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Volumn 14, Issue 4, 1997, Pages 155-165

The structure and function of band 3 (AE1): Recent developments (review)

Author keywords

Anion exchanger; Hereditary spherocytosis; Red cell membrane; Renal tubular acidosis

Indexed keywords

ANION EXCHANGE; CARBOXY TERMINAL SEQUENCE; ELLIPTOCYTOSIS; ERYTHROCYTE DISORDER; ERYTHROCYTE MEMBRANE; GENE MUTATION; GENE SEQUENCE; KIDNEY DISEASE; KIDNEY TUBULE ACIDOSIS; MEMBRANE STRUCTURE; MOLECULAR GENETICS; PRIORITY JOURNAL; REVIEW;

EID: 0031466796     PISSN: 09687688     EISSN: None     Source Type: Journal    
DOI: 10.3109/09687689709048178     Document Type: Review
Times cited : (189)

References (120)
  • 1
    • 0026070573 scopus 로고
    • The band 3-related anion exchanger family
    • Alper, S. L. (1991) The band 3-related anion exchanger family. Annual Reviews of Physiology, 53, 549-564.
    • (1991) Annual Reviews of Physiology , vol.53 , pp. 549-564
    • Alper, S.L.1
  • 2
    • 0002148088 scopus 로고
    • Renal acidification: Cellular mechanisms of tubular transport and regulation
    • E. E. Windhager, ed. (Oxford: Oxford University Press)
    • Alpern, R. J. and Rector, F. C. (1992) Renal acidification: cellular mechanisms of tubular transport and regulation. In Handbook of Physiology: Section 8, Renal Physiology, E. E. Windhager, ed. (Oxford: Oxford University Press), pp. 767-812.
    • (1992) Handbook of Physiology: Section 8, Renal Physiology , vol.8 , pp. 767-812
    • Alpern, R.J.1    Rector, F.C.2
  • 3
    • 0024804353 scopus 로고
    • Anion transport in oocytes of Xenopus laevis induced by expression of mouse erythroid band 3 protein-encoding cRNA and of a cRNA derivative obtained by site-directed mutagenesis at the stilbene disulphonate binding site
    • Bartel, D., Lepke, S., Layh-Schmitt, G., Legrum, B. and Passow, H. (1989) Anion transport in oocytes of Xenopus laevis induced by expression of mouse erythroid band 3 protein-encoding cRNA and of a cRNA derivative obtained by site-directed mutagenesis at the stilbene disulphonate binding site. EMBO Journal, 8, 3601-3609.
    • (1989) EMBO Journal , vol.8 , pp. 3601-3609
    • Bartel, D.1    Lepke, S.2    Layh-Schmitt, G.3    Legrum, B.4    Passow, H.5
  • 4
    • 0030280772 scopus 로고    scopus 로고
    • Poly-N-acetyllactosaminyl saccharide chains as determinants for anti-band 3 autoantibody binding to senescent and oxidised erythrocytes
    • Beppu, M., Ando, K. and Kikugawa, K. (1996) Poly-N-acetyllactosaminyl saccharide chains as determinants for anti-band 3 autoantibody binding to senescent and oxidised erythrocytes. Molecular and Cellular Biology, 42, 1007-1024.
    • (1996) Molecular and Cellular Biology , vol.42 , pp. 1007-1024
    • Beppu, M.1    Ando, K.2    Kikugawa, K.3
  • 5
    • 0027312707 scopus 로고
    • Band 3 HT, a human red cell variant associated with acanthocytosis and increased anion transport, carries the mutation Pro868→Leu in the membrane domain of band 3
    • Bruce, L. J., Kay, M. M. B., Lawrence, C. and Tanner, M. J. A. (1993) Band 3 HT, a human red cell variant associated with acanthocytosis and increased anion transport, carries the mutation Pro868→Leu in the membrane domain of band 3. Biochemical Journal, 293, 317-320.
    • (1993) Biochemical Journal , vol.293 , pp. 317-320
    • Bruce, L.J.1    Kay, M.M.B.2    Lawrence, C.3    Tanner, M.J.A.4
  • 8
    • 0003253899 scopus 로고
    • Southeast Asian ovalocytic (SAO) erythrocytes have a cold sensitive cation leak: Implications for studies of in vitro invasion of stored SAO red cells by Plasmodium falciparum malarial parasites
    • Bruce, L. J., Ring, S. M., Ridgwell, K., Reardon, D. M., Seymour, C., Van Dort, H. M., Low, P. S., Anstee, D. J. and Tanner, M. J. A. (1995a) Southeast Asian ovalocytic (SAO) erythrocytes have a cold sensitive cation leak: implications for studies of in vitro invasion of stored SAO red cells by Plasmodium falciparum malarial parasites. Blood, 86(Suppl. 1), 470a.
    • (1995) Blood , vol.86 , Issue.1 SUPPL.
    • Bruce, L.J.1    Ring, S.M.2    Ridgwell, K.3    Reardon, D.M.4    Seymour, C.5    Van Dort, H.M.6    Low, P.S.7    Anstee, D.J.8    Tanner, M.J.A.9
  • 9
    • 0028909047 scopus 로고
    • Changes in the blood group Wright antigens are associated with a mutation at amino acid 658 in band 3: A site of interaction of band 3 and glycophorin a under certain circumstances
    • Bruce, L. J., Ring, S. M., Anstee, D. J., Reid, M. E., Wilkinson, S. and Tanner, M. J. A. (1995b) Changes in the blood group Wright antigens are associated with a mutation at amino acid 658 in band 3: a site of interaction of band 3 and glycophorin A under certain circumstances. Blood, 85, 541-547.
    • (1995) Blood , vol.85 , pp. 541-547
    • Bruce, L.J.1    Ring, S.M.2    Anstee, D.J.3    Reid, M.E.4    Wilkinson, S.5    Tanner, M.J.A.6
  • 10
    • 0142064871 scopus 로고    scopus 로고
    • Structure-function relationships of band 3 variants
    • Bruce, L. J. and Tanner, M. J. A. (1996) Structure-function relationships of band 3 variants. Molecular and Cellular Biology, 42, 953-974.
    • (1996) Molecular and Cellular Biology , vol.42 , pp. 953-974
    • Bruce, L.J.1    Tanner, M.J.A.2
  • 13
    • 0026848311 scopus 로고
    • Human erythrocyte glycophorins: Protein and gene structure analysis
    • Cartron, J. P. and Rahuel, C. (1992) Human erythrocyte glycophorins: protein and gene structure analysis. Transfusion Medicine Reviews, 6, 63-92
    • (1992) Transfusion Medicine Reviews , vol.6 , pp. 63-92
    • Cartron, J.P.1    Rahuel, C.2
  • 14
    • 0026684606 scopus 로고
    • Enzymatic deglycosylation of human band 3, the anion transport protein of the erythrocyte membrane: Effect on protein structure and transport properties
    • Casey, J. R., Pirraglia, C. A. and Reithmeier, R. A. F. (1992) Enzymatic deglycosylation of human band 3, the anion transport protein of the erythrocyte membrane: effect on protein structure and transport properties. Journal of Biological Chemistry, 267, 11940-11948.
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 11940-11948
    • Casey, J.R.1    Pirraglia, C.A.2    Reithmeier, R.A.F.3
  • 15
    • 0028942944 scopus 로고
    • The role of cysteine residues in the erythrocyte plasma membrane anion exchange protein, AE1
    • Casey, J. R., Ding, Y. and Kopito, R. R. (1995) The role of cysteine residues in the erythrocyte plasma membrane anion exchange protein, AE1. Journal of Biological Chemistry, 270, 8521-8527.
    • (1995) Journal of Biological Chemistry , vol.270 , pp. 8521-8527
    • Casey, J.R.1    Ding, Y.2    Kopito, R.R.3
  • 16
    • 0028901486 scopus 로고
    • Loss of rotational mobility of band 3 proteins in human erythrocyte membranes induced by antibodies to glycophorin A
    • Che, A. and Cherry, R. J. (1995) Loss of rotational mobility of band 3 proteins in human erythrocyte membranes induced by antibodies to glycophorin A. Biophysical Journal, 68, 1881-1887.
    • (1995) Biophysical Journal , vol.68 , pp. 1881-1887
    • Che, A.1    Cherry, R.J.2
  • 17
    • 0027186112 scopus 로고
    • Aggregation of band 3 in hereditary ovalocytic red blood cell membranes. Electron microscopy and protein rotational diffusion studies
    • Che, A., Cherry, R. J., Bannister, L. H. and Dluzewski, A. R. (1993) Aggregation of band 3 in hereditary ovalocytic red blood cell membranes. Electron microscopy and protein rotational diffusion studies. Journal of Cell Science, 105, 655-660.
    • (1993) Journal of Cell Science , vol.105 , pp. 655-660
    • Che, A.1    Cherry, R.J.2    Bannister, L.H.3    Dluzewski, A.R.4
  • 18
    • 0029088843 scopus 로고
    • Four variant chicken erythroid anion exchangers. Role of alternative N-terminal sequences in intracellular targeting in transfected human erythroleukemia cells
    • Cox, K. H., Adair-Kirk, T. and Cox, J. V. (1995) Four variant chicken erythroid anion exchangers. Role of alternative N-terminal sequences in intracellular targeting in transfected human erythroleukemia cells. Journal of Biological Chemistry, 270, 19752-19760.
    • (1995) Journal of Biological Chemistry , vol.270 , pp. 19752-19760
    • Cox, K.H.1    Adair-Kirk, T.2    Cox, J.V.3
  • 19
    • 0030087575 scopus 로고    scopus 로고
    • Expression and characterisation of the human erythrocyte anion exchanger in a baculovirus/Sf-9 cell system
    • Dale, W. E., Textor, J. A., Mercer, R. W. and Simchowitz, L. (1996) Expression and characterisation of the human erythrocyte anion exchanger in a baculovirus/Sf-9 cell system. Protein Expression and Purification, 7, 1-11.
    • (1996) Protein Expression and Purification , vol.7 , pp. 1-11
    • Dale, W.E.1    Textor, J.A.2    Mercer, R.W.3    Simchowitz, L.4
  • 20
    • 0029084972 scopus 로고
    • Genetic disorders of red cell membranes
    • Delauney, J. (1995) Genetic disorders of red cell membranes. FEBS Letters, 369, 34-37.
    • (1995) FEBS Letters , vol.369 , pp. 34-37
    • Delauney, J.1
  • 22
    • 0028670772 scopus 로고
    • The major kidney AE1 isoform does not bind ankyrin (ANK1) in vitro
    • Ding, Y., Casey, J. R. and Kopito, R. R. (1994) The major kidney AE1 isoform does not bind ankyrin (ANK1) in vitro. Journal of Biological Chemistry, 269, 32201-32208.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 32201-32208
    • Ding, Y.1    Casey, J.R.2    Kopito, R.R.3
  • 23
    • 0027155339 scopus 로고
    • Human erythrocyte membrane band 3: Solubilisation and reconstitution into two-dimensional crystals
    • Dolder, M., Walz, T., Hefti, A. and Engel, A. (1993) Human erythrocyte membrane band 3: solubilisation and reconstitution into two-dimensional crystals. Journal of Molecular Biology, 231, 119-132.
    • (1993) Journal of Molecular Biology , vol.231 , pp. 119-132
    • Dolder, M.1    Walz, T.2    Hefti, A.3    Engel, A.4
  • 24
    • 0026778949 scopus 로고
    • Invasion of hereditary ovalocytes by Plasmodium falciparum in vitro and its relationship to intracellular ATP concentration
    • Dluzewski, A. R., Nash, G. B., Wilson, R. J. M., Rearden, D. M. and Gratzer, W. B. (1992) Invasion of hereditary ovalocytes by Plasmodium falciparum in vitro and its relationship to intracellular ATP concentration. Molecular and Biochemical Parasitology, 55, 1-8.
    • (1992) Molecular and Biochemical Parasitology , vol.55 , pp. 1-8
    • Dluzewski, A.R.1    Nash, G.B.2    Wilson, R.J.M.3    Rearden, D.M.4    Gratzer, W.B.5
  • 25
    • 0028784047 scopus 로고
    • Expression of band 3 anion exchanger induces chloride current and taurine transport: Structure-function analysis
    • Fievet, B., Gabillat, N., Borgese, F. and Motais, R. (1995) Expression of band 3 anion exchanger induces chloride current and taurine transport: structure-function analysis. EMBO Journal, 14, 5158-5169.
    • (1995) EMBO Journal , vol.14 , pp. 5158-5169
    • Fievet, B.1    Gabillat, N.2    Borgese, F.3    Motais, R.4
  • 26
    • 0021265108 scopus 로고
    • Structure of branched lactosaminoglycan, the carbohydrate moeity of band 3 isolated from adult erythrocytes
    • Fukuda, M., Dell, A., Oates, J. E. and Fukuda, M. N. (1984) Structure of branched lactosaminoglycan, the carbohydrate moeity of band 3 isolated from adult erythrocytes. Journal of Biological Chemistry, 259, 8260-8279.
    • (1984) Journal of Biological Chemistry , vol.259 , pp. 8260-8279
    • Fukuda, M.1    Dell, A.2    Oates, J.E.3    Fukuda, M.N.4
  • 27
    • 0024316827 scopus 로고
    • Lysine 539 of human band 3 is not essential for anion transport or inhibition by stilbene disulphonates
    • Garcia, A. M. and Lodish, H. F. (1989) Lysine 539 of human band 3 is not essential for anion transport or inhibition by stilbene disulphonates. Journal of Biological Chemistry, 264, 19607-19613.
    • (1989) Journal of Biological Chemistry , vol.264 , pp. 19607-19613
    • Garcia, A.M.1    Lodish, H.F.2
  • 29
    • 18844480226 scopus 로고    scopus 로고
    • Three different actions of phenylglyoxal on band 3 protein-mediated anion transport across the red blood cell membrane
    • Gartner, E. M., Liebold, K., Legrum, B., Fasold, H. and Passow, H. (1997) Three different actions of phenylglyoxal on band 3 protein-mediated anion transport across the red blood cell membrane. Biochimica et Biophysica Acta, 1323, 208-222.
    • (1997) Biochimica et Biophysica Acta , vol.1323 , pp. 208-222
    • Gartner, E.M.1    Liebold, K.2    Legrum, B.3    Fasold, H.4    Passow, H.5
  • 31
    • 0027166252 scopus 로고
    • Interaction between band 3 and ankyrin begins in early compartments of the secretory pathway and is essential for band 3 processing
    • Gomez, S. and Morgans, C. (1993) Interaction between band 3 and ankyrin begins in early compartments of the secretory pathway and is essential for band 3 processing. Journal of Biological Chemistry, 268, 19593-19597.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 19593-19597
    • Gomez, S.1    Morgans, C.2
  • 32
    • 0017813685 scopus 로고
    • Anion transport in relation to proteolytic dissection of band 3 protein
    • Grinstein, S., Ship, S. and Rothstein, A. (1978) Anion transport in relation to proteolytic dissection of band 3 protein. Biochimica et Biophysica Acta, 507, 294-304.
    • (1978) Biochimica et Biophysica Acta , vol.507 , pp. 294-304
    • Grinstein, S.1    Ship, S.2    Rothstein, A.3
  • 33
    • 0026499518 scopus 로고
    • Glycophorin a facilitates the expression of human band 3-mediated anion transport in Xenopus oocytes
    • Groves, J. D. and Tanner, M. J. A. (1992) Glycophorin A facilitates the expression of human band 3-mediated anion transport in Xenopus oocytes. Journal of Biological Chemistry, 267, 2163-2170.
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 2163-2170
    • Groves, J.D.1    Tanner, M.J.A.2
  • 34
    • 0028248240 scopus 로고
    • The role of N-glycosylation in the expression of human band 3-mediated anion transport
    • Groves, J. D. and Tanner, M. J. A. (1994a) The role of N-glycosylation in the expression of human band 3-mediated anion transport. Molecular Membrane Biology, 11, 31-38.
    • (1994) Molecular Membrane Biology , vol.11 , pp. 31-38
    • Groves, J.D.1    Tanner, M.J.A.2
  • 35
    • 0028363028 scopus 로고
    • The effects of glycophorin a on the expression of the human red cell anion transporter (band 3) in Xenopus oocytes
    • Groves, J. D. and Tanner, M. J. A. (1994b) The effects of glycophorin A on the expression of the human red cell anion transporter (band 3) in Xenopus oocytes. Journal of Membrane Biology, 140, 81-88.
    • (1994) Journal of Membrane Biology , vol.140 , pp. 81-88
    • Groves, J.D.1    Tanner, M.J.A.2
  • 36
    • 0028918239 scopus 로고
    • Co-expressed fragments of the human red cell anion exchanger (Band 3; AE1) generate stilbene disulfonate sensitive anion transport
    • Groves, J. D. and Tanner, M. J. A. (1995) Co-expressed fragments of the human red cell anion exchanger (Band 3; AE1) generate stilbene disulfonate sensitive anion transport. Journal of Biological Chemistry, 270, 9077-9105.
    • (1995) Journal of Biological Chemistry , vol.270 , pp. 9077-9105
    • Groves, J.D.1    Tanner, M.J.A.2
  • 37
    • 0029998532 scopus 로고    scopus 로고
    • Cell surface expression of the functional human red cell anion exchanger (band 3;AE1) in the yeast Saccharomyces cerevisiae
    • Groves, J. D., Falson, P., le Maire, M. and Tanner, M. J. A. (1996) Cell surface expression of the functional human red cell anion exchanger (band 3;AE1) in the yeast Saccharomyces cerevisiae. Proceedings of the National Academy of Sciences USA, 93, 12245-12250.
    • (1996) Proceedings of the National Academy of Sciences USA , vol.93 , pp. 12245-12250
    • Groves, J.D.1    Falson, P.2    Le Maire, M.3    Tanner, M.J.A.4
  • 38
    • 0030278948 scopus 로고    scopus 로고
    • Band 3 protein: Physiology, function and structure
    • Hamasaki, N. and Okubo, K. (1996) Band 3 protein: physiology, function and structure. Molecular and Cellular Biology, 42, 1025-1039.
    • (1996) Molecular and Cellular Biology , vol.42 , pp. 1025-1039
    • Hamasaki, N.1    Okubo, K.2
  • 40
    • 0026775240 scopus 로고
    • Biogenesis of normal and abnormal red blood cell membrane skeletons
    • Hanspal, M. and Palek, J. (1992) Biogenesis of normal and abnormal red blood cell membrane skeletons. Seminars in Hematology, 29, 305-325.
    • (1992) Seminars in Hematology , vol.29 , pp. 305-325
    • Hanspal, M.1    Palek, J.2
  • 41
    • 0029825262 scopus 로고    scopus 로고
    • Hereditary spherocytosis: A review of the clinical and molecular aspects of the disease
    • Hassoun, H. and Palek, J. (1996) Hereditary spherocytosis: a review of the clinical and molecular aspects of the disease. Blood Reviews, 10, 129-147.
    • (1996) Blood Reviews , vol.10 , pp. 129-147
    • Hassoun, H.1    Palek, J.2
  • 42
    • 0028131474 scopus 로고
    • Topology of the Glut1 glucose transporter deduced from glycosylation scanning mutagenesis
    • Hresko, R. C., Kruse, M., Strube, M. and Mueckler, M. (1994) Topology of the Glut1 glucose transporter deduced from glycosylation scanning mutagenesis. Journal of Biological Chemistry, 269, 20482-20488.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 20482-20488
    • Hresko, R.C.1    Kruse, M.2    Strube, M.3    Mueckler, M.4
  • 43
    • 0021885318 scopus 로고
    • A new variant of the anion transport protein in human erythrocytes
    • Hsu, L. and Morrison, M. (1985) A new variant of the anion transport protein in human erythrocytes. Biochemistry, 24, 3086-3090.
    • (1985) Biochemistry , vol.24 , pp. 3086-3090
    • Hsu, L.1    Morrison, M.2
  • 44
    • 0029921113 scopus 로고    scopus 로고
    • Human red cell Wright antigens: A genetic and evolutionary perspective on glycophorin A-band 3 interaction
    • Huang, C.-H., Reid, M. E., Xie, S.-S. and Blumenfeld, O. O. (1996) Human red cell Wright antigens: a genetic and evolutionary perspective on glycophorin A-band 3 interaction. Blood, 87, 3942-3947.
    • (1996) Blood , vol.87 , pp. 3942-3947
    • Huang, C.-H.1    Reid, M.E.2    Xie, S.-S.3    Blumenfeld, O.O.4
  • 47
    • 2642655570 scopus 로고    scopus 로고
    • Phenotypic diversity of band 3 mutations
    • N. Hamasaki and K. Mihara, eds (Basel, Karger)
    • Jarolim, P. (1997) Phenotypic diversity of band 3 mutations. In Membrane Proteins: Structure, function and expression control, N. Hamasaki and K. Mihara, eds (Basel, Karger), pp. 325-337.
    • (1997) Membrane Proteins: Structure, Function and Expression Control , pp. 325-337
    • Jarolim, P.1
  • 48
    • 0026767441 scopus 로고
    • Band 3 Memphis: A widespread polymorphism with abnormal electrophoretic mobility of band 3 protein caused by substitution AAG→GAG (Lys→Glu) in codon 56
    • Jarolim, P., Rubin, H. L., Zhai, S., Sahr, K. H., Liu, S. C., Mueller, T. J. and Palek, J. (1992) Band 3 Memphis: a widespread polymorphism with abnormal electrophoretic mobility of band 3 protein caused by substitution AAG→GAG (Lys→Glu) in codon 56. Blood, 80, 1592-1598.
    • (1992) Blood , vol.80 , pp. 1592-1598
    • Jarolim, P.1    Rubin, H.L.2    Zhai, S.3    Sahr, K.H.4    Liu, S.C.5    Mueller, T.J.6    Palek, J.7
  • 49
    • 0030610266 scopus 로고    scopus 로고
    • A Thr552→Ile substitution in erythroid band 3 gives rise to the Warrior blood group antigen
    • Jarolim, P., Murray, J. L., Rubin, H. L., Coghlan, G. and Zelinski, T. (1997) A Thr552→Ile substitution in erythroid band 3 gives rise to the Warrior blood group antigen. Transfusion, 37, 398-405.
    • (1997) Transfusion , vol.37 , pp. 398-405
    • Jarolim, P.1    Murray, J.L.2    Rubin, H.L.3    Coghlan, G.4    Zelinski, T.5
  • 51
    • 15144338599 scopus 로고
    • Evidence for an access channel leading to the outward-facing substrate in human red blood cell band 3
    • N. Hamasaki and M. L. Jennings, eds. (Oxford, Elsevier)
    • Jennings, M. L. (1989b) Evidence for an access channel leading to the outward-facing substrate in human red blood cell band 3. Anion Transport Protein of the Red Blood Cell Membrane, N. Hamasaki and M. L. Jennings, eds. (Oxford, Elsevier), pp. 59-72.
    • (1989) Anion Transport Protein of the Red Blood Cell Membrane , pp. 59-72
    • Jennings, M.L.1
  • 53
    • 0028965134 scopus 로고
    • Anion exchange protein in Southeast Asian ovalocytes: Heterodimer formation between normal and variant subunits
    • Jennings, M. L. and Gosselink, P. G. (1995) Anion exchange protein in Southeast Asian ovalocytes: heterodimer formation between normal and variant subunits. Biochemistry, 34, 3588-3595.
    • (1995) Biochemistry , vol.34 , pp. 3588-3595
    • Jennings, M.L.1    Gosselink, P.G.2
  • 54
    • 0030024722 scopus 로고    scopus 로고
    • Toplogical disposition of Tyrosine 486 in anion exchanger from human erythrocytes
    • Kalo, M. S. (1996) Toplogical disposition of Tyrosine 486 in anion exchanger from human erythrocytes. Biochemistry, 35, 999-1009.
    • (1996) Biochemistry , vol.35 , pp. 999-1009
    • Kalo, M.S.1
  • 56
    • 0028017770 scopus 로고
    • Anion transport function of mouse erythrocyte band 3 protein (AE1) does not require acylation of cysteine residue 861
    • Kang, D., Karbach, D. and Passow, H. (1994) Anion transport function of mouse erythrocyte band 3 protein (AE1) does not require acylation of cysteine residue 861. Biochimica et Biophysica Acta, 1194, 341-344.
    • (1994) Biochimica et Biophysica Acta , vol.1194 , pp. 341-344
    • Kang, D.1    Karbach, D.2    Passow, H.3
  • 57
    • 0343989755 scopus 로고    scopus 로고
    • Band 3 anion transporters in health and disease
    • Kay, M. M. B. ed. (1996) Band 3 anion transporters in health and disease. Molecular and Cellular Biology, 42, 905-1118.
    • (1996) Molecular and Cellular Biology , vol.42 , pp. 905-1118
    • Kay, M.M.B.1
  • 60
    • 0025690859 scopus 로고
    • Molecular biology of the anion exchanger gene family
    • Kopito, R. R. (1990) Molecular biology of the anion exchanger gene family. International Reviews of Cytology, 123, 549-564.
    • (1990) International Reviews of Cytology , vol.123 , pp. 549-564
    • Kopito, R.R.1
  • 61
    • 0028040839 scopus 로고
    • Asparagine-linked oligosaccharides are localised to single extracytosolic segments in multi-span membrane glycoproteins
    • Landolt-Marticorena, C. and Reithmeier, R. A. F. (1994) Asparagine-linked oligosaccharides are localised to single extracytosolic segments in multi-span membrane glycoproteins. Biochemical Journal, 302, 253-260.
    • (1994) Biochemical Journal , vol.302 , pp. 253-260
    • Landolt-Marticorena, C.1    Reithmeier, R.A.F.2
  • 63
    • 0017202108 scopus 로고
    • Effects of incorporated trypsin on anion exchange and membrane proteins in human red blood cell ghosts
    • Lepke, S. and Passow, H. (1976) Effects of incorporated trypsin on anion exchange and membrane proteins in human red blood cell ghosts. Biochimica et Biophysica Acta, 455, 353-370.
    • (1976) Biochimica et Biophysica Acta , vol.455 , pp. 353-370
    • Lepke, S.1    Passow, H.2
  • 64
    • 0026545038 scopus 로고
    • Mediation of inorganic anion transport by the hydrophobic domain of mouse erythroid band 3 protein expressed in oocytes of Xenopus laevis
    • Lepke, S., Becker, A. and Passow, H. (1992) Mediation of inorganic anion transport by the hydrophobic domain of mouse erythroid band 3 protein expressed in oocytes of Xenopus laevis. Biochimica et Biophysica Acta, 1106, 13-16.
    • (1992) Biochimica et Biophysica Acta , vol.1106 , pp. 13-16
    • Lepke, S.1    Becker, A.2    Passow, H.3
  • 65
    • 0028027718 scopus 로고
    • The homozygous state for the band 3 protein mutation in Southeast Asian Ovalocytosis may be lethal
    • Liu, S. C., Jarolim, P., Rubin, H. L., Palek, J., Amato, D., Hassan, K., Zaik, M. and Sapak, P. (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    Hassan, K.6    Zaik, M.7    Sapak, P.8
  • 66
    • 0029029602 scopus 로고
    • Molecular basis of altered red cell membrane properties in Southeast Asian ovalocytosis: Role of the mutant band 3 protein in band 3 oligomerisation and retention by the membrane skeleton
    • Liu, S. C., Palek, J., Yi, S. J., Nichols, P. E., Derick, L. H., Chiou, S. S., Amato, D., Corbett, J. D., Cho, M. R. and Golan, D. E. (1995) Molecular basis of altered red cell membrane properties in Southeast Asian ovalocytosis: role of the mutant band 3 protein in band 3 oligomerisation and retention by the membrane skeleton. Blood, 86, 349-358.
    • (1995) Blood , vol.86 , pp. 349-358
    • Liu, S.C.1    Palek, J.2    Yi, S.J.3    Nichols, P.E.4    Derick, L.H.5    Chiou, S.S.6    Amato, D.7    Corbett, J.D.8    Cho, M.R.9    Golan, D.E.10
  • 67
    • 0003147477 scopus 로고
    • Disorders of the red cell membrane
    • R. I. Handin, S. E. Lux and T. P. Stossel, eds (Philadelphia: J. B. Lippincott Co)
    • Lux, S. E. and Palek, J. (1995) Disorders of the red cell membrane. In Blood: Principles and practice of hematology, R. I. Handin, S. E. Lux and T. P. Stossel, eds (Philadelphia: J. B. Lippincott Co), pp. 1701-1817.
    • (1995) Blood: Principles and Practice of Hematology , pp. 1701-1817
    • Lux, S.E.1    Palek, J.2
  • 68
    • 0022108670 scopus 로고
    • Mediation of anion transport in oocytes of Xenopus laevis by biosynthetically inserted band 3 protein from mouse spleen erythroid cells
    • Morgan, M., Hanke, P., Grygorczyk, R., Tintschl, A., Fasold, H. and Passow, H. (1985) Mediation of anion transport in oocytes of Xenopus laevis by biosynthetically inserted band 3 protein from mouse spleen erythroid cells. EMBO Journal, 4, 1927-1931.
    • (1985) EMBO Journal , vol.4 , pp. 1927-1931
    • Morgan, M.1    Hanke, P.2    Grygorczyk, R.3    Tintschl, A.4    Fasold, H.5    Passow, H.6
  • 69
    • 0029616179 scopus 로고
    • A structural study of the carboxy terminal region of the human erythrocyte band 3 protein
    • Mori, A., Okubo, K., Kang, D. and Hamasaki, N. (1995) A structural study of the carboxy terminal region of the human erythrocyte band 3 protein. Journal of Biochemistry (Tokyo), 118, 1192-1198.
    • (1995) Journal of Biochemistry (Tokyo) , vol.118 , pp. 1192-1198
    • Mori, A.1    Okubo, K.2    Kang, D.3    Hamasaki, N.4
  • 71
    • 0002657045 scopus 로고    scopus 로고
    • Inherited disorders of the renal tubule
    • B. M. Brenner, ed. (Philadelphia: W. B. Saunders)
    • Morris, R. C. and Ives, H. E. (1996) Inherited disorders of the renal tubule. In The Kidney, B. M. Brenner, ed. (Philadelphia: W. B. Saunders), pp. 1764-1827.
    • (1996) The Kidney , pp. 1764-1827
    • Morris, R.C.1    Ives, H.E.2
  • 73
    • 0027717715 scopus 로고
    • Different sequences of expression of band 3, spectrin and ankyrin during normal erythropoeisis and erythroleukemia
    • Nehls, V., Zeitler-Zapf, P. and Drenckhahn, D. (1993) Different sequences of expression of band 3, spectrin and ankyrin during normal erythropoeisis and erythroleukemia. American Journal of Pathology, 142, 1565-1573.
    • (1993) American Journal of Pathology , vol.142 , pp. 1565-1573
    • Nehls, V.1    Zeitler-Zapf, P.2    Drenckhahn, D.3
  • 74
    • 0019152595 scopus 로고
    • Band 3-glycophorin a association in erythrocyte membrane demonstrated by combining protein diffusion measurements with antibody-induced crosslinking
    • Nigg, E. A., Bron, E. A., Girardet, M. and Cherry, R. J. (1980) Band 3-glycophorin A association in erythrocyte membrane demonstrated by combining protein diffusion measurements with antibody-induced crosslinking. Biochemistry, 19, 1887-1893.
    • (1980) Biochemistry , vol.19 , pp. 1887-1893
    • Nigg, E.A.1    Bron, E.A.2    Girardet, M.3    Cherry, R.J.4
  • 75
    • 0027417476 scopus 로고
    • Determination of the distance between the oligosaccharyltransferase and the endoplasmic reticulum membrane
    • Nilsson, I. and von Heijne, G. (1993) Determination of the distance between the oligosaccharyltransferase and the endoplasmic reticulum membrane. Journal of Biological Chemistry, 268, 5798-5801.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 5798-5801
    • Nilsson, I.1    Von Heijne, G.2
  • 76
    • 0021863630 scopus 로고
    • Conformation and stability of the anion transport protein of human erythrocyte membranes
    • Oikawa, K., Lieberman, D. M. and Reithmeier, R. A. F. (1985) Conformation and stability of the anion transport protein of human erythrocyte membranes. Biochemistry, 24, 2843-2848.
    • (1985) Biochemistry , vol.24 , pp. 2843-2848
    • Oikawa, K.1    Lieberman, D.M.2    Reithmeier, R.A.F.3
  • 77
    • 0026075781 scopus 로고
    • Palmitoylation of cysteine 69 from the COOH-terminal of band 3 protein in the human erythrocyte membrane
    • Okubo, K., Hamasaki, N., Hara, K. and Kageura, M. (1991) Palmitoylation of cysteine 69 from the COOH-terminal of band 3 protein in the human erythrocyte membrane. Journal of Biological Chemistry, 266, 16420-16424.
    • (1991) Journal of Biological Chemistry , vol.266 , pp. 16420-16424
    • Okubo, K.1    Hamasaki, N.2    Hara, K.3    Kageura, M.4
  • 79
    • 2642596370 scopus 로고    scopus 로고
    • The carboxy terminal region of the human AE1 (erythrocyte band 3 protein)
    • N. Hamasaki and K. Mihara, eds. (Basel: Karger)
    • Okubo, K., Kang, D. and Hamasaki, N. (1997) The carboxy terminal region of the human AE1 (erythrocyte band 3 protein). In Membrane Proteins: Structure, function and expression control, N. Hamasaki and K. Mihara, eds. (Basel: Karger), pp. 339-352.
    • (1997) Membrane Proteins: Structure, Function and Expression Control , pp. 339-352
    • Okubo, K.1    Kang, D.2    Hamasaki, N.3
  • 80
    • 0343879925 scopus 로고
    • Evaluation of the mechanism of mouse erythroid band 3-mediated anion exchange by site-directed mutagenesis
    • E. Bamberg and H. Passow, eds. Progress in Cell Research (Oxford: Elsevier)
    • Passow, H., Lepke, S. and Wood, P. G. (1992) Evaluation of the mechanism of mouse erythroid band 3-mediated anion exchange by site-directed mutagenesis. In The Band 3 Proteins: Anion transporters, binding proteins and senescent antigens, E. Bamberg and H. Passow, eds. Progress in Cell Research Vol. 2 (Oxford: Elsevier), pp. 85-98.
    • (1992) The Band 3 Proteins: Anion Transporters, Binding Proteins and Senescent Antigens , vol.2 , pp. 85-98
    • Passow, H.1    Lepke, S.2    Wood, P.G.3
  • 83
    • 0025249842 scopus 로고
    • Membrane protein folding and oligomerisation: The two-stage model
    • Popot, J.-L. and Engelman, D. M. (1990) Membrane protein folding and oligomerisation: the two-stage model. Biochemistry, 29, 4031-4037.
    • (1990) Biochemistry , vol.29 , pp. 4031-4037
    • Popot, J.-L.1    Engelman, D.M.2
  • 84
    • 0030745799 scopus 로고    scopus 로고
    • Mapping the ends of transmembrane segments in a polytopic membrane protein. Scanning N-glycosylation mutagenesis of extracytosololic loops in the anion exchanger, band 3
    • Popov, M., Tam, L. Y., Li, J. and Reithmeier, R. A. F. (1997) Mapping the ends of transmembrane segments in a polytopic membrane protein. Scanning N-glycosylation mutagenesis of extracytosololic loops in the anion exchanger, band 3. Journal of Biological Chemistry, 272, 18325-18332.
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 18325-18332
    • Popov, M.1    Tam, L.Y.2    Li, J.3    Reithmeier, R.A.F.4
  • 86
    • 2642603500 scopus 로고    scopus 로고
    • Structure and N-glycosylation of human band 3, the erythocyte anion exchanger
    • N. Hamasaki and K. Mihara, eds (Basel: Karger)
    • Reithmeier, R. A. F. (1997) Structure and N-glycosylation of human band 3, the erythocyte anion exchanger. In Membrane Proteins: Structure, function and expression control, N. Hamasaki and K. Mihara, eds (Basel: Karger), pp. 317-324.
    • (1997) Membrane Proteins: Structure, Function and Expression Control , pp. 317-324
    • Reithmeier, R.A.F.1
  • 88
    • 0029993499 scopus 로고    scopus 로고
    • Examining rhodopsin folding and assembly through expression of polypeptide fragments
    • Ridge, K. D., Lee, S. S. J. and Abdulaev, N. G. (1996) Examining rhodopsin folding and assembly through expression of polypeptide fragments. Journal of Biological Chemistry, 271, 7860-7867.
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 7860-7867
    • Ridge, K.D.1    Lee, S.S.J.2    Abdulaev, N.G.3
  • 89
    • 0027399690 scopus 로고
    • Functional activation of plasma membrane anion exchangers occurs in a pre-Golgi compartment
    • Ruetz, S., Lindsey, A. E., Ward, C. L. and Kopito, R. R. (1993) Functional activation of plasma membrane anion exchangers occurs in a pre-Golgi compartment. Journal of Cell Biology, 121, 37-48.
    • (1993) Journal of Cell Biology , vol.121 , pp. 37-48
    • Ruetz, S.1    Lindsey, A.E.2    Ward, C.L.3    Kopito, R.R.4
  • 90
    • 0030277084 scopus 로고    scopus 로고
    • Transport-related conformational states of the band 3 protein: Probing with 1-fluoro-2,4-dinitrobenzene
    • Ruffing, W., Gartner, E. M., Lepke, S., Legrum, B. and Passow, H. (1996) Transport-related conformational states of the band 3 protein: probing with 1-fluoro-2,4-dinitrobenzene. Molecular and Cellular Biology, 42, 1097-1118.
    • (1996) Molecular and Cellular Biology , vol.42 , pp. 1097-1118
    • Ruffing, W.1    Gartner, E.M.2    Lepke, S.3    Legrum, B.4    Passow, H.5
  • 91
    • 0028585820 scopus 로고
    • The structure and organisation of the human erythroid anion exchanger (AE1) gene
    • Sahr, K. E., Taylor, W. M., Daniels, B. P., Rubin, H. L. and Jarolim, P. (1994) The structure and organisation of the human erythroid anion exchanger (AE1) gene. Genomics, 24, 491-501.
    • (1994) Genomics , vol.24 , pp. 491-501
    • Sahr, K.E.1    Taylor, W.M.2    Daniels, B.P.3    Rubin, H.L.4    Jarolim, P.5
  • 92
    • 0030279607 scopus 로고    scopus 로고
    • Allosteric effects in stilbene disulphonate binding to band 3 protein (AE1)
    • Salhany, J. M. (1996) Allosteric effects in stilbene disulphonate binding to band 3 protein (AE1). Molecular and Cellular Biology, 42, 1065-1096.
    • (1996) Molecular and Cellular Biology , vol.42 , pp. 1065-1096
    • Salhany, J.M.1
  • 94
    • 0030067347 scopus 로고    scopus 로고
    • Interactions between mutant and wild-type band 3 subunits in hereditary Southeast Asian ovalocytic red blood cell membranes
    • Salhany, J. and Schopfer, L. M. (1996) Interactions between mutant and wild-type band 3 subunits in hereditary Southeast Asian ovalocytic red blood cell membranes. Biochemistry, 35, 251-257.
    • (1996) Biochemistry , vol.35 , pp. 251-257
    • Salhany, J.1    Schopfer, L.M.2
  • 95
    • 0030015620 scopus 로고    scopus 로고
    • Characterisation of the stilbenedisulphonate binding site on band 3 Memphis variant II (Pro854→Leu)
    • Salhany, J. M., Sloan, R. L. and Schopfer, L. M. (1996) Characterisation of the stilbenedisulphonate binding site on band 3 Memphis variant II (Pro854→Leu). Biochemical Journal, 317, 509-514.
    • (1996) Biochemical Journal , vol.317 , pp. 509-514
    • Salhany, J.M.1    Sloan, R.L.2    Schopfer, L.M.3
  • 96
    • 0027263968 scopus 로고
    • Molecular characterisation of the band 3 protein from Southeast Asian ovalocytes
    • Sarabia, V. E., Casey, J. R. and Reithmeier, R. A. F. (1993) Molecular characterisation of the band 3 protein from Southeast Asian ovalocytes. Journal of Biological Chemistry, 268, 10676-10680.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 10676-10680
    • Sarabia, V.E.1    Casey, J.R.2    Reithmeier, R.A.F.3
  • 97
    • 0029151926 scopus 로고
    • High level expression, partial purification and functional reconstitution of the human AE1 anion exchanger in Saccharomyces cerevisiae
    • Sekler, I., Kopito, R. R. and Casey, J. R. (1995a) High level expression, partial purification and functional reconstitution of the human AE1 anion exchanger in Saccharomyces cerevisiae. Journal of Biological Chemistry, 270, 21028-21034.
    • (1995) Journal of Biological Chemistry , vol.270 , pp. 21028-21034
    • Sekler, I.1    Kopito, R.R.2    Casey, J.R.3
  • 98
    • 0029070830 scopus 로고
    • Sulfate transport mediated by the mammalian anion exchangers in reconstituted proteoliposomes
    • Sekler, I., Lo, R. S., Mastrocola, T. and Kopito, R. R. (1995b) Sulfate transport mediated by the mammalian anion exchangers in reconstituted proteoliposomes. Journal of Biological Chemistry, 270, 11251-11256.
    • (1995) Journal of Biological Chemistry , vol.270 , pp. 11251-11256
    • Sekler, I.1    Lo, R.S.2    Mastrocola, T.3    Kopito, R.R.4
  • 99
    • 0028065446 scopus 로고
    • The structure of the human red blood cell anion exchanger (EPB3, AE1, Band 3) gene
    • Schofield, A. E., Martin, P. G., Spillett, D. and Tanner, M. J. A. (1994) The structure of the human red blood cell anion exchanger (EPB3, AE1, Band 3) gene. Blood, 84, 2000-2012.
    • (1994) Blood , vol.84 , pp. 2000-2012
    • Schofield, A.E.1    Martin, P.G.2    Spillett, D.3    Tanner, M.J.A.4
  • 100
    • 0029053332 scopus 로고
    • Monoclonal antibodies recognising epitopes on the extracellular face and intracellular N-terminus of the human erythrocyte anion transporter (Band 3) and their application to the analysis of Southeast Asian ovalocytes
    • Smythe, J. S., Spring, F. A., Gardner, B., Parsons, S. F., Judson, P. A. and Anstee, D. J. (1995) Monoclonal antibodies recognising epitopes on the extracellular face and intracellular N-terminus of the human erythrocyte anion transporter (Band 3) and their application to the analysis of Southeast Asian ovalocytes. Blood, 85, 2929-2936.
    • (1995) Blood , vol.85 , pp. 2929-2936
    • Smythe, J.S.1    Spring, F.A.2    Gardner, B.3    Parsons, S.F.4    Judson, P.A.5    Anstee, D.J.6
  • 101
    • 0029821217 scopus 로고    scopus 로고
    • Targeted disruption of the murine erythroid band 3 gene results in spherocytosis and severe hemolytic anamia despite a normal membrane skeleton
    • Southgate, C. D., Chishti, A. H., Mitchell, B., Yi, S. J. and Palek, J. (1996) Targeted disruption of the murine erythroid band 3 gene results in spherocytosis and severe hemolytic anamia despite a normal membrane skeleton. Nature Genetics, 2, 227-230.
    • (1996) Nature Genetics , vol.2 , pp. 227-230
    • Southgate, C.D.1    Chishti, A.H.2    Mitchell, B.3    Yi, S.J.4    Palek, J.5
  • 103
    • 0028605308 scopus 로고
    • Identification of an internal topogenic signal sequence in human band 3, the erythrocyte anion exchanger
    • Tam, L. Y., Loo, T. W., Clarke, D. M. and Reithmeier, R. A. F. (1994) Identification of an internal topogenic signal sequence in human band 3, the erythrocyte anion exchanger. Journal of Biological Chemistry, 269, 32542-32550.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 32542-32550
    • Tam, L.Y.1    Loo, T.W.2    Clarke, D.M.3    Reithmeier, R.A.F.4
  • 104
    • 0027410647 scopus 로고
    • Molecular and cellular biology of the erythrocyte anion exchanger
    • Tanner, M. J. A. (1993) Molecular and cellular biology of the erythrocyte anion exchanger. Seminars in Hematology, 30, 34-57.
    • (1993) Seminars in Hematology , vol.30 , pp. 34-57
    • Tanner, M.J.A.1
  • 105
    • 0029894442 scopus 로고    scopus 로고
    • The acid test for band 3
    • Tanner, M. J. A. (1996) The acid test for band 3. Nature, 382, 209-210.
    • (1996) Nature , vol.382 , pp. 209-210
    • Tanner, M.J.A.1
  • 106
    • 0002198359 scopus 로고    scopus 로고
    • The expression of the erythrocyte anion transporter (band 3, AE1)
    • N. Hamasaki and K. Mihara, eds (Basel: Karger)
    • Tanner, M. J. A., Bruce, L. J. and Groves, J. D. (1997) The expression of the erythrocyte anion transporter (band 3, AE1). In Membrane Proteins: Structure, function and expression control, N. Hamasaki and K. Mihara, eds (Basel: Karger), pp. 353-372.
    • (1997) Membrane Proteins: Structure, Function and Expression Control , pp. 353-372
    • Tanner, M.J.A.1    Bruce, L.J.2    Groves, J.D.3
  • 107
    • 0025162398 scopus 로고
    • b antigen to an interaction between glycophorin a and band 3
    • b antigen to an interaction between glycophorin A and band 3. Blood, 76, 842-848.
    • (1990) Blood , vol.76 , pp. 842-848
    • Telen, M.J.1    Chasis, J.A.2
  • 109
    • 0028298801 scopus 로고
    • Band 3 protein: Structure, flexibility and function
    • Wang, D. N. (1994) Band 3 protein: structure, flexibility and function. FEBS Letters, 346, 26-31.
    • (1994) FEBS Letters , vol.346 , pp. 26-31
    • Wang, D.N.1
  • 110
    • 0027096402 scopus 로고
    • Expression, purification and characterisation of functional dimeric cytoplasmic domain of human erythrocyte band 3 in E. coli
    • Wang, C. C., Badylak, J. A., Lux, S. E., Moriyama, R., Dixon, J. E. and Low, P. S. (1992) Expression, purification and characterisation of functional dimeric cytoplasmic domain of human erythrocyte band 3 in E. coli. Protein Science, 1, 1206-1214.
    • (1992) Protein Science , vol.1 , pp. 1206-1214
    • Wang, C.C.1    Badylak, J.A.2    Lux, S.E.3    Moriyama, R.4    Dixon, J.E.5    Low, P.S.6
  • 111
    • 0027266988 scopus 로고
    • Two dimensional structure of the membrane domain of human band 3, the anion transport protein of the erythrocyte membrane
    • Wang, D. N., Kuhlbrandt, W., Sarabia, V. E. and Reithmeier, R. A. F. (1993) Two dimensional structure of the membrane domain of human band 3, the anion transport protein of the erythrocyte membrane. EMBO Journal, 12, 2233-2239.
    • (1993) EMBO Journal , vol.12 , pp. 2233-2239
    • Wang, D.N.1    Kuhlbrandt, W.2    Sarabia, V.E.3    Reithmeier, R.A.F.4
  • 112
    • 0028339981 scopus 로고
    • Three-dimensional map of the dimeric membrane domain of the human erythrocyte anion exchanger, band 3
    • Wang, D. N., Sarabia, V. E., Reithmeier, R. A. F. and Kuhlbrandt, W. (1994) Three-dimensional map of the dimeric membrane domain of the human erythrocyte anion exchanger, band 3. EMBO Journal, 13, 3230-3235.
    • (1994) EMBO Journal , vol.13 , pp. 3230-3235
    • Wang, D.N.1    Sarabia, V.E.2    Reithmeier, R.A.F.3    Kuhlbrandt, W.4
  • 113
    • 0030888062 scopus 로고    scopus 로고
    • Complementation studies with co-expressed fragments of the human red cell anion transporter (Band 3; AE1): Role of some exofacial loops in anion transport
    • Wang, L., Groves, J. D., Mawby, W. J. and Tanner, M. J. A. (1997) Complementation studies with co-expressed fragments of the human red cell anion transporter (Band 3; AE1): role of some exofacial loops in anion transport. Journal of Biological Chemistry, 272, 10631-10638.
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 10631-10638
    • Wang, L.1    Groves, J.D.2    Mawby, W.J.3    Tanner, M.J.A.4
  • 114
    • 2642605656 scopus 로고    scopus 로고
    • What can glycosylation mapping tell us about membrane protein assembly and structure?
    • N. Hamasaki and K. Mihara, eds. (Basel: Karger)
    • Whitley, P. and von Heijne, G. (1997) What can glycosylation mapping tell us about membrane protein assembly and structure? In Membrane Proteins: Structure, function and expression control, N. Hamasaki and K. Mihara, eds. (Basel: Karger), pp. 117-126.
    • (1997) Membrane Proteins: Structure, Function and Expression Control , pp. 117-126
    • Whitley, P.1    Von Heijne, G.2
  • 115
    • 0000119277 scopus 로고
    • The anion exchange proteins: Homology and secondary structure
    • E. Bamberg and H. Passow, eds. Progress in Cell Research Amsterdam: Elsevier
    • Wood, P. G. (1992) The anion exchange proteins: homology and secondary structure. In The Band 3 Proteins: Anion transporters, binding proteins and senescent antigens, E. Bamberg and H. Passow, eds. Progress in Cell Research Vol. 2 (Amsterdam: Elsevier), pp. 325-352.
    • (1992) The Band 3 Proteins: Anion Transporters, Binding Proteins and Senescent Antigens , vol.2 , pp. 325-352
    • Wood, P.G.1
  • 116
    • 0029823248 scopus 로고    scopus 로고
    • Unravelling of the molecular mechanism of kidney stones
    • Wrong, O., Unwin, R., Cohen, E., Tanner, M. and Thakker, R. (1996) Unravelling of the molecular mechanism of kidney stones. Lancet, 348, 1561-1565.
    • (1996) Lancet , vol.348 , pp. 1561-1565
    • Wrong, O.1    Unwin, R.2    Cohen, E.3    Tanner, M.4    Thakker, R.5
  • 117
    • 0026006230 scopus 로고
    • Human erythrocyte band 3 polymorphism (band 3 Memphis): Characterisation of the structural modification (Lys56→Glu) by protein chemistry methods
    • Yannoukakos, D., Vasseur, C., Driancourt, C., Blouquit, Y., Delaunay, J., Wajcman, J. and Bursaux, E. (1991) Human erythrocyte band 3 polymorphism (band 3 Memphis): characterisation of the structural modification (Lys56→Glu) by protein chemistry methods. Blood, 78, 1117-1120.
    • (1991) Blood , vol.78 , pp. 1117-1120
    • Yannoukakos, D.1    Vasseur, C.2    Driancourt, C.3    Blouquit, Y.4    Delaunay, J.5    Wajcman, J.6    Bursaux, E.7
  • 118
    • 0028812838 scopus 로고
    • Structure of the third cytoplasmic loop of bovine rhodopsin
    • Yeagle, P. L., Alderfer, J. L. and Albert, A. D. (1995) Structure of the third cytoplasmic loop of bovine rhodopsin. Biochemistry, 34, 14261-14265.
    • (1995) Biochemistry , vol.34 , pp. 14261-14265
    • Yeagle, P.L.1    Alderfer, J.L.2    Albert, A.D.3
  • 119
    • 0030964858 scopus 로고    scopus 로고
    • The first and second cytoplasmic loops of the G-protein receptor, rhodopsin, independently form β-turns
    • Yeagle, P. L., Alderfer, J. L., Salloum, A. C., Ali, L. and Albert, A. D. (1997) The first and second cytoplasmic loops of the G-protein receptor, rhodopsin, independently form β-turns. Biochemistry, 36, 3864-3869.
    • (1997) Biochemistry , vol.36 , pp. 3864-3869
    • Yeagle, P.L.1    Alderfer, J.L.2    Salloum, A.C.3    Ali, L.4    Albert, A.D.5
  • 120
    • 0030278906 scopus 로고    scopus 로고
    • Chemical labelling of arginyl-residues involved in anion transport mediated by human band 3 protein and some aspects of its location in the polypeptide chain
    • Zaki, L., Bohm, R. and Merckel, M. (1996) Chemical labelling of arginyl-residues involved in anion transport mediated by human band 3 protein and some aspects of its location in the polypeptide chain. Molecular and Cellular Biology, 42, 1053-1063.
    • (1996) Molecular and Cellular Biology , vol.42 , pp. 1053-1063
    • Zaki, L.1    Bohm, R.2    Merckel, M.3


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