-
1
-
-
8944262299
-
-
note
-
Abbreviations: acyclo-TMP, 1-[(2-phosphoethoxy)methyl]thymine; AZT, 3′-azido-3′-deoxythymidine; AZT phosphonate, 3′-azido-3′-deoxythymidine 5′-methylenephosphonate; BVdU, 5-(bromovinyl)-2′-deoxyuridine; EDTA, ethylenediaminetetraacetic acid, Na salt; Gal, galactose; Glc, glucose; GalNAc, N-acetylgalactosamine; GlcNAc, N-acetylglucosamine; NeuAc, N-acetyl-neuraminic acid; ER, endoplasmic reticulum.
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-
-
-
2
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0021740347
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Mechanisms of Glycosylation and Sulfation in the Golgi Apparatus: Evidence for Nucleotide Sugar/Nucleoside Monophosphate and Nucleotide Sulfate/ Nucleoside Monophosphate Antiports in the Golgi Apparatus Membrane
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Capasso, J. M.; Hirschberg, C. B. Mechanisms of Glycosylation and Sulfation in the Golgi Apparatus: Evidence for Nucleotide Sugar/Nucleoside Monophosphate and Nucleotide Sulfate/ Nucleoside Monophosphate Antiports in the Golgi Apparatus Membrane. Proc. Natl. Acad. Sci. U.S.A. 1984,81, 7051-7055.
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Capasso, J.M.1
Hirschberg, C.B.2
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3
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0023068345
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Topography of Glycosylation in the Rough Endoplasmic Reticulum and Golgi Apparatus
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Hirschberg, C. B.; Snider, M. D. Topography of Glycosylation in the Rough Endoplasmic Reticulum and Golgi Apparatus. Annu. Rev. Biochem. 1987, 56, 63-87.
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0004820396
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5
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0021709384
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Effect of Nucleotides on Translocation of Sugar Nucleotides and Adenosine 3′-Phosphate 5′-Phosphosulfate into Golgi Apparatus Vesicles
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Capasso, J. M.; Hirschberg, C. B. Effect of Nucleotides on Translocation of Sugar Nucleotides and Adenosine 3′-Phosphate 5′-Phosphosulfate into Golgi Apparatus Vesicles. Biochim. Biophys. Acta 1984, 777, 133-139.
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0023951483
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Regulation of Human Thymidine Kinase during the Cell Cycle
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0023868605
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Balzarini, J.; Pauwels, R.; Baba, M.; Herdewijn, P.; DeClercq, E.; Broder, S.; Jones, D. G. The In Vitro and In Vivo Antiretrovirus Activity, and Intracellular Metabolism of 3′-Azido-2′,3′-dideoxythymidine and 2′,3′-Dideoxycytidine Are Highly Dependent on the Cell Species. Biochem. Pharmacol. 1988,37, 897-903.
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Jones, D.G.7
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8
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0022996630
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Phosphorylation of 3′-Azido-3′-Deoxythymidine and Selective Interaction of the 5′-Triphosphate with HIV Reverse Transcriptase
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Furman, P. A.; Fyfe, J. A.; St. Clair, M. H.; Weinhold, K.; Rideout, J. L.; Freeman, G. A.; Nusinoff-Lehrman, S.; Bolognesi, D. P.; Broder, S.; Mitsuya, H.; Barry, D. W. Phosphorylation of 3′-Azido-3′-Deoxythymidine and Selective Interaction of the 5′-Triphosphate with HIV Reverse Transcriptase. Proc. Natl. Acad. Sci. U.S.A. 1986, 83, 8333-8337.
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Barry, D.W.11
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9
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0029157098
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3′-Azidothymidine (Zidovudine) Inhibits Glycosylation and Dramatically Alters Glycosphingolipid Synthesis in Whole Cells at Clinically Relevant Concentrations
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Van, J.-P.; Ilsley, D. D.; Frohlick, C.; Steet, R.; Hall, E. T.; Kuchta, R. D.; Melançon, P. 3′-Azidothymidine (Zidovudine) Inhibits Glycosylation and Dramatically Alters Glycosphingolipid Synthesis in Whole Cells at Clinically Relevant Concentrations. J. Biol. Chem. 1995, 270, 22836-22841.
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0023718636
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Inhibition of Terminal N- and O-glycosylation Specific for Herpesvirus-Infected Cells: Mechanism of an Inhibitor of Sugar Nucleotide Transport across Golgi Membranes
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Olofsson, S.; Milla, M.; Hirschberg, C.; DeClercq, E.; Datema, R. Inhibition of Terminal N- and O-glycosylation Specific for Herpesvirus-Infected Cells: Mechanism of an Inhibitor of Sugar Nucleotide Transport across Golgi Membranes. Virology 1988, 166, 440-450.
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11
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0027356711
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5-Propyl-2-deoxyuridine Induced Interference with Glycosylation in Herpes Simplex Virus Infected Cells
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Olofsson, S.; Sjoblom, I.; Hellstrand, K.; Shugar, D.; Clairmont, C.; Hirschberg, H. 5-Propyl-2-deoxyuridine Induced Interference with Glycosylation in Herpes Simplex Virus Infected Cells. Arch. Virol. 1993, 128, 241-256.
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12
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8944223609
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note
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The extent of accumulation varied among different preparations of Golgi membranes. This variability likely reflects the presence of differing amounts of membranes derived from other organelles in the Golgi-enriched membrane fraction.
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13
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0024596802
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Reconstitution of Golgi Vesicle CMP-sialic Acid and Adenosine 3′-Phosphate 5′-Phosphosulfate Transport into Proteoliposomes
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Milla, M. E.; Hirschberg, C. B. Reconstitution of Golgi Vesicle CMP-sialic Acid and Adenosine 3′-Phosphate 5′-Phosphosulfate Transport into Proteoliposomes. Proc. Natl. Acad. Sci. U.S.A. 1989,86, 1786-1790.
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0025134183
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UDP-GlcNAc Transport across the Golgi Membrane: Electroneutral Exchange for Dianionic UMP
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0002548426
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Saenger, W. In Principles of Nucleic Acid Structure; Cantor, C. R., Eds.; Springer-Verlag: New York, 1984; pp 51-104.
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Saenger, W.1
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0017196304
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Conformation in Aqueous Medium of the Neutral, Protonated and Anionic Forms of 9-β-D-Arabinofuranosyladenine
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Remin, M.; Darzynkiewicz, E.; Ekiel, I.; Shugar, D. Conformation in Aqueous Medium of the Neutral, Protonated and Anionic Forms of 9-β-D-Arabinofuranosyladenine. Biochim. Biophys. Acta 1976, 435, 405-416.
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19
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8944238057
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note
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-1 membranes was only 3 min. Thus, the results from these previous studies are likely due to the UMP released during hydrolysis of UDP.
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20
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0028332852
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3′-Azido-3′-deoxythymidine Potently Inhibits Protein Glycosylation
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Hall, E. T.; Yan, J.-P.; Melançon, P.; Kuchta, R. D. 3′-Azido-3′-deoxythymidine Potently Inhibits Protein Glycosylation. J. Biol. Chem. 1994, 269, 14355-14358.
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0021702358
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Translocation across Golgi Vesicle Membranes: A CHO Glycosylation Mutant Deficient in CMP-Sialic Acid Transport
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Deutscher, S. L.; Nuwayhid, N.; Stanbley, P.; Griles, E. I. B.; Hirschberg, C. B. Translocation across Golgi Vesicle Membranes: A CHO Glycosylation Mutant Deficient in CMP-Sialic Acid Transport. Cell 1984, 39, 295-299.
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8944247368
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D values for UDP-GlcNAc are similar
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D values for UDP-GlcNAc are similar.
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24
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Isolation of Wheat Germ Agglutinin-resistant Clones of Chinese Hamster Ovary Cells Deficient in Membrane Sialic Acid and Galactose
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