메뉴 건너뛰기




Volumn 50, Issue 8, 2011, Pages 934-944

Quercetin-iron chelates are transported via glucose transporters

Author keywords

Deferiprone; Desferrioxamine; Flavonoids; Free radicals; HaberWeissFenton reaction; Iron chelotherapy; Reactive oxygen species

Indexed keywords

3,6 DIHYDROXYFLAVONE; CATECHOL; CHRYSIN; CYTOCHALASIN B; DEFERIPRONE; DEFEROXAMINE; FERROUS ION; FLAVONE DERIVATIVE; FLAVONONE B; GLUCOSE TRANSPORTER 1; HYDROGEN PEROXIDE; HYDROXYL RADICAL; LUTEOLIN; PHLORETIN; QUERCETIN; RUTOSIDE; UNCLASSIFIED DRUG;

EID: 79952439249     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2011.01.005     Document Type: Article
Times cited : (72)

References (54)
  • 1
    • 0029888671 scopus 로고    scopus 로고
    • Effects of positive iron status at a cellular level
    • J.M. McCord Effects of positive iron status at a cellular level Nutr. Rev. 54 1996 85 88 (Pubitemid 26176136)
    • (1996) Nutrition Reviews , vol.54 , Issue.3 , pp. 85-88
    • McCord, J.M.1
  • 2
    • 0037108199 scopus 로고    scopus 로고
    • The labile iron pool: Characterization, measurement, and participation in cellular processes
    • O. Kakhlon, and Z.I. Cabantchik The labile iron pool: characterization, measurement, and participation in cellular processes Free Radic. Biol. Med. 33 2002 1037 1046
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 1037-1046
    • Kakhlon, O.1    Cabantchik, Z.I.2
  • 3
    • 0035874476 scopus 로고    scopus 로고
    • Subcellular distribution of chelatable iron: A laser scanning microscopic study in isolated hepatocytes and liver endothelial cells
    • DOI 10.1042/0264-6021:3560061
    • F. Petrat, H. de Groot, and U. Rauen Subcellular distribution of chelatable iron: a laser scanning microscopic study in isolated hepatocytes and liver endothelial cells Biochem. J. 356 2001 61 69 (Pubitemid 34275706)
    • (2001) Biochemical Journal , vol.356 , Issue.1 , pp. 61-69
    • Petrat, F.1    De Groot, H.2    Rauen, U.3
  • 4
    • 0001101920 scopus 로고
    • Chelation of ferrous sulphate solutions by desferrioxamine B
    • J.F. Goodwin, and C.F. Whitten Chelation of ferrous sulphate solutions by desferrioxamine B Nature 205 1965 281 283
    • (1965) Nature , vol.205 , pp. 281-283
    • Goodwin, J.F.1    Whitten, C.F.2
  • 5
    • 55149104161 scopus 로고    scopus 로고
    • Quercetin: Potentials in the prevention and therapy of disease
    • S.C. Bischoff Quercetin: potentials in the prevention and therapy of disease Curr. Opin. Clin. Nutr. Metab. Care 11 2008 733 740
    • (2008) Curr. Opin. Clin. Nutr. Metab. Care , vol.11 , pp. 733-740
    • Bischoff, S.C.1
  • 6
    • 0344875670 scopus 로고    scopus 로고
    • Human red blood cells as a natural flavonoid reservoir
    • DOI 10.1080/10715760310001615998
    • M. Fiorani, A. Accorsi, and O. Cantoni Human red blood cells as a natural flavonoid reservoir Free Radic. Res. 37 2003 1331 1338 (Pubitemid 37441716)
    • (2003) Free Radical Research , vol.37 , Issue.12 , pp. 1331-1338
    • Fiorani, M.1    Accorsi, A.2    Cantoni, O.3
  • 7
    • 33646836322 scopus 로고    scopus 로고
    • Docking studies show that D-glucose and quercetin slide through the transporter GLUT1
    • DOI 10.1074/jbc.M509422200
    • P. Cunningham, I. Afzal-Ahmed, and R.J. Naftalin Docking studies show that D-glucose and quercetin slide through the transporter GLUT1 J. Biol. Chem. 281 2006 5797 5803 (Pubitemid 43847679)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.9 , pp. 5797-5803
    • Cunningham, P.1    Afzal-Ahmed, I.2    Naftalin, R.J.3
  • 8
    • 15944419535 scopus 로고    scopus 로고
    • Myricetin, quercetin and catechin-gallate inhibit glucose uptake in isolated rat adipocytes
    • DOI 10.1042/BJ20040703
    • P. Strobel, C. Allard, T. Perez-Acle, R. Calderon, R. Aldunate, and F. Leighton Myricetin, quercetin and catechin-gallate inhibit glucose uptake in isolated rat adipocytes Biochem. J. 386 2005 471 478 (Pubitemid 40445871)
    • (2005) Biochemical Journal , vol.386 , Issue.3 , pp. 471-478
    • Strobel, P.1    Allard, C.2    Perez-Acle, T.3    Calderon, R.4    Aldunate, R.5    Leighton, F.6
  • 9
    • 0029737292 scopus 로고    scopus 로고
    • Differential targeting of facilitative glucose transporters in polarized epithelial cells
    • W.S. Pascoe, K. Inukai, Y. Oka, J.W. Slot, and D.E. James Differential targeting of facilitative glucose transporters in polarized epithelial cells Am. J. Physiol. Cell Physiol. 271 1996 C547 C554
    • (1996) Am. J. Physiol. Cell Physiol. , vol.271
    • Pascoe, W.S.1    Inukai, K.2    Oka, Y.3    Slot, J.W.4    James, D.E.5
  • 10
    • 0027291905 scopus 로고
    • Intake of potentially anticarcinogenic flavonoids and their determinants in adults in The Netherlands
    • M. Hertog, P. Hollman, M. Katan, and D. Kromhout Intake of potentially anticarcinogenic flavonoids and their determinants in adults in The Netherlands Nutr. Cancer 20 1993 21 29 (Pubitemid 23225364)
    • (1993) Nutrition and Cancer , vol.20 , Issue.1 , pp. 21-29
    • Hertog, M.G.L.1    Hollman, P.C.H.2    Katan, M.B.3    Kromhout, D.4
  • 11
    • 0036915813 scopus 로고    scopus 로고
    • 4-induced hepatotoxicity in rodents
    • DOI 10.1016/S0367-326X(02)00217-4, PII S0367326X02002174
    • 4-induced hepatotoxicity in rodents Fitoterapia 73 2002 557 563 (Pubitemid 35477750)
    • (2002) Fitoterapia , vol.73 , Issue.7-8 , pp. 557-563
    • Janbaz, K.H.1    Saeed, S.A.2    Gilani, A.H.3
  • 12
    • 32544446910 scopus 로고    scopus 로고
    • Transport kinetics of iron chelators and their chelates in Caco-2 cells
    • DOI 10.1007/s11095-005-9258-5
    • X.P. Huang, M. Spino, and J.J. Thiessen Transport kinetics of iron chelators and their chelates in Caco-2 cells Pharm. Res. 23 2006 280 290 (Pubitemid 43237859)
    • (2006) Pharmaceutical Research , vol.23 , Issue.2 , pp. 280-290
    • Huang, X.-P.1    Spino, M.2    Thiessen, J.J.3
  • 13
    • 44449159838 scopus 로고    scopus 로고
    • Dcytb (Cybrd1) functions as both a ferric and a cupric reductase in vitro
    • S. Wyman, R.J. Simpson, A.T. McKie, and P.A. Sharp Dcytb (Cybrd1) functions as both a ferric and a cupric reductase in vitro FEBS Lett. 582 2008 1901 1906
    • (2008) FEBS Lett. , vol.582 , pp. 1901-1906
    • Wyman, S.1    Simpson, R.J.2    McKie, A.T.3    Sharp, P.A.4
  • 14
    • 0033564218 scopus 로고    scopus 로고
    • Analysis of reactive oxygen species generated by neutrophils using a chemiluminescence probe L-012
    • DOI 10.1006/abio.1999.4107
    • I. Imada, E.F. Sato, M. Miyamoto, Y. Ichimori, Y. Minamiyama, R. Konaka, and M. Inoue Analysis of reactive oxygen species generated by neutrophils using a chemiluminescence probe L-012 Anal. Biochem. 271 1999 53 58 (Pubitemid 29287850)
    • (1999) Analytical Biochemistry , vol.271 , Issue.1 , pp. 53-58
    • Imada, I.1    Sato, E.F.2    Miyamoto, M.3    Ichimori, Y.4    Minamiyama, Y.5    Konaka, R.6    Inoue, M.7
  • 15
    • 0035450560 scopus 로고    scopus 로고
    • Direct measurement of ferrous ion transport across membranes using a sensitive fluorometric assay
    • DOI 10.1006/abio.2001.5209
    • R. Shingles, M. North, and R.E. McCarty Direct measurement of ferrous ion transport across membranes using a sensitive fluorometric assay Anal. Biochem. 296 2001 106 113 (Pubitemid 32808401)
    • (2001) Analytical Biochemistry , vol.296 , Issue.1 , pp. 106-113
    • Shingles, R.1    North, M.2    McCarty, R.E.3
  • 17
  • 18
    • 0037064468 scopus 로고    scopus 로고
    • Iron and copper chelation by flavonoids: an electrospray mass spectrometry study
    • DOI 10.1016/S0162-0134(02)00511-1, PII S0162013402005111
    • M.T. Fernandez, M.L. Mira, M.H. Florencio, and K.R. Jennings Iron and copper chelation by flavonoids: an electrospray mass spectrometry study J. Inorg. Biochem. 92 2002 105 111 (Pubitemid 35190339)
    • (2002) Journal of Inorganic Biochemistry , vol.92 , Issue.2 , pp. 105-111
    • Fernandez, M.T.1    Mira, M.L.2    Florencio, M.H.3    Jennings, K.R.4
  • 20
    • 11244303574 scopus 로고    scopus 로고
    • Interaction of flavonoids with bovine serum albumin: A fluorescence quenching study
    • DOI 10.1021/jf048693g
    • A. Papadopoulou, R.J. Green, and R.A. Frazier Interaction of flavonoids with bovine serum albumin: a fluorescence quenching study J. Agric. Food Chem. 53 2005 158 163 (Pubitemid 40066484)
    • (2005) Journal of Agricultural and Food Chemistry , vol.53 , Issue.1 , pp. 158-163
    • Papadopoulou, A.1    Green, R.J.2    Frazier, R.A.3
  • 21
    • 0030726667 scopus 로고    scopus 로고
    • Iron-binding antioxidant potential of plasma albumin
    • A. Loban, R. Kime, and H. Powers Iron-binding antioxidant potential of plasma albumin Clin. Sci. (London) 93 1997 445 451 (Pubitemid 27489940)
    • (1997) Clinical Science , vol.93 , Issue.5 , pp. 445-451
    • Loban, A.1    Kime, R.2    Powers, H.3
  • 23
    • 0034054257 scopus 로고    scopus 로고
    • Intracellular accumulation of ascorbic acid is inhibited by flavonoids via blocking of dehydroascorbic acid and ascorbic acid uptakes in HL-60, U937 and Jurkat cells
    • J.B. Park, and M. Levine Intracellular accumulation of ascorbic acid is inhibited by flavonoids via blocking of dehydroascorbic acid and ascorbic acid uptakes in HL-60, U937 and Jurkat cells J. Nutr. 130 2000 1297 1302 (Pubitemid 30233283)
    • (2000) Journal of Nutrition , vol.130 , Issue.5 , pp. 1297-1302
    • Park, J.B.1    Levine, M.2
  • 24
    • 11844253806 scopus 로고    scopus 로고
    • Flavonoid-serum albumin complexation: Determination of binding constants and binding sites by fluorescence spectroscopy
    • DOI 10.1016/j.bbagen.2004.10.013, PII S0304416504002843
    • C. Dufour, and O. Dangles Flavonoid-serum albumin complexation: determination of binding constants and binding sites by fluorescence spectroscopy Biochim. Biophys. Acta 1721 2005 164 173 (Pubitemid 40093524)
    • (2005) Biochimica et Biophysica Acta - General Subjects , vol.1721 , Issue.1-3 , pp. 164-173
    • Dufour, C.1    Dangles, O.2
  • 25
    • 0002383467 scopus 로고
    • Sugar transport in the red blood cell: Structure-activity relationships in substrates and antagonists
    • P. LeFevre Sugar transport in the red blood cell: structure-activity relationships in substrates and antagonists Pharmacol. Rev. 13 1961 39 70
    • (1961) Pharmacol. Rev. , vol.13 , pp. 39-70
    • Lefevre, P.1
  • 26
    • 0018199174 scopus 로고
    • Asymmetry of the hexose transfer system in human erythrocytes. Comparison of the effects of cytochalasin B, phloretin and maltose as competitive inhibitors
    • D. Basketter, and W. Widdas Asymmetry of the hexose transfer system in human erythrocytes: comparison of the effects of cytochalasin B, phloretin and maltose as competitive inhibitors J. Physiol. 278 1978 389 401 (Pubitemid 8342390)
    • (1978) Journal of Physiology , vol.278 , pp. 389-401
    • Basketter, D.A.1    Widdas, W.F.2
  • 27
    • 12344321851 scopus 로고    scopus 로고
    • Predicting the three-dimensional structure of the human facilitative glucose transporter Glut1 by a novel evolutionary homology strategy: Insights on the molecular mechanism of substrate migration, and binding for glucose and inhibitory molecules
    • DOI 10.1529/biophysj.104.047886
    • A. Salas-Burgos, P. Iserovich, F. Zuniga, J. Vera, and J. Fischbarg Predicting the three-dimensional structure of the human facilitative glucose transporter glut1 by a novel evolutionary homology strategy: insights on the molecular mechanism of substrate migration, and binding sites for glucose and inhibitory molecules Biophys. J. 87 2004 2990 2999 (Pubitemid 40468559)
    • (2004) Biophysical Journal , vol.87 , Issue.5 , pp. 2990-2999
    • Salas-Burgos, A.1    Iserovich, P.2    Zuniga, F.3    Vera, J.C.4    Fischbarg, J.5
  • 28
    • 0035951093 scopus 로고    scopus 로고
    • The red blood cell glucose transporter presents multiple, nucleotide-sensitive sugar exit sites
    • DOI 10.1021/bi015586w
    • E. Cloherty, K. Levine, and A. Carruthers The red blood cell glucose transporter presents multiple, nucleotide-sensitive sugar exit sites Biochemistry 40 2001 15549 15561 (Pubitemid 34015182)
    • (2001) Biochemistry , vol.40 , Issue.51 , pp. 15549-15561
    • Cloherty, E.K.1    Levine, K.B.2    Carruthers, A.3
  • 29
    • 0036532552 scopus 로고    scopus 로고
    • Iron release, oxidative stress and erythrocyte ageing
    • DOI 10.1016/S0891-5849(02)00759-1, PII S0891584902007591
    • M. Comporti, C. Signorini, G. Buonocore, and L. Ciccoli Iron release, oxidative stress and erythrocyte ageing Free Radic. Biol. Med. 32 2002 568 576 (Pubitemid 34241489)
    • (2002) Free Radical Biology and Medicine , vol.32 , Issue.7 , pp. 568-576
    • Comporti, M.1    Signorini, C.2    Buonocore, G.3    Ciccoli, L.4
  • 31
    • 0032951707 scopus 로고    scopus 로고
    • Determination of the chelatable iron pool of isolated rat hepatocytes by digital fluorescence microscopy using the fluorescent probe, phen green SK
    • F. Petrat, U. Rauen, and H. de Groot Determination of the chelatable iron pool of isolated rat hepatocytes by digital fluorescence microscopy using the fluorescent probe, Phen Green SK Hepatology 29 1999 1171 1179 (Pubitemid 29168752)
    • (1999) Hepatology , vol.29 , Issue.4 , pp. 1171-1179
    • Petrat, F.1    Rauen, U.2    De Groot, H.3
  • 33
    • 73149092511 scopus 로고    scopus 로고
    • Optimizing iron chelation strategies in beta-thalassaemia major
    • J.B. Porter Optimizing iron chelation strategies in beta-thalassaemia major Blood Rev. 23 Suppl. 1 2009 S3 S7
    • (2009) Blood Rev. , vol.23 , Issue.SUPPL. 1
    • Porter, J.B.1
  • 34
    • 0034783438 scopus 로고    scopus 로고
    • Chelation therapy in β-thalassemia: An optimistic update
    • P.J. Giardina, and R.W. Grady Chelation therapy in beta-thalassemia: an optimistic update Semin. Hematol. 38 2001 360 366 (Pubitemid 32995605)
    • (2001) Seminars in Hematology , vol.38 , Issue.4 , pp. 360-366
    • Giardina, P.J.1    Grady, R.W.2
  • 36
    • 42449122220 scopus 로고    scopus 로고
    • SVCT1 and SVCT2: Key proteins for vitamin C uptake
    • DOI 10.1007/s00726-007-0555-7
    • I. Savini, A. Rossi, C. Pierro, L. Avigliano, and M. Catani SVCT1 and SVCT2: key proteins for vitamin C uptake Amino Acids 34 2008 347 355 (Pubitemid 351569766)
    • (2008) Amino Acids , vol.34 , Issue.3 , pp. 347-355
    • Savini, I.1    Rossi, A.2    Pierro, C.3    Avigliano, L.4    Catani, M.V.5
  • 37
    • 0142153877 scopus 로고    scopus 로고
    • Interactions of androgens, green tea catechins and the antiandrogen flutamide with the external glucose-binding site of the human erythrocyte glucose transporter GLUT1
    • DOI 10.1038/sj.bjp.0705460
    • R. Naftalin, I. Afzal, P. Cunningham, M. Halai, C. Ross, N. Salleh, and S. Milligan Interactions of androgens, green tea catechins and the antiandrogen flutamide with the external glucose-binding site of the human erythrocyte glucose transporter GLUT1 Br. J. Pharmacol. 140 2003 487 499 (Pubitemid 37330493)
    • (2003) British Journal of Pharmacology , vol.140 , Issue.3 , pp. 487-499
    • Naftalin, R.J.1    Afzal, I.2    Cunningham, P.3    Halai, M.4    Ross, C.5    Salleh, N.6    Milligan, S.R.7
  • 38
    • 3042745488 scopus 로고    scopus 로고
    • Piracetam and TRH analogues antagonise inhibition by barbiturates, diazepam, melatonin and galanin of human erythrocyte D-glucose transport
    • DOI 10.1038/sj.bjp.0705798
    • R. Naftalin, P. Cunningham, and I. Afzal-Ahmed Piracetam and TRH analogues antagonise inhibition by barbiturates, diazepam, melatonin and galanin of human erythrocyte D-glucose transport Br. J. Pharmacol. 142 2004 594 608 (Pubitemid 38869874)
    • (2004) British Journal of Pharmacology , vol.142 , Issue.3 , pp. 594-608
    • Naftalin, R.J.1    Cunningham, P.2    Afzal-Ahmed, I.3
  • 39
    • 58349102278 scopus 로고    scopus 로고
    • The effects of midazolam on the acquisition and expression of fructose- and maltodextrin-based flavour preferences
    • D. Dwyer The effects of midazolam on the acquisition and expression of fructose- and maltodextrin-based flavour preferences Pharmacol. Biochem. Behav. 91 2009 503 510
    • (2009) Pharmacol. Biochem. Behav. , vol.91 , pp. 503-510
    • Dwyer, D.1
  • 40
    • 34547135694 scopus 로고    scopus 로고
    • +/glucose transporter when expressed in Xenopus laevis oocytes, but effectively inhibit electrogenic glucose uptake
    • DOI 10.1124/jpet.107.124040
    • +/glucose transporter when expressed in Xenopus laevis oocytes, but effectively inhibit electrogenic glucose uptake J. Pharmacol. Exp. Ther. 322 2007 829 835 (Pubitemid 47105799)
    • (2007) Journal of Pharmacology and Experimental Therapeutics , vol.322 , Issue.2 , pp. 829-835
    • Kottra, G.1    Daniel, H.2
  • 41
    • 33846469955 scopus 로고    scopus 로고
    • Flavonoids modulate monocarboxylate transporter-1-mediated transport of γ-hydroxybutyrate in vitro and in vivo
    • DOI 10.1124/dmd.106.012369
    • Q. Wang, and M. Morris Flavonoids modulate monocarboxylate transporter-1-mediated transport of gamma-hydroxybutyrate in vitro and in vivo Drug Metab. Dispos. 35 2007 201 208 (Pubitemid 46151668)
    • (2007) Drug Metabolism and Disposition , vol.35 , Issue.2 , pp. 201-208
    • Wang, Q.1    Morris, M.E.2
  • 42
    • 22144455747 scopus 로고    scopus 로고
    • Interactions of mefloquine with ABC proteins, MRP1 (ABCC1) and MRP4 (ABCC4) that are present in human red cell membranes
    • DOI 10.1016/j.bcp.2005.05.022, PII S0006295205003576
    • C.P. Wu, A. Klokouzas, S.B. Hladky, S.V. Ambudkar, and M.A. Barrand Interactions of mefloquine with ABC proteins, MRP1 (ABCC1) and MRP4 (ABCC4) that are present in human red cell membranes Biochem. Pharmacol. 70 2005 500 510 (Pubitemid 40978539)
    • (2005) Biochemical Pharmacology , vol.70 , Issue.4 , pp. 500-510
    • Wu, C.-P.1    Klokouzas, A.2    Hladky, S.B.3    Ambudkar, S.V.4    Barrand, M.A.5
  • 43
    • 73849174442 scopus 로고
    • Variations of the parameters of glucose transfer across the human erythrocyte membrane in the presence of inhibitors of transfer
    • A. Sen, and W. Widdas Variations of the parameters of glucose transfer across the human erythrocyte membrane in the presence of inhibitors of transfer J. Physiol. 160 1962 404 416
    • (1962) J. Physiol. , vol.160 , pp. 404-416
    • Sen, A.1    Widdas, W.2
  • 44
    • 0035951696 scopus 로고    scopus 로고
    • Interaction of quercetin glucosides with the intestinal sodium/glucose co-transporter (SGLT-1)
    • DOI 10.1016/S0304-3835(00)00645-5, PII S0304383500006455
    • P. Ader, M. Blöck, S. Pietzsch, and S. Wolffram Interaction of quercetin glucosides with the intestinal sodium/glucose co-transporter (SGLT-1) Cancer Lett. 162 2001 175 180 (Pubitemid 32056286)
    • (2001) Cancer Letters , vol.162 , Issue.2 , pp. 175-180
    • Ader, P.1    Block, M.2    Pietzsch, S.3    Wolffram, S.4
  • 45
    • 0009797111 scopus 로고    scopus 로고
    • Iron chelation: Combined therapy could be a better approach
    • R.W. Grady, V.A. Berdoukas, and P.J. Giardina Iron chelation: combined therapy could be a better approach Blood 92 1998 3046
    • (1998) Blood , vol.92 , pp. 3046
    • Grady, R.W.1    Berdoukas, V.A.2    Giardina, P.J.3
  • 46
    • 0038663082 scopus 로고    scopus 로고
    • Emerging understanding of the advantage of small molecules such as hydroxypyridinones in the treatment of iron overload
    • DOI 10.2174/0929867033457629
    • R.C. Hider, and Z.D. Liu Emerging understanding of the advantage of small molecules such as hydroxypyridinones in the treatment of iron overload Curr. Med. Chem. 10 2003 1051 1064 (Pubitemid 36582248)
    • (2003) Current Medicinal Chemistry , vol.10 , Issue.12 , pp. 1051-1064
    • Hider, R.C.1    Liu, Z.D.2
  • 48
    • 0030781313 scopus 로고    scopus 로고
    • Protection against oxidative damage of erythrocyte membrane by the flavonoid quercetin and its relation to iron chelating activity
    • DOI 10.1016/S0014-5793(97)01182-4, PII S0014579397011824
    • M. Ferrali, C. Signorini, B. Caciotti, L. Sugherini, L. Ciccoli, D. Giachetti, and M. Comporti Protection against oxidative damage of erythrocyte membrane by the flavonoid quercetin and its relation to iron chelating activity FEBS Lett. 416 1997 123 129 (Pubitemid 27462770)
    • (1997) FEBS Letters , vol.416 , Issue.2 , pp. 123-129
    • Ferrali, M.1    Signorini, C.2    Caciotti, B.3    Sugherini, L.4    Ciccoli, L.5    Giachetti, D.6    Comporti, M.7
  • 49
    • 0008006984 scopus 로고
    • Enzymic glycosylation of quercetin to rutin
    • G.A. Barber Enzymic glycosylation of quercetin to rutin Biochemistry 1 1962 463 468
    • (1962) Biochemistry , vol.1 , pp. 463-468
    • Barber, G.A.1
  • 50
    • 1542605222 scopus 로고    scopus 로고
    • Flavonoids: Antioxidants or signalling molecules?
    • DOI 10.1016/j.freeradbiomed.2004.01.001, PII S0891584904000334
    • R.J. Williams, J.P. Spencer, and C. Rice-Evans Flavonoids: antioxidants or signalling molecules? Free Radic. Biol. Med. 36 2004 838 849 (Pubitemid 38352901)
    • (2004) Free Radical Biology and Medicine , vol.36 , Issue.7 , pp. 838-849
    • Williams, R.J.1    Spencer, J.P.E.2    Rice-Evans, C.3
  • 51
    • 77956512504 scopus 로고    scopus 로고
    • Mitochondrial GLUT10 facilitates dehydroascorbic acid import and protects cells against oxidative stress: Mechanistic insight into arterial tortuosity syndrome
    • Y. Lee, H. Huang, C. Chang, C. Cheng, and Y. Chen Mitochondrial GLUT10 facilitates dehydroascorbic acid import and protects cells against oxidative stress: mechanistic insight into arterial tortuosity syndrome Hum. Mol. Genet. 19 2010 3721 3733
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 3721-3733
    • Lee, Y.1    Huang, H.2    Chang, C.3    Cheng, C.4    Chen, Y.5
  • 52
    • 33746510896 scopus 로고    scopus 로고
    • Bioavailability of quercetin from berries and the diet
    • DOI 10.1207/s15327914nc5401-3
    • I. Erlund, R. Freese, J. Marniemi, P. Hakala, and G. Alfthan Bioavailability of quercetin from berries and the diet Nutr. Cancer 54 2006 13 17 (Pubitemid 44141332)
    • (2006) Nutrition and Cancer , vol.54 , Issue.1 , pp. 13-17
    • Erlund, I.1    Freese, R.2    Marniemi, J.3    Hakala, P.4    Alfthan, G.5
  • 54
    • 34248525277 scopus 로고    scopus 로고
    • Preeclampsia inactivates glucose-6-phosphate dehydrogenase and impairs the redox status of erythrocytes and fetal endothelial cells
    • DOI 10.1016/j.freeradbiomed.2007.02.032, PII S0891584907001852
    • I. Afzal-Ahmed, G. Mann, A. Shennan, L. Poston, and R. Naftalin Preeclampsia inactivates glucose-6-phosphate dehydrogenase and impairs the redox status of erythrocytes and fetal endothelial cells Free Radic. Biol. Med. 42 2007 1781 1790 (Pubitemid 46754755)
    • (2007) Free Radical Biology and Medicine , vol.42 , Issue.12 , pp. 1781-1790
    • Afzal-Ahmed, I.1    Mann, G.E.2    Shennan, A.H.3    Poston, L.4    Naftalin, R.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.