. 1991 Apr;95(4):1250-3. doi: 10.1104/pp.95.4.1250.

Sweet potato (Ipomoea batatas) starch phosphorylase cDNA clones were isolated by screening an expression library prepared from the young root poly(A)(+) RNA successively with an antiserum, a monoclonal antibody, and a specific oligonucleotide probe. One cDNA clone had 3292...

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Lin CT, Yeh KW, Lee PD, et al. Primary structure of sweet potato starch phosphorylase deduced from its cDNA sequence. Plant Physiol. 1991;95(4):1250-3doi: 10.1104/pp.95.4.1250.
Lin, C. T., Yeh, K. W., Lee, P. D., & Su, J. C. (1991). Primary structure of sweet potato starch phosphorylase deduced from its cDNA sequence. Plant physiology, 95(4), 1250-3. https://doi.org/10.1104/pp.95.4.1250
Lin, C T, et al. "Primary structure of sweet potato starch phosphorylase deduced from its cDNA sequence." Plant physiology vol. 95,4 (1991): 1250-3. doi: https://doi.org/10.1104/pp.95.4.1250
Lin CT, Yeh KW, Lee PD, Su JC. Primary structure of sweet potato starch phosphorylase deduced from its cDNA sequence. Plant Physiol. 1991 Apr;95(4):1250-3. doi: 10.1104/pp.95.4.1250. PMID: 16668119; PMCID: PMC1077680.
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Dynamics and regulation of sucrose phosphorylase formation in Leuconostoc mesenteroides fermentations.

Biotechnology and bioengineering

Vandamme EJ, Van Loo J, De Laporte A.
PMID: 18561123
Biotechnol Bioeng. 1987 Jan;29(1):8-15. doi: 10.1002/bit.260290103.

The production of Leuconostoc mesenteroides sucrose phosphorylase has been studied in 10- and 20-L batch fermentations. A fermentation medium was devised combining rapid growth, high cell yield, and high enzyme levels. Overall fermentation dynamics and enzyme fermentation patterns are...

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Vandamme EJ, Van Loo J, De Laporte A. Dynamics and regulation of sucrose phosphorylase formation in Leuconostoc mesenteroides fermentations. Biotechnol Bioeng. 1987;29(1):8-15doi: 10.1002/bit.260290103.
Vandamme, E. J., Van Loo, J., & De Laporte, A. (1987). Dynamics and regulation of sucrose phosphorylase formation in Leuconostoc mesenteroides fermentations. Biotechnology and bioengineering, 29(1), 8-15. https://doi.org/10.1002/bit.260290103
Vandamme, E J, et al. "Dynamics and regulation of sucrose phosphorylase formation in Leuconostoc mesenteroides fermentations." Biotechnology and bioengineering vol. 29,1 (1987): 8-15. doi: https://doi.org/10.1002/bit.260290103
Vandamme EJ, Van Loo J, De Laporte A. Dynamics and regulation of sucrose phosphorylase formation in Leuconostoc mesenteroides fermentations. Biotechnol Bioeng. 1987 Jan;29(1):8-15. doi: 10.1002/bit.260290103. PMID: 18561123.
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Compositional and enzymatic characteristics of the Longissimus Dorsi muscle from large white, halothane-positive and halothane-negative pietrain, and hampshire pigs.

Meat science

Monin G, Talmant A, Laborde D, Zabari M, Sellier P.
PMID: 22055085
Meat Sci. 1986;16(4):307-16. doi: 10.1016/0309-1740(86)90041-0.

One-hundred-and-twenty-nine pigs from four genetic types-Large Whites, halothane-negative (HN) and halothane-positive (HP) Pietrains and Hampshires-were used to study some compositional and enzymatic muscle traits. Water, nitrogen, hydroxyproline and lipid contents, as well as lactate dehydrogenase and citrate synthase activities,...

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Monin G, Talmant A, Laborde D, et al. Compositional and enzymatic characteristics of the Longissimus Dorsi muscle from large white, halothane-positive and halothane-negative pietrain, and hampshire pigs. Meat Sci. 1986;16(4):307-16doi: 10.1016/0309-1740(86)90041-0.
Monin, G., Talmant, A., Laborde, D., Zabari, M., & Sellier, P. (1986). Compositional and enzymatic characteristics of the Longissimus Dorsi muscle from large white, halothane-positive and halothane-negative pietrain, and hampshire pigs. Meat science, 16(4), 307-16. https://doi.org/10.1016/0309-1740(86)90041-0
Monin, G, et al. "Compositional and enzymatic characteristics of the Longissimus Dorsi muscle from large white, halothane-positive and halothane-negative pietrain, and hampshire pigs." Meat science vol. 16,4 (1986): 307-16. doi: https://doi.org/10.1016/0309-1740(86)90041-0
Monin G, Talmant A, Laborde D, Zabari M, Sellier P. Compositional and enzymatic characteristics of the Longissimus Dorsi muscle from large white, halothane-positive and halothane-negative pietrain, and hampshire pigs. Meat Sci. 1986;16(4):307-16. doi: 10.1016/0309-1740(86)90041-0. PMID: 22055085.
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Influence of breed and muscle metabolic type on muscle glycolytic potential and meat pH in pigs.

Meat science

Monin G, Mejenes-Quijano A, Talmant A, Sellier P.
PMID: 22056171
Meat Sci. 1987;20(2):149-58. doi: 10.1016/0309-1740(87)90034-9.

Glycolytic potential and activities of myofibrillar ATPase, lactate dehydrogenase, citrate synthase, glycogen synthetases and glycogen phosphorylases were measured in five muscles from five Large White, eight Pietrain, seven Belgian Landrace and eight Penshire pigs (Penshire is a composite line...

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Monin G, Mejenes-Quijano A, Talmant A, et al. Influence of breed and muscle metabolic type on muscle glycolytic potential and meat pH in pigs. Meat Sci. 1987;20(2):149-58doi: 10.1016/0309-1740(87)90034-9.
Monin, G., Mejenes-Quijano, A., Talmant, A., & Sellier, P. (1987). Influence of breed and muscle metabolic type on muscle glycolytic potential and meat pH in pigs. Meat science, 20(2), 149-58. https://doi.org/10.1016/0309-1740(87)90034-9
Monin, G, et al. "Influence of breed and muscle metabolic type on muscle glycolytic potential and meat pH in pigs." Meat science vol. 20,2 (1987): 149-58. doi: https://doi.org/10.1016/0309-1740(87)90034-9
Monin G, Mejenes-Quijano A, Talmant A, Sellier P. Influence of breed and muscle metabolic type on muscle glycolytic potential and meat pH in pigs. Meat Sci. 1987;20(2):149-58. doi: 10.1016/0309-1740(87)90034-9. PMID: 22056171.
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[The metabolism of starch : II. The conversion of starch into sucrose in the cotyledons of vicia faba].

Planta

de Fekete MA.
PMID: 24504781
Planta. 1969 Dec;87(4):324-32. doi: 10.1007/BF00388317.

The determination of the activities of the enzymes which could be involved in the starch-sucrose conversion showed that the first step of this transfer is a phosphorolysis of starch. Both phosphorylases are able to attack the starch granules. The...

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de Fekete MA. Zum Stoffwechsel der Stärke : II. Die Umwandlung der Stärke in Saccharose in den Kotyledonen von Vicia faba. [The metabolism of starch : II. The conversion of starch into sucrose in the cotyledons of vicia faba]. Planta. 1969;87(4):324-32doi: 10.1007/BF00388317.
de Fekete, M. A. (1969). Zum Stoffwechsel der Stärke : II. Die Umwandlung der Stärke in Saccharose in den Kotyledonen von Vicia faba. [The metabolism of starch : II. The conversion of starch into sucrose in the cotyledons of vicia faba]. Planta, 87(4), 324-32. https://doi.org/10.1007/BF00388317
de Fekete, M A. "Zum Stoffwechsel der Stärke : II. Die Umwandlung der Stärke in Saccharose in den Kotyledonen von Vicia faba." [The metabolism of starch : II. The conversion of starch into sucrose in the cotyledons of vicia faba]. Planta vol. 87,4 (1969): 324-32. doi: https://doi.org/10.1007/BF00388317
de Fekete MA. Zum Stoffwechsel der Stärke : II. Die Umwandlung der Stärke in Saccharose in den Kotyledonen von Vicia faba. [The metabolism of starch : II. The conversion of starch into sucrose in the cotyledons of vicia faba]. Planta. 1969 Dec;87(4):324-32. doi: 10.1007/BF00388317. German. PMID: 24504781.
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Substrate spectra of nucleoside phosphorylases and their potential in the production of pharmaceutically active compounds.

Current pharmaceutical design

Yehia H, Kamel S, Paulick K, Wagner A, Neubauer P.
PMID: 29076414
Curr Pharm Des. 2017 Oct 24; doi: 10.2174/1381612823666171024155811. Epub 2017 Oct 24.

BACKGROUND: Nucleoside phosphorylases catalyze the reversible phosphorolysis of pyrimidine and purine nucleosides in the presence of phosphate. They are relevant to the appropriate function of the immune system in mammals and interesting drug targets for cancer treatment. Next to...

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Yehia H, Kamel S, Paulick K, et al. Substrate spectra of nucleoside phosphorylases and their potential in the production of pharmaceutically active compounds. Curr Pharm Des. 2017;doi: 10.2174/1381612823666171024155811.
Yehia, H., Kamel, S., Paulick, K., Wagner, A., & Neubauer, P. (2017). Substrate spectra of nucleoside phosphorylases and their potential in the production of pharmaceutically active compounds. Current pharmaceutical design, . https://doi.org/10.2174/1381612823666171024155811
Yehia, Heba, et al. "Substrate spectra of nucleoside phosphorylases and their potential in the production of pharmaceutically active compounds." Current pharmaceutical design vol. (2017). doi: https://doi.org/10.2174/1381612823666171024155811
Yehia H, Kamel S, Paulick K, Wagner A, Neubauer P. Substrate spectra of nucleoside phosphorylases and their potential in the production of pharmaceutically active compounds. Curr Pharm Des. 2017 Oct 24; doi: 10.2174/1381612823666171024155811. Epub 2017 Oct 24. PMID: 29076414.
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Structure of a bacterial α-1,2-glucosidase defines mechanisms of hydrolysis and substrate specificity in GH65 family hydrolases.

The Journal of biological chemistry

Nakamura S, Nihira T, Kurata R, Nakai H, Funane K, Park EY, Miyazaki T.
PMID: 34728215
J Biol Chem. 2021 Dec;297(6):101366. doi: 10.1016/j.jbc.2021.101366. Epub 2021 Oct 30.

Glycoside hydrolase family 65 (GH65) comprises glycoside hydrolases (GHs) and glycoside phosphorylases (GPs) that act on α-glucosidic linkages in oligosaccharides. All previously reported bacterial GH65 enzymes are GPs, whereas all eukaryotic GH65 enzymes known are GHs. In addition, to...

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Nakamura S, Nihira T, Kurata R, et al. Structure of a bacterial α-1,2-glucosidase defines mechanisms of hydrolysis and substrate specificity in GH65 family hydrolases. J Biol Chem. 2021;297(6):101366doi: 10.1016/j.jbc.2021.101366.
Nakamura, S., Nihira, T., Kurata, R., Nakai, H., Funane, K., Park, E. Y., & Miyazaki, T. (2021). Structure of a bacterial α-1,2-glucosidase defines mechanisms of hydrolysis and substrate specificity in GH65 family hydrolases. The Journal of biological chemistry, 297(6), 101366. https://doi.org/10.1016/j.jbc.2021.101366
Nakamura, Shuntaro, et al. "Structure of a bacterial α-1,2-glucosidase defines mechanisms of hydrolysis and substrate specificity in GH65 family hydrolases." The Journal of biological chemistry vol. 297,6 (2021): 101366. doi: https://doi.org/10.1016/j.jbc.2021.101366
Nakamura S, Nihira T, Kurata R, Nakai H, Funane K, Park EY, Miyazaki T. Structure of a bacterial α-1,2-glucosidase defines mechanisms of hydrolysis and substrate specificity in GH65 family hydrolases. J Biol Chem. 2021 Dec;297(6):101366. doi: 10.1016/j.jbc.2021.101366. Epub 2021 Oct 30. PMID: 34728215; PMCID: PMC8626586.
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Structure of a bacterial α-1,2-glucosidase defines mechanisms of hydrolysis and substrate specificity in GH65 family hydrolases.

The Journal of biological chemistry

Nakamura S, Nihira T, Kurata R, Nakai H, Funane K, Park EY, Miyazaki T.
PMID: 34728215
J Biol Chem. 2021 Oct 30;297(6):101366. doi: 10.1016/j.jbc.2021.101366. Epub 2021 Oct 30.

Glycoside hydrolase family 65 (GH65) comprises glycoside hydrolases (GHs) and glycoside phosphorylases (GPs) that act on α-glucosidic linkages in oligosaccharides. All previously reported bacterial GH65 enzymes are GPs, whereas all eukaryotic GH65 enzymes known are GHs. In addition, to...

Cite
Nakamura S, Nihira T, Kurata R, et al. Structure of a bacterial α-1,2-glucosidase defines mechanisms of hydrolysis and substrate specificity in GH65 family hydrolases. J Biol Chem. 2021;297(6):101366doi: 10.1016/j.jbc.2021.101366.
Nakamura, S., Nihira, T., Kurata, R., Nakai, H., Funane, K., Park, E. Y., & Miyazaki, T. (2021). Structure of a bacterial α-1,2-glucosidase defines mechanisms of hydrolysis and substrate specificity in GH65 family hydrolases. The Journal of biological chemistry, 297(6), 101366. https://doi.org/10.1016/j.jbc.2021.101366
Nakamura, Shuntaro, et al. "Structure of a bacterial α-1,2-glucosidase defines mechanisms of hydrolysis and substrate specificity in GH65 family hydrolases." The Journal of biological chemistry vol. 297,6 (2021): 101366. doi: https://doi.org/10.1016/j.jbc.2021.101366
Nakamura S, Nihira T, Kurata R, Nakai H, Funane K, Park EY, Miyazaki T. Structure of a bacterial α-1,2-glucosidase defines mechanisms of hydrolysis and substrate specificity in GH65 family hydrolases. J Biol Chem. 2021 Oct 30;297(6):101366. doi: 10.1016/j.jbc.2021.101366. Epub 2021 Oct 30. PMID: 34728215; PMCID: PMC8626586.
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Structure of a bacterial α-1,2-glucosidase defines mechanisms of hydrolysis and substrate specificity in GH65 family hydrolases.

The Journal of biological chemistry

Nakamura S, Nihira T, Kurata R, Nakai H, Funane K, Park EY, Miyazaki T.
PMID: 34728215
J Biol Chem. 2021 Oct 30;297(6):101366. doi: 10.1016/j.jbc.2021.101366. Epub 2021 Oct 30.

Glycoside hydrolase family 65 (GH65) comprises glycoside hydrolases (GHs) and glycoside phosphorylases (GPs) that act on α-glucosidic linkages in oligosaccharides. All previously reported bacterial GH65 enzymes are GPs, whereas all eukaryotic GH65 enzymes known are GHs. In addition, to...

Cite
Nakamura S, Nihira T, Kurata R, et al. Structure of a bacterial α-1,2-glucosidase defines mechanisms of hydrolysis and substrate specificity in GH65 family hydrolases. J Biol Chem. 2021;297(6):101366doi: 10.1016/j.jbc.2021.101366.
Nakamura, S., Nihira, T., Kurata, R., Nakai, H., Funane, K., Park, E. Y., & Miyazaki, T. (2021). Structure of a bacterial α-1,2-glucosidase defines mechanisms of hydrolysis and substrate specificity in GH65 family hydrolases. The Journal of biological chemistry, 297(6), 101366. https://doi.org/10.1016/j.jbc.2021.101366
Nakamura, Shuntaro, et al. "Structure of a bacterial α-1,2-glucosidase defines mechanisms of hydrolysis and substrate specificity in GH65 family hydrolases." The Journal of biological chemistry vol. 297,6 (2021): 101366. doi: https://doi.org/10.1016/j.jbc.2021.101366
Nakamura S, Nihira T, Kurata R, Nakai H, Funane K, Park EY, Miyazaki T. Structure of a bacterial α-1,2-glucosidase defines mechanisms of hydrolysis and substrate specificity in GH65 family hydrolases. J Biol Chem. 2021 Oct 30;297(6):101366. doi: 10.1016/j.jbc.2021.101366. Epub 2021 Oct 30. PMID: 34728215; PMCID: PMC8626586.
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Showing 1 to 12 of 57 entries