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Original Article

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

Pages 155-165 | Received 04 Aug 1997, Published online: 09 Jul 2009

References

  • Alper S. L. The band 3-related anion exchanger family. Annual Reviews of Physiology 1991; 53: 549–564
  • Alpern R. J., Rector F. C. Renal acidification: cellular mechanisms of tubular transport and regulation. Handbook of Physiology: Section 8, Renal Physiology, E. E. Windhager. Oxford University Press, Oxford 1992; 767–812
  • Bartel D., Lepke S., Layh-Schmitt G., Legrum B., Passow H. 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 1989; 8: 3601–3609
  • Beppu M., Ando K., Kikugawa K. Poly-N-acetyllactosa-minyl saccharide chains as determinants for anti-band 3 autoantibody binding to senescent and oxidised erythrocytes. Molecular and Cellular Biology 1996; 42: 1007–1024
  • Bruce L. J., Kay M. M. B., Lawrence C., Tanner M. J. A. Band 3 HT, a human red cell variant associated with acanthocy-tosis and increased anion transport, carries the mutation Pro868→Leu in the membrane domain of band 3. Biochemical Journal 1993; 293: 317–320
  • Bruce L. J., Anstee D. J., Spring F. A., Tanner M. J. A. Band 3 Memphis variant II. Altered stilbene disulphonate binding and the Diego (Dia) antigen are associated with the human erythrocyte band 3 mutation Pro854→Leu. Journal of Biological Chemistry 1994a; 269: 16155–16158
  • Bruce L. J., Groves J. D., Okubo Y., Thilaganathan B., Tanner M. J. A. Altered band 3 structure and function in glycophorin A- and B-deficient (MkMk) red blood cells. Blood 1994b; 84: 916–922
  • Bruce L. J., Ring S. M., Ridgwell K., Reardon D. M., Seymour C., Van Dort H. M., Low P. S., Anstee D. J., Tanner M. J. A. 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 1995a; 86(Suppl. 1)470a
  • Bruce L. J., Ring S. M., Anstee D. J., Reid M. E., Wilkinson S., Tanner M. J. A. 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 1995b; 85: 541–547
  • Bruce L. J., Tanner M. J. A. Structure-function relationships of band 3 variants. Molecular and Cellular Biology 1996; 42: 953–974
  • Bruce L. J., Zelinski T., Ridgwell K., Tanner M. J. A. The low incidence blood group antigen, Wda, is associated with the substitution Val557→Met in human erythrocyte band 3 (AE1). Vox Sanguinis 1996; 71: 118–120
  • Bruce L. J., Cope D. L., Jones G. K., Schofield A. E., Burley M., Povey S., Unwin R. J., Wrong O., Tanner M. J. A. Familial renal tubular acidosis is associated with mutations in the red cell anion exchanger (band 3: AE1) gene. Journal of Clinical Investigation 1997; 100: 1693–1707
  • Cartron J. P., Rahuel C. Human erythrocyte glycophor-ins: protein and gene structure analysis. Transfusion Medicine Reviews 1992; 6: 63–92
  • Casey J. R., Pirraglia C. A., Reithmeier R. A. F. 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 1992; 267: 11940–11948
  • Casey J. R., Ding Y., Kopito R. R. The role of cysteine residues in the erythrocyte plasma membrane anion exchange protein, AE1. Journal of Biological Chemistry 1995; 270: 8521–8527
  • Che A., Cherry R. J. Loss of rotational mobility of band 3 proteins in human erythrocyte membranes induced by antibodies to glycophorin A. Biophysical Journal 1995; 68: 1881–1887
  • Che A., Cherry R. J., Bannister L. H., Dluzewski A. R. Aggregation of band 3 in hereditary ovalocytic red blood cell membranes. Electron microscopy and protein rotational diffusion studies. Journal of Cell Science 1993; 105: 655–660
  • Cox K. H., Adair-Kirk T., Cox J. V. Four variant chicken erythroid anion exchangers. Role of alternative N-terminal sequences in intracellular targeting in transfected human erythro-leukemia cells. Journal of Biological Chemistry 1995; 270: 19752–19760
  • Dale W. E., Textor J. A., Mercer R. W., Simchowitz L. Expression and characterisation of the human erythrocyte anion exchanger in a baculovirus/Sf-9 cell system. Protein Expression and Purification 1996; 7: 1–11
  • Delauney J. Genetic disorders of red cell membranes. FEBS Letters 1995; 369: 34–37
  • Delaunay J., Alloisio N., Morle L., Baklouti F., DallaVenezia N., Maillet P., Wilmotte R. Molecular genetics of hereditary elliptocytosis and hereditary spherocytosis. Annates de Genetique 1996; 39: 209–221
  • Ding Y., Casey J. R., Kopito R. R. The major kidney AE1 isoform does not bind ankyrin (ANK1) in vitro. Journal of Biological Chemistry 1994; 269: 32201–32208
  • Dolder M., Walz T., Hefti A., Engel A. Human erythrocyte membrane band 3: solubilisation and reconstitution into two-dimensional crystals. Journal of Molecular Biology 1993; 231: 119–132
  • Dluzewski A. R., Nash G. B., Wilson R. J. M., Rearden D. M., Gratzer W. B. Invasion of hereditary ovalocytes by Plasmodium falciparum in vitro and its relationship to intracellular ATP concentration. Molecular and Biochemical Parasitology 1992; 55: 1–8
  • Fievet B., Gabillat N., Borgese F., Motais R. Expression of band 3 anion exchanger induces chloride current and taurine transport: structure-function analysis. EMBO Journal 1995; 14: 5158–5169
  • Fukuda M., Dell A., Oates J. E., Fukuda M. N. Structure of branched lactosaminoglycan, the carbohydrate moeity of band 3 isolated from adult erythrocytes. Journal of Biological Chemistry 1984; 259: 8260–8279
  • Garcia A. M., Lodish H. F. Lysine 539 of human band 3 is not essential for anion transport or inhibition by stilbene disulphonates. Journal of Biological Chemistry 1989; 264: 19607–19613
  • Gargaro A. R., Bloomberg G. B., Dempsey C. E., Murray M., Tanner M. J. A. The solution structures of the first and second transmembrane-spanning segments of band 3. European Journal of Biochemistry 1994; 221: 445–454
  • Gartner E. M., Liebold K., Legrum B., Fasold H., Passow H. Three different actions of phenylglyoxal on band 3 protein-mediated anion transport across the red blood cell membrane. Biochimica et Biophysica Acta 1997; 1323: 208–222
  • Genton B., Al-Yaman F., Mgone C. S., Alexander N., Paniu M. M., Alpers M. P., Mokela D. Ovalocytosis and cerebral malaria. Nature 1995; 378: 564–565
  • Gomez S., Morgans C. 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 1993; 268: 19593–19597
  • Grinstein S., Ship S., Rothstein A. Anion transport in relation to proteolytic dissection of band 3 protein. Biochimica et Biophysica Acta 1978; 507: 294–304
  • Groves J. D., Tanner M. J. A. Glycophorin A facilitates the expression of human band 3-mediated anion transport in Xenopus oocytes. Journal of Biological Chemistry 1992; 267: 2163–2170
  • Groves J. D., Tanner M. J. A. The role of N-glycosylation in the expression of human band 3-mediated anion transport. Molecular Membrane Biology 1994a; 11: 31–38
  • Groves J. D., Tanner M. J. A. The effects of glycophorin A on the expression of the human red cell anion transporter (band 3) in Xenopus oocytes. Journal of Membrane Biology 1994b; 140: 81–88
  • Groves J. D., Tanner M. J. A. Co-expressed fragments of the human red cell anion exchanger (Band 3; AE1) generate stilbene disulfonate sensitive anion transport. Journal of Biological Chemistry 1995; 270: 9077–9105
  • Groves J. D., Falson P., le Maire M., Tanner M. J. A. 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 1996; 93: 12245–12250
  • Hamasaki N., Okubo K. Band 3 protein: physiology, function and structure. Molecular and Cellular Biology 1996; 42: 1025–1039
  • Membrane Proteins: Structure, function and expression control, N. Hamasaki, K. Mihara. Karger, Basel 1997; 317–404
  • Hanspal M., Palek J. Biogenesis of normal and abnormal red blood cell membrane skeletons. Seminars in Hematology 1992; 29: 305–325
  • Hassoun H., Palek J. Hereditary spherocytosis: a review of the clinical and molecular aspects of the disease. Blood Reviews 1996; 10: 129–147
  • Hresko R. C., Kruse M., Strube M., Mueckler M. Topology of the Glutl glucose transporter deduced from glycosy-lation scanning mutagenesis. Journal of Biological Chemistry 1994; 269: 20482–20488
  • Hsu L., Morrison M. A new variant of the anion transport protein in human erythrocytes. Biochemistry 1985; 24: 3086–3090
  • Huang C.-H., Reid M. E., Xie S.-S., Blumenfeld O. O. Human red cell Wright antigens: a genetic and evolutionary perspective on glycophorin A-band 3 interaction. Blood 1996; 87: 3942–3947
  • Ideguchi H., Okubo K., Ishikawa A., Futata Y., Hamasaki N. Band 3 Memphis is associated with a lower transport rate of phosphoenolpyruvate. British Journal of Haematology 1992; 82: 122–125
  • Inaba M., Yawata A., Koshino I., Sat K., Takeuchi M., Takeuchi Y., Manno S., Yawata Y., Kanzaki A., Sakai J., Ban A., Ono K., Maede Y. 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. Journal of Clinical Investigation 1996; 97: 1804–1817
  • Jarolim P. Phenotypic diversity of band 3 mutations. Membrane Proteins: Structure, function and expression control, N. Hamasaki, K. Mihara. Karger, Basel 1997; 325–337
  • Jarolim P., Rubin H. L., Zhai S., Sahr K. H., Liu S. C., Mueller T. J., Palek J. 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 1992; 80: 1592–1598
  • Jarolim P., Murray J. L., Rubin H. L., Coghlan G., Zelinski T. A Thr552→IIe substitution in erythroid band 3 gives rise to the Warrior blood group antigen. Transfusion 1997; 37: 398–405
  • Jennings M. L. Structure and function of the red cell anion transport protein. Annual Reviews of Biophysics and Biophysical Chemistry 1989a; 18: 397–430
  • Jennings M. L. 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, M. L. Jennings. Elsevier, Oxford 1989b; 59–72
  • Jennings M. L., Anderson M. P., Monaghan R. Monoclonal antibodies against erythrocyte band 3 protein. Journal of Biological Chemistry 1986; 261: 9002–9010
  • Jennings M. L., Gosselink P. G. Anion exchange protein in Southeast Asian ovalocytes: heterodimer formation between normal and variant subunits. Biochemistry 1995; 34: 3588–3595
  • Kalo M. S. Toplogical disposition of Tyrosine 486 in anion exchanger from human erythrocytes. Biochemistry 1996; 35: 999–1009
  • Kang D., Okubo K., Hamasaki N., Kuroda N., Shiraki H. A structural study of the membrane domain of band 3 by tryptic digestion. Journal of Biological Chemistry 1992; 267: 19211–19217
  • Kang D., Karbach D., Passow H. Anion transport function of mouse erythrocyte band 3 protein (AE1) does not require acylation of cysteine residue 861. Biochimica et Biophy-sicaActa 1994; 1194: 341–344
  • Band 3 anion transporters in health and disease. Molecular and Cellular Biology 1996; 42: 905–1118, Kay, M. M. B. ed.
  • Kiyatkin A. B., Natarajan P., Munshi S., Minor W., Johnson J. E., Low P. S. Crystallisation and preliminary X-ray analysis of the cytoplasmic domain of human erythrocyte band 3. Proteins: Structure, Function and Genetics 1995; 22: 293–297
  • Kollert-Jons A., Wagner S., Hubner S., Appelhans H., Drenckhahn D. Anion exchanger 1 in human kidney and oncocytoma differs from erythroid AE1 in its NH2 terminus. American Journal of Physiology 1993; 265: F813–F821
  • Kopito R. R. Molecular biology of the anion exchanger gene family. International Reviews of Cytology 1990; 123: 549–564
  • Landolt-Marticorena C., Reithmeier R. A. F. Asparagine-linked oligosaccharides are localised to single extracytosolic segments in multi-span membrane glycoproteins. Biochemical Journal 1994; 302: 253–260
  • Landolt-Marticorena C., Casey J. R., Reithmeier R. A. F. Transmembrane helix-helix interactions and accessibility of H2DIDS on labelled band 3, the erythrocyte anion exchange protein. Molecular Membrane Biology 1995; 12: 173–182
  • Lepke S., Passow H. Effects of incorporated trypsin on anion exchange and membrane proteins in human red blood cell ghosts. Biochimica et Biophysics Acta 1976; 455: 353–370
  • Lepke S., Becker A., Passow H. 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 1992; 1106: 13–16
  • Liu S. C., Jarolim P., Rubin H. L., Palek J., Amato D., Hassan K., Zaik M., Sapak P. The homozygous state for the band 3 protein mutation in Southeast Asian Ovalocytosis may be lethal. Blood 1994; 84: 3590–3591
  • 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., Golan D. E. 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 1995; 86: 349–358
  • Lux S. E., Palek J. Disorders of the red cell membrane. Blood: Principles and practice of hematology, R. I. Handin, S. E. Lux, T. P. Stossel. J. B. Lippincott Co, Philadelphia 1995; 1701–1817
  • Morgan M., Hanke P., Grygorczyk R., Tintschl A., Fasold H., Passow H. Mediation of anion transport in oocytes of Xenopus laevis by biosynthetically inserted band 3 protein from mouse spleen erythroid cells. EMBO Journal 1985; 4: 1927–1931
  • Mori A., Okubo K., Kang D., Hamasaki N. A structural study of the carboxy terminal region of the human erythrocyte band 3 protein. Journal of Biochemistry (Tokyo) 1995; 118: 1192–1198
  • Moriyama R., Ideguchi H., Lombardo C. R., van Dort H. M., Low P. S. Structural and functional characterisation of band 3 from Southeast Asian ovalocytes. Journal of Biological Chemistry 1992; 267: 25792–25797
  • Morris R. C., Ives H. E. Inherited disorders of the renal tubule. The Kidney, B. M. Brenner. W. B. Saunders, Philadelphia 1996; 1764–1827
  • Muller-Berger S., Karbach D., Konig J., Lepke S., Wood P. G., Appelhans H., Passow H. Inhibition of mouse erythroid band 3-mediated chloride transport by site-directed mutagenesis of histidine residues and its reversal by second site mutation of Lys 558, the locus of covalent H2DIDS binding. Biochemistry 1995; 34: 9315–9324
  • Nehls V., Zeitler-Zapf P., Drenckhahn D. Different sequences of expression of band 3, spectrin and ankyrin during normal erythropoeisis and erythroleukemia. American Journal of Pathology 1993; 142: 1565–1573
  • Nigg E. A., Bron E. A., Girardet M., Cherry R. J. Band 3-glycophorin A association in erythrocyte membrane demonstrated by combining protein diffusion measurements with antibody-induced crosslinking. Biochemistry 1980; 19: 1887–1893
  • Nilsson I., von Heijne G. Determination of the distance between the oligosaccharyltransferase and the endoplasmic reticulum membrane. Journal of Biological Chemistry 1993; 268: 5798–5801
  • Oikawa K., Lieberman D. M., Reithmeier R. A. F. Conformation and stability of the anion transport protein of human erythrocyte membranes. Biochemistry 1985; 24: 2843–2848
  • Okubo K., Hamasaki N., Hara K., Kageura M. Palmitoylation of cysteine 69 from the COOH-terminal of band 3 protein in the human erythrocyte membrane. Journal of Biological Chemistry 1991; 266: 16420–16424
  • Okubo K., Kang D., Hamasaki N., Jennings M. L. Red cell band 3: lysine 539 and lysine 851 react with the same H2DIDS molecule. Journal of Biological Chemistry 1994; 269: 1918–1926
  • Okubo K., Kang D., Hamasaki N. The carboxy terminal region of the human AE1 (erythrocyte band 3 protein). Membrane Proteins: Structure, function and expression control, N. Hamasaki, K. Mihara. Karger, Basel 1997; 339–352
  • Passow H., Lepke S., Wood P. G. Evaluation of the mechanism of mouse erythroid band 3-mediated anion exchange by site-directed mutagenesis. The Band 3 Proteins: Anion transporters, binding proteins and senescent antigens, E. Bamberg, H. Passow. Elsevier, Oxford 1992; 2: 85–98, Progress in Cell Research
  • Passow H., Karbach D., Aranibar N., Liebold K., Wood P. G., Lepke S. Studies on the pH dependence of band 3-mediated anion transport. Facts and speculations. Membrane Proteins: Structure, function and expression control, N. Hamasaki, K. Mihara. Karger, Basel 1997; 373–404
  • Peters L. L., Shivdasani R. A., Liu S.-C., Hanspal M., John K. M., Gonzalez J. M., Brugnara C., Gwynn B., Mohandas N., Alper S. L., Orkin S. H., Lux S. E. Anion exchanger 1 (band 3) is required to prevent erythrocyte membrane surface loss but not to form the membrane skeleton. Cell 1996; 86: 917–927
  • Popot J.-L., Engelman D. M. Membrane protein folding and oligomerisation: the two-stage model. Biochemistry 1990; 29: 4031–4037
  • Popov M., Tarn L. Y., Li J., Reithmeier R. A. F. 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 1997; 272: 18325–18332
  • Reithmeier R. A. F. The erythrocyte anion transport (band 3). Current Opinion in Structural Biology 1993; 3: 515–523
  • Reithmeier R. A. F. Structure and N-glycosylation of human band 3, the erythocyte anion exchanger. Membrane Proteins: Structure, function and expression control, N. Hamasaki, K. Mihara. Karger, Basel 1997; 317–324
  • Ridge K. D., Lee S. S. J., Yao L. L. In vivo assembly of rhodopsin from expressed polypeptide fragments. Proceedings of the National Academy of Sciences USA 1995; 92: 3204–3208
  • Ridge K. D., Lee S. S. J., Abdulaev N. G. Examining rhodopsin folding and assembly through expression of polypeptide fragments. Journal of Biological Chemistry 1996; 271: 7860–7867
  • Ruetz S., Lindsey A. E., Ward C. L., Kopito R. R. Functional activation of plasma membrane anion exchangers occurs in a pre-Golgi compartment. Journal of Cell Biology 1993; 121: 37–48
  • Ruffing W., Gartner E. M., Lepke S., Legrum B., Passow H. Transport-related conformational states of the band 3 protein: probing with 1-fluoro-2, 4-dinitrobenzene. Molecular and Cellular Biology 1996; 42: 1097–1118
  • Sahr K. E., Taylor W. M., Daniels B. P., Rubin H. L., Jarolim P. The structure and organisation of the human erythroid anion exchanger (AE1) gene. Genomics 1994; 24: 491–501
  • Salhany J. M. Allosteric effects in stilbene disulphonate binding to band 3 protein (AE1). Molecular and Cellular Biology 1996; 42: 1065–1096
  • Salhany J. M., Schopfer L. M., Kay M. M. B., Gamble D. N., Lawrence C. Differential sensitivity of stilbenedisulfonates in their reaction with band 3 (Pro868→Leu). Proceedings of the National Academy of Sciences USA 1995; 92: 11844–11848
  • Salhany J., Schopfer L. M. Interactions between mutant and wild-type band 3 subunits in hereditary Southeast Asian ovalocytic red blood cell membranes. Biochemistry 1996; 35: 251–257
  • Salhany J. M., Sloan R. L., Schopfer L. M. Characterisation of the stilbenedisulphonate binding site on band 3 Memphis variant II (Pro854→Leu). Biochemical Journal 1996; 317: 509–514
  • Sarabia V. E., Casey J. R., Reithmeier R. A. F. Molecular characterisation of the band 3 protein from Southeast Asian ovalocytes. Journal of Biological Chemistry 1993; 268: 10676–10680
  • Sekler I., Kopito R. R., Casey J. R. High level expression, partial purification and functional reconstitution of the human AE1 anion exchanger in Saccharomyces cerevisiae. Journal of Biological Chemistry 1995a; 270: 21028–21034
  • Sekler I., Lo R. S., Mastrocola T., Kopito R. R. Sulfate transport mediated by the mammalian anion exchangers in reconstituted proteoliposomes. Journal of Biological Chemistry 1995b; 270: 11251–11256
  • Schofield A. E., Martin P. G., Spillett D., Tanner M. J. A. The structure of the human red blood cell anion exchanger (EPB3, AE1, Band 3) gene. Blood 1994; 84: 2000–2012
  • Smythe J. S., Spring F. A., Gardner B., Parsons S. F., Judson P. A., Anstee D. J. 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 1995; 85: 2929–2936
  • Southgate C. D., Chishti A. H., Mitchell B., Yi S. J., Palek J. Targeted disruption of the murine erythroid band 3 gene results in spherocytosis and severe hemolytic anamia despite a normal membrane skeleton. Nature Genetics 1996; 2: 227–230
  • Spring F. A., Bruce L. J., Anstee D. J., Tanner M. J. A. A red cell variant with altered stilbene-disulphonate binding is associated with the Diego (Dia) blood group antigen. Biochemical Journal 1992; 288: 713–716
  • Tam L. Y., Loo T. W., Clarke D. M., Reithmeier R. A. F. Identification of an internal topogenic signal sequence in human band 3, the erythrocyte anion exchanger. Journal of Biological Chemistry 1994; 269: 32542–32550
  • Tanner M. J. A. Molecular and cellular biology of the erythrocyte anion exchanger. Seminars in Hematology 1993; 30: 34–57
  • Tanner M. J. A. The acid test for band 3. Nature 1996; 382: 209–210
  • Tanner M. J. A., Bruce L. J., Groves J. D. The expression of the erythrocyte anion transporter (band 3, AE1). Membrane Proteins: Structure, function and expression control, N. Hamasaki, K. Mihara. Karger, Basel 1997; 353–372
  • Telen M. J., Chasis J. A. Relationship of the human erythrocyte Wrb antigen to an interaction between glycophorin A and band 3. Blood 1990; 76: 842–848
  • Vince J. W., Reithmeier R. A. F. Structure of the band 3 transmembrane domain. Molecular and Cellular Biology 1996; 42: 1041–1051
  • Wang D. N. Band 3 protein: structure, flexibility and function. FEBS Letters 1994; 346: 26–31
  • Wang C. C., Badylak J. A., Lux S. E., Moriyama R., Dixon J. E., Low P. S. Expression, purification and characterisation of functional dimeric cytoplasmic domain of human erythrocyte band 3 in E. coli. Protein Science 1992; 1: 1206–1214
  • Wang D. N., Kuhlbrandt W., Sarabia V. E., Reithmeier R. A. F. Two dimensional structure of the membrane domain of human band 3, the anion transport protein of the erythrocyte membrane. EMBO Journal 1993; 12: 2233–2239
  • Wang D. N., Sarabia V. E., Reithmeier R. A. F., Kuhlbrandt W. Three-dimensional map of the dimeric membrane domain of the human erythrocyte anion exchanger, band 3. EMBO Journal 1994; 13: 3230–3235
  • Wang L., Groves J. D., Mawby W. J., Tanner M. J. A. 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 1997; 272: 10631–10638
  • Whitley P., von Heijne G. What can glycosylation mapping tell us about membrane protein assembly and structure. Membrane Proteins: Structure, function and expression control, N. Hamasaki, K. Mihara. Karger, Basel 1997; 117–126
  • Wood P. G. The anion exchange proteins: homology and secondary structure. The Band 3 Proteins: Anion transporters, binding proteins and senescent antigens, E. Bamberg, H. Passow. Elsevier, Amsterdam 1992; 2: 325–352, Progress in Cell Research
  • Wrong O., Unwin R., Cohen E., Tanner M., Thakker R. Unravelling of the molecular mechanism of kidney stones. Lancet 1996; 348: 1561–1565
  • Yannoukakos D., Vasseur C., Driancourt C., Blouquit Y., Delaunay J., Wajcman J., Bursaux E. Human erythrocyte band 3 polymorphism (band 3 Memphis): characterisation of the structural modification (Lys56-Glu) by protein chemistry methods. Blood 1991; 78: 1117–1120
  • Yeagle P. L., Alderfer J. L., Albert A. D. Structure of the third cytoplasmic loop of bovine rhodopsin. Biochemistry 1995; 34: 14261–14265
  • Yeagle P. L., Alderfer J. L., Salloum A. C., Ali L., Albert A. D. The first and second cytoplasmic loops of the G-protein receptor, rhodopsin, independently form β-turns. Biochemistry 1997; 36: 3864–3869
  • Zaki L., Bohm R., Merckel M. 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 1996; 42: 1053–1063

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