메뉴 건너뛰기




Volumn 67, Issue , 2014, Pages 377-386

Inborn defects in the antioxidant systems of human red blood cells

Author keywords

Erythrocytes; Favism; Free radicals; G6PD deficiency; Glutathione; Hemolytic anemia; Methemoglobin; Oxidative stress; Pentose phosphate pathway; Red blood cells; Sickle cell trait; Thalassemia

Indexed keywords

ANTIOXIDANT; CATALASE; CYTOCHROME B5 REDUCTASE; GLUTATHIONE; HEMOGLOBIN; IRON; METHEMOGLOBIN; METHEMOGLOBIN REDUCTASE; PENTOSE; PEROXIREDOXIN; PHOSPHATE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SUPEROXIDE DISMUTASE; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; HEME; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 84891586833     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2013.11.022     Document Type: Review
Times cited : (100)

References (155)
  • 1
    • 0015442295 scopus 로고
    • Red cell metabolism. A. Defects not causing hemolytic disease. B. Environmental modification
    • E. Beutler Red cell metabolism. A. Defects not causing hemolytic disease. B. Environmental modification Biochimie 54 1972 759 764
    • (1972) Biochimie , vol.54 , pp. 759-764
    • Beutler, E.1
  • 3
    • 77950890099 scopus 로고    scopus 로고
    • Protective effect of resveratrol on formation of membrane protein carbonyls and lipid peroxidation in erythrocytes subjected to oxidative stress
    • K.B. Pandey, and S.I. Rizvi Protective effect of resveratrol on formation of membrane protein carbonyls and lipid peroxidation in erythrocytes subjected to oxidative stress Appl. Physiol. Nutr. Metab. 34 2009 1093 1097
    • (2009) Appl. Physiol. Nutr. Metab. , vol.34 , pp. 1093-1097
    • Pandey, K.B.1    Rizvi, S.I.2
  • 4
    • 33645099414 scopus 로고    scopus 로고
    • Age-associated analysis of oxidative stress parameters in human plasma and erythrocytes
    • L. Gil, W. Siems, B. Mazurek, J. Gross, P. Schroeder, and P. Voss et al. Age-associated analysis of oxidative stress parameters in human plasma and erythrocytes Free Radic. Res. 40 2006 495 505
    • (2006) Free Radic. Res. , vol.40 , pp. 495-505
    • Gil, L.1    Siems, W.2    Mazurek, B.3    Gross, J.4    Schroeder, P.5    Voss, P.6
  • 5
    • 0037834629 scopus 로고    scopus 로고
    • Evidence that peroxiredoxins are novel members of the thioredoxin fold superfamily
    • E. Schroder, and C.P. Ponting Evidence that peroxiredoxins are novel members of the thioredoxin fold superfamily Protein Sci. 7 1998 2465 2468 (Pubitemid 28506964)
    • (1998) Protein Science , vol.7 , Issue.11 , pp. 2465-2468
    • Schroder, E.1    Ponting, C.P.2
  • 6
    • 74149084415 scopus 로고    scopus 로고
    • The effects of disruption of genes for peroxiredoxin-2, glutathione peroxidase-1, and catalase on erythrocyte oxidative metabolism
    • R.M. Johnson, Y.S. Ho, D.Y. Yu, F.A. Kuypers, Y. Ravindranath, and G.W. Goyette The effects of disruption of genes for peroxiredoxin-2, glutathione peroxidase-1, and catalase on erythrocyte oxidative metabolism Free Radic. Biol. Med. 48 2010 519 525
    • (2010) Free Radic. Biol. Med. , vol.48 , pp. 519-525
    • Johnson, R.M.1    Ho, Y.S.2    Yu, D.Y.3    Kuypers, F.A.4    Ravindranath, Y.5    Goyette, G.W.6
  • 7
    • 0014691273 scopus 로고
    • The utility of superoxide dismutase in studying free radical reactions. I. Radicals generated by the interaction of sulfite, dimethyl sulfoxide, and oxygen
    • J.M. McCord, and I. Fridovich The utility of superoxide dismutase in studying free radical reactions. I. Radicals generated by the interaction of sulfite, dimethyl sulfoxide, and oxygen J. Biol. Chem. 244 1969 6056 6063
    • (1969) J. Biol. Chem. , vol.244 , pp. 6056-6063
    • McCord, J.M.1    Fridovich, I.2
  • 8
    • 0023205825 scopus 로고
    • Lipid peroxidation in erythrocytes
    • DOI 10.1016/0009-3084(87)90068-5
    • M.R. Clemens, and H.D. Waller Lipid peroxidation in erythrocytes Chem. Phys. Lipids 45 1987 251 268 (Pubitemid 17152337)
    • (1987) Chemistry and Physics of Lipids , vol.45 , Issue.2-4 , pp. 251-268
    • Clemens, M.R.1    Waller, H.D.2
  • 9
    • 0003159170 scopus 로고    scopus 로고
    • Ascorbate function and metabolism in the human erythrocyte
    • J.M. May Ascorbate function and metabolism in the human erythrocyte Front. Biosci. 3 1998 d1 10
    • (1998) Front. Biosci. , vol.3 , pp. 1-10
    • May, J.M.1
  • 11
    • 40849102818 scopus 로고    scopus 로고
    • Erythrocyte Glut1 Triggers Dehydroascorbic Acid Uptake in Mammals Unable to Synthesize Vitamin C
    • DOI 10.1016/j.cell.2008.01.042, PII S0092867408002043
    • A. Montel-Hagen, S. Kinet, N. Manel, C. Mongellaz, R. Prohaska, and J.L. Battini et al. Erythrocyte Glut1 triggers dehydroascorbic acid uptake in mammals unable to synthesize vitamin C Cell 132 2008 1039 1048 (Pubitemid 351391954)
    • (2008) Cell , vol.132 , Issue.6 , pp. 1039-1048
    • Montel-Hagen, A.1    Kinet, S.2    Manel, N.3    Mongellaz, C.4    Prohaska, R.5    Battini, J.-L.6    Delaunay, J.7    Sitbon, M.8    Taylor, N.9
  • 12
    • 84891608030 scopus 로고
    • The ratios of iron to oxygen, iron to colour and oxygen to colour in the blood of men and women
    • Q.H. Gibson, and D.C. Harrison The ratios of iron to oxygen, iron to colour and oxygen to colour in the blood of men and women J. Physiol. 105 1946 1
    • (1946) J. Physiol. , vol.105 , pp. 1
    • Gibson, Q.H.1    Harrison, D.C.2
  • 13
    • 42049097088 scopus 로고    scopus 로고
    • 5 reductase deficiency
    • DOI 10.1111/j.1365-2141.2008.07017.x
    • M.J. Percy, and T.R. Lappin Recessive congenital methaemoglobinaemia: cytochrome b(5) reductase deficiency Br. J. Haematol. 141 2008 298 308 (Pubitemid 351521146)
    • (2008) British Journal of Haematology , vol.141 , Issue.3 , pp. 298-308
    • Percy, M.J.1    Lappin, T.R.2
  • 17
    • 53149120605 scopus 로고    scopus 로고
    • Glucose metabolism is accelerated by exposure to t-butylhydroperoxide during NADH consumption in human erythrocytes
    • Y. Ogasawara, M. Funakoshi, and K. Ishii Glucose metabolism is accelerated by exposure to t-butylhydroperoxide during NADH consumption in human erythrocytes Blood Cells Mol. Dis. 41 2008 237 243
    • (2008) Blood Cells Mol. Dis. , vol.41 , pp. 237-243
    • Ogasawara, Y.1    Funakoshi, M.2    Ishii, K.3
  • 18
    • 0029057960 scopus 로고
    • Hexokinase mutations that produce nonspherocytic hemolytic anemia
    • M. Bianchi, and M. Magnani Hexokinase mutations that produce nonspherocytic hemolytic anemia Blood Cells Mol. Dis. 21 1995 2 8
    • (1995) Blood Cells Mol. Dis. , vol.21 , pp. 2-8
    • Bianchi, M.1    Magnani, M.2
  • 19
    • 0036720556 scopus 로고    scopus 로고
    • Homozygous intragenic deletion of type I hexokinase gene causes lethal hemolytic anemia of the affected fetus [6]
    • DOI 10.1182/blood-2002-05-1599
    • H. Kanno, K. Murakami, Y. Hariyama, K. Ishikawa, S. Miwa, and H. Fujii Homozygous intragenic deletion of type I hexokinase gene causes lethal hemolytic anemia of the affected fetus Blood 100 2002 1930 (Pubitemid 34925182)
    • (2002) Blood , vol.100 , Issue.5 , pp. 1930
    • Kanno, H.1    Murakami, K.2    Hariyama, Y.3    Ishikawa, K.4    Miwa, S.5    Fujli, H.6
  • 21
    • 33847386720 scopus 로고    scopus 로고
    • Simulation study of methemoglobin reduction in erythrocytes: Differential contributions of two pathways to tolerance to oxidative stress
    • DOI 10.1111/j.1742-4658.2007.05685.x
    • A. Kinoshita, Y. Nakayama, T. Kitayama, and M. Tomita Simulation study of methemoglobin reduction in erythrocytes: differential contributions of two pathways to tolerance to oxidative stress FEBS J. 274 2007 1449 1458 (Pubitemid 46333737)
    • (2007) FEBS Journal , vol.274 , Issue.6 , pp. 1449-1458
    • Kinoshita, A.1    Nakayama, Y.2    Kitayama, T.3    Tomita, M.4
  • 22
    • 34250023771 scopus 로고    scopus 로고
    • Pyruvate kinase deficiency: The genotype-phenotype association
    • DOI 10.1016/j.blre.2007.01.001, PII S0268960X07000021
    • A. Zanella, E. Fermo, P. Bianchi, L.R. Chiarelli, and G. Valentini Pyruvate kinase deficiency: the genotype-phenotype association Blood Rev. 21 2007 217 231 (Pubitemid 46887628)
    • (2007) Blood Reviews , vol.21 , Issue.4 , pp. 217-231
    • Zanella, A.1    Fermo, E.2    Bianchi, P.3    Chiarelli, L.R.4    Valentini, G.5
  • 23
    • 61649103978 scopus 로고    scopus 로고
    • Fifteen novel mutations in PKLR associated with pyruvate kinase (PK) deficiency: Structural implications of amino acid substitutions in PK
    • R. van Wijk, E.G. Huizinga, A.C. van Wesel, B.A. van Oirschot, M.A. Hadders, and W.W. van Solinge Fifteen novel mutations in PKLR associated with pyruvate kinase (PK) deficiency: structural implications of amino acid substitutions in PK Hum. Mutat. 30 2009 446 453
    • (2009) Hum. Mutat. , vol.30 , pp. 446-453
    • Van Wijk, R.1    Huizinga, E.G.2    Van Wesel, A.C.3    Van Oirschot, B.A.4    Hadders, M.A.5    Van Solinge, W.W.6
  • 25
    • 0020571179 scopus 로고
    • Inhibition of the pentose phosphate shunt by 2,3-diphosphoglycerate in erythrocyte pyruvate kinase deficiency
    • A. Tomoda, N.A. Lachant, N.A. Noble, and K.R. Tanaka Inhibition of the pentose phosphate shunt by 2,3-diphosphoglycerate in erythrocyte pyruvate kinase deficiency Br. J. Haematol. 54 1983 475 484 (Pubitemid 13054569)
    • (1983) British Journal of Haematology , vol.54 , Issue.3 , pp. 475-484
    • Tomoda, A.1    Lachant, N.A.2    Noble, N.A.3    Tanaka, K.R.4
  • 26
    • 0015390986 scopus 로고
    • Factors affecting pentose phosphate pathway activity in human red cells
    • W.D. Davidson, and K.R. Tanaka Factors affecting pentose phosphate pathway activity in human red cells Br. J. Haematol. 23 1972 371 385
    • (1972) Br. J. Haematol. , vol.23 , pp. 371-385
    • Davidson, W.D.1    Tanaka, K.R.2
  • 27
    • 77949267064 scopus 로고    scopus 로고
    • Glycolytic network restructuring integral to the energetics of embryonic stem cell cardiac differentiation
    • S. Chung, D.K. Arrell, R.S. Faustino, A. Terzic, and P.P. Dzeja Glycolytic network restructuring integral to the energetics of embryonic stem cell cardiac differentiation J. Mol. Cell. Cardiol. 48 2010 725 734
    • (2010) J. Mol. Cell. Cardiol. , vol.48 , pp. 725-734
    • Chung, S.1    Arrell, D.K.2    Faustino, R.S.3    Terzic, A.4    Dzeja, P.P.5
  • 28
    • 1842592038 scopus 로고    scopus 로고
    • Ribose-5-Phosphate Isomerase Deficiency: New Inborn Error in the Pentose Phosphate Pathway Associated with a Slowly Progressive Leukoencephalopathy
    • DOI 10.1086/383204
    • J.H. Huck, N.M. Verhoeven, E.A. Struys, G.S. Salomons, C. Jakobs, and M.S. van der Knaap Ribose-5-phosphate isomerase deficiency: new inborn error in the pentose phosphate pathway associated with a slowly progressive leukoencephalopathy Am. J. Hum. Genet. 74 2004 745 751 (Pubitemid 38420104)
    • (2004) American Journal of Human Genetics , vol.74 , Issue.4 , pp. 745-751
    • Huck, J.H.J.1    Verhoeven, N.M.2    Struys, E.A.3    Salomons, G.S.4    Jakobs, C.5    Van Der Knaap, M.S.6
  • 29
    • 34347396343 scopus 로고    scopus 로고
    • The pathogenesis of transaldolase deficiency
    • DOI 10.1080/15216540701387188, PII 779717634
    • A. Perl The pathogenesis of transaldolase deficiency IUBMB Life 59 2007 365 373 (Pubitemid 47027116)
    • (2007) IUBMB Life , vol.59 , Issue.6 , pp. 365-373
    • Perl, A.1
  • 30
    • 57649178844 scopus 로고    scopus 로고
    • The biochemistry, metabolism and inherited defects of the pentose phosphate pathway: A review
    • M.M. Wamelink, E.A. Struys, and C. Jakobs The biochemistry, metabolism and inherited defects of the pentose phosphate pathway: a review J. Inherit. Metab. Dis. 31 2008 703 717
    • (2008) J. Inherit. Metab. Dis. , vol.31 , pp. 703-717
    • Wamelink, M.M.1    Struys, E.A.2    Jakobs, C.3
  • 31
    • 0006236102 scopus 로고
    • A new inherited enzymatic deficiency of human erythrocytes: 6-phosphogluconate dehydrogenase deficiency
    • G.J. Brewer, and R.J. Dern A new inherited enzymatic deficiency of human erythrocytes: 6-phosphogluconate dehydrogenase deficiency Am. J. Hum. Genet. 16 1964 472 476
    • (1964) Am. J. Hum. Genet. , vol.16 , pp. 472-476
    • Brewer, G.J.1    Dern, R.J.2
  • 32
    • 0014089977 scopus 로고
    • Inherited quantitative variations of human phosphogluconate dehydrogenase
    • C.W. Parr, and L.I. Fitch Inherited quantitative variations of human phosphogluconate dehydrogenase Ann. Hum. Genet. 30 1967 339 353
    • (1967) Ann. Hum. Genet. , vol.30 , pp. 339-353
    • Parr, C.W.1    Fitch, L.I.2
  • 33
    • 10544231459 scopus 로고    scopus 로고
    • Congenital 6-phosphogluconate dehydrogenase (6PGD) deficiency associated with chronic hemolytic anemia in a Spanish family
    • DOI 10.1002/(SICI)1096-8652(199612) 53:4<221::AID-AJH2>3.0.CO;2-#
    • J.L. Vives Corrons, D. Colomer, A. Pujades, A. Rovira, M. Aymerich, and A. Merino et al. Congenital 6-phosphogluconate dehydrogenase (6PGD) deficiency associated with chronic hemolytic anemia in a Spanish family Am. J. Hematol. 53 1996 221 227 (Pubitemid 26419707)
    • (1996) American Journal of Hematology , vol.53 , Issue.4 , pp. 221-227
    • Corrons, J.L.V.1    Colomer, D.2    Pujades, A.3    Rovira, A.4    Aymerich, M.5    Merino, A.6
  • 35
    • 0022363712 scopus 로고
    • 6-Phosphogluconolactonase deficiency, a hereditary erythrocyte enzyme deficiency: Possible interaction with glucose-6-phosphate dehydrogenase deficiency
    • DOI 10.1073/pnas.82.11.3876
    • E. Beutler, W. Kuhl, and T. Gelbart 6-Phosphogluconolactonase deficiency, a hereditary erythrocyte enzyme deficiency: possible interaction with glucose-6-phosphate dehydrogenase deficiency Proc. Natl. Acad. Sci. USA 82 1985 3876 3878 (Pubitemid 15246455)
    • (1985) Proceedings of the National Academy of Sciences of the United States of America , vol.82 , Issue.11 , pp. 3876-3878
    • Beutler, E.1    Kuhl, W.2    Gelbart, T.3
  • 37
    • 8644222226 scopus 로고    scopus 로고
    • G6PD is indispensable for erythropoiesis after the embryonic-adult hemoglobin switch
    • DOI 10.1182/blood-2004-03-0835
    • F. Paglialunga, A. Fico, I. Iaccarino, R. Notaro, L. Luzzatto, and G. Martini et al. G6PD is indispensable for erythropoiesis after the embryonic-adult hemoglobin switch Blood 104 2004 3148 3152 (Pubitemid 39507128)
    • (2004) Blood , vol.104 , Issue.10 , pp. 3148-3152
    • Paglialunga, F.1    Fico, A.2    Iaccarino, I.3    Notaro, R.4    Luzzatto, L.5    Martini, G.6    Filosa, S.7
  • 38
    • 0345437424 scopus 로고
    • Survival of 51Cr-labelled red cells in subjects with thalassemia-trait or G6PD deficiency or both abnormalities
    • L. Bernini, B. Latte, M. Siniscalco, S. Piomelli, U. Spada, and M. Adinolfi et al. Survival of 51Cr-labelled red cells in subjects with thalassemia-trait or G6PD deficiency or both abnormalities Br. J. Haematol. 10 1964 171 180
    • (1964) Br. J. Haematol. , vol.10 , pp. 171-180
    • Bernini, L.1    Latte, B.2    Siniscalco, M.3    Piomelli, S.4    Spada, U.5    Adinolfi, M.6
  • 40
    • 5444248971 scopus 로고    scopus 로고
    • The relationship between the enzyme activity, lipid peroxidation and red blood cells deformability in hemizygous and heterozygous glucose-6-phosphate dehydrogenase deficient individuals
    • N. Gurbuz, O. Yalcin, T.A. Aksu, and O.K. Baskurt The relationship between the enzyme activity, lipid peroxidation and red blood cells deformability in hemizygous and heterozygous glucose-6-phosphate dehydrogenase deficient individuals Clin. Hemorheol. Microcirc. 31 2004 235 242 (Pubitemid 39362724)
    • (2004) Clinical Hemorheology and Microcirculation , vol.31 , Issue.3 , pp. 235-242
    • Gurbuz, N.1    Yalcin, O.2    Aksu, T.A.3    Baskurt, O.K.4
  • 41
    • 0021668870 scopus 로고
    • Mechanism of action of divicine in a cell-free system and in glucose-6-phosphate dehydrogenase-deficient red cells
    • M.A. Baker, A. Bosia, G. Pescarmona, F. Turrini, and P. Arese Mechanism of action of divicine in a cell-free system and in glucose-6-phosphate dehydrogenase-deficient red cells Toxicol. Pathol. 12 1984 331 336 (Pubitemid 15100116)
    • (1984) Toxicologic Pathology , vol.12 , Issue.4 , pp. 331-336
    • Baker, M.A.1    Bosia, A.2    Pescarmona, G.3
  • 42
    • 33750083939 scopus 로고    scopus 로고
    • Glucose 6-phosphate dehydrogenase deficiency: From genotype to phenotype
    • L. Luzzatto Glucose 6-phosphate dehydrogenase deficiency: from genotype to phenotype Haematologica 91 2006 1303 1306 (Pubitemid 44574287)
    • (2006) Haematologica , vol.91 , Issue.10 , pp. 1303-1306
    • Luzzatto, L.1
  • 43
    • 0029743435 scopus 로고    scopus 로고
    • Active involvement of catalase during hemolytic crises of favism
    • G.F. Gaetani, M. Rolfo, S. Arena, R. Mangerini, G.F. Meloni, and A.M. Ferraris Active involvement of catalase during hemolytic crises of favism Blood 88 1996 1084 1088 (Pubitemid 26333335)
    • (1996) Blood , vol.88 , Issue.3 , pp. 1084-1088
    • Gaetani, G.F.1    Rolfo, M.2    Arena, S.3    Mangerini, R.4    Meloni, G.F.5    Ferraris, A.M.6
  • 46
    • 0027940492 scopus 로고
    • G6PD deficiency
    • E. Beutler G6PD deficiency Blood 84 1994 3613 3636 (Pubitemid 24362456)
    • (1994) Blood , vol.84 , Issue.11 , pp. 3613-3636
    • Beutler, E.1
  • 47
    • 0015322180 scopus 로고
    • Complete deficiency of leukocyte glucose-6-phosphate dehydrogenase with defective bactericidal activity
    • M.R. Cooper, L.R. DeChatelet, C.E. McCall, M.F. LaVia, C.L. Spurr, and R.L. Baehner Complete deficiency of leukocyte glucose-6-phosphate dehydrogenase with defective bactericidal activity J. Clin. Invest. 51 1972 769 778
    • (1972) J. Clin. Invest. , vol.51 , pp. 769-778
    • Cooper, M.R.1    Dechatelet, L.R.2    McCall, C.E.3    Lavia, M.F.4    Spurr, C.L.5    Baehner, R.L.6
  • 48
    • 0015910925 scopus 로고
    • Neutrophil dysfunction, chronic granulomatous disease, and non-spherocytic haemolytic anaemia caused by complete deficiency of glucose-6-phosphate dehydrogenase
    • G.R. Gray, G. Stamatoyannopoulos, S.C. Naiman, M.R. Kliman, S.J. Klebanoff, and T. Austin et al. Neutrophil dysfunction, chronic granulomatous disease, and non-spherocytic haemolytic anaemia caused by complete deficiency of glucose-6-phosphate dehydrogenase Lancet 2 1973 530 534
    • (1973) Lancet , vol.2 , pp. 530-534
    • Gray, G.R.1    Stamatoyannopoulos, G.2    Naiman, S.C.3    Kliman, M.R.4    Klebanoff, S.J.5    Austin, T.6
  • 49
    • 0020054476 scopus 로고
    • Severe glucose-6-phosphate dehydrogenase (G6PD) deficiency associated with chronic hemolytic anemia, granulocyte dysfunction, and increased susceptibility to infections: Description of a new molecular variant (G6PD Barcelona)
    • J.L. Vives Corrons, E. Feliu, M.A. Pujades, F. Cardellach, C. Rozman, and A. Carreras et al. Severe-glucose-6-phosphate dehydrogenase (G6PD) deficiency associated with chronic hemolytic anemia, granulocyte dysfunction, and increased susceptibility to infections: description of a new molecular variant (G6PD Barcelona) Blood 59 1982 428 434 (Pubitemid 12172036)
    • (1982) Blood , vol.59 , Issue.2 , pp. 428-434
    • Vives Corrons, J.L.1    Feliu, E.2    Pujades, M.A.3
  • 52
    • 33644830349 scopus 로고    scopus 로고
    • Hereditary erythrocyte pyrimidine 5′-nucleotidase deficiency: A biochemical, genetic and clinical overview
    • DOI 10.1080/10245330500276667, PII K4701604557866
    • L.R. Chiarelli, E. Fermo, A. Zanella, and G. Valentini Hereditary erythrocyte pyrimidine 5'-nucleotidase deficiency: a biochemical, genetic and clinical overview Hematology 11 2006 67 72 (Pubitemid 43354965)
    • (2006) Hematology , vol.11 , Issue.1 , pp. 67-72
    • Chiarelli, L.R.1    Fermo, E.2    Zanella, A.3    Valentini, G.4
  • 53
    • 33645085288 scopus 로고    scopus 로고
    • Hereditary pyrimidine 5'-nucleotidase deficiency: From genetics to clinical manifestations
    • A. Zanella, P. Bianchi, E. Fermo, and G. Valentini Hereditary pyrimidine 5'-nucleotidase deficiency: from genetics to clinical manifestations Br. J. Haematol. 133 2006 113 123
    • (2006) Br. J. Haematol. , vol.133 , pp. 113-123
    • Zanella, A.1    Bianchi, P.2    Fermo, E.3    Valentini, G.4
  • 54
    • 0020383946 scopus 로고
    • Hemolytic anemia in hereditary pyrimidine 5'-nucleotidase deficiency: Nucleotide inhibition of G6PD and the pentose phosphate shunt
    • A. Tomoda, N.A. Noble, N.A. Lachant, and K.R. Tanaka Hemolytic anemia in hereditary pyrimidine 5'-nucleotidase deficiency: nucleotide inhibition of G6PD and the pentose phosphate shunt Blood 60 1982 1212 1218 (Pubitemid 13242305)
    • (1982) Blood , vol.60 , Issue.5 , pp. 1212-1218
    • Tomoda, A.1    Noble, N.A.2    Lachant, N.A.3    Tanaka, K.R.4
  • 56
    • 37549026846 scopus 로고    scopus 로고
    • Glucose-6-phosphate dehydrogenase deficiency
    • M.D. Cappellini, and G. Fiorelli Glucose-6-phosphate dehydrogenase deficiency Lancet 371 2008 64 74
    • (2008) Lancet , vol.371 , pp. 64-74
    • Cappellini, M.D.1    Fiorelli, G.2
  • 57
    • 77955567583 scopus 로고    scopus 로고
    • Medications and glucose-6-phosphate dehydrogenase deficiency: An evidence-based review
    • I. Youngster, L. Arcavi, R. Schechmaster, Y. Akayzen, H. Popliski, and J. Shimonov et al. Medications and glucose-6-phosphate dehydrogenase deficiency: an evidence-based review Drug Saf. 33 2010 713 726
    • (2010) Drug Saf. , vol.33 , pp. 713-726
    • Youngster, I.1    Arcavi, L.2    Schechmaster, R.3    Akayzen, Y.4    Popliski, H.5    Shimonov, J.6
  • 58
    • 0021368186 scopus 로고
    • Excretion of superoxide by phagocytes measured with cytochrome c entrapped in resealed erythrocyte ghosts
    • D. Roos, C.M. Eckmann, M. Yazdanbakhsh, M.N. Hamers, and M. de Boer Excretion of superoxide by phagocytes measured with cytochrome c entrapped in resealed erythrocyte ghosts J. Biol. Chem. 259 1984 1770 1775 (Pubitemid 14146565)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.3 , pp. 1770-1775
    • Roos, D.1    Eckmann, C.M.2    Yazdanbakhsh, M.3
  • 59
    • 74549133551 scopus 로고    scopus 로고
    • Biopreservation of red blood cells - The struggle with hemoglobin oxidation
    • T. Kanias, and J.P. Acker Biopreservation of red blood cells - the struggle with hemoglobin oxidation FEBS J. 277 2010 343 356
    • (2010) FEBS J. , vol.277 , pp. 343-356
    • Kanias, T.1    Acker, J.P.2
  • 60
    • 84934437356 scopus 로고    scopus 로고
    • Role of the red blood cell in nitric oxide homeostasis and hypoxic vasodilation
    • M.T. Gladwin Role of the red blood cell in nitric oxide homeostasis and hypoxic vasodilation Adv. Exp. Med. Biol. 588 2006 189 205
    • (2006) Adv. Exp. Med. Biol. , vol.588 , pp. 189-205
    • Gladwin, M.T.1
  • 62
    • 84876892476 scopus 로고    scopus 로고
    • Hemoglobin redox reactions and red blood cell aging
    • J.M. Rifkind, and E. Nagababu Hemoglobin redox reactions and red blood cell aging Antioxid. Redox Signaling 18 2013 2274 2283
    • (2013) Antioxid. Redox Signaling , vol.18 , pp. 2274-2283
    • Rifkind, J.M.1    Nagababu, E.2
  • 64
    • 79961025290 scopus 로고    scopus 로고
    • Nitric oxide scavenging by red blood cell microparticles and cell-free hemoglobin as a mechanism for the red cell storage lesion
    • C. Donadee, N.J. Raat, T. Kanias, J. Tejero, J.S. Lee, and E.E. Kelley et al. Nitric oxide scavenging by red blood cell microparticles and cell-free hemoglobin as a mechanism for the red cell storage lesion Circulation 124 2011 465 476
    • (2011) Circulation , vol.124 , pp. 465-476
    • Donadee, C.1    Raat, N.J.2    Kanias, T.3    Tejero, J.4    Lee, J.S.5    Kelley, E.E.6
  • 65
    • 77953187009 scopus 로고    scopus 로고
    • Uric acid transport and disease
    • A. So, and B. Thorens Uric acid transport and disease J. Clin. Invest. 120 2010 1791 1799
    • (2010) J. Clin. Invest. , vol.120 , pp. 1791-1799
    • So, A.1    Thorens, B.2
  • 67
    • 0030008268 scopus 로고    scopus 로고
    • Fenton chemistry: An introduction
    • DOI 10.2307/3579270
    • P. Wardman, and L.P. Candeias Fenton chemistry: an introduction Radiat. Res. 145 1996 523 531 (Pubitemid 26127159)
    • (1996) Radiation Research , vol.145 , Issue.5 , pp. 523-531
    • Wardman, P.1    Candeias, L.P.2
  • 68
    • 84859731256 scopus 로고    scopus 로고
    • Hemolysis and cell-free hemoglobin drive an intrinsic mechanism for human disease
    • M.T. Gladwin, T. Kanias, and D.B. Kim-Shapiro Hemolysis and cell-free hemoglobin drive an intrinsic mechanism for human disease J. Clin. Invest 122 2012 1205 1208
    • (2012) J. Clin. Invest , vol.122 , pp. 1205-1208
    • Gladwin, M.T.1    Kanias, T.2    Kim-Shapiro, D.B.3
  • 70
    • 24044471309 scopus 로고    scopus 로고
    • Superoxide dismutases and their impact upon human health
    • DOI 10.1016/j.mam.2005.07.006, PII S0098299705000361
    • F. Johnson, and C. Giulivi Superoxide dismutases and their impact upon human health Mol. Aspects Med. 26 2005 340 352 (Pubitemid 41225357)
    • (2005) Molecular Aspects of Medicine , vol.26 , Issue.4-5 SPEC. ISSUE. , pp. 340-352
    • Johnson, F.1    Giulivi, C.2
  • 71
    • 58949085248 scopus 로고    scopus 로고
    • The effects of superoxide dismutase knockout on the oxidative stress parameters and survival of mouse erythrocytes
    • A. Grzelak, M. Kruszewski, E. Macierzynska, L. Piotrowski, L. Pulaski, and B. Rychlik et al. The effects of superoxide dismutase knockout on the oxidative stress parameters and survival of mouse erythrocytes Cell. Mol. Biol. Lett. 14 2009 23 34
    • (2009) Cell. Mol. Biol. Lett. , vol.14 , pp. 23-34
    • Grzelak, A.1    Kruszewski, M.2    MacIerzynska, E.3    Piotrowski, L.4    Pulaski, L.5    Rychlik, B.6
  • 72
    • 33947476438 scopus 로고
    • Glutathione peroxidase: The primary agents for the elimination of hydrogen peroxide in erythrocytes
    • G. Cohen, and P. Hochstein Glutathione peroxidase: the primary agents for the elimination of hydrogen peroxide in erythrocytes Biochemistry 2 1963 1420 1428
    • (1963) Biochemistry , vol.2 , pp. 1420-1428
    • Cohen, G.1    Hochstein, P.2
  • 73
    • 0000296829 scopus 로고
    • Progressive oral gangrene probably due to lack of catalase in the blood (acatalasaemia); Report of nine cases
    • S. Takahara Progressive oral gangrene probably due to lack of catalase in the blood (acatalasaemia); report of nine cases Lancet 2 1952 1101 1104
    • (1952) Lancet , vol.2 , pp. 1101-1104
    • Takahara, S.1
  • 74
    • 16344389174 scopus 로고    scopus 로고
    • Catalase enzyme mutations and their association with diseases
    • DOI 10.2165/00066982-200408030-00001
    • L. Goth, P. Rass, and A. Pay Catalase enzyme mutations and their association with diseases Mol. Diagn. 8 2004 141 149 (Pubitemid 40468779)
    • (2004) Molecular Diagnosis , vol.8 , Issue.3 , pp. 141-149
    • Goth, L.1    Rass, P.2    Pay, A.3
  • 75
    • 3543040601 scopus 로고    scopus 로고
    • Mice lacking catalase develop normally but show differential sensitivity to oxidant tissue injury
    • DOI 10.1074/jbc.M404800200
    • Y.S. Ho, Y. Xiong, W. Ma, A. Spector, and D.S. Ho Mice lacking catalase develop normally but show differential sensitivity to oxidant tissue injury J. Biol. Chem. 279 2004 32804 32812 (Pubitemid 39014740)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.31 , pp. 32804-32812
    • Ho, Y.-S.1    Xiong, Y.2    Ma, W.3    Spector, A.4    Ho, D.S.5
  • 76
    • 84861235219 scopus 로고    scopus 로고
    • Structural and functional analysis of native peroxiredoxin 2 in human red blood cells
    • Y. Ogasawara, T. Ohminato, Y. Nakamura, and K. Ishii Structural and functional analysis of native peroxiredoxin 2 in human red blood cells Int. J. Biochem. Cell Biol. 44 2012 1072 1077
    • (2012) Int. J. Biochem. Cell Biol. , vol.44 , pp. 1072-1077
    • Ogasawara, Y.1    Ohminato, T.2    Nakamura, Y.3    Ishii, K.4
  • 80
    • 0025797725 scopus 로고
    • Glutathione peroxidase deficiency and childhood seizures
    • E. Beutler, J.T. Curnutte, and L. Forman Glutathione peroxidase deficiency and childhood seizures Lancet 338 1991 700
    • (1991) Lancet , vol.338 , pp. 700
    • Beutler, E.1    Curnutte, J.T.2    Forman, L.3
  • 81
    • 0013879131 scopus 로고
    • Congenital nonspherocytic hemolytic anemia, associated with glutathione deficiency of the erythrocytes: Hematologic, biochemical and genetic studies
    • H.K. Prins, M. Oort, C. Zurcher, and T. Beckers Congenital nonspherocytic hemolytic anemia, associated with glutathione deficiency of the erythrocytes: hematologic, biochemical and genetic studies Blood 27 1966 145 166
    • (1966) Blood , vol.27 , pp. 145-166
    • Prins, H.K.1    Oort, M.2    Zurcher, C.3    Beckers, T.4
  • 82
    • 12944252974 scopus 로고    scopus 로고
    • A missense mutation in the heavy subunit of gamma-glutamylcysteine synthetase gene causes hemolytic anemia
    • E. Ristoff, C. Augustson, J. Geissler, T. de Rijk, K. Carlsson, and J.L. Luo et al. A missense mutation in the heavy subunit of gamma-glutamylcysteine synthetase gene causes hemolytic anemia Blood 95 2000 2193 2196
    • (2000) Blood , vol.95 , pp. 2193-2196
    • Ristoff, E.1    Augustson, C.2    Geissler, J.3    De Rijk, T.4    Carlsson, K.5    Luo, J.L.6
  • 83
    • 0037818355 scopus 로고    scopus 로고
    • A novel missense mutation in the γ-glutamylcysteine synthetase catalytic subunit gene causes both decreased enzymatic activity and glutathione production
    • DOI 10.1182/blood-2002-11-3622
    • D. Hamilton, J.H. Wu, M. Alaoui-Jamali, and G. Batist A novel missense mutation in the gamma-glutamylcysteine synthetase catalytic subunit gene causes both decreased enzymatic activity and glutathione production Blood 102 2003 725 730 (Pubitemid 36841998)
    • (2003) Blood , vol.102 , Issue.2 , pp. 725-730
    • Hamilton, D.1    Wu, J.H.2    Alaoui-Jamali, M.3    Batist, G.4
  • 84
    • 0032879826 scopus 로고    scopus 로고
    • The molecular basis of a case of γ-glutamylcysteine synthetase deficiency
    • E. Beutler, T. Gelbart, T. Kondo, and A.T. Matsunaga The molecular basis of a case of gamma-glutamylcysteine synthetase deficiency Blood 94 1999 2890 2894 (Pubitemid 29477318)
    • (1999) Blood , vol.94 , Issue.8 , pp. 2890-2894
    • Beutler, E.1    Gelbart, T.2    Kondo, T.3    Matsunaga, A.T.4
  • 85
    • 65049084484 scopus 로고    scopus 로고
    • Chronic non-spherocytic hemolytic anemia associated with severe neurological disease due to gamma-glutamylcysteine synthetase deficiency in a patient of Moroccan origin
    • P.M. Manu, T. Gelbart, E. Ristoff, K.C. Crain, J.M. Bergua, and L.A. Lopez et al. Chronic non-spherocytic hemolytic anemia associated with severe neurological disease due to gamma-glutamylcysteine synthetase deficiency in a patient of Moroccan origin Haematologica 92 2007 e102 e105
    • (2007) Haematologica , vol.92
    • Manu, P.M.1    Gelbart, T.2    Ristoff, E.3    Crain, K.C.4    Bergua, J.M.5    Lopez, L.A.6
  • 86
    • 77955657972 scopus 로고    scopus 로고
    • An ethnic-specific polymorphism in the catalytic subunit of glutamate-cysteine ligase impairs the production of glutathione intermediates in vitro
    • T.M. Le, A.S. Willis, F.E. Barr, G.R. Cunningham, J.A. Canter, and S.E. Owens et al. An ethnic-specific polymorphism in the catalytic subunit of glutamate-cysteine ligase impairs the production of glutathione intermediates in vitro Mol. Genet. Metab. 101 2010 55 61
    • (2010) Mol. Genet. Metab. , vol.101 , pp. 55-61
    • Le, T.M.1    Willis, A.S.2    Barr, F.E.3    Cunningham, G.R.4    Canter, J.A.5    Owens, S.E.6
  • 87
    • 0034980722 scopus 로고    scopus 로고
    • Evidence for functionally significant polymorphism of human glutamate cysteine ligase catalytic subunit: Association with glutathione levels and drug resistance in the National Cancer Institute tumor cell line panel
    • DOI 10.1093/toxsci/61.2.218
    • A.C. Walsh, J.A. Feulner, and A. Reilly Evidence for functionally significant polymorphism of human glutamate cysteine ligase catalytic subunit: association with glutathione levels and drug resistance in the National Cancer Institute tumor cell line panel Toxicol. Sci. 61 2001 218 223 (Pubitemid 32499389)
    • (2001) Toxicological Sciences , vol.61 , Issue.2 , pp. 218-223
    • Walsh J, A.C.1    Feulner, A.2    Reilly, A.3
  • 88
    • 0030876935 scopus 로고    scopus 로고
    • Missense mutations in the human glutathione synthetase gene result in severe metabolic acidosis, 5-oxoprolinuria, hemolytic anemia and neurological dysfunction
    • DOI 10.1093/hmg/6.7.1147
    • N. Dahl, M. Pigg, E. Ristoff, R. Gali, B. Carlsson, and B. Mannervik et al. Missense mutations in the human glutathione synthetase gene result in severe metabolic acidosis, 5-oxoprolinuria, hemolytic anemia and neurological dysfunction Hum. Mol. Genet. 6 1997 1147 1152 (Pubitemid 27308401)
    • (1997) Human Molecular Genetics , vol.6 , Issue.7 , pp. 1147-1152
    • Dahl, N.1    Pigg, M.2    Ristoff, E.3    Gali, R.4    Carlsson, B.5    Mannervik, B.6    Larsson, A.7    Board, P.8
  • 89
    • 0030292360 scopus 로고    scopus 로고
    • Mutations in the glutathione synthetase gene cause 5-oxoprolinuria
    • Z.Z. Shi, G.M. Habib, W.J. Rhead, W.A. Gahl, X. He, and S. Sazer et al. Mutations in the glutathione synthetase gene cause 5-oxoprolinuria Nat. Genet. 14 1996 361 365
    • (1996) Nat. Genet. , vol.14 , pp. 361-365
    • Shi, Z.Z.1    Habib, G.M.2    Rhead, W.J.3    Gahl, W.A.4    He, X.5    Sazer, S.6
  • 90
    • 32744462165 scopus 로고    scopus 로고
    • Diagnostics in patients with glutathione synthetase deficiency but without mutations in the exons of the GSS gene
    • R. Njalsson, K. Carlsson, A. Winkler, A. Larsson, and S. Norgren Diagnostics in patients with glutathione synthetase deficiency but without mutations in the exons of the GSS gene Hum. Mutat. 22 2003 497
    • (2003) Hum. Mutat. , vol.22 , pp. 497
    • Njalsson, R.1    Carlsson, K.2    Winkler, A.3    Larsson, A.4    Norgren, S.5
  • 91
    • 14844283016 scopus 로고    scopus 로고
    • Genotype, enzyme activity, glutathione level, and clinical phenotype in patients with glutathione synthetase deficiency
    • DOI 10.1007/s00439-005-1255-6
    • R. Njalsson, E. Ristoff, K. Carlsson, A. Winkler, A. Larsson, and S. Norgren Genotype, enzyme activity, glutathione level, and clinical phenotype in patients with glutathione synthetase deficiency Hum. Genet. 116 2005 384 389 (Pubitemid 40521115)
    • (2005) Human Genetics , vol.116 , Issue.5 , pp. 384-389
    • Njalsson, R.1    Ristoff, E.2    Carlsson, K.3    Winkler, A.4    Larsson, A.5    Norgren, S.6
  • 92
    • 0036881444 scopus 로고    scopus 로고
    • Glutathione synthetase deficiency: Is γ-glutamylcysteine accumulation a way to cope with oxidative stress in cells with insufficient levels of glutathione?
    • DOI 10.1023/A:1022095324407
    • E. Ristoff, C. Hebert, R. Njalsson, S. Norgren, O. Rooyackers, and A. Larsson Glutathione synthetase deficiency: is gamma-glutamylcysteine accumulation a way to cope with oxidative stress in cells with insufficient levels of glutathione? J. Inherit. Metab. Dis. 25 2002 577 584 (Pubitemid 36266993)
    • (2002) Journal of Inherited Metabolic Disease , vol.25 , Issue.7 , pp. 577-584
    • Ristoff, E.1    Hebert, C.2    Njalsson, R.3    Norgren, S.4    Rooyackers, O.5    Larsson, A.6
  • 94
    • 0034964577 scopus 로고    scopus 로고
    • Long-term clinical outcome in patients with glutathione synthetase deficiency
    • DOI 10.1067/mpd.2001.114480
    • E. Ristoff, E. Mayatepek, and A. Larsson Long-term clinical outcome in patients with glutathione synthetase deficiency J. Pediatr. 139 2001 79 84 (Pubitemid 32613991)
    • (2001) Journal of Pediatrics , vol.139 , Issue.1 , pp. 79-84
    • Ristoff, E.1    Mayatepek, E.2    Larsson, A.3
  • 95
    • 0020033792 scopus 로고
    • The structure of partially oxygenated hemoglobin. A highly reactive intermediate toward a sulfhydryl titrant
    • N. Makino, and Y. Sugita The structure of partially oxygenated hemoglobin: a highly reactive intermediate toward a sulfhydryl titrant J. Biol. Chem. 257 1982 163 168 (Pubitemid 12109767)
    • (1982) Journal of Biological Chemistry , vol.257 , Issue.1 , pp. 163-168
    • Makino, N.1    Sugita, Y.2
  • 98
    • 0023780057 scopus 로고
    • Erythrocyte glutathione S-transferase deficiency and hemolytic anemia
    • E. Beutler, D. Dunning, I.B. Dabe, and L. Forman Erythrocyte glutathione S-transferase deficiency and hemolytic anemia Blood 72 1988 73 77
    • (1988) Blood , vol.72 , pp. 73-77
    • Beutler, E.1    Dunning, D.2    Dabe, I.B.3    Forman, L.4
  • 99
    • 0020414542 scopus 로고
    • FAD-binding site of glutathione reductase
    • DOI 10.1016/0022-2836(82)90177-2
    • G.E. Schulz, R.H. Schirmer, and E.F. Pai FAD-binding site of glutathione reductase J. Mol. Biol. 160 1982 287 308 (Pubitemid 13239303)
    • (1982) Journal of Molecular Biology , vol.160 , Issue.2 , pp. 287-308
    • Schulz, G.E.1    Schirmer, R.H.2    Pai, E.F.3
  • 100
    • 34147164690 scopus 로고    scopus 로고
    • Mild riboflavin deficiency is highly prevalent in school-age children but does not increase risk for anaemia in Coôte d'Ivoire
    • DOI 10.1017/S0007114507665180
    • F. Rohner, M.B. Zimmermann, R. Wegmueller, A.B. Tschannen, and R.F. Hurrell Mild riboflavin deficiency is highly prevalent in school-age children but does not increase risk for anaemia in Cote d'Ivoire Br. J. Nutr. 97 2007 970 976 (Pubitemid 46554412)
    • (2007) British Journal of Nutrition , vol.97 , Issue.5 , pp. 970-976
    • Rohner, F.1    Zimmermann, M.B.2    Wegmueller, R.3    Tschannen, A.B.4    Hurrell, R.F.5
  • 101
    • 0029166966 scopus 로고
    • Deficiency of two red-cell flavin enzymes in a population in Sardinia: Was glutathione reductase deficiency specifically selected for by malaria?
    • B.B. Anderson, L. Corda, G.M. Perry, D. Pilato, M. Giuberti, and C. Vullo Deficiency of two red-cell flavin enzymes in a population in Sardinia: was glutathione reductase deficiency specifically selected for by malaria? Am. J. Hum. Genet. 57 1995 674 681
    • (1995) Am. J. Hum. Genet. , vol.57 , pp. 674-681
    • Anderson, B.B.1    Corda, L.2    Perry, G.M.3    Pilato, D.4    Giuberti, M.5    Vullo, C.6
  • 103
    • 70350234635 scopus 로고    scopus 로고
    • Inherited glutathione reductase deficiency and Plasmodium falciparum malaria - A case study
    • V. Gallo, E. Schwarzer, S. Rahlfs, R.H. Schirmer, R. van Zwieten, and D. Roos et al. Inherited glutathione reductase deficiency and Plasmodium falciparum malaria - a case study PLoS One 4 2009 e7303
    • (2009) PLoS One , vol.4 , pp. 7303
    • Gallo, V.1    Schwarzer, E.2    Rahlfs, S.3    Schirmer, R.H.4    Van Zwieten, R.5    Roos, D.6
  • 104
    • 0017062372 scopus 로고
    • Familial deficiency of glutathione reductase in human blood cells
    • H. Loos, D. Roos, R. Weening, and J. Houwerzijl Familial deficiency of glutathione reductase in human blood cells Blood 48 1976 53 62
    • (1976) Blood , vol.48 , pp. 53-62
    • Loos, H.1    Roos, D.2    Weening, R.3    Houwerzijl, J.4
  • 106
    • 0034704081 scopus 로고    scopus 로고
    • The thioredoxin system of the malaria parasite Plasmodium falciparum
    • DOI 10.1074/jbc.M007633200
    • S.M. Kanzok, R.H. Schirmer, I. Turbachova, R. Iozef, and K. Becker The thioredoxin system of the malaria parasite Plasmodium falciparum: glutathione reduction revisited J. Biol. Chem. 275 2000 40180 40186 (Pubitemid 32064647)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.51 , pp. 40180-40186
    • Kanzok, S.M.1    Schirmer, R.H.2    Turbachova, I.3    Iozef, R.4    Becker, K.5
  • 107
    • 34247868881 scopus 로고    scopus 로고
    • Inborn errors in the metabolism of glutathione
    • E. Ristoff, and A. Larsson Inborn errors in the metabolism of glutathione Orphanet J. Rare Dis. 2 2007 16
    • (2007) Orphanet J. Rare Dis. , vol.2 , pp. 16
    • Ristoff, E.1    Larsson, A.2
  • 108
    • 5344280431 scopus 로고    scopus 로고
    • Genetically altered mice to evaluate glutathione homeostasis in health and disease
    • DOI 10.1016/j.freeradbiomed.2004.06.040, PII S0891584904005349
    • T.P. Dalton, Y. Chen, S.N. Schneider, D.W. Nebert, and H.G. Shertzer Genetically altered mice to evaluate glutathione homeostasis in health and disease Free Radic. Biol. Med. 37 2004 1511 1526 (Pubitemid 39349798)
    • (2004) Free Radical Biology and Medicine , vol.37 , Issue.10 , pp. 1511-1526
    • Dalton, T.P.1    Chen, Y.2    Schneider, S.N.3    Nebert, D.W.4    Shertzer, H.G.5
  • 109
    • 10044237714 scopus 로고    scopus 로고
    • Analyses of glutathione reductase hypomorphic mice indicate a genetic knockout
    • DOI 10.1093/toxsci/kfh268
    • L.K. Rogers, T. Tamura, B.J. Rogers, S.E. Welty, T.N. Hansen, and C.V. Smith Analyses of glutathione reductase hypomorphic mice indicate a genetic knockout Toxicol. Sci. 82 2004 367 373 (Pubitemid 39600063)
    • (2004) Toxicological Sciences , vol.82 , Issue.2 , pp. 367-373
    • Rogers, L.K.1    Tamura, T.2    Rogers, B.J.3    Welty, S.E.4    Hansen, T.N.5    Smith, C.V.6
  • 110
    • 0032710821 scopus 로고    scopus 로고
    • Methemoglobinemia: Etiology, pharmacology, and clinical management
    • DOI 10.1016/S0196-0644(99)70167-8
    • R.O. Wright, W.J. Lewander, and A.D. Woolf Methemoglobinemia: etiology, pharmacology, and clinical management Ann. Emerg. Med. 34 1999 646 656 (Pubitemid 29510918)
    • (1999) Annals of Emergency Medicine , vol.34 , Issue.5 , pp. 646-656
    • Wright, R.O.1    Lewander, W.J.2    Woolf, A.D.3
  • 111
    • 0022868307 scopus 로고
    • Enzymopenic hereditary methemoglobinemia: A clinical/biochemical classification
    • E.R. Jaffe Enzymopenic hereditary methemoglobinemia: a clinical/biochemical classification Blood Cells 12 1986 81 90 (Pubitemid 17056716)
    • (1986) Blood Cells , vol.12 , Issue.1 , pp. 81-90
    • Jaffe, E.R.1
  • 113
    • 0017273607 scopus 로고
    • Haemoglobin M Hyde Park occurring as a fresh mutation: Diagnostic, structural, and genetic considerations
    • G. Stamatoyannopoulos, P.E. Nute, E. Giblett, J. Detter, and R. Chard Haemoglobin M Hyde Park occurring as a fresh mutation: diagnostic, structural, and genetic considerations J. Med. Genet. 13 1976 142 147
    • (1976) J. Med. Genet. , vol.13 , pp. 142-147
    • Stamatoyannopoulos, G.1    Nute, P.E.2    Giblett, E.3    Detter, J.4    Chard, R.5
  • 114
    • 84857045310 scopus 로고    scopus 로고
    • Framing the research agenda for sickle cell trait: Building on the current understanding of clinical events and their potential implications
    • J.C. Goldsmith, V.L. Bonham, C.H. Joiner, G.J. Kato, A.S. Noonan, and M.H. Steinberg Framing the research agenda for sickle cell trait: building on the current understanding of clinical events and their potential implications Am. J. Hematol. 87 2012 340 346
    • (2012) Am. J. Hematol. , vol.87 , pp. 340-346
    • Goldsmith, J.C.1    Bonham, V.L.2    Joiner, C.H.3    Kato, G.J.4    Noonan, A.S.5    Steinberg, M.H.6
  • 115
    • 84861357425 scopus 로고    scopus 로고
    • The role of ineffective erythropoiesis in non-transfusion-dependent thalassemia
    • S. Rivella The role of ineffective erythropoiesis in non-transfusion- dependent thalassemia Blood Rev. 26 Suppl. 1 2012 S12 S15
    • (2012) Blood Rev. , vol.26 , Issue.SUPPL. 1
    • Rivella, S.1
  • 116
    • 80054838641 scopus 로고    scopus 로고
    • Beta-Thalassemia: A model for elucidating the dynamic regulation of ineffective erythropoiesis and iron metabolism
    • Y. Ginzburg, and S. Rivella beta-Thalassemia: a model for elucidating the dynamic regulation of ineffective erythropoiesis and iron metabolism Blood 118 2011 4321 4330
    • (2011) Blood , vol.118 , pp. 4321-4330
    • Ginzburg, Y.1    Rivella, S.2
  • 117
    • 35348950927 scopus 로고    scopus 로고
    • Redox-dependent impairment of vascular function in sickle cell disease
    • DOI 10.1016/j.freeradbiomed.2007.08.014, PII S0891584907005837
    • M. Aslan, and B.A. Freeman Redox-dependent impairment of vascular function in sickle cell disease Free Radic. Biol. Med. 43 2007 1469 1483 (Pubitemid 47615401)
    • (2007) Free Radical Biology and Medicine , vol.43 , Issue.11 , pp. 1469-1483
    • Aslan, M.1    Freeman, B.A.2
  • 118
    • 70449726798 scopus 로고    scopus 로고
    • Hemoglobin disorders and endothelial cell interactions
    • N. Conran, and F.F. Costa Hemoglobin disorders and endothelial cell interactions Clin. Biochem. 42 2009 1824 1838
    • (2009) Clin. Biochem. , vol.42 , pp. 1824-1838
    • Conran, N.1    Costa, F.F.2
  • 119
    • 77249118223 scopus 로고    scopus 로고
    • Acetaminophen inhibits hemoprotein-catalyzed lipid peroxidation and attenuates rhabdomyolysis-induced renal failure
    • O. Boutaud, K.P. Moore, B.J. Reeder, D. Harry, A.J. Howie, and S. Wang et al. Acetaminophen inhibits hemoprotein-catalyzed lipid peroxidation and attenuates rhabdomyolysis-induced renal failure Proc. Natl. Acad. Sci. USA 107 2010 2699 2704
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 2699-2704
    • Boutaud, O.1    Moore, K.P.2    Reeder, B.J.3    Harry, D.4    Howie, A.J.5    Wang, S.6
  • 120
    • 84867821480 scopus 로고    scopus 로고
    • Methemoglobinemia and ascorbate deficiency in hemoglobin e beta thalassemia: Metabolic and clinical implications
    • A. Allen, C. Fisher, A. Premawardhena, D. Bandara, A. Perera, and S. Allen et al. Methemoglobinemia and ascorbate deficiency in hemoglobin E beta thalassemia: metabolic and clinical implications Blood 120 2012 2939 2944
    • (2012) Blood , vol.120 , pp. 2939-2944
    • Allen, A.1    Fisher, C.2    Premawardhena, A.3    Bandara, D.4    Perera, A.5    Allen, S.6
  • 121
    • 27544476504 scopus 로고    scopus 로고
    • L-glutamine therapy reduces endothelial adhesion of sickle red blood cells to human umbilical vein endothelial cells
    • Y. Niihara, N.M. Matsui, Y.M. Shen, D.A. Akiyama, C.S. Johnson, and M.A. Sunga et al. L-glutamine therapy reduces endothelial adhesion of sickle red blood cells to human umbilical vein endothelial cells BMC Blood Disord. 5 2005 4
    • (2005) BMC Blood Disord. , vol.5 , pp. 4
    • Niihara, Y.1    Matsui, N.M.2    Shen, Y.M.3    Akiyama, D.A.4    Johnson, C.S.5    Sunga, M.A.6
  • 122
    • 38049129666 scopus 로고    scopus 로고
    • Erythrocyte glutamine depletion, altered redox environment, and pulmonary hypertension in sickle cell disease
    • C.R. Morris, J.H. Suh, W. Hagar, S. Larkin, D.A. Bland, and M.H. Steinberg et al. Erythrocyte glutamine depletion, altered redox environment, and pulmonary hypertension in sickle cell disease Blood 111 2008 402 410
    • (2008) Blood , vol.111 , pp. 402-410
    • Morris, C.R.1    Suh, J.H.2    Hagar, W.3    Larkin, S.4    Bland, D.A.5    Steinberg, M.H.6
  • 124
    • 77955905915 scopus 로고    scopus 로고
    • The role of antioxidants and iron chelators in the treatment of oxidative stress in thalassemia
    • E. Fibach, and E.A. Rachmilewitz The role of antioxidants and iron chelators in the treatment of oxidative stress in thalassemia Ann. N. Y. Acad. Sci. 1202 2010 10 16
    • (2010) Ann. N. Y. Acad. Sci. , vol.1202 , pp. 10-16
    • Fibach, E.1    Rachmilewitz, E.A.2
  • 125
    • 0035007589 scopus 로고    scopus 로고
    • Oral supplements of vitamin E improve measures of oxidative stress in plasma and reduce oxidative damage to LDL and erythrocytes in β-thalassemia intermedia patients
    • L. Tesoriere, D. D'Arpa, D. Butera, M. Allegra, D. Renda, and A. Maggio et al. Oral supplements of vitamin E improve measures of oxidative stress in plasma and reduce oxidative damage to LDL and erythrocytes in beta-thalassemia intermedia patients Free Radic. Res. 34 2001 529 540 (Pubitemid 32492691)
    • (2001) Free Radical Research , vol.34 , Issue.5 , pp. 529-540
    • Tesoriere, L.1    D'Arpa, D.2    Butera, D.3    Allegra, M.4    Renda, D.5    Maggio, A.6    Bongiorno, A.7    Livrea, M.A.8
  • 126
    • 0022261911 scopus 로고
    • Biochemical and clinical effects of vitamin E administration in homozygous beta-thalassemia
    • O. Giardini, A. Cantani, A. Donfrancesco, F. Martino, O. Mannarino, and P. D'Eufemia et al. Biochemical and clinical effects of vitamin E administration in homozygous beta-thalassemia Acta Vitaminol. Enzymol. 7 1985 55 60 (Pubitemid 15010749)
    • (1985) Acta Vitaminologica et Enzymologica , vol.7 , Issue.1-2 , pp. 55-60
    • Giardini, O.1    Cantani, A.2    Donfrancesco, A.3
  • 127
    • 72449144673 scopus 로고    scopus 로고
    • Effect of combination therapy of hydroxyurea with l-carnitine and magnesium chloride on hematologic parameters and cardiac function of patients with beta-thalassemia intermedia
    • M. Karimi, F. Mohammadi, F. Behmanesh, S.M. Samani, M. Borzouee, and H. Amoozgar et al. Effect of combination therapy of hydroxyurea with l-carnitine and magnesium chloride on hematologic parameters and cardiac function of patients with beta-thalassemia intermedia Eur. J. Haematol. 84 2010 52 58
    • (2010) Eur. J. Haematol. , vol.84 , pp. 52-58
    • Karimi, M.1    Mohammadi, F.2    Behmanesh, F.3    Samani, S.M.4    Borzouee, M.5    Amoozgar, H.6
  • 129
    • 0023898154 scopus 로고
    • Effects of glucose-6-phosphate dehydrogenase deficiency upon sickle cell anemia
    • M.H. Steinberg, M.S. West, D. Gallagher, and W. Mentzer Effects of glucose-6-phosphate dehydrogenase deficiency upon sickle cell anemia Blood 71 1988 748 752
    • (1988) Blood , vol.71 , pp. 748-752
    • Steinberg, M.H.1    West, M.S.2    Gallagher, D.3    Mentzer, W.4
  • 131
    • 0022973922 scopus 로고
    • Redox and energetic state of red blood cells in G6PD deficiency, heterozygous β-thalassemia and the combination of both
    • M. Magnani, V. Stocchi, F. Canestrari, L. Cucchiarini, O. Stocchi, and G.V. Coppa et al. Redox and energetic state of red blood cells in G6PD deficiency, heterozygous beta-thalassemia and the combination of both Acta Haematol. 75 1986 211 214 (Pubitemid 17184144)
    • (1986) Acta Haematologica , vol.75 , Issue.4 , pp. 211-214
    • Magnani, M.1    Stocchi, V.2    Canestrari, F.3
  • 132
    • 84872060345 scopus 로고    scopus 로고
    • The triumph of good over evil: Protection by the sickle gene against malaria
    • H.F. Bunn The triumph of good over evil: protection by the sickle gene against malaria Blood 121 2013 20 25
    • (2013) Blood , vol.121 , pp. 20-25
    • Bunn, H.F.1
  • 133
    • 0018854950 scopus 로고
    • Superoxide dismutase, glutathione peroxidase, catalase and lipid peroxidation of normal and sickled erythrocytes
    • S.K. Das, and R.C. Nair Superoxide dismutase, glutathione peroxidase, catalase and lipid peroxidation of normal and sickled erythrocytes Br. J. Haematol. 44 1980 87 92 (Pubitemid 10201711)
    • (1980) British Journal of Haematology , vol.44 , Issue.1 , pp. 87-92
    • Das, S.K.1    Nair, R.C.2
  • 134
    • 0021367031 scopus 로고
    • A novel phospholipid in irreversibly sickled cells: Evidence for in vivo peroxidative membrane damage in sickle cell disease
    • S.K. Jain, and S.B. Shohet A novel phospholipid in irreversibly sickled cells: evidence for in vivo peroxidative membrane damage in sickle cell disease Blood 63 1984 362 367 (Pubitemid 14188883)
    • (1984) Blood , vol.63 , Issue.2 , pp. 362-367
    • Jain, S.K.1    Shohet, S.B.2
  • 135
    • 0021280297 scopus 로고
    • Phagocytosis of sickle erythrocytes: Immunologic and oxidative determinants of hemolytic anemia
    • R.P. Hebbel, and W.J. Miller Phagocytosis of sickle erythrocytes: immunologic and oxidative determinants of hemolytic anemia Blood 64 1984 733 741 (Pubitemid 14073496)
    • (1984) Blood , vol.64 , Issue.3 , pp. 733-741
    • Hebbel, R.P.1    Miller, W.J.2
  • 136
    • 0021799078 scopus 로고
    • Abnormal redox status of membrane-protein thiols in sickle erythrocytes
    • B.H. Rank, J. Carlsson, and R.P. Hebbel Abnormal redox status of membrane-protein thiols in sickle erythrocytes J. Clin. Invest. 75 1985 1531 1537 (Pubitemid 15041445)
    • (1985) Journal of Clinical Investigation , vol.75 , Issue.5 , pp. 1531-1537
    • Rank, B.H.1    Carlsson, J.2    Hebbel, R.P.3
  • 137
    • 0023937376 scopus 로고
    • Excess heme in sickle erythrocyte inside-out membranes: Possible role in thiol oxidation
    • S.A. Kuross, B.H. Rank, and R.P. Hebbel Excess heme in sickle erythrocyte inside-out membranes: possible role in thiol oxidation Blood 71 1988 876 882
    • (1988) Blood , vol.71 , pp. 876-882
    • Kuross, S.A.1    Rank, B.H.2    Hebbel, R.P.3
  • 138
    • 0026099699 scopus 로고
    • Beyond hemoglobin polymerization: The red blood cell membrane and sickle disease pathophysiology
    • R.P. Hebbel Beyond hemoglobin polymerization: the red blood cell membrane and sickle disease pathophysiology Blood 77 1991 214 237
    • (1991) Blood , vol.77 , pp. 214-237
    • Hebbel, R.P.1
  • 139
    • 0035013525 scopus 로고    scopus 로고
    • Oxidative stress and erythrocyte damage in Kenyan children with severe Plasmodium falciparum malaria
    • DOI 10.1046/j.1365-2141.2001.02758.x
    • M.J. Griffiths, F. Ndungu, K.L. Baird, D.P. Muller, K. Marsh, and C.R. Newton Oxidative stress and erythrocyte damage in Kenyan children with severe Plasmodium falciparum malaria Br. J. Haematol. 113 2001 486 491 (Pubitemid 32523160)
    • (2001) British Journal of Haematology , vol.113 , Issue.2 , pp. 486-491
    • Griffiths, M.J.1    Ndungu, F.2    Baird, K.L.3    Muller, D.P.R.4    Marsh, K.5    Newton, C.R.J.C.6
  • 140
    • 0014944278 scopus 로고
    • Increased sickling of parasitised erythrocytes as mechanism of resistance against malaria in the sickle-cell trait
    • L. Luzzatto, E.S. Nwachuku-Jarrett, and S. Reddy Increased sickling of parasitised erythrocytes as mechanism of resistance against malaria in the sickle-cell trait Lancet 1 1970 319 321
    • (1970) Lancet , vol.1 , pp. 319-321
    • Luzzatto, L.1    Nwachuku-Jarrett, E.S.2    Reddy, S.3
  • 141
    • 0018125642 scopus 로고
    • Sickling rates of human AS red cells infected in vitro with Plasmodium falciparum malaria
    • E.F. Roth Jr., M. Friedman, Y. Ueda, I. Tellez, W. Trager, and R.L. Nagel Sickling rates of human AS red cells infected in vitro with Plasmodium falciparum malaria Science 202 1978 650 652 (Pubitemid 9055627)
    • (1978) Science , vol.202 , Issue.4368 , pp. 650-652
    • Roth Jr., E.F.1    Friedman, M.2    Ueda, Y.3
  • 142
    • 0018410383 scopus 로고
    • Oxidant damage mediates variant red cell resistance to malaria
    • DOI 10.1038/280245a0
    • M.J. Friedman Oxidant damage mediates variant red cell resistance to malaria Nature 280 1979 245 247 (Pubitemid 9227919)
    • (1979) Nature , vol.280 , Issue.5719 , pp. 245-247
    • Friedman, M.J.1
  • 143
    • 27844579180 scopus 로고    scopus 로고
    • Band 3/complement-mediated recognition and removal of normally senescent and pathological human erythrocytes
    • DOI 10.1159/000089839
    • P. Arese, F. Turrini, and E. Schwarzer Band 3/complement-mediated recognition and removal of normally senescent and pathological human erythrocytes Cell. Physiol. Biochem. 16 2005 133 146 (Pubitemid 41643014)
    • (2005) Cellular Physiology and Biochemistry , vol.16 , Issue.4-6 , pp. 133-146
    • Arese, P.1    Turrini, F.2    Schwarzer, E.3
  • 144
  • 145
    • 79960843530 scopus 로고    scopus 로고
    • Methaemalbumin formation in sickle cell disease: Effect on oxidative protein modification and HO-1 induction
    • M.S. Hanson, B. Piknova, A. Keszler, A.R. Diers, X. Wang, and M.T. Gladwin et al. Methaemalbumin formation in sickle cell disease: effect on oxidative protein modification and HO-1 induction Br. J. Haematol. 154 2011 502 511
    • (2011) Br. J. Haematol. , vol.154 , pp. 502-511
    • Hanson, M.S.1    Piknova, B.2    Keszler, A.3    Diers, A.R.4    Wang, X.5    Gladwin, M.T.6
  • 146
    • 78049442406 scopus 로고    scopus 로고
    • Signaling to heme oxygenase-1 and its anti-inflammatory therapeutic potential
    • A. Paine, B. Eiz-Vesper, R. Blasczyk, and S. Immenschuh Signaling to heme oxygenase-1 and its anti-inflammatory therapeutic potential Biochem. Pharmacol. 80 2010 1895 1903
    • (2010) Biochem. Pharmacol. , vol.80 , pp. 1895-1903
    • Paine, A.1    Eiz-Vesper, B.2    Blasczyk, R.3    Immenschuh, S.4
  • 147
    • 33645945014 scopus 로고    scopus 로고
    • Heme oxygenase-1/carbon monoxide: From basic science to therapeutic applications
    • S.W. Ryter, J. Alam, and A.M. Choi Heme oxygenase-1/carbon monoxide: from basic science to therapeutic applications Physiol. Rev. 86 2006 583 650
    • (2006) Physiol. Rev. , vol.86 , pp. 583-650
    • Ryter, S.W.1    Alam, J.2    Choi, A.M.3
  • 148
    • 0029052741 scopus 로고
    • Cloning the P. Falciparum gene encoding PfEMP1 a malarial variant antigen and adherence receptor on the surface of parasitized human erythrocytes
    • D.I. Baruch, B.L. Pasloske, H.B. Singh, X. Bi, X.C. Ma, and M. Feldman et al. Cloning the P. falciparum gene encoding PfEMP1, a malarial variant antigen and adherence receptor on the surface of parasitized human erythrocytes Cell 82 1995 77 87
    • (1995) Cell , vol.82 , pp. 77-87
    • Baruch, D.I.1    Pasloske, B.L.2    Singh, H.B.3    Bi, X.4    Ma, X.C.5    Feldman, M.6
  • 149
    • 84863836958 scopus 로고    scopus 로고
    • Abnormal PfEMP1/knob display on Plasmodium falciparum-infected erythrocytes containing hemoglobin variants: Fresh insights into malaria pathogenesis and protection
    • R.M. Fairhurst, C.D. Bess, and M.A. Krause Abnormal PfEMP1/knob display on Plasmodium falciparum-infected erythrocytes containing hemoglobin variants: fresh insights into malaria pathogenesis and protection Microbes Infect. 14 2012 851 862
    • (2012) Microbes Infect. , vol.14 , pp. 851-862
    • Fairhurst, R.M.1    Bess, C.D.2    Krause, M.A.3
  • 150
    • 0015123715 scopus 로고
    • Plasmodium falciparum malaria: Ultrastructure of parasitized erythrocytes in cardiac vessels
    • S.A. Luse, and L.H. Miller Plasmodium falciparum malaria: ultrastructure of parasitized erythrocytes in cardiac vessels Am. J. Trop. Med. Hyg. 20 1971 655 660
    • (1971) Am. J. Trop. Med. Hyg. , vol.20 , pp. 655-660
    • Luse, S.A.1    Miller, L.H.2
  • 153
    • 84862062566 scopus 로고    scopus 로고
    • Alpha-Thalassemia impairs the cytoadherence of Plasmodium falciparum-infected erythrocytes
    • M.A. Krause, S.A. Diakite, T.M. Lopera-Mesa, C. Amaratunga, T. Arie, and K. Traore et al. alpha-Thalassemia impairs the cytoadherence of Plasmodium falciparum-infected erythrocytes PLoS One 7 2012 e37214
    • (2012) PLoS One , vol.7 , pp. 37214
    • Krause, M.A.1    Diakite, S.A.2    Lopera-Mesa, T.M.3    Amaratunga, C.4    Arie, T.5    Traore, K.6
  • 154
    • 84865151210 scopus 로고    scopus 로고
    • Translocation of sickle cell erythrocyte microRNAs into Plasmodium falciparum inhibits parasite translation and contributes to malaria resistance
    • G. LaMonte, N. Philip, J. Reardon, J.R. Lacsina, W. Majoros, and L. Chapman et al. Translocation of sickle cell erythrocyte microRNAs into Plasmodium falciparum inhibits parasite translation and contributes to malaria resistance Cell Host Microbe 12 2012 187 199
    • (2012) Cell Host Microbe , vol.12 , pp. 187-199
    • Lamonte, G.1    Philip, N.2    Reardon, J.3    Lacsina, J.R.4    Majoros, W.5    Chapman, L.6
  • 155
    • 78349257725 scopus 로고    scopus 로고
    • An improved red blood cell additive solution maintains 2,3-diphosphoglycerate and adenosine triphosphate levels by an enhancing effect on phosphofructokinase activity during cold storage
    • P. Burger, H. Korsten, D. De Korte, E. Rombout, R. Van Bruggen, and A.J. Verhoeven An improved red blood cell additive solution maintains 2,3-diphosphoglycerate and adenosine triphosphate levels by an enhancing effect on phosphofructokinase activity during cold storage Transfusion 50 2010 2386 2392
    • (2010) Transfusion , vol.50 , pp. 2386-2392
    • Burger, P.1    Korsten, H.2    De Korte, D.3    Rombout, E.4    Van Bruggen, R.5    Verhoeven, A.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.