메뉴 건너뛰기




Volumn 97, Issue 8, 1996, Pages 1804-1817

Defective anion transport and marked spherocytosis with membrane instability caused by hereditary total deficiency of red cell band 3 in cattle due to a nonsense mutation

Author keywords

acid base homeostasis; anion transport; band 3; hereditary spherocytosis; red cell membrane

Indexed keywords

ERYTHROCYTE BAND 3 PROTEIN;

EID: 15844377239     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/JCI118610     Document Type: Article
Times cited : (170)

References (62)
  • 1
    • 0022555859 scopus 로고
    • Structural aspects of the red cell anion exchanger protein
    • Jay. D., and L. Cantley. 1986. Structural aspects of the red cell anion exchanger protein Annu. Rev. Biochem. 55 511-538.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 511-538
    • Jay, D.1    Cantley, L.2
  • 2
    • 0024534816 scopus 로고
    • Structure and function of the red blood cell anion transport protein
    • Jennings, M.L. 1989. Structure and function of the red blood cell anion transport protein. Annu. Rev. Biophys. Biophys Chem. 18 397-430.
    • (1989) Annu. Rev. Biophys. Biophys Chem. , vol.18 , pp. 397-430
    • Jennings, M.L.1
  • 3
    • 0026070573 scopus 로고
    • The band 3-related anion exchanger (AE) gene family
    • Alper, S.L. 1991. The band 3-related anion exchanger (AE) gene family Annu Rev. Physiol. 53:549-564.
    • (1991) Annu Rev. Physiol. , vol.53 , pp. 549-564
    • Alper, S.L.1
  • 4
    • 0027410647 scopus 로고
    • Molecular and cellular biology of the erythrocyte anion exchanger (AE1)
    • Tanner, M.J A. 1993. Molecular and cellular biology of the erythrocyte anion exchanger (AE1). Semin. Hematol. 30:34-57.
    • (1993) Semin. Hematol. , vol.30 , pp. 34-57
    • Tanner, M.J.A.1
  • 5
    • 0020347505 scopus 로고
    • Chloride-bicarbonate exchanger in red blood cells: Physiology of transport and chemical modification of binding sites
    • Wieth, J.O., O.S. Andersen, J. Brahm. P.J. Bjerrum, and C.L. Borders. Jr. 1982 Chloride-bicarbonate exchanger in red blood cells: physiology of transport and chemical modification of binding sites. Phil. Trans. R. Soc. Lond. B299:383-399.
    • (1982) Phil. Trans. R. Soc. Lond. , vol.B299 , pp. 383-399
    • Wieth, J.O.1    Andersen, O.S.2    Brahm, J.3    Bjerrum, P.J.4    Borders Jr., C.L.5
  • 6
    • 0013547957 scopus 로고
    • pH equilibrium across the red cell membrane
    • J.C. Ellory and V.L Lew. editors. Academic Press, London
    • Hladkey, S.B., and TJ Rink. 1977. pH equilibrium across the red cell membrane. In Membrane Transport in Red Cells. J.C. Ellory and V.L Lew. editors. Academic Press, London. 115-135.
    • (1977) Membrane Transport in Red Cells , pp. 115-135
    • Hladkey, S.B.1    Rink, T.J.2
  • 7
    • 0023637333 scopus 로고
    • Immunochemical characterization of a band 3-like anion exchanger in collecting duct of human kidney
    • Wagner, S., R. Vogel, R. Lietzke, R Koob, and D. Drenckhahn. 1987. Immunochemical characterization of a band 3-like anion exchanger in collecting duct of human kidney Am. J Physiol 22:F213-F221.
    • (1987) Am. J Physiol , vol.22
    • Wagner, S.1    Vogel, R.2    Lietzke, R.3    Koob, R.4    Drenckhahn, D.5
  • 9
    • 0025896582 scopus 로고
    • Contribution of the band 3-ankyrin interaction to erythrocyte membrane mechanical stability
    • Low, P.S., B.M. Willardson, N. Mohandas, M Rossi, and S. Shohet 1991 Contribution of the band 3-ankyrin interaction to erythrocyte membrane mechanical stability. Blood 77:1581-1586.
    • (1991) Blood , vol.77 , pp. 1581-1586
    • Low, P.S.1    Willardson, B.M.2    Mohandas, N.3    Rossi, M.4    Shohet, S.5
  • 10
    • 0026549630 scopus 로고
    • Molecular basis for membrane rigidity of hereditary ovalocytosis. A novel mechanism involving the cytoplasmic domain of band 3
    • Mohandas, N., R. Winardi, D. Knowles, A. Leung, M. Parra, E. George, J. Conboy, and J. Chasis 1992. Molecular basis for membrane rigidity of hereditary ovalocytosis. A novel mechanism involving the cytoplasmic domain of band 3 J. Clin, Invest. 89:686-692.
    • (1992) J. Clin, Invest. , vol.89 , pp. 686-692
    • Mohandas, N.1    Winardi, R.2    Knowles, D.3    Leung, A.4    Parra, M.5    George, E.6    Conboy, J.7    Chasis, J.8
  • 12
    • 85086295599 scopus 로고
    • Melanesian hereditary ovalocytes have a deletion in red cell band 3
    • Tanner, M J.A., L. Brace, P G. Martin, D.M. Rearden, and G L. Jones. 1991. Melanesian hereditary ovalocytes have a deletion in red cell band 3 Blood 78.2785-2787
    • (1991) Blood , vol.78 , pp. 2785-2787
    • Tanner, M.J.A.1    Brace, L.2    Martin, P.G.3    Rearden, D.M.4    Jones, G.L.5
  • 14
    • 0026584441 scopus 로고
    • Defective anion transport activity of the abnormal band 3 in hereditary ovalocytic red blood cells
    • Schofield, A E., D.M. Reardon, and M.J.A. Tanner 1992. Defective anion transport activity of the abnormal band 3 in hereditary ovalocytic red blood cells. Nature (Lond ). 355.836-838.
    • (1992) Nature (Lond ) , vol.355 , pp. 836-838
    • Schofield, A.E.1    Reardon, D.M.2    Tanner, M.J.A.3
  • 15
    • 0026696751 scopus 로고
    • 327 substitution in the cytoplasmic domain of erythrocyte band 3 protein associated with spherocytic hemolytic anemia and partial deficiency of protein 4.2
    • 327 substitution in the cytoplasmic domain of erythrocyte band 3 protein associated with spherocytic hemolytic anemia and partial deficiency of protein 4.2. Blood. 80:523-529.
    • (1992) Blood , vol.80 , pp. 523-529
    • Jarolim, P.1    Palek, J.2    Rubin, H.L.3    Prchal, J.T.4    Korsgren, C.5    Cohen, C.M.6
  • 18
    • 0028939295 scopus 로고
    • Mutations of conserved arginines in the membrane domain of erythroid band 3 lead to a decrease in membrane-associated band 3 and to the phenotype of hereditary spherocytosis
    • Jarolim, P, H.L. Rubin, V. Brabec, L. Chrobak, A S. Zolotarev, S L Alper, C. Brugnara, H. Wichterle, and J. Palek. 1995 Mutations of conserved arginines in the membrane domain of erythroid band 3 lead to a decrease in membrane-associated band 3 and to the phenotype of hereditary spherocytosis. Blood 85:634-640.
    • (1995) Blood , vol.85 , pp. 634-640
    • Jarolim, P.1    Rubin, H.L.2    Brabec, V.3    Chrobak, L.4    Zolotarev, A.S.5    Alper, S.L.6    Brugnara, C.7    Wichterle, H.8    Palek, J.9
  • 19
    • 0026628758 scopus 로고
    • Mutations of the red blood cell membrane proteins, from clinical evaluation to detection of the underlying genetic defect
    • Palek, J., and K.E. Sahr. 1992. Mutations of the red blood cell membrane proteins, from clinical evaluation to detection of the underlying genetic defect. Blood. 80:308-330.
    • (1992) Blood , vol.80 , pp. 308-330
    • Palek, J.1    Sahr, K.E.2
  • 20
    • 0027429066 scopus 로고
    • Clinical expression and laboratory detection of red blood cell membrane protein mutations
    • Palek, J., and P. Jarolim. 1993 Clinical expression and laboratory detection of red blood cell membrane protein mutations. Semin. Hematol 30:249-283.
    • (1993) Semin. Hematol , vol.30 , pp. 249-283
    • Palek, J.1    Jarolim, P.2
  • 21
    • 0002751459 scopus 로고
    • Hereditary spherocytosis, elliptocytosis. and related disorders
    • E. Beutler, M.A. Lichtman, B.S. Coller, and TJ Kipps. editors. McGraw-Hill Inc., New York
    • Palek, J., and P. Jarolim. 1995. Hereditary spherocytosis, elliptocytosis. and related disorders. In Williams Hematology. 5th ed. E. Beutler, M.A. Lichtman, B.S. Coller, and TJ Kipps. editors. McGraw-Hill Inc., New York. 536-557.
    • (1995) Williams Hematology. 5th Ed. , pp. 536-557
    • Palek, J.1    Jarolim, P.2
  • 22
    • 0028027718 scopus 로고
    • The homozygous state for the band 3 protein mutation in Southeast Asian ovalocytosis may be lethal
    • Liu, S -C , P. Jarolim, H L. Rubin, J. Palek, D. Amato, K. Hassen, M. Zaik, and P. Sapak. 1994. The homozygous state for the band 3 protein mutation in Southeast Asian ovalocytosis may be lethal. Blood. 84.3590-3591
    • (1994) Blood , vol.84 , pp. 3590-3591
    • Liu, S.C.1    Jarolim, P.2    Rubin, H.L.3    Palek, J.4    Amato, D.5    Hassen, K.6    Zaik, M.7    Sapak, P.8
  • 23
    • 0013693875 scopus 로고
    • Osmotic fragility
    • W.J. Williams. E. Beutler, A.J. Erslev. and M.A Lichtman, editors. McGraw-Hill Inc., New York
    • Beutler, E. 1990 Osmotic fragility In Hematology. 4th ed. W.J. Williams. E. Beutler, A.J. Erslev. and M.A Lichtman, editors. McGraw-Hill Inc., New York. 1726-1728.
    • (1990) Hematology. 4th Ed. , pp. 1726-1728
    • Beutler, E.1
  • 24
    • 0024297285 scopus 로고
    • A new major transmembrane glycoprotein, gp155, in goat erythrocytes. Isolation and characterization of its association to cytoskeleton through binding with band 3-ankyrin complex
    • Inaba, M., and Y. Maede. 1988. A new major transmembrane glycoprotein, gp155, in goat erythrocytes. Isolation and characterization of its association to cytoskeleton through binding with band 3-ankyrin complex. J. Biol. Chem. 263:17763-17771
    • (1988) J. Biol. Chem. , vol.263 , pp. 17763-17771
    • Inaba, M.1    Maede, Y.2
  • 25
    • 0021360448 scopus 로고
    • Proteolytic digestion of band 3 from bovine erythrocyte membranes in membrane-bound and solubilized states
    • Makino, S., R. Monyama. T Kitahara, and S Koga 1984. Proteolytic digestion of band 3 from bovine erythrocyte membranes in membrane-bound and solubilized states. J. Biochem. (Tokyo). 95:1019-1029.
    • (1984) J. Biochem. (Tokyo) , vol.95 , pp. 1019-1029
    • Makino, S.1    Monyama, R.2    Kitahara, T.3    Koga, S.4
  • 26
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M M. 1976. A rapid and sensitive method for quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond.). 227:680-685.
    • (1970) Nature (Lond.) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 0022969120 scopus 로고
    • Na.K-ATPase in dog red cells, Immunolngical identification and maturation-associated degradation by the proteolytic system
    • Inaba, M., and Y. Maede. 1986. Na.K-ATPase in dog red cells, Immunolngical identification and maturation-associated degradation by the proteolytic system. J Biol. Chem 261:16099-16105.
    • (1986) J Biol. Chem , vol.261 , pp. 16099-16105
    • Inaba, M.1    Maede, Y.2
  • 29
    • 0024747461 scopus 로고
    • Antigenic determinants of the cytoplasmic domain of band 3 from bovine erythrocyte membrane
    • Moriyama, R., S. Kawamatsu, Y Kondo, M. Tomida, and S. Makino. 1989. Antigenic determinants of the cytoplasmic domain of band 3 from bovine erythrocyte membrane. Arch. Biochem. Biophys. 274:130-137.
    • (1989) Arch. Biochem. Biophys. , vol.274 , pp. 130-137
    • Moriyama, R.1    Kawamatsu, S.2    Kondo, Y.3    Tomida, M.4    Makino, S.5
  • 30
    • 0023918104 scopus 로고
    • Localization of the pyridoxal phosphate binding site at the COOH-terminal region of erythrocyte band 3 protein
    • Kawano, Y., K. Okubo, F Tokunaga, T. Miyata, S. Iwanaga, and N Hamasaki 1988 Localization of the pyridoxal phosphate binding site at the COOH-terminal region of erythrocyte band 3 protein. J. Biol Chem. 263:8232-8238.
    • (1988) J. Biol Chem. , vol.263 , pp. 8232-8238
    • Kawano, Y.1    Okubo, K.2    Tokunaga, F.3    Miyata, T.4    Iwanaga, S.5    Hamasaki, N.6
  • 31
    • 0025164978 scopus 로고
    • Two novel molecular isoforms of band 4.2 in Japanese Sika deer (Cervus nippon vesoensis, Heude) erythrocytes
    • Inaba, M., Y. Amano, and Y. Maede. 1990. Two novel molecular isoforms of band 4.2 in Japanese Sika deer (Cervus nippon vesoensis, Heude) erythrocytes. Biochim Biophys Acta. 1021:101-104.
    • (1990) Biochim Biophys Acta. , vol.1021 , pp. 101-104
    • Inaba, M.1    Amano, Y.2    Maede, Y.3
  • 32
    • 0024264841 scopus 로고
    • The complete amino acid sequence of the human erythrocyte membrane anion-transport protein deduced from the cDNA
    • Tanner, M.J.A., P.G Martin, and S. High. 1988. The complete amino acid sequence of the human erythrocyte membrane anion-transport protein deduced from the cDNA. Biochem. J 256.703-712.
    • (1988) Biochem. J , vol.256 , pp. 703-712
    • Tanner, M.J.A.1    Martin, P.G.2    High, S.3
  • 33
    • 0024316871 scopus 로고
    • Cloning and characterization of band 3, the human erythrocyte anion-exchange protein (AE1)
    • Lux, S.E., K.M. John, R.R. Koipito, and H.F. Lodish. 1989. Cloning and characterization of band 3, the human erythrocyte anion-exchange protein (AE1). Proc. Natl. Acad. Sci. USA. 86:9089-9093.
    • (1989) Proc. Natl. Acad. Sci. USA. , vol.86 , pp. 9089-9093
    • Lux, S.E.1    John, K.M.2    Koipito, R.R.3    Lodish, H.F.4
  • 34
    • 0028176402 scopus 로고
    • Amino acid sequences around exofacial proteolytic cleavage sites of band 3 from bovine and porcine erythrocytes
    • Moriyama, R., Y. Nagatomi, F Hoshino. and S. Makino. 1994. Amino acid sequences around exofacial proteolytic cleavage sites of band 3 from bovine and porcine erythrocytes. Int. J Biochem. 26:133-137.
    • (1994) Int. J Biochem. , vol.26 , pp. 133-137
    • Moriyama, R.1    Nagatomi, Y.2    Hoshino, F.3    Makino, S.4
  • 35
    • 0018217047 scopus 로고
    • Asymmetry of the red cell anion exchange system. Different mechanisms of reversible inhibition by N-(4-azido-2-nitorophenyl)-2-aminoethylsulfonate (NAP-taurine) at the inside and outside of the membrane
    • Knauf, P.A , S. Ship, W. Breuer, L. McCulloch, and A. Rothstein 1978 Asymmetry of the red cell anion exchange system. Different mechanisms of reversible inhibition by N-(4-azido-2-nitorophenyl)-2-aminoethylsulfonate (NAP-taurine) at the inside and outside of the membrane. J Gen Physiol. 72:607-630.
    • (1978) J Gen Physiol. , vol.72 , pp. 607-630
    • Knauf, P.A.1    Ship, S.2    Breuer, W.3    McCulloch, L.4    Rothstein, A.5
  • 36
    • 0018235775 scopus 로고
    • N-(4-Azido-2-nitrophenyl)-2-aminoethylsulfonate (NAP-taurine) as a photoaffinity probe for identifying membrane components containing the modifier site of the human red blood cell anion exchanger system
    • Knauf, P.A., W. Breuer, L. McCulloch, and A. Rothstein. 1978 N-(4-Azido-2-nitrophenyl)-2-aminoethylsulfonate (NAP-taurine) as a photoaffinity probe for identifying membrane components containing the modifier site of the human red blood cell anion exchanger system. J. Gen Physiol 72:631-649.
    • (1978) J. Gen Physiol , vol.72 , pp. 631-649
    • Knauf, P.A.1    Breuer, W.2    McCulloch, L.3    Rothstein, A.4
  • 37
    • 0020649864 scopus 로고
    • K562 cell anion exchange differs markedly from that of mature red blood cells
    • Law, F.-Y., R. Steinfeld, and P.A. Knauf 1983. K562 cell anion exchange differs markedly from that of mature red blood cells. Am J. Physiol. 244-C68-C74.
    • (1983) Am J. Physiol. , vol.244
    • Law, F.-Y.1    Steinfeld, R.2    Knauf, P.A.3
  • 40
    • 0028209353 scopus 로고
    • Red cell membrane protein band 4.2: Phenotypic, genetic, and electron microscopic aspects
    • Yawata, Y. 1994. Red cell membrane protein band 4.2: phenotypic, genetic, and electron microscopic aspects. Biochim. Biophys. Acta 1204:131-148
    • (1994) Biochim. Biophys. Acta , vol.1204 , pp. 131-148
    • Yawata, Y.1
  • 42
    • 0030043891 scopus 로고    scopus 로고
    • Electron microscopic evidence of impaired intramembrane particles and instability of the cytoskeletal network in band 4.2 deficiency in human red cells
    • Yawala, Y., A. Yawata, A Kanzaki, T Inoue, N. Okamoto, K. Uehira, M. Yasunaga, and Y. Nakamura. 1996. Electron microscopic evidence of impaired intramembrane particles and instability of the cytoskeletal network in band 4.2 deficiency in human red cells. Cell Motil. Cytoskeleton. 33:95-105.
    • (1996) Cell Motil. Cytoskeleton. , vol.33 , pp. 95-105
    • Yawala, Y.1    Yawata, A.2    Kanzaki, A.3    Inoue, T.4    Okamoto, N.5    Uehira, K.6    Yasunaga, M.7    Nakamura, Y.8
  • 43
    • 0023150141 scopus 로고
    • Visualization of the hexagonal lattice in the erythrocyte membrane skeleton
    • Liu, S.-C., L.H. Derick, and J. Palek. 1987. Visualization of the hexagonal lattice in the erythrocyte membrane skeleton. J. Cell Biol. 104:527-536.
    • (1987) J. Cell Biol. , vol.104 , pp. 527-536
    • Liu, S.-C.1    Derick, L.H.2    Palek, J.3
  • 44
    • 0344264678 scopus 로고
    • Haematology of the ox
    • R.K. Archer, and L.B Jeffcott, editors. Blackwell Scientific Publications, Oxford. UK
    • Doxey, D L. 1977 Haematology of the ox. In Comparative Clinical Hematology. R.K. Archer, and L.B Jeffcott, editors. Blackwell Scientific Publications, Oxford. UK. 215 pp.
    • (1977) Comparative Clinical Hematology
    • Doxey, D.L.1
  • 45
    • 0022922389 scopus 로고
    • Structure and function of the cytoplasmic domain of band 3: Center of erythrocyte membrane-peripheral protein interactions
    • Low, P.S. 1986. Structure and function of the cytoplasmic domain of band 3: center of erythrocyte membrane-peripheral protein interactions. Biochim. Biophys. Acta. 864:145-167.
    • (1986) Biochim. Biophys. Acta. , vol.864 , pp. 145-167
    • Low, P.S.1
  • 46
    • 0018279059 scopus 로고
    • The anion transport system of the red blood cell. The role of membrane protein evaluated by the use of 'probes '
    • Cabantchik, Z.I. , P.A. Knauf, and A. Rothstein. 1978. The anion transport system of the red blood cell. The role of membrane protein evaluated by the use of 'probes ' Biochim. Biophys. Acta. 515:239-302.
    • (1978) Biochim. Biophys. Acta. , vol.515 , pp. 239-302
    • Cabantchik, Z.I.1    Knauf, P.A.2    Rothstein, A.3
  • 47
    • 0025242929 scopus 로고
    • Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis
    • Cheng, S H., R.J. Gregory, J. Marshall, S Paul, D.W. Souza, G.A. White. C.R. O'Riordan, and A.E. Smith. 1990. Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis. Cell. 63: 827-834.
    • (1990) Cell , vol.63 , pp. 827-834
    • Cheng, S.H.1    Gregory, R.J.2    Marshall, J.3    Paul, S.4    Souza, D.W.5    White, G.A.6    O'Riordan, C.R.7    Smith, A.E.8
  • 48
    • 0028006681 scopus 로고
    • Intracellular turnover of cystic fibrosis transmembrane conductance regulator: Insufficient processing and rapid degradation of wild-type and mutant proteins
    • Ward, C.L., and R.R. Kopito. 1994. Intracellular turnover of cystic fibrosis transmembrane conductance regulator: insufficient processing and rapid degradation of wild-type and mutant proteins. J. Biol. Chem. 269.25710-25718.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25710-25718
    • Ward, C.L.1    Kopito, R.R.2
  • 49
    • 0028918239 scopus 로고
    • Co-expressed complementary fragments of the human red cell anion exchanger (band 3, AE1) generate stilbene disulfonate-sensitive anion transport
    • Groves, J.D., and M.J.A. Tanner. 1995. Co-expressed complementary fragments of the human red cell anion exchanger (band 3, AE1) generate stilbene disulfonate-sensitive anion transport. J Biol. Chem 270:9097-9105.
    • (1995) J Biol. Chem , vol.270 , pp. 9097-9105
    • Groves, J.D.1    Tanner, M.J.A.2
  • 50
    • 0000672457 scopus 로고
    • Metabolic regulation via intracellular pH
    • Busa, W.B., and R. Nuccitelli, 1984. Metabolic regulation via intracellular pH. Am. J. Physiol. 246:R409-R438.
    • (1984) Am. J. Physiol. , vol.246
    • Busa, W.B.1    Nuccitelli, R.2
  • 51
    • 0019554835 scopus 로고
    • Intracellular pH
    • Roos, A , and W.F. Boron. 1981. Intracellular pH. Physiol. Rev. 61:296-434.
    • (1981) Physiol. Rev. , vol.61 , pp. 296-434
    • Roos, A.1    Boron, W.F.2
  • 53
    • 0020006750 scopus 로고
    • Intracellular pH mediates action of insulin on glycolysis in frog skeletal muscle
    • Fidelman, M.L., S.H Seeholzer, K B. Walsh, and R.D. Moore. 1982. Intracellular pH mediates action of insulin on glycolysis in frog skeletal muscle. Am J. Physiol. 242:C87-C93.
    • (1982) Am J. Physiol. , vol.242
    • Fidelman, M.L.1    Seeholzer, S.H.2    Walsh, K.B.3    Moore, R.D.4
  • 54
    • 0018582489 scopus 로고
    • Correlation between insulin action upon glycolysis and changes in intracellular pH
    • Moore, R D., M.L. Fidelman, and S.H, Seeholzer. 1979. Correlation between insulin action upon glycolysis and changes in intracellular pH. Biochem. Biophys Res Commun. 91:905-910.
    • (1979) Biochem. Biophys Res Commun. , vol.91 , pp. 905-910
    • Moore, R.D.1    Fidelman, M.L.2    Seeholzer, S.H.3
  • 56
    • 0020076111 scopus 로고
    • The erythrocyte anion transport protein is cotranslationally inserted into microsomes
    • Braell, W.A., and H F Lodish. 1982. The erythrocyte anion transport protein is cotranslationally inserted into microsomes. Cell. 28-23-31
    • (1982) Cell , vol.28 , pp. 23-31
    • Braell, W.A.1    Lodish, H.F.2
  • 57
    • 0023021576 scopus 로고
    • Control of erythroid differentiation asynchronous expression of the anion transporter and the peripheral components of the membrane skeleton in AFV- and S13-transformed cells
    • Woods, C.M., B. Boyer, P.K. Vogt, and E. Lazarides. 1986 Control of erythroid differentiation asynchronous expression of the anion transporter and the peripheral components of the membrane skeleton in AFV- and S13-transformed cells J Cell Biol. 103:1789-1798
    • (1986) J Cell Biol. , vol.103 , pp. 1789-1798
    • Woods, C.M.1    Boyer, B.2    Vogt, P.K.3    Lazarides, E.4
  • 58
    • 0023583790 scopus 로고
    • Changes in erythroid membrane proteins during erythropoietin-mediated terminal differentiation
    • Koury, M.J., M.C. Bondurant, and S.S. Rana. 1987. Changes in erythroid membrane proteins during erythropoietin-mediated terminal differentiation. J. Cell Physiol 133:438-448.
    • (1987) J. Cell Physiol , vol.133 , pp. 438-448
    • Koury, M.J.1    Bondurant, M.C.2    Rana, S.S.3
  • 59
    • 0026747194 scopus 로고
    • Asynchronous synthesis of membrane skeletal proteins during terminal maturation of murine erythroblasts
    • Hanspal, M. J.S. Hanspal, R. Kalraiya, S.-C. Liu, K.E. Sahr, D. Howard, and J Palek. 1992. Asynchronous synthesis of membrane skeletal proteins during terminal maturation of murine erythroblasts. Blood. 80:530-539.
    • (1992) Blood , vol.80 , pp. 530-539
    • Hanspal, M.1    Hanspal, J.S.2    Kalraiya, R.3    Liu, S.-C.4    Sahr, K.E.5    Howard, D.6    Palek, J.7
  • 60
    • 0024461106 scopus 로고
    • Reticulocyte maturation and exosome release. Transferrin receptor containing exosomes shows multiple plasma membrane functions
    • Johnstone, R.M., A. Bianchini. and K. Teng. 1989. Reticulocyte maturation and exosome release. Transferrin receptor containing exosomes shows multiple plasma membrane functions. Blood. 74:1844-1851
    • (1989) Blood , vol.74 , pp. 1844-1851
    • Johnstone, R.M.1    Bianchini, A.2    Teng, K.3
  • 61
    • 0026719184 scopus 로고
    • Deamidation of human erythrocyte protein 4.1: Possible role in aging
    • Inaba, M , K.C Gupta, M. Kuwabara, T. Takahashi, E.J. Benz, Jr . and Y. Maede. 1992. Deamidation of human erythrocyte protein 4.1: possible role in aging. Blood. 79:3355-3361.
    • (1992) Blood , vol.79 , pp. 3355-3361
    • Inaba, M.1    Gupta, K.C.2    Kuwabara, M.3    Takahashi, T.4    Benz Jr., E.J.5    Maede, Y.6
  • 62
    • 0017727283 scopus 로고
    • Temperature-dependent changes of chloride transport kinetics in human red cells
    • Brahm. J. 1977. Temperature-dependent changes of chloride transport kinetics in human red cells. J. Gen. Physiol. 70:283-306.
    • (1977) J. Gen. Physiol. , vol.70 , pp. 283-306
    • Brahm, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.