메뉴 건너뛰기




Volumn 47, Issue 2, 2011, Pages 85-94

Retraction notice to "Comparative proteomics reveals deficiency of NHE-1 (Slc9a1) in RBCs from the beta-adducin knockout mouse model of hemolytic anemia" [Blood Cells Mol. Dis. 47 (2011) 85-94];Comparative proteomics reveals deficiency of NHE-1 (Slc9a1) in RBCs from the beta-adducin knockout mouse model of hemolytic anemia

Author keywords

Adducin; Anemia; Label free proteomics; NHE 1; Red blood cell; Reticulocyte

Indexed keywords

ADDUCIN; ADENOSINE TRIPHOSPHATASE (CALCIUM); ALPHA ADDUCIN; BETA ADDUCIN; BETA3 INTEGRIN; CALNEXIN; CARRIER PROTEINS AND BINDING PROTEINS; CD71 ANTIGEN; CD98 ANTIGEN; CHAPERONIN CONTAINING TCP1; ERYTHROCYTE BAND 4.1 PROTEIN; FODRIN; GAMMA ADDUCIN 3; GLUCOSE REGULATED PROTEIN 78; HEAT SHOCK COGNATE PROTEIN 71; HEAT SHOCK PROTEIN; HEMOGLOBIN A; HEMOGLOBIN BETA CHAIN; HISTONE H2B; PHENYLHYDRAZINE; POLYADENYLIC ACID BINDING PROTEIN; POLYADENYLIC ACID BINDING PROTEIN 1; PROTEIN CAPZ; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; SODIUM PROTON EXCHANGE PROTEIN; SODIUM PROTON EXCHANGE PROTEIN 1; SOLUTE CARRIER FAMILY 14 MEMBER 1; THROMBOCYTE FACTOR 4; TROPOMODULIN; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 79960841051     PISSN: 10799796     EISSN: 10960961     Source Type: Journal    
DOI: 10.1016/j.bcmd.2011.12.007     Document Type: Erratum
Times cited : (1)

References (55)
  • 1
    • 0027333413 scopus 로고
    • The spectrin-based membrane skeleton and micron-scale organization of the plasma membrane
    • Bennett V., Gilligan D.M. The spectrin-based membrane skeleton and micron-scale organization of the plasma membrane. Annu. Rev. Cell Biol. 1993, 9:27-66.
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 27-66
    • Bennett, V.1    Gilligan, D.M.2
  • 2
    • 0022510339 scopus 로고
    • Erythrocyte membrane deformability and stability: two distinct membrane properties that are independently regulated by skeletal protein associations
    • Chasis J.A., Mohandas N. Erythrocyte membrane deformability and stability: two distinct membrane properties that are independently regulated by skeletal protein associations. J. Cell Biol. 1986, 103(2):343-350.
    • (1986) J. Cell Biol. , vol.103 , Issue.2 , pp. 343-350
    • Chasis, J.A.1    Mohandas, N.2
  • 3
    • 0027272883 scopus 로고
    • Red blood cell deformability, membrane material properties and shape: regulation by transmembrane, skeletal and cytosolic proteins and lipids
    • Mohandas N., Chasis J.A. Red blood cell deformability, membrane material properties and shape: regulation by transmembrane, skeletal and cytosolic proteins and lipids. Semin. Hematol. 1993, 30(3):171-192.
    • (1993) Semin. Hematol. , vol.30 , Issue.3 , pp. 171-192
    • Mohandas, N.1    Chasis, J.A.2
  • 4
    • 0020788331 scopus 로고
    • Red cell membrane skeletal defects in hereditary and acquired hemolytic anemias
    • Palek J., Lux S.E. Red cell membrane skeletal defects in hereditary and acquired hemolytic anemias. Semin. Hematol. 1983, 20(3):189-224.
    • (1983) Semin. Hematol. , vol.20 , Issue.3 , pp. 189-224
    • Palek, J.1    Lux, S.E.2
  • 5
    • 7944225427 scopus 로고    scopus 로고
    • Hereditary haemolytic anaemias: unexpected sequelae of mutations in the genes for erythroid membrane skeletal proteins
    • Birkenmeier C.S., Barker J.E. Hereditary haemolytic anaemias: unexpected sequelae of mutations in the genes for erythroid membrane skeletal proteins. J. Pathol. 2004, 204(4):450-459.
    • (2004) J. Pathol. , vol.204 , Issue.4 , pp. 450-459
    • Birkenmeier, C.S.1    Barker, J.E.2
  • 7
    • 1842422320 scopus 로고    scopus 로고
    • Identification of quantitative trait loci that modify the severity of hereditary spherocytosis in wan, a new mouse model of band-3 deficiency
    • Peters L.L., et al. Identification of quantitative trait loci that modify the severity of hereditary spherocytosis in wan, a new mouse model of band-3 deficiency. Blood 2004, 103(8):3233-3240.
    • (2004) Blood , vol.103 , Issue.8 , pp. 3233-3240
    • Peters, L.L.1
  • 8
    • 34547680212 scopus 로고    scopus 로고
    • Regulation of erythrocyte lifespan: do reactive oxygen species set the clock?
    • Hattangadi S.M., Lodish H.F. Regulation of erythrocyte lifespan: do reactive oxygen species set the clock?. J. Clin. Invest. 2007, 117(8):2075-2077.
    • (2007) J. Clin. Invest. , vol.117 , Issue.8 , pp. 2075-2077
    • Hattangadi, S.M.1    Lodish, H.F.2
  • 9
    • 34547699517 scopus 로고    scopus 로고
    • Foxo3 is required for the regulation of oxidative stress in erythropoiesis
    • Marinkovic D., et al. Foxo3 is required for the regulation of oxidative stress in erythropoiesis. J. Clin. Invest. 2007, 117(8):2133-2144.
    • (2007) J. Clin. Invest. , vol.117 , Issue.8 , pp. 2133-2144
    • Marinkovic, D.1
  • 10
    • 4944225788 scopus 로고    scopus 로고
    • SOD2-deficiency anemia: protein oxidation and altered protein expression reveal targets of damage, stress response, and antioxidant responsiveness
    • Friedman J.S., et al. SOD2-deficiency anemia: protein oxidation and altered protein expression reveal targets of damage, stress response, and antioxidant responsiveness. Blood 2004, 104(8):2565-2573.
    • (2004) Blood , vol.104 , Issue.8 , pp. 2565-2573
    • Friedman, J.S.1
  • 11
    • 0023682520 scopus 로고
    • Does the chemical instability of aspartyl and asparaginyl residues in proteins contribute to erythrocyte aging? The role of protein carboxyl methylation reactions
    • Lowenson J., Clarke S. Does the chemical instability of aspartyl and asparaginyl residues in proteins contribute to erythrocyte aging? The role of protein carboxyl methylation reactions. Blood Cells 1988, 14(1):103-118.
    • (1988) Blood Cells , vol.14 , Issue.1 , pp. 103-118
    • Lowenson, J.1    Clarke, S.2
  • 12
    • 0025996446 scopus 로고
    • Structural elements affecting the recognition of L-isoaspartyl residues by the L-isoaspartyl/D-aspartyl protein methyltransferase. Implications for the repair hypothesis
    • Lowenson J.D., Clarke S. Structural elements affecting the recognition of L-isoaspartyl residues by the L-isoaspartyl/D-aspartyl protein methyltransferase. Implications for the repair hypothesis. J. Biol. Chem. 1991, 266(29):19396-19406.
    • (1991) J. Biol. Chem. , vol.266 , Issue.29 , pp. 19396-19406
    • Lowenson, J.D.1    Clarke, S.2
  • 13
    • 1842493516 scopus 로고    scopus 로고
    • Spontaneous and targeted mutations in erythrocyte membrane skeleton genes: mouse models of hereditary spherocytosis
    • Oxford Press, New York, L.I. Zon (Ed.)
    • Peters L., Barker J. Spontaneous and targeted mutations in erythrocyte membrane skeleton genes: mouse models of hereditary spherocytosis. Clinical Medicine 2001, 582-608. Oxford Press, New York. L.I. Zon (Ed.).
    • (2001) Clinical Medicine , pp. 582-608
    • Peters, L.1    Barker, J.2
  • 14
    • 1942509531 scopus 로고    scopus 로고
    • Hereditary spherocytosis-defects in proteins that connect the membrane skeleton to the lipid bilayer
    • Eber S., Lux S.E. Hereditary spherocytosis-defects in proteins that connect the membrane skeleton to the lipid bilayer. Semin. Hematol. 2004, 41(2):118-141.
    • (2004) Semin. Hematol. , vol.41 , Issue.2 , pp. 118-141
    • Eber, S.1    Lux, S.E.2
  • 15
    • 0003050993 scopus 로고
    • Synthesis of spectrin and its assembly into the red blood cell cytoskeleton of normal and mutant mice
    • Liss, New York, NY, V. Beneet, S.E. Lux, C.M. Cohen, J. Palek (Eds.)
    • Barker JE B.D., Birkenmeier C.S. Synthesis of spectrin and its assembly into the red blood cell cytoskeleton of normal and mutant mice. Membrane Skeletons and Cytoskeletal-Membrane Associations 1986, 313-324. Liss, New York, NY. V. Beneet, S.E. Lux, C.M. Cohen, J. Palek (Eds.).
    • (1986) Membrane Skeletons and Cytoskeletal-Membrane Associations , pp. 313-324
    • Barker, J.E.B.D.1    Birkenmeier, C.S.2
  • 16
    • 0032521480 scopus 로고    scopus 로고
    • Complete deficiency of glycophorin A in red blood cells from mice with targeted inactivation of the band 3 (AE1) gene
    • Hassoun H., et al. Complete deficiency of glycophorin A in red blood cells from mice with targeted inactivation of the band 3 (AE1) gene. Blood 1998, 91(6):2146-2151.
    • (1998) Blood , vol.91 , Issue.6 , pp. 2146-2151
    • Hassoun, H.1
  • 17
    • 0032701977 scopus 로고    scopus 로고
    • Mild spherocytosis and altered red cell ion transport in protein 4. 2-null mice
    • Peters L.L., et al. Mild spherocytosis and altered red cell ion transport in protein 4. 2-null mice. J. Clin. Invest. 1999, 103(11):1527-1537.
    • (1999) J. Clin. Invest. , vol.103 , Issue.11 , pp. 1527-1537
    • Peters, L.L.1
  • 18
    • 0032844524 scopus 로고    scopus 로고
    • Targeted disruption of the beta adducin gene (Add2) causes red blood cell spherocytosis in mice
    • Gilligan D.M., et al. Targeted disruption of the beta adducin gene (Add2) causes red blood cell spherocytosis in mice. Proc. Natl. Acad. Sci. U. S. A. 1999, 96(19):10717-10722.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , Issue.19 , pp. 10717-10722
    • Gilligan, D.M.1
  • 19
    • 0022625338 scopus 로고
    • A new erythrocyte membrane-associated protein with calmodulin binding activity. Identification and purification
    • Gardner K., Bennett V. A new erythrocyte membrane-associated protein with calmodulin binding activity. Identification and purification. J. Biol. Chem. 1986, 261(3):1339-1348.
    • (1986) J. Biol. Chem. , vol.261 , Issue.3 , pp. 1339-1348
    • Gardner, K.1    Bennett, V.2
  • 20
    • 0034660403 scopus 로고    scopus 로고
    • Mild spherocytic hereditary elliptocytosis and altered levels of alpha- and gamma-adducins in beta-adducin-deficient mice
    • Muro A.F., et al. Mild spherocytic hereditary elliptocytosis and altered levels of alpha- and gamma-adducins in beta-adducin-deficient mice. Blood 2000, 95(12):3978-3985.
    • (2000) Blood , vol.95 , Issue.12 , pp. 3978-3985
    • Muro, A.F.1
  • 21
    • 33746616420 scopus 로고    scopus 로고
    • In-depth analysis of the membrane and cytosolic proteome of red blood cells
    • Pasini E.M., et al. In-depth analysis of the membrane and cytosolic proteome of red blood cells. Blood 2006, 108(3):791-801.
    • (2006) Blood , vol.108 , Issue.3 , pp. 791-801
    • Pasini, E.M.1
  • 22
    • 47549099572 scopus 로고    scopus 로고
    • SILAC mouse for quantitative proteomics uncovers kindlin-3 as an essential factor for red blood cell function
    • Kruger M., et al. SILAC mouse for quantitative proteomics uncovers kindlin-3 as an essential factor for red blood cell function. Cell 2008, 134(2):353-364.
    • (2008) Cell , vol.134 , Issue.2 , pp. 353-364
    • Kruger, M.1
  • 23
    • 39449131119 scopus 로고    scopus 로고
    • Label-free comparative analysis of proteomics mixtures using chromatographic alignment of high-resolution muLC-MS data
    • Finney G.L., et al. Label-free comparative analysis of proteomics mixtures using chromatographic alignment of high-resolution muLC-MS data. Anal. Chem. 2008, 80(4):961-971.
    • (2008) Anal. Chem. , vol.80 , Issue.4 , pp. 961-971
    • Finney, G.L.1
  • 24
    • 0017185162 scopus 로고
    • The removal of leukocytes and platelets from whole blood
    • Beutler E., West C., Blume K.G. The removal of leukocytes and platelets from whole blood. J. Lab. Clin. Med. 1976, 88(2):328-333.
    • (1976) J. Lab. Clin. Med. , vol.88 , Issue.2 , pp. 328-333
    • Beutler, E.1    West, C.2    Blume, K.G.3
  • 25
    • 0022897086 scopus 로고
    • The mechanism of removal of leukocytes by cellulose columns
    • Beutler E., Gelbart T. The mechanism of removal of leukocytes by cellulose columns. Blood Cells 1986, 12(1):57-64.
    • (1986) Blood Cells , vol.12 , Issue.1 , pp. 57-64
    • Beutler, E.1    Gelbart, T.2
  • 26
    • 0018865853 scopus 로고
    • Unequal alpha and beta globin mRNA in reticulocytes of normal and mutant f/f fetal mice
    • Chui D.H., Patterson M., Bayley S.T. Unequal alpha and beta globin mRNA in reticulocytes of normal and mutant f/f fetal mice. Br. J. Haematol. 1980, 44(3):431-439.
    • (1980) Br. J. Haematol. , vol.44 , Issue.3 , pp. 431-439
    • Chui, D.H.1    Patterson, M.2    Bayley, S.T.3
  • 27
    • 0242287052 scopus 로고    scopus 로고
    • Statistical methods for identifying differentially expressed genes in DNA microarrays
    • Storey J.D., Tibshirani R. Statistical methods for identifying differentially expressed genes in DNA microarrays. Methods Mol. Biol. 2003, 224:149-157.
    • (2003) Methods Mol. Biol. , vol.224 , pp. 149-157
    • Storey, J.D.1    Tibshirani, R.2
  • 28
    • 35748972060 scopus 로고    scopus 로고
    • Semi-supervised learning for peptide identification from shotgun proteomics datasets
    • Kall L., et al. Semi-supervised learning for peptide identification from shotgun proteomics datasets. Nat. Methods 2007, 4(11):923-925.
    • (2007) Nat. Methods , vol.4 , Issue.11 , pp. 923-925
    • Kall, L.1
  • 29
    • 2642551423 scopus 로고    scopus 로고
    • The human erythrocyte proteome: analysis by ion trap mass spectrometry
    • Kakhniashvili D.G., Bulla L.A., Goodman S.R. The human erythrocyte proteome: analysis by ion trap mass spectrometry. Mol. Cell. Proteomics 2004, 3(5):501-509.
    • (2004) Mol. Cell. Proteomics , vol.3 , Issue.5 , pp. 501-509
    • Kakhniashvili, D.G.1    Bulla, L.A.2    Goodman, S.R.3
  • 30
    • 14044251591 scopus 로고    scopus 로고
    • Assembly and regulation of a glycolytic enzyme complex on the human erythrocyte membrane
    • Campanella M.E., Chu H., Low P.S. Assembly and regulation of a glycolytic enzyme complex on the human erythrocyte membrane. Proc. Natl. Acad. Sci. U. S. A. 2005, 102(7):2402-2407.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , Issue.7 , pp. 2402-2407
    • Campanella, M.E.1    Chu, H.2    Low, P.S.3
  • 31
    • 34147162785 scopus 로고    scopus 로고
    • Proteomics: a review and an example using the reticulocyte membrane proteome
    • Prenni J.E., Avery A.C., Olver C.S. Proteomics: a review and an example using the reticulocyte membrane proteome. Vet. Clin. Pathol. 2007, 36(1):13-24.
    • (2007) Vet. Clin. Pathol. , vol.36 , Issue.1 , pp. 13-24
    • Prenni, J.E.1    Avery, A.C.2    Olver, C.S.3
  • 32
    • 0029022939 scopus 로고
    • Adducin: a physical model with implications for function in assembly of spectrin-actin complexes
    • Hughes C.A., Bennett V. Adducin: a physical model with implications for function in assembly of spectrin-actin complexes. J. Biol. Chem. 1995, 270(32):18990-18996.
    • (1995) J. Biol. Chem. , vol.270 , Issue.32 , pp. 18990-18996
    • Hughes, C.A.1    Bennett, V.2
  • 33
    • 4944242962 scopus 로고    scopus 로고
    • The erythrocyte skeletons of beta-adducin deficient mice have altered levels of tropomyosin, tropomodulin and EcapZ
    • Porro F., et al. The erythrocyte skeletons of beta-adducin deficient mice have altered levels of tropomyosin, tropomodulin and EcapZ. FEBS Lett. 2004, 576(1-2):36-40.
    • (2004) FEBS Lett. , vol.576 , Issue.1-2 , pp. 36-40
    • Porro, F.1
  • 34
    • 0032907043 scopus 로고    scopus 로고
    • Red blood cell membrane disorders
    • Tse W.T., Lux S.E. Red blood cell membrane disorders. Br. J. Haematol. 1999, 104(1):2-13.
    • (1999) Br. J. Haematol. , vol.104 , Issue.1 , pp. 2-13
    • Tse, W.T.1    Lux, S.E.2
  • 35
    • 33947495172 scopus 로고    scopus 로고
    • Combined deletion of mouse dematin-headpiece and beta-adducin exerts a novel effect on the spectrin-actin junctions leading to erythrocyte fragility and hemolytic anemia
    • Chen H., et al. Combined deletion of mouse dematin-headpiece and beta-adducin exerts a novel effect on the spectrin-actin junctions leading to erythrocyte fragility and hemolytic anemia. J. Biol. Chem. 2007, 282(6):4124-4135.
    • (2007) J. Biol. Chem. , vol.282 , Issue.6 , pp. 4124-4135
    • Chen, H.1
  • 36
    • 14644420159 scopus 로고    scopus 로고
    • Impairment of sodium pump and Na/H exchanger in erythrocytes from non-insulin dependent diabetes mellitus patients: effect of tea catechins
    • Rizvi S.I., Zaid M.A. Impairment of sodium pump and Na/H exchanger in erythrocytes from non-insulin dependent diabetes mellitus patients: effect of tea catechins. Clin. Chim. Acta 2005, 354(1-2):59-67.
    • (2005) Clin. Chim. Acta , vol.354 , Issue.1-2 , pp. 59-67
    • Rizvi, S.I.1    Zaid, M.A.2
  • 37
    • 38849204390 scopus 로고    scopus 로고
    • The plasma membrane calcium ATPase and disease
    • Tempel B.L., Shilling D.J. The plasma membrane calcium ATPase and disease. Subcell. Biochem. 2007, 45:365-383.
    • (2007) Subcell. Biochem. , vol.45 , pp. 365-383
    • Tempel, B.L.1    Shilling, D.J.2
  • 38
    • 1942541308 scopus 로고    scopus 로고
    • The hereditary stomatocytoses: genetic disorders of the red cell membrane permeability to monovalent cations
    • Delaunay J. The hereditary stomatocytoses: genetic disorders of the red cell membrane permeability to monovalent cations. Semin. Hematol. 2004, 41(2):165-172.
    • (2004) Semin. Hematol. , vol.41 , Issue.2 , pp. 165-172
    • Delaunay, J.1
  • 39
    • 0026578551 scopus 로고
    • Isolation of cDNA coding for an ubiquitous membrane protein deficient in high Na+, low K+ stomatocytic erythrocytes
    • Stewart G.W., et al. Isolation of cDNA coding for an ubiquitous membrane protein deficient in high Na+, low K+ stomatocytic erythrocytes. Blood 1992, 79(6):1593-1601.
    • (1992) Blood , vol.79 , Issue.6 , pp. 1593-1601
    • Stewart, G.W.1
  • 40
    • 0042338079 scopus 로고    scopus 로고
    • The "stomatin" gene and protein in overhydrated hereditary stomatocytosis
    • Fricke B., et al. The "stomatin" gene and protein in overhydrated hereditary stomatocytosis. Blood 2003, 102(6):2268-2277.
    • (2003) Blood , vol.102 , Issue.6 , pp. 2268-2277
    • Fricke, B.1
  • 41
    • 0033121167 scopus 로고    scopus 로고
    • Stomatocytosis is absent in "stomatin"-deficient murine red blood cells
    • Zhu Y., et al. Stomatocytosis is absent in "stomatin"-deficient murine red blood cells. Blood 1999, 93(7):2404-2410.
    • (1999) Blood , vol.93 , Issue.7 , pp. 2404-2410
    • Zhu, Y.1
  • 42
    • 0032708149 scopus 로고    scopus 로고
    • Association of stomatin with lipid-protein complexes in the plasma membrane and the endocytic compartment
    • Snyers L., Umlauf E., Prohaska R. Association of stomatin with lipid-protein complexes in the plasma membrane and the endocytic compartment. Eur. J. Cell Biol. 1999, 78(11):802-812.
    • (1999) Eur. J. Cell Biol. , vol.78 , Issue.11 , pp. 802-812
    • Snyers, L.1    Umlauf, E.2    Prohaska, R.3
  • 43
  • 44
    • 48549106230 scopus 로고    scopus 로고
    • NHE-1: a molecular target for signalling and cell matrix interactions
    • Koliakos G., Paletas K., Kaloyianni M. NHE-1: a molecular target for signalling and cell matrix interactions. Connect. Tissue Res. 2008, 49(3):157-161.
    • (2008) Connect. Tissue Res. , vol.49 , Issue.3 , pp. 157-161
    • Koliakos, G.1    Paletas, K.2    Kaloyianni, M.3
  • 45
    • 0344826013 scopus 로고    scopus 로고
    • Distribution of plasma membrane Ca2+ pump activity in normal human red blood cells
    • Lew V.L., et al. Distribution of plasma membrane Ca2+ pump activity in normal human red blood cells. Blood 2003, 102(12):4206-4213.
    • (2003) Blood , vol.102 , Issue.12 , pp. 4206-4213
    • Lew, V.L.1
  • 46
    • 34249088614 scopus 로고    scopus 로고
    • Plasma membrane calcium pump activity is affected by the membrane protein concentration: evidence for the involvement of the actin cytoskeleton
    • Vanagas L., et al. Plasma membrane calcium pump activity is affected by the membrane protein concentration: evidence for the involvement of the actin cytoskeleton. Biochim. Biophys. Acta 2007, 1768(6):1641-1649.
    • (2007) Biochim. Biophys. Acta , vol.1768 , Issue.6 , pp. 1641-1649
    • Vanagas, L.1
  • 47
    • 33745184932 scopus 로고    scopus 로고
    • Novel placental expression of 2,3-bisphosphoglycerate mutase
    • Pritlove D.C., et al. Novel placental expression of 2,3-bisphosphoglycerate mutase. Placenta 2006, 27(8):924-927.
    • (2006) Placenta , vol.27 , Issue.8 , pp. 924-927
    • Pritlove, D.C.1
  • 48
    • 27544472837 scopus 로고    scopus 로고
    • Ineffective erythropoiesis in mutant mice with deficient pyruvate kinase activity
    • Aizawa S., et al. Ineffective erythropoiesis in mutant mice with deficient pyruvate kinase activity. Exp. Hematol. 2005, 33(11):1292-1298.
    • (2005) Exp. Hematol. , vol.33 , Issue.11 , pp. 1292-1298
    • Aizawa, S.1
  • 49
    • 34447651120 scopus 로고    scopus 로고
    • Glycolytic inhibition by mutation of pyruvate kinase gene increases oxidative stress and causes apoptosis of a pyruvate kinase deficient cell line
    • Aisaki K., et al. Glycolytic inhibition by mutation of pyruvate kinase gene increases oxidative stress and causes apoptosis of a pyruvate kinase deficient cell line. Exp. Hematol. 2007, 35(8):1190-1200.
    • (2007) Exp. Hematol. , vol.35 , Issue.8 , pp. 1190-1200
    • Aisaki, K.1
  • 50
    • 46449103811 scopus 로고    scopus 로고
    • Peroxiredoxin 2 and peroxide metabolism in the erythrocyte
    • Low F.M., Hampton M.B., Winterbourn C.C. Peroxiredoxin 2 and peroxide metabolism in the erythrocyte. Antioxid. Redox Signal. 2008, 10(9):1621-1630.
    • (2008) Antioxid. Redox Signal. , vol.10 , Issue.9 , pp. 1621-1630
    • Low, F.M.1    Hampton, M.B.2    Winterbourn, C.C.3
  • 51
    • 10744233389 scopus 로고    scopus 로고
    • Peroxiredoxin II is essential for sustaining life span of erythrocytes in mice
    • Lee T.H., et al. Peroxiredoxin II is essential for sustaining life span of erythrocytes in mice. Blood 2003, 101(12):5033-5038.
    • (2003) Blood , vol.101 , Issue.12 , pp. 5033-5038
    • Lee, T.H.1
  • 52
    • 44449117859 scopus 로고    scopus 로고
    • Presence of cytosolic peroxiredoxin 2 in the erythrocyte membrane of patients with hereditary spherocytosis
    • Rocha S., et al. Presence of cytosolic peroxiredoxin 2 in the erythrocyte membrane of patients with hereditary spherocytosis. Blood Cells Mol. Dis. 2008, 41(1):5-9.
    • (2008) Blood Cells Mol. Dis. , vol.41 , Issue.1 , pp. 5-9
    • Rocha, S.1
  • 53
    • 68649102973 scopus 로고    scopus 로고
    • Linkage of cytosolic peroxiredoxin 2 to erythrocyte membrane imposed by hydrogen peroxide-induced oxidative stress
    • Rocha S., et al. Linkage of cytosolic peroxiredoxin 2 to erythrocyte membrane imposed by hydrogen peroxide-induced oxidative stress. Blood Cells Mol. Dis. 2009, 43(1):68-73.
    • (2009) Blood Cells Mol. Dis. , vol.43 , Issue.1 , pp. 68-73
    • Rocha, S.1
  • 54
    • 58149176138 scopus 로고    scopus 로고
    • Targeted deletion of alpha-adducin results in absent beta- and gamma-adducin, compensated hemolytic anemia, and lethal hydrocephalus in mice
    • Robledo R.F., et al. Targeted deletion of alpha-adducin results in absent beta- and gamma-adducin, compensated hemolytic anemia, and lethal hydrocephalus in mice. Blood 2008, 112:4298-4307.
    • (2008) Blood , vol.112 , pp. 4298-4307
    • Robledo, R.F.1
  • 55
    • 77950343144 scopus 로고    scopus 로고
    • Analysis of novel sph (spherocytosis) alleles in mice reveals allele-specific loss of band 3 and adducin in alpha-spectrin-deficient red cells
    • Robledo R.F., et al. Analysis of novel sph (spherocytosis) alleles in mice reveals allele-specific loss of band 3 and adducin in alpha-spectrin-deficient red cells. Blood 2010, 115:1804-1814.
    • (2010) Blood , vol.115 , pp. 1804-1814
    • Robledo, R.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.