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Volumn 17, Issue 3, 2010, Pages 151-164

Red blood cell proteomics;Protéomique du globule rouge

Author keywords

Comparative proteomics; Proteomics; Red blood cell; Transfusion medicine

Indexed keywords

ALPHA TUBULIN; ANKYRIN; CARBON DIOXIDE; CARRIER PROTEIN; CATALASE; CHAPERONIN; CYTOSKELETON PROTEIN; ERYTHROCYTE BAND 4.1 PROTEIN; ERYTHROCYTE BAND 4.9 PROTEIN; ERYTHROCYTE ENZYME; FLOTILLIN 1; HEAT SHOCK PROTEIN; MEMBRANE PROTEIN; OXYGEN; PEROXIREDOXIN 1; PEROXIREDOXIN 3; PROTEASOME; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; RAB PROTEIN; STOMATIN; TROPOMYOSIN;

EID: 77955852283     PISSN: 12467820     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tracli.2010.05.010     Document Type: Short Survey
Times cited : (17)

References (92)
  • 4
    • 0002694308 scopus 로고
    • Haematologick studie u. psychotiku
    • Jansky J. Haematologick studie u. psychotiku. Sborn. Klinick 1907, 8:85-139.
    • (1907) Sborn. Klinick , vol.8 , pp. 85-139
    • Jansky, J.1
  • 5
    • 0000843125 scopus 로고
    • Zur Kenntnis der antifermentative, lytische und agglutinierenden Wirkungen des Blutzerums under der Lymphe
    • Landsteiner K. Zur Kenntnis der antifermentative, lytische und agglutinierenden Wirkungen des Blutzerums under der Lymphe. Zentralblatt Bakteriologie 1900, 27:357-362.
    • (1900) Zentralblatt Bakteriologie , vol.27 , pp. 357-362
    • Landsteiner, K.1
  • 6
    • 70449309280 scopus 로고
    • Structure of hemoglobin
    • Perutz M.F. Structure of hemoglobin. Brookhaven Symp Biol 1960, 13:165-183.
    • (1960) Brookhaven Symp Biol , vol.13 , pp. 165-183
    • Perutz, M.F.1
  • 7
    • 0036265634 scopus 로고    scopus 로고
    • Comparison of mechanisms of anemia in mice with sickle cell disease and beta-thalassemia: peripheral destruction, ineffective erythropoiesis, and phospholipid scramblase-mediated phosphatidylserine exposure
    • Kean L.S., Brown L.E., Nichols J.W., Mohandas N., Archer D.R., Hsu L.L. Comparison of mechanisms of anemia in mice with sickle cell disease and beta-thalassemia: peripheral destruction, ineffective erythropoiesis, and phospholipid scramblase-mediated phosphatidylserine exposure. Exp Hematol 2002, 30:394-402.
    • (2002) Exp Hematol , vol.30 , pp. 394-402
    • Kean, L.S.1    Brown, L.E.2    Nichols, J.W.3    Mohandas, N.4    Archer, D.R.5    Hsu, L.L.6
  • 8
    • 0034584411 scopus 로고    scopus 로고
    • Murine recessive hereditary spherocytosis, sph/sph, is caused by a mutation in the erythroid alpha-spectrin gene
    • Wandersee N.J., Birkenmeier C.S., Gifford E.J., Mohandas N., Barker J.E. Murine recessive hereditary spherocytosis, sph/sph, is caused by a mutation in the erythroid alpha-spectrin gene. Hematol J 2000, 1:235-242.
    • (2000) Hematol J , vol.1 , pp. 235-242
    • Wandersee, N.J.1    Birkenmeier, C.S.2    Gifford, E.J.3    Mohandas, N.4    Barker, J.E.5
  • 9
    • 0035469888 scopus 로고    scopus 로고
    • Short survival of phosphatidylserine-exposing red blood cells in murine sickle cell anemia
    • De Jong K., Emerson R.K., Butler J., Bastacky J., Mohandas N., Kuypers F.A. Short survival of phosphatidylserine-exposing red blood cells in murine sickle cell anemia. Blood 2001, 98:1577-1584.
    • (2001) Blood , vol.98 , pp. 1577-1584
    • De Jong, K.1    Emerson, R.K.2    Butler, J.3    Bastacky, J.4    Mohandas, N.5    Kuypers, F.A.6
  • 10
    • 0025239986 scopus 로고
    • The role of membrane skeletal-associated alpha-globin in the pathophysiology of beta-thalassemia
    • Sorensen S., Rubin E., Polster H., Mohandas N., Schrier S. The role of membrane skeletal-associated alpha-globin in the pathophysiology of beta-thalassemia. Blood 1990, 75:1333-1336.
    • (1990) Blood , vol.75 , pp. 1333-1336
    • Sorensen, S.1    Rubin, E.2    Polster, H.3    Mohandas, N.4    Schrier, S.5
  • 11
    • 0344337820 scopus 로고
    • Quantitative analysis of the normal and four alternative degrees of an inherited macrocytic anemia in the house mouse. I. Number and size of erythrocytes
    • Russel E.S., Fondal E.L. Quantitative analysis of the normal and four alternative degrees of an inherited macrocytic anemia in the house mouse. I. Number and size of erythrocytes. Blood 1951, 6:892-905.
    • (1951) Blood , vol.6 , pp. 892-905
    • Russel, E.S.1    Fondal, E.L.2
  • 12
    • 0013975185 scopus 로고
    • Development of mammalian erythroid cells
    • Marks P.A., Kovach J.S. Development of mammalian erythroid cells. Curr Top Dev Biol 1966, 1:213-252.
    • (1966) Curr Top Dev Biol , vol.1 , pp. 213-252
    • Marks, P.A.1    Kovach, J.S.2
  • 13
    • 0015172853 scopus 로고
    • The differentiation of haemopoietic stem cells
    • Dunn C.D. The differentiation of haemopoietic stem cells. Ser Haematol 1971, 4:1-71.
    • (1971) Ser Haematol , vol.4 , pp. 1-71
    • Dunn, C.D.1
  • 14
    • 0028843398 scopus 로고
    • The role of hematopoietic growth factors in transfusion medicine
    • Whitsett C.F. The role of hematopoietic growth factors in transfusion medicine. Hematol Oncol Clin North Am. 1985, 9:23-26.
    • (1985) Hematol Oncol Clin North Am. , vol.9 , pp. 23-26
    • Whitsett, C.F.1
  • 15
    • 0016074693 scopus 로고
    • Control of gene expression during erythroid cell differentiation
    • Marks P.A., Rifkind R.A., Bank A. Control of gene expression during erythroid cell differentiation. Adv Exp Med Biol 1974, 44:221-224.
    • (1974) Adv Exp Med Biol , vol.44 , pp. 221-224
    • Marks, P.A.1    Rifkind, R.A.2    Bank, A.3
  • 16
    • 77955851692 scopus 로고    scopus 로고
    • Deep-coverage rhesus red blood cell proteome: first comparison with the human and mouse red blood
    • Pasini EM, Kirkegaard M, Mortensen P, Mann M and Thomas AW. Deep-coverage rhesus red blood cell proteome: first comparison with the human and mouse red blood cell Blood Transfus 2010;8(Suppl 3):s126-39.
    • (2010) cell Blood Transfus , vol.8 , Issue.SUPPL. 3 , pp. 126-139
    • Pasini, E.M.1    Kirkegaard, M.2    Mortensen, P.3    Mann, M.4    Thomas, A.W.5
  • 17
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold R., Mann M. Mass spectrometry-based proteomics. Nature 2003, 422:198-207.
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 18
    • 67349266694 scopus 로고    scopus 로고
    • Universal sample preparation method for proteome analysis
    • Wiśniewski J.R., Zougman A., Nagaraj N., Mann M. Universal sample preparation method for proteome analysis. Nat Methods 2009, 6:359-362.
    • (2009) Nat Methods , vol.6 , pp. 359-362
    • Wiśniewski, J.R.1    Zougman, A.2    Nagaraj, N.3    Mann, M.4
  • 19
    • 51649107845 scopus 로고    scopus 로고
    • Highly efficient depletion strategy for the two most abundant erythrocyte soluble proteins improves proteome coverage dramatically
    • Ringrose J.H., van Solinge W.W., Mohammed S., O'Flaherty M.C., van Wijk R., Heck A.J., et al. Highly efficient depletion strategy for the two most abundant erythrocyte soluble proteins improves proteome coverage dramatically. J Proteome Res 2008, 7:3060-3063.
    • (2008) J Proteome Res , vol.7 , pp. 3060-3063
    • Ringrose, J.H.1    van Solinge, W.W.2    Mohammed, S.3    O'Flaherty, M.C.4    van Wijk, R.5    Heck, A.J.6
  • 20
    • 43149086780 scopus 로고    scopus 로고
    • Extensive analysis of the cytoplasmic proteome of human erythrocytes using the peptide ligand library technology and advanced mass spectrometry
    • Roux-Dalvai F., Gonzalez de Peredo A., Simó C., Guerrier L., Bouyssié D., Zanella A., et al. Extensive analysis of the cytoplasmic proteome of human erythrocytes using the peptide ligand library technology and advanced mass spectrometry. Mol Cell Proteomics 2008, 7:2254-2269.
    • (2008) Mol Cell Proteomics , vol.7 , pp. 2254-2269
    • Roux-Dalvai, F.1    Gonzalez de Peredo, A.2    Simó, C.3    Guerrier, L.4    Bouyssié, D.5    Zanella, A.6
  • 21
    • 0035107435 scopus 로고    scopus 로고
    • The effect of protease inhibitors on the two-dimensional electrophoresis pattern of red blood cell membranes
    • Olivieri E., Herbert B., Righetti P.G. The effect of protease inhibitors on the two-dimensional electrophoresis pattern of red blood cell membranes. Electrophoresis 2001, 22:560-565.
    • (2001) Electrophoresis , vol.22 , pp. 560-565
    • Olivieri, E.1    Herbert, B.2    Righetti, P.G.3
  • 22
    • 43949144961 scopus 로고    scopus 로고
    • Performance of combinatorial peptide libraries in capturing the low-abundance proteome of red blood cells. 2. Behavior of resins containing individual amino acids
    • Bachi A., Sim C., Restuccia U., Guerrier L., Fortis F., Boschetti E. Performance of combinatorial peptide libraries in capturing the low-abundance proteome of red blood cells. 2. Behavior of resins containing individual amino acids. Anal Chem 2008, 80:3557-3565.
    • (2008) Anal Chem , vol.80 , pp. 3557-3565
    • Bachi, A.1    Sim, C.2    Restuccia, U.3    Guerrier, L.4    Fortis, F.5    Boschetti, E.6
  • 23
    • 43949113653 scopus 로고    scopus 로고
    • Performance of combinatorial peptide libraries in capturing the low-abundance proteome of red blood cells. 1. Behavior of mono- to hexapeptides
    • Simo C., Bachi A., Cattaneo A., Guerrier L., Fortis F., Boschetti E. Performance of combinatorial peptide libraries in capturing the low-abundance proteome of red blood cells. 1. Behavior of mono- to hexapeptides. Anal Chem 2008, 80:3547-3556.
    • (2008) Anal Chem , vol.80 , pp. 3547-3556
    • Simo, C.1    Bachi, A.2    Cattaneo, A.3    Guerrier, L.4    Fortis, F.5    Boschetti, E.6
  • 24
    • 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, 36:13-24.
    • (2007) Vet Clin Pathol , vol.36 , pp. 13-24
    • Prenni, J.E.1    Avery, A.C.2    Olver, C.S.3
  • 25
    • 33746616420 scopus 로고    scopus 로고
    • In-depth analysis of the membrane and cytosolic proteome of red blood cells
    • Pasini E.M., Kirkegaard M., Mortensen P., Lutz H.U., Thomas A.W., Mann M. In-depth analysis of the membrane and cytosolic proteome of red blood cells. Blood 2006, 108:791-801.
    • (2006) Blood , vol.108 , pp. 791-801
    • Pasini, E.M.1    Kirkegaard, M.2    Mortensen, P.3    Lutz, H.U.4    Thomas, A.W.5    Mann, M.6
  • 26
    • 72149101507 scopus 로고    scopus 로고
    • Current knowledge about the functional roles of phosphorylative changes of membrane proteins in normal and diseased red cells
    • Pantaleo A., De Franceschi L., Ferru E., Vono R., Turrini F. Current knowledge about the functional roles of phosphorylative changes of membrane proteins in normal and diseased red cells. J Proteomics. 2010, 73(3):445-455.
    • (2010) J Proteomics. , vol.73 , Issue.3 , pp. 445-455
    • Pantaleo, A.1    De Franceschi, L.2    Ferru, E.3    Vono, R.4    Turrini, F.5
  • 27
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • Cox J., Mann M. MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat Biotechnol 2008, 26:1367-1372.
    • (2008) Nat Biotechnol , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 29
    • 0020788120 scopus 로고
    • The molecular organization of the red cell membrane skeleton
    • Cohen C.M. The molecular organization of the red cell membrane skeleton. Semin Hematol 1983, 20:141-158.
    • (1983) Semin Hematol , vol.20 , pp. 141-158
    • Cohen, C.M.1
  • 30
    • 0026697407 scopus 로고
    • Molecular anatomy of the red blood cell membrane skeleton: structure-function relationships
    • Liu S.C., Derick L.H. Molecular anatomy of the red blood cell membrane skeleton: structure-function relationships. Semin Hematol 1992, 29:231-243.
    • (1992) Semin Hematol , vol.29 , pp. 231-243
    • Liu, S.C.1    Derick, L.H.2
  • 33
    • 35348927453 scopus 로고    scopus 로고
    • Brain uptake and utilization of fatty acids, lipids & lipoproteins: recommendations for future research
    • Katz R., Hamilton J.A., Pownall H.J., Deckelbaum R.J. Brain uptake and utilization of fatty acids, lipids & lipoproteins: recommendations for future research. J Mol Neurosci 2007, 33:146-150.
    • (2007) J Mol Neurosci , vol.33 , pp. 146-150
    • Katz, R.1    Hamilton, J.A.2    Pownall, H.J.3    Deckelbaum, R.J.4
  • 35
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown D.A., London E. Functions of lipid rafts in biological membranes. Annu Rev Cell Dev Biol 1998, 14:111-136.
    • (1998) Annu Rev Cell Dev Biol , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 36
    • 0035865744 scopus 로고    scopus 로고
    • Stomatin, flotillin-1, and flotillin-2 are major integral proteins of erythrocyte lipid rafts
    • Salzer U., Prohaska R. Stomatin, flotillin-1, and flotillin-2 are major integral proteins of erythrocyte lipid rafts. Blood 2001, 97:1141-1143.
    • (2001) Blood , vol.97 , pp. 1141-1143
    • Salzer, U.1    Prohaska, R.2
  • 37
    • 72149110713 scopus 로고
    • Grune and Stratton, New York, R.I. Weed, E.R. Jaffe, P.A. Miescher (Eds.)
    • Cooper R.A. The red cell membrane 1970, 48-74. Grune and Stratton, New York. R.I. Weed, E.R. Jaffe, P.A. Miescher (Eds.).
    • (1970) The red cell membrane , pp. 48-74
    • Cooper, R.A.1
  • 38
    • 0017750532 scopus 로고
    • Abnormalities of cell-membrane fluidity in the pathogenesis of disease
    • Cooper R.A. Abnormalities of cell-membrane fluidity in the pathogenesis of disease. N Engl J Med 1977, 297:371-377.
    • (1977) N Engl J Med , vol.297 , pp. 371-377
    • Cooper, R.A.1
  • 39
  • 40
    • 10644245953 scopus 로고    scopus 로고
    • Use of mass spectrometry-based lipidomics to probe PITPalpha (phosphatidylinositol transfer protein alpha) function inside the nuclei of PITPalpha+/+ and PITPalpha-/- cells
    • Hunt A.N., Alb J.G., Koster G., Postle A.D., Bankaitis V.A. Use of mass spectrometry-based lipidomics to probe PITPalpha (phosphatidylinositol transfer protein alpha) function inside the nuclei of PITPalpha+/+ and PITPalpha-/- cells. Biochem Soc Trans 2004, 32:1063-1065.
    • (2004) Biochem Soc Trans , vol.32 , pp. 1063-1065
    • Hunt, A.N.1    Alb, J.G.2    Koster, G.3    Postle, A.D.4    Bankaitis, V.A.5
  • 41
    • 10644219528 scopus 로고    scopus 로고
    • Lipidomic analysis of the molecular specificity of a cholinephosphotransferase in situ
    • Hunt A.N., Fenn H.C., Clark G.T., Wright M.M. Lipidomic analysis of the molecular specificity of a cholinephosphotransferase in situ. Biochem Soc Trans 2004, 32:1060-1062.
    • (2004) Biochem Soc Trans , vol.32 , pp. 1060-1062
    • Hunt, A.N.1    Fenn, H.C.2    Clark, G.T.3    Wright, M.M.4
  • 42
    • 33947261547 scopus 로고    scopus 로고
    • Alterations in lipid homeostasis of mouse dorsal root ganglia induced by apolipoprotein E deficiency: a shotgun lipidomics study
    • Cheng H., Jiang X., Han X. Alterations in lipid homeostasis of mouse dorsal root ganglia induced by apolipoprotein E deficiency: a shotgun lipidomics study. J Neurochem 2007, 101:57-76.
    • (2007) J Neurochem , vol.101 , pp. 57-76
    • Cheng, H.1    Jiang, X.2    Han, X.3
  • 43
    • 34547840225 scopus 로고    scopus 로고
    • Exploring the lipoprotein composition using Bayesian regression on serum lipidomic profiles
    • Sysi-Aho M., Vehtari A., Velagapudi V.R., Westerbacka J. Exploring the lipoprotein composition using Bayesian regression on serum lipidomic profiles. Bioinformatics 2007, 23:i519-528.
    • (2007) Bioinformatics , vol.23
    • Sysi-Aho, M.1    Vehtari, A.2    Velagapudi, V.R.3    Westerbacka, J.4
  • 44
    • 70350735945 scopus 로고    scopus 로고
    • Enrichment of glycopeptides for glycan structure and attachment site identification
    • Nilsson J., Rüetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., et al. Enrichment of glycopeptides for glycan structure and attachment site identification. Nat Methods. 2009, 6(11):809-811.
    • (2009) Nat Methods. , vol.6 , Issue.11 , pp. 809-811
    • Nilsson, J.1    Rüetschi, U.2    Halim, A.3    Hesse, C.4    Carlsohn, E.5    Brinkmalm, G.6
  • 45
    • 24644454168 scopus 로고    scopus 로고
    • Extraction of leukemia specific glycan motifs in humans by computational glycomics
    • Hizukuri Y., Yamanishi Y., Nakamura O., Yagi F., Goto S., Kanehisa M. Extraction of leukemia specific glycan motifs in humans by computational glycomics. Carbohydr Res 2005, 340:2270-2278.
    • (2005) Carbohydr Res , vol.340 , pp. 2270-2278
    • Hizukuri, Y.1    Yamanishi, Y.2    Nakamura, O.3    Yagi, F.4    Goto, S.5    Kanehisa, M.6
  • 46
    • 33846609097 scopus 로고    scopus 로고
    • 2-D DIGE analysis of liver and red blood cells provides further evidence for oxidative stress in schizophrenia
    • Prabakaran S., Wengenroth M., Lockstone H.E., Lilley K., Leweke F.M., Bahn S. 2-D DIGE analysis of liver and red blood cells provides further evidence for oxidative stress in schizophrenia. J Proteome Res 2007, 6:141-149.
    • (2007) J Proteome Res , vol.6 , pp. 141-149
    • Prabakaran, S.1    Wengenroth, M.2    Lockstone, H.E.3    Lilley, K.4    Leweke, F.M.5    Bahn, S.6
  • 47
    • 0036746499 scopus 로고    scopus 로고
    • Separation of human erythrocyte membrane associated proteins with one-dimensional and two-dimensional gel electrophoresis followed by identification with matrix-assisted laser desorption/ionization-time of flight mass spectrometry
    • Low T.Y., Seow T.K., Chung M.C. Separation of human erythrocyte membrane associated proteins with one-dimensional and two-dimensional gel electrophoresis followed by identification with matrix-assisted laser desorption/ionization-time of flight mass spectrometry. Proteomics 2002, 2:1229-1239.
    • (2002) Proteomics , vol.2 , pp. 1229-1239
    • Low, T.Y.1    Seow, T.K.2    Chung, M.C.3
  • 48
    • 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, 3:501-509.
    • (2004) Mol Cell Proteomics , vol.3 , pp. 501-509
    • Kakhniashvili, D.G.1    Bulla, L.A.2    Goodman, S.R.3
  • 49
    • 20844445270 scopus 로고    scopus 로고
    • Proteomic profiling of erythrocyte proteins by proteolytic digestion chip and identification using two-dimensional electrospray ionization tandem mass spectrometry
    • Tyan Y.C., Jong S.B., Liao J.D., Liao P.C., Yang M.H., Liu C.Y., et al. Proteomic profiling of erythrocyte proteins by proteolytic digestion chip and identification using two-dimensional electrospray ionization tandem mass spectrometry. J Proteome Res 2005, 4:748-757.
    • (2005) J Proteome Res , vol.4 , pp. 748-757
    • Tyan, Y.C.1    Jong, S.B.2    Liao, J.D.3    Liao, P.C.4    Yang, M.H.5    Liu, C.Y.6
  • 52
    • 73649136853 scopus 로고    scopus 로고
    • The red blood cell proteome and interactome: an update
    • D'Alessandro A., Righetti P.G., Zolla L. The red blood cell proteome and interactome: an update. J Proteome Res. 2010, 9(1):144-163.
    • (2010) J Proteome Res. , vol.9 , Issue.1 , pp. 144-163
    • D'Alessandro, A.1    Righetti, P.G.2    Zolla, L.3
  • 53
    • 0029001840 scopus 로고
    • In vivo transfer of GPI-linked complement restriction factors from erythrocytes to the endothelium
    • Kooyman D.L., Byrne G.W., McClellan S., Nielsen D., Tone M., Waldmann H., et al. In vivo transfer of GPI-linked complement restriction factors from erythrocytes to the endothelium. Science 1995, 269:89-92.
    • (1995) Science , vol.269 , pp. 89-92
    • Kooyman, D.L.1    Byrne, G.W.2    McClellan, S.3    Nielsen, D.4    Tone, M.5    Waldmann, H.6
  • 54
    • 0347064345 scopus 로고    scopus 로고
    • C3b2-IgG complexes retain dimeric C3 fragments at all levels of inactivation
    • Jelezarova E., Luginbuehl A., Lutz H.U. C3b2-IgG complexes retain dimeric C3 fragments at all levels of inactivation. J Biol Chem 2003, 278:51806-51812.
    • (2003) J Biol Chem , vol.278 , pp. 51806-51812
    • Jelezarova, E.1    Luginbuehl, A.2    Lutz, H.U.3
  • 55
    • 0027337635 scopus 로고
    • Degradation of human erythrocyte surface components by human neutrophil elastase and cathepsin G: preferential digestion of glycophorins
    • Bykowska K., Duk M., Kusnierz-Alejska G., Kopec M., Lisowska E. Degradation of human erythrocyte surface components by human neutrophil elastase and cathepsin G: preferential digestion of glycophorins. Br J Haematol 1993, 84(4):736-742.
    • (1993) Br J Haematol , vol.84 , Issue.4 , pp. 736-742
    • Bykowska, K.1    Duk, M.2    Kusnierz-Alejska, G.3    Kopec, M.4    Lisowska, E.5
  • 56
    • 0024334725 scopus 로고
    • Novel action of carnitine: inhibition of aggregation of dispersed cells elicited by clusterin in vitro
    • Fritz I.B., Burdzy K. Novel action of carnitine: inhibition of aggregation of dispersed cells elicited by clusterin in vitro. J Cell Physiol 1989, 140(1):18-28.
    • (1989) J Cell Physiol , vol.140 , Issue.1 , pp. 18-28
    • Fritz, I.B.1    Burdzy, K.2
  • 57
    • 0028217573 scopus 로고
    • The adhesive specificity of the soluble human lectin, IgE-binding protein, toward lipid-linked oligosaccharides. Presence of the blood group A, B, B-like, and H monosaccharides confers a binding activity to tetrasaccharide (lacto-N-tetraose and lacto-N-neotetraose) backbones
    • Feizi T., Solomon J.C., Yuen C.T., Jeng K.C., Frigeri L.G., Hsu D.K., et al. The adhesive specificity of the soluble human lectin, IgE-binding protein, toward lipid-linked oligosaccharides. Presence of the blood group A, B, B-like, and H monosaccharides confers a binding activity to tetrasaccharide (lacto-N-tetraose and lacto-N-neotetraose) backbones. Biochemistry 1994, 33(20):6342-6349.
    • (1994) Biochemistry , vol.33 , Issue.20 , pp. 6342-6349
    • Feizi, T.1    Solomon, J.C.2    Yuen, C.T.3    Jeng, K.C.4    Frigeri, L.G.5    Hsu, D.K.6
  • 58
    • 0042386123 scopus 로고    scopus 로고
    • Analysis of selected blood and immune cell responses to carbohydrate-dependent surface binding of proto- and chimera-type galectins
    • Timoshenko A.V., Gorudko I.V., Maslakova O.V., Andre S., Kuwabara I., Liu F.T., et al. Analysis of selected blood and immune cell responses to carbohydrate-dependent surface binding of proto- and chimera-type galectins. Mol Cell Biochem 2003, 250(1-2):139-149.
    • (2003) Mol Cell Biochem , vol.250 , Issue.1-2 , pp. 139-149
    • Timoshenko, A.V.1    Gorudko, I.V.2    Maslakova, O.V.3    Andre, S.4    Kuwabara, I.5    Liu, F.T.6
  • 59
    • 0037351207 scopus 로고    scopus 로고
    • Lactoferrin-protector against oxidative stress and regulator of glycolysis in human erythrocytes
    • Maneva A., Taleva B., Maneva L. Lactoferrin-protector against oxidative stress and regulator of glycolysis in human erythrocytes. Z Naturforsch [C] 2003, 58:256-262.
    • (2003) Z Naturforsch [C] , vol.58 , pp. 256-262
    • Maneva, A.1    Taleva, B.2    Maneva, L.3
  • 60
    • 0026636590 scopus 로고
    • Antigenic determinants of senescent antigen of human erythrocytes are located in sialylated carbohydrate chains of band-3 glycoprotein
    • Beppu M., Mizukami A., Ando K., Kikugawa K. Antigenic determinants of senescent antigen of human erythrocytes are located in sialylated carbohydrate chains of band-3 glycoprotein. J Biol Chem 1992, 267:14691-14696.
    • (1992) J Biol Chem , vol.267 , pp. 14691-14696
    • Beppu, M.1    Mizukami, A.2    Ando, K.3    Kikugawa, K.4
  • 61
    • 0346079412 scopus 로고
    • Naturally occurring anti-band 3 antibodies and complement together mediate phagocytosis of oxidatively stressed human red blood cells
    • Lutz H.U., Bussolino F., Flepp R., Fasler S., Stammler P., Kazatchkine M.D., et al. Naturally occurring anti-band 3 antibodies and complement together mediate phagocytosis of oxidatively stressed human red blood cells. Proc Natl Acad Sci U S A 1987, 84:7368-7372.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 7368-7372
    • Lutz, H.U.1    Bussolino, F.2    Flepp, R.3    Fasler, S.4    Stammler, P.5    Kazatchkine, M.D.6
  • 62
    • 0027493863 scopus 로고
    • Naturally occurring anti-band 3 antibodies bind to protein rather than to carbohydrate on band 3
    • Lutz H.U., Gianora O., Nater M., Schweizer E., Stammler P. Naturally occurring anti-band 3 antibodies bind to protein rather than to carbohydrate on band 3. J Biol Chem 1993, 268:23562-23566.
    • (1993) J Biol Chem , vol.268 , pp. 23562-23566
    • Lutz, H.U.1    Gianora, O.2    Nater, M.3    Schweizer, E.4    Stammler, P.5
  • 63
    • 0023201992 scopus 로고
    • Prolactin binding sites in human erythrocytes and lymphocytes
    • Bellussi G., Muccioli G., Ghe C., Di Carlo R. Prolactin binding sites in human erythrocytes and lymphocytes. Life Sci 1987, 41(8):951-959.
    • (1987) Life Sci , vol.41 , Issue.8 , pp. 951-959
    • Bellussi, G.1    Muccioli, G.2    Ghe, C.3    Di Carlo, R.4
  • 64
    • 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, 30:171-192.
    • (1993) Semin Hematol , vol.30 , pp. 171-192
    • Mohandas, N.1    Chasis, J.A.2
  • 65
    • 72149106170 scopus 로고    scopus 로고
    • Red blood cell (RBC) membrane proteomics-Part I: Proteomics and RBC physiology
    • Pasini E.M., Lutz H.U., Mann M., Thomas A.W. Red blood cell (RBC) membrane proteomics-Part I: Proteomics and RBC physiology. J Proteomics 2010, 73:403-420.
    • (2010) J Proteomics , vol.73 , pp. 403-420
    • Pasini, E.M.1    Lutz, H.U.2    Mann, M.3    Thomas, A.W.4
  • 66
    • 72149087442 scopus 로고    scopus 로고
    • Red blood cell (RBC) membrane proteomics-Part II: Comparative proteomics and RBC patho-physiology
    • Pasini E.M., Lutz H.U., Mann M., Thomas A.W. Red blood cell (RBC) membrane proteomics-Part II: Comparative proteomics and RBC patho-physiology. J Proteomics 2010, 73(3):421-435.
    • (2010) J Proteomics , vol.73 , Issue.3 , pp. 421-435
    • Pasini, E.M.1    Lutz, H.U.2    Mann, M.3    Thomas, A.W.4
  • 67
    • 47749086651 scopus 로고    scopus 로고
    • Proteomics and transfusion medicine
    • Zolla L. Proteomics and transfusion medicine. Blood Transfus 2008, 6:67-69.
    • (2008) Blood Transfus , vol.6 , pp. 67-69
    • Zolla, L.1
  • 68
    • 34548181867 scopus 로고    scopus 로고
    • Proteomic analysis of RBC membrane protein degradation during blood storage
    • D'Amici G.M., Rinalducci S., Zolla L. Proteomic analysis of RBC membrane protein degradation during blood storage. J Proteome Res 2007, 6:3242-3255.
    • (2007) J Proteome Res , vol.6 , pp. 3242-3255
    • D'Amici, G.M.1    Rinalducci, S.2    Zolla, L.3
  • 69
    • 26944439128 scopus 로고    scopus 로고
    • Proteomic analysis of supernatants of stored red blood cell products
    • Anniss A.M., Glenister K.M., Killian J.J., Sparrow R.L. Proteomic analysis of supernatants of stored red blood cell products. Transfusion 2005, 45:1426-1433.
    • (2005) Transfusion , vol.45 , pp. 1426-1433
    • Anniss, A.M.1    Glenister, K.M.2    Killian, J.J.3    Sparrow, R.L.4
  • 70
  • 72
    • 32344450806 scopus 로고    scopus 로고
    • Red blood cell age determines the impact of storage and leukocyte burden on cell adhesion molecules, glycophorin A and the release of annexin V
    • Sparrow R.L., Healey G., Patton K.A., Veale M.F. Red blood cell age determines the impact of storage and leukocyte burden on cell adhesion molecules, glycophorin A and the release of annexin V. Transfus Apher Sci 2006, 34:15-23.
    • (2006) Transfus Apher Sci , vol.34 , pp. 15-23
    • Sparrow, R.L.1    Healey, G.2    Patton, K.A.3    Veale, M.F.4
  • 74
    • 31444450865 scopus 로고    scopus 로고
    • ETO2 coordinates cellular proliferation and differentiation during erythropoiesis
    • Goardon N., Lambert J.A., Rodriguez P., Nissaire P. ETO2 coordinates cellular proliferation and differentiation during erythropoiesis. Embo J 2006, 25:357-366.
    • (2006) Embo J , vol.25 , pp. 357-366
    • Goardon, N.1    Lambert, J.A.2    Rodriguez, P.3    Nissaire, P.4
  • 75
    • 33744926266 scopus 로고    scopus 로고
    • Quantitative proteomics reveals posttranslational control as a regulatory factor in primary hematopoietic stem cells
    • Unwin R.D., Smith D.L., Blinco D., Wilson C.L. Quantitative proteomics reveals posttranslational control as a regulatory factor in primary hematopoietic stem cells. Blood 2006, 107:4687-4694.
    • (2006) Blood , vol.107 , pp. 4687-4694
    • Unwin, R.D.1    Smith, D.L.2    Blinco, D.3    Wilson, C.L.4
  • 76
    • 10744223084 scopus 로고    scopus 로고
    • Dynamic changes in transcription factor complexes during erythroid differentiation revealed by quantitative proteomics
    • Brand M., Ranish J.A., Kummer N.T., Hamilton J. Dynamic changes in transcription factor complexes during erythroid differentiation revealed by quantitative proteomics. Nat Struct Mol Biol 2004, 11:73-80.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 73-80
    • Brand, M.1    Ranish, J.A.2    Kummer, N.T.3    Hamilton, J.4
  • 78
    • 20644450797 scopus 로고    scopus 로고
    • A quantitative proteomic approach using two-dimensional gel electrophoresis and isotope-coded affinity tag labeling for studying human 20S proteasome heterogeneity
    • Froment C., Uttenweiler-Joseph S., Bousquet-Dubouch M.P., Matondo M. A quantitative proteomic approach using two-dimensional gel electrophoresis and isotope-coded affinity tag labeling for studying human 20S proteasome heterogeneity. Proteomics 2005, 5:2351-2363.
    • (2005) Proteomics , vol.5 , pp. 2351-2363
    • Froment, C.1    Uttenweiler-Joseph, S.2    Bousquet-Dubouch, M.P.3    Matondo, M.4
  • 79
    • 38349078489 scopus 로고    scopus 로고
    • Membrane raft actin deficiency and altered Ca(2+)-induced vesiculation in stomatin-deficient overhydrated hereditary stomatocytosis
    • Wilkinson D.K., Turner E.J., Parkin E.T., Garner A.E. Membrane raft actin deficiency and altered Ca(2+)-induced vesiculation in stomatin-deficient overhydrated hereditary stomatocytosis. Biochim Biophys Acta 2008, 1778:125-132.
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 125-132
    • Wilkinson, D.K.1    Turner, E.J.2    Parkin, E.T.3    Garner, A.E.4
  • 80
    • 41149083080 scopus 로고    scopus 로고
    • Characterization of the N-glycosylation phenotype of erythrocyte membrane proteins in congenital dyserythropoietic anemia type II (CDA II/HEMPAS)
    • Denecke J., Kranz C., Nimtz M., Conradt H.S. Characterization of the N-glycosylation phenotype of erythrocyte membrane proteins in congenital dyserythropoietic anemia type II (CDA II/HEMPAS). Glycoconj J 2008, 25:375-382.
    • (2008) Glycoconj J , vol.25 , pp. 375-382
    • Denecke, J.1    Kranz, C.2    Nimtz, M.3    Conradt, H.S.4
  • 81
    • 55849100726 scopus 로고    scopus 로고
    • PTPepsilon has a critical role in signaling transduction pathways and phosphoprotein network topology in red cells
    • De Franceschi L., Biondani A., Carta F., Turrini F., Laudanna C., Deana R., et al. PTPepsilon has a critical role in signaling transduction pathways and phosphoprotein network topology in red cells. Proteomics 2008, 8:4695-4708.
    • (2008) Proteomics , vol.8 , pp. 4695-4708
    • De Franceschi, L.1    Biondani, A.2    Carta, F.3    Turrini, F.4    Laudanna, C.5    Deana, R.6
  • 82
    • 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., Lopez M.F., Fleming M.D., Rivera A. SOD2-deficiency anemia: protein oxidation and altered protein expression reveal targets of damage, stress response, and antioxidant responsiveness. Blood 2004, 104:2565-2573.
    • (2004) Blood , vol.104 , pp. 2565-2573
    • Friedman, J.S.1    Lopez, M.F.2    Fleming, M.D.3    Rivera, A.4
  • 83
    • 5444239857 scopus 로고    scopus 로고
    • Innate immune and non-immune mediators of erythrocyte clearance
    • Lutz H.U. Innate immune and non-immune mediators of erythrocyte clearance. Cell Mol Biol (Noisy-le-grand) 2004, 50:107-116.
    • (2004) Cell Mol Biol (Noisy-le-grand) , vol.50 , pp. 107-116
    • Lutz, H.U.1
  • 84
    • 28944446014 scopus 로고    scopus 로고
    • The proteomics of sickle cell disease: profiling of erythrocyte membrane proteins by 2D-DIGE and tandem mass spectrometry
    • Kakhniashvili D.G., Griko N.B., Bulla L.A., Goodman S.R. The proteomics of sickle cell disease: profiling of erythrocyte membrane proteins by 2D-DIGE and tandem mass spectrometry. Exp Biol Med (Maywood) 2005, 230:787-792.
    • (2005) Exp Biol Med (Maywood) , vol.230 , pp. 787-792
    • Kakhniashvili, D.G.1    Griko, N.B.2    Bulla, L.A.3    Goodman, S.R.4
  • 85
    • 33749348212 scopus 로고    scopus 로고
    • Activated neutrophil-mediated sickle red blood cell adhesion to lung vascular endothelium: role of phosphatidylserine-exposed sickle red blood cells
    • Haynes J., Obiako B., King J.A., Hester R.B., Ofori-Acquah S. Activated neutrophil-mediated sickle red blood cell adhesion to lung vascular endothelium: role of phosphatidylserine-exposed sickle red blood cells. Am J Physiol Heart Circ Physiol 2006, 291:H1679-1685.
    • (2006) Am J Physiol Heart Circ Physiol , vol.291
    • Haynes, J.1    Obiako, B.2    King, J.A.3    Hester, R.B.4    Ofori-Acquah, S.5
  • 86
    • 38149032285 scopus 로고    scopus 로고
    • Hydroxyurea attenuates activated neutrophil-mediated sickle erythrocyte membrane phosphatidylserine exposure and adhesion to pulmonary vascular endothelium
    • Haynes J., Obiako B., Hester R.B., Baliga B.S., Stevens T. Hydroxyurea attenuates activated neutrophil-mediated sickle erythrocyte membrane phosphatidylserine exposure and adhesion to pulmonary vascular endothelium. Am J Physiol Heart Circ Physiol 2008, 294:H379-385.
    • (2008) Am J Physiol Heart Circ Physiol , vol.294
    • Haynes, J.1    Obiako, B.2    Hester, R.B.3    Baliga, B.S.4    Stevens, T.5
  • 87
    • 58749089719 scopus 로고    scopus 로고
    • Pharmaco-proteomic study of hydroxyurea-induced modifications in the sickle red blood cell membrane proteome
    • Ghatpande S.S., Choudhary P.K., Quinn C.T., Goodman S.R. Pharmaco-proteomic study of hydroxyurea-induced modifications in the sickle red blood cell membrane proteome. Exp Biol Med (Maywood) 2008, 233:1510-1517.
    • (2008) Exp Biol Med (Maywood) , vol.233 , pp. 1510-1517
    • Ghatpande, S.S.1    Choudhary, P.K.2    Quinn, C.T.3    Goodman, S.R.4
  • 89
    • 0043237377 scopus 로고    scopus 로고
    • Protein disregulation in red blood cell membranes of type 2 diabetic patients
    • Jiang M., Jia L., Jiang W., Hu X. Protein disregulation in red blood cell membranes of type 2 diabetic patients. Biochem Biophys Res Commun 2003, 309:196-200.
    • (2003) Biochem Biophys Res Commun , vol.309 , pp. 196-200
    • Jiang, M.1    Jia, L.2    Jiang, W.3    Hu, X.4
  • 90
    • 0036270751 scopus 로고    scopus 로고
    • Regulated transport of the glucose transporter GLUT4
    • Bryant N.J., Govers R., James D.E. Regulated transport of the glucose transporter GLUT4. Nat Rev Mol Cell Biol 2002, 3:267-277.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 267-277
    • Bryant, N.J.1    Govers, R.2    James, D.E.3
  • 91
    • 37849187930 scopus 로고    scopus 로고
    • Arginase-flotillin interaction brings arginase to red blood cell membrane
    • Jiang M., Ding Y., Su Y., Hu X. Arginase-flotillin interaction brings arginase to red blood cell membrane. FEBS Lett 2006, 580:6561-6564.
    • (2006) FEBS Lett , vol.580 , pp. 6561-6564
    • Jiang, M.1    Ding, Y.2    Su, Y.3    Hu, X.4


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