메뉴 건너뛰기




Volumn 137, Issue 3, 2002, Pages 322-332

Importance of detergent and phospholipid in the crystallization of the human erythrocyte anion-exchanger membrane domain

Author keywords

Anion exchanger 1; Band 3; Crystallization; Detergent; Lipid; Membrane protein

Indexed keywords

CARBON; CYCLOHEXYLHEXYLMALTOSIDE; DECYLTHIOMALTOSIDE; DETERGENT; DODECYLMALTOSIDE; ERYTHROCYTE BAND 3 PROTEIN; PHOSPHOLIPID; UNCLASSIFIED DRUG;

EID: 0036427425     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1047-8477(02)00010-2     Document Type: Article
Times cited : (58)

References (64)
  • 1
    • 0035810954 scopus 로고    scopus 로고
    • High-yield expression and functional analysis of Escherichia coli glycerol-3-phosphate transporter
    • Auer, M., Kim, M.J., Lemieux, M.J., Villa, A., Song, J., Li, X.D., Wang, D.N., 2001. High-yield expression and functional analysis of Escherichia coli glycerol-3-phosphate transporter. Biochemistry 40, 6628-6635.
    • (2001) Biochemistry , vol.40 , pp. 6628-6635
    • Auer, M.1    Kim, M.J.2    Lemieux, M.J.3    Villa, A.4    Song, J.5    Li, X.D.6    Wang, D.N.7
  • 2
    • 0034959596 scopus 로고    scopus 로고
    • Purification and characterization of human erythrocyte glucose transporter in decylmaltoside detergent solution
    • Boulter, J.M., Wang, D.N., 2001. Purification and characterization of human erythrocyte glucose transporter in decylmaltoside detergent solution. Prot. Expr. Purif. 22, 337-348.
    • (2001) Prot. Expr. Purif. , vol.22 , pp. 337-348
    • Boulter, J.M.1    Wang, D.N.2
  • 3
    • 0027312707 scopus 로고
    • Bnad 3 HT, A human red-cell variant associated with acanthocytosis and increased anion transport, carries the mutation Pro-868→Leu in the membrane domain of band 3
    • Bruce, L.J., Kay, M.M., Lawrence, C., Tanner, M.J., 1993. Bnad 3 HT, A human red-cell variant associated with acanthocytosis and increased anion transport, carries the mutation Pro-868→Leu in the membrane domain of band 3. Biochem. J. 293, 317-320.
    • (1993) Biochem. J. , vol.293 , pp. 317-320
    • Bruce, L.J.1    Kay, M.M.2    Lawrence, C.3    Tanner, M.J.4
  • 4
    • 0034669677 scopus 로고    scopus 로고
    • A robust, detergent friendly method for mass spectrometry analysis of integral membrane proteins
    • Cadene, M., Chait, B., 2000. A robust, detergent friendly method for mass spectrometry analysis of integral membrane proteins. Anal. Chem. 72, 5655-5658.
    • (2000) Anal. Chem. , vol.72 , pp. 5655-5658
    • Cadene, M.1    Chait, B.2
  • 5
  • 6
    • 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., Reithmeier, R.A., 1992. Enzymatic deglycosylation of human Band 3, the anion transport protein of the erythrocyte membrane. Effect on protein structure and transport properties. J. Biol. Chem. 267, 11940-11948.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11940-11948
    • Casey, J.R.1    Pirraglia, C.A.2    Reithmeier, R.A.3
  • 7
    • 0025938224 scopus 로고
    • Analysis of the oligomeric state of Band 3, the anion transport protein of the human erythrocyte membrane, by size exclusion high performance liquid chromatography. Oligomeric stability and origin of heterogeneity
    • Casey, J.R., Reithmeier, R.A., 1991. Analysis of the oligomeric state of Band 3, the anion transport protein of the human erythrocyte membrane, by size exclusion high performance liquid chromatography. Oligomeric stability and origin of heterogeneity. J. Biol. Chem. 266, 15726-15737.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15726-15737
    • Casey, J.R.1    Reithmeier, R.A.2
  • 8
    • 0027510320 scopus 로고
    • Detergent interaction with Band 3, a model polytopic membrane protein
    • Casey, J.R., Reithmeier, R.A., 1993. Detergent interaction with Band 3, a model polytopic membrane protein. Biochemistry 32, 1172-1179.
    • (1993) Biochemistry , vol.32 , pp. 1172-1179
    • Casey, J.R.1    Reithmeier, R.A.2
  • 9
    • 4244120872 scopus 로고
    • Microdetermination of phosphorous
    • Chen, P.S., Toribara, T.Y., Warner, H., 1956. Microdetermination of phosphorous. Anal. Chem. 28, 1756-1758.
    • (1956) Anal. Chem. , vol.28 , pp. 1756-1758
    • Chen, P.S.1    Toribara, T.Y.2    Warner, H.3
  • 10
    • 0031148680 scopus 로고    scopus 로고
    • Mass spectrometry of whole proteins eluted from sodium dodecyl sulfate- polyacrylamide gel electrophoresis gels
    • Cohen, S.L., Chait, B.T., 1997. Mass spectrometry of whole proteins eluted from sodium dodecyl sulfate- polyacrylamide gel electrophoresis gels. Anal. Biochem. 247, 257-267.
    • (1997) Anal. Biochem. , vol.247 , pp. 257-267
    • Cohen, S.L.1    Chait, B.T.2
  • 11
    • 0020431632 scopus 로고
    • Characterization of the calorimetric C transition of the human erythrocyte membrane
    • Davio, S.R., Low, P.S., 1982. Characterization of the calorimetric C transition of the human erythrocyte membrane. Biochemistry 21, 3585-3593.
    • (1982) Biochemistry , vol.21 , pp. 3585-3593
    • Davio, S.R.1    Low, P.S.2
  • 12
    • 0030879136 scopus 로고    scopus 로고
    • Membrane cation and anion transport activities in erythrocytes of hereditary spherocytosis: Effects of different membrane protein defects
    • De Franceschi, L., Olivieri, O., Giudice, E., Perrotta, S., Sabato, V., Corrocher, R., Iolascon, A., 1997. Membrane cation and anion transport activities in erythrocytes of hereditary spherocytosis: Effects of different membrane protein defects. Am. J. Hematol. 55, 121-128.
    • (1997) Am. J. Hematol. , vol.55 , pp. 121-128
    • De Franceschi, L.1    Olivieri, O.2    Giudice, E.3    Perrotta, S.4    Sabato, V.5    Corrocher, R.6    Iolascon, A.7
  • 13
    • 0022424027 scopus 로고
    • Specificity of lipid-protein interactions as determined by spectroscopic techniques
    • Devaux, P.F., Seigneuret, M., 1985. Specificity of lipid-protein interactions as determined by spectroscopic techniques. Biochim. Biophys. Acta 822, 63-125.
    • (1985) Biochim. Biophys. Acta , vol.822 , pp. 63-125
    • Devaux, P.F.1    Seigneuret, M.2
  • 14
    • 0027155339 scopus 로고
    • Human erythrocyte band 3. Solubilization and reconstitution into two-dimensional crystals
    • Dolder, M., Walz, T., Hefti, A., Engel, A., 1993. Human erythrocyte band 3. Solubilization and reconstitution into two-dimensional crystals. J. Mol. Biol. 231, 119-132.
    • (1993) J. Mol. Biol. , vol.231 , pp. 119-132
    • Dolder, M.1    Walz, T.2    Hefti, A.3    Engel, A.4
  • 15
    • 0028773466 scopus 로고
    • Use of dynamic light scattering to assess crystallizability of macromolecules and macromolecular assemblies
    • Ferre-D'Amare, A.R., Burley, S.K., 1994. Use of dynamic light scattering to assess crystallizability of macromolecules and macromolecular assemblies. Structure 2, 357-359.
    • (1994) Structure , vol.2 , pp. 357-359
    • Ferre-D'Amare, A.R.1    Burley, S.K.2
  • 16
    • 70449158340 scopus 로고
    • A simple method for the isolation and purification of total lipids from animal tissues
    • Folch, J., Lees, M., Stanley, G.H.S., 1957. A simple method for the isolation and purification of total lipids from animal tissues. J. Biol. Chem. 226, 497-509.
    • (1957) J. Biol. Chem. , vol.226 , pp. 497-509
    • Folch, J.1    Lees, M.2    Stanley, G.H.S.3
  • 17
    • 0021265108 scopus 로고
    • Structure of branched lactosaminoglycan, the carbohydrate moiety of band 3 isolated from adult human erythrocytes
    • Fukuda, M., Dell, A., Oates, J.E., Fukuda, M.N., 1984. Structure of branched lactosaminoglycan, the carbohydrate moiety of band 3 isolated from adult human erythrocytes. J. Biol. Chem. 259, 8260-8273.
    • (1984) J. Biol. Chem. , vol.259 , pp. 8260-8273
    • Fukuda, M.1    Dell, A.2    Oates, J.E.3    Fukuda, M.N.4
  • 18
    • 0031417692 scopus 로고    scopus 로고
    • Hematologically important mutations: Band 3 and protein 4.2 variants in hereditary spherocytosis
    • Gallagher, P.G., Forget, B.G., 1997. Hematologically important mutations: Band 3 and protein 4.2 variants in hereditary spherocytosis. Blood Cells Mol. Dis. 23, 417-421.
    • (1997) Blood Cells Mol. Dis. , vol.23 , pp. 417-421
    • Gallagher, P.G.1    Forget, B.G.2
  • 20
    • 0019036909 scopus 로고
    • Three-dimensional crystals of an integral membrane protein: An initial x-ray analysis
    • Garavito, R.M., Rosenbusch, J.P., 1980. Three-dimensional crystals of an integral membrane protein: An initial x-ray analysis. J. Cell Biol. 86, 327-329.
    • (1980) J. Cell Biol. , vol.86 , pp. 327-329
    • Garavito, R.M.1    Rosenbusch, J.P.2
  • 21
    • 0029142564 scopus 로고
    • Overexpression of integral membrane proteins for structural studies
    • Grisshammer, R., Tate, C.G., 1995. Overexpression of integral membrane proteins for structural studies. Quart. Rev. Biophys. 28, 315-422.
    • (1995) Quart. Rev. Biophys. , vol.28 , pp. 315-422
    • Grisshammer, R.1    Tate, C.G.2
  • 22
    • 0029998532 scopus 로고    scopus 로고
    • Functional cell surface expression of the anion transport domain of human red cell band 3 (AE1) in the yeast Saccharomyces cerevisiae
    • Groves, J.D., Falson, P., Maire, M., Tanner, M.J., 1996. Functional cell surface expression of the anion transport domain of human red cell band 3 (AE1) in the yeast Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 93, 12245-12250.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12245-12250
    • Groves, J.D.1    Falson, P.2    Maire, M.3    Tanner, M.J.4
  • 23
    • 0028890265 scopus 로고
    • Calibration of size-exclusion chromatography: Use of a double Gaussian distribution function to describe pore sizes
    • Harlan, J.E., Picot, D., Loll, P.J., Garavito, R.M., 1995. Calibration of size-exclusion chromatography: Use of a double Gaussian distribution function to describe pore sizes. Anal. Biochem. 224, 557-563.
    • (1995) Anal. Biochem. , vol.224 , pp. 557-563
    • Harlan, J.E.1    Picot, D.2    Loll, P.J.3    Garavito, R.M.4
  • 25
    • 0022555859 scopus 로고
    • Structural aspects of the red cell anion exchange protein
    • Jay, D., Cantley, L., 1986. Structural aspects of the red cell anion exchange protein. Annu. Rev. Biochem. 55, 511-538.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 511-538
    • Jay, D.1    Cantley, L.2
  • 26
    • 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. Ann. Rev. Biophys. Chem. 18, 397-430.
    • (1989) Ann. Rev. Biophys. Chem. , vol.18 , pp. 397-430
    • Jennings, M.L.1
  • 27
    • 0018746219 scopus 로고
    • Anion transport across the erythrocyte membrane, in situ proteolysis of band 3 protein, and cross-linking of proteolytic fragments by 4,4″-diisothiocyano dihydrostilbene-2,2″-disulfonate
    • Jennings, M.L., Passow, H., 1979. Anion transport across the erythrocyte membrane, in situ proteolysis of band 3 protein, and cross-linking of proteolytic fragments by 4,4″-diisothiocyano dihydrostilbene-2,2″-disulfonate. Biochim. Biophys. Acta 554, 498-519.
    • (1979) Biochim. Biophys. Acta , vol.554 , pp. 498-519
    • Jennings, M.L.1    Passow, H.2
  • 28
    • 0032459092 scopus 로고    scopus 로고
    • Pre-steady state transport by erythrocyte band 3 protein: Uphill countertransport induced by the impermeant inhibitor H2DIDS
    • Jennings, M.L., Whitlock, J., Shinde, A., 1998. Pre-steady state transport by erythrocyte band 3 protein: Uphill countertransport induced by the impermeant inhibitor H2DIDS. Biochem. Cell Biol. 76, 807-813.
    • (1998) Biochem. Cell Biol. , vol.76 , pp. 807-813
    • Jennings, M.L.1    Whitlock, J.2    Shinde, A.3
  • 29
    • 0004097382 scopus 로고
    • North-Holland Publications, Amsterdam
    • Kates, M., 1972. Techniques in Lipidology. North-Holland Publications, Amsterdam.
    • (1972) Techniques in Lipidology
    • Kates, M.1
  • 30
    • 0029992660 scopus 로고    scopus 로고
    • Lipid cubic phases: A novel concept for the crystallization of membrane proteins
    • Landau, E.M., Rosenbusch, J., 1996. Lipid cubic phases: A novel concept for the crystallization of membrane proteins. Proc. Natl. Acad. Sci. 93, 14532-14535.
    • (1996) Proc. Natl. Acad. Sci. , vol.93 , pp. 14532-14535
    • Landau, E.M.1    Rosenbusch, J.2
  • 31
    • 0029286220 scopus 로고
    • Transmembrane helix-helix interactions and accessibility of H2DIDS on labelled band 3, the erythrocyte anion exchange protein
    • Landolt-Marticorena, C., Casey, J.R., Reithmeier, R.A., 1995. Transmembrane helix-helix interactions and accessibility of H2DIDS on labelled band 3, the erythrocyte anion exchange protein. Mol. Membr. Biol. 12, 173-182.
    • (1995) Mol. Membr. Biol. , vol.12 , pp. 173-182
    • Landolt-Marticorena, C.1    Casey, J.R.2    Reithmeier, R.A.3
  • 32
    • 0022453762 scopus 로고
    • The use of high-performance liquid chromatography for the determination of size and molecular weight of proteins: A caution and a list of membrane proteins suitable as standards
    • Le Maire, M., Aggerbeck, L.P., Monteilhet, C., Andersen, J.P., Moller, J.V., 1986. The use of high-performance liquid chromatography for the determination of size and molecular weight of proteins: A caution and a list of membrane proteins suitable as standards. Anal. Biochem. 154, 525-535.
    • (1986) Anal. Biochem. , vol.154 , pp. 525-535
    • Le Maire, M.1    Aggerbeck, L.P.2    Monteilhet, C.3    Andersen, J.P.4    Moller, J.V.5
  • 33
    • 0035853476 scopus 로고    scopus 로고
    • Monomeric state and ligand binding of recombinant GABA transporter from Escherichia coli
    • Li, X.D., Villa, A., Gownley, C., Kim, M.J., Song, J.M., Auer, M., Wang, D.N., 2001. Monomeric state and ligand binding of recombinant GABA transporter from Escherichia coli. FEBS Lett. 494, 165-169.
    • (2001) FEBS Lett. , vol.494 , pp. 165-169
    • Li, X.D.1    Villa, A.2    Gownley, C.3    Kim, M.J.4    Song, J.M.5    Auer, M.6    Wang, D.N.7
  • 34
    • 0022495613 scopus 로고
    • Carboxyl methylation of human erythrocyte band 3 in intact cells. Relation to anion transport activity
    • Lou, L.L., Clarke, S., 1986. Carboxyl methylation of human erythrocyte band 3 in intact cells. Relation to anion transport activity. Biochem. J. 235, 183-187.
    • (1986) Biochem. J. , vol.235 , pp. 183-187
    • Lou, L.L.1    Clarke, S.2
  • 35
    • 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
  • 36
    • 0023768321 scopus 로고
    • Structural stability of the erythrocyte anion transporter, band 3, in different lipid environments. A differential scanning calorimetric study
    • Maneri, L.R., Low, P.S., 1988. Structural stability of the erythrocyte anion transporter, band 3, in different lipid environments. A differential scanning calorimetric study. J. Biol. Chem. 263, 16170-16178.
    • (1988) J. Biol. Chem. , vol.263 , pp. 16170-16178
    • Maneri, L.R.1    Low, P.S.2
  • 37
    • 0024510381 scopus 로고
    • Fatty acid composition of lipids which copurify with band 3
    • Maneri, L.R., Low, P.S., 1989. Fatty acid composition of lipids which copurify with band 3. Biochem. Biophys. Res. Commun. 159, 1012-1019.
    • (1989) Biochem. Biophys. Res. Commun. , vol.159 , pp. 1012-1019
    • Maneri, L.R.1    Low, P.S.2
  • 38
    • 0021043946 scopus 로고
    • Fatty acids in plasma and red cell membranes in normal humans
    • Manku, M.S., Horrobin, D.F., Huang, Y.S., Morse, N., 1983. Fatty acids in plasma and red cell membranes in normal humans. Lipids 18, 906-908.
    • (1983) Lipids , vol.18 , pp. 906-908
    • Manku, M.S.1    Horrobin, D.F.2    Huang, Y.S.3    Morse, N.4
  • 39
    • 0020475570 scopus 로고
    • Three-dimensional crystals of a membrane protein complex
    • Michel, H., 1982. Three-dimensional crystals of a membrane protein complex. J. Mol. Biol. 158, 567-572.
    • (1982) J. Mol. Biol. , vol.158 , pp. 567-572
    • Michel, H.1
  • 40
    • 85143328503 scopus 로고
    • General and practical aspects of membrane protein crystallization
    • Michel, H. (Ed.). CRC Press, Boca Raton
    • Michel, H., 1991. General and practical aspects of membrane protein crystallization. In: Michel, H. (Ed.), Crystallization of Membrane Proteins. CRC Press, Boca Raton, pp. 73-88.
    • (1991) Crystallization of Membrane Proteins , pp. 73-88
    • Michel, H.1
  • 41
    • 0027452052 scopus 로고
    • Lipid-protein interactions in crystals of plant light-harvesting complex
    • Nussberger, S., Dörr, K., Wang, D.N., Kühlbrandt, W., 1993. Lipid-protein interactions in crystals of plant light-harvesting complex. J. Mol. Biol. 234, 347-356.
    • (1993) J. Mol. Biol. , vol.234 , pp. 347-356
    • Nussberger, S.1    Dörr, K.2    Wang, D.N.3    Kühlbrandt, W.4
  • 42
    • 0026075781 scopus 로고
    • Palmitoylation of cysteine 69 from the COOH-terminal of band 3 protein in the human erythrocyte membrane. Acylation occurs in the middle of the consensus sequence of F-I-IICLAVL found in band 3 protein and G2 protein of Rift Valley fever virus
    • Okubo, K., Hamasaki, N., Hara, K., Kageura, M., 1991. Palmitoylation of cysteine 69 from the COOH-terminal of band 3 protein in the human erythrocyte membrane. Acylation occurs in the middle of the consensus sequence of F-I-IICLAVL found in band 3 protein and G2 protein of Rift Valley fever virus. J. Biol. Chem. 266, 16420-16424.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16420-16424
    • Okubo, K.1    Hamasaki, N.2    Hara, K.3    Kageura, M.4
  • 43
    • 0028006541 scopus 로고
    • Red blood cell band 3. Lysine 539 and lysine 851 react with the same H2DIDS (4,4′-diisothiocyanodihydrostilbene-2,2′-disulfonic acid) molecule
    • Okubo, K., Kang, D., Hamasaki, N., Jennings, M.L., 1994. Red blood cell band 3. Lysine 539 and lysine 851 react with the same H2DIDS (4,4′-diisothiocyanodihydrostilbene-2,2′-disulfonic acid) molecule. J. Biol. Chem. 269, 1918-1926.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1918-1926
    • Okubo, K.1    Kang, D.2    Hamasaki, N.3    Jennings, M.L.4
  • 44
    • 0022615649 scopus 로고
    • Molecular aspects of band 3 protein-mediated anion transport across the red blood cell membrane
    • Passow, H., 1986. Molecular aspects of band 3 protein-mediated anion transport across the red blood cell membrane. Rev. Physiol. Biochem. Pharmacol. 103, 61-203.
    • (1986) Rev. Physiol. Biochem. Pharmacol. , vol.103 , pp. 61-203
    • Passow, H.1
  • 45
    • 0027991674 scopus 로고
    • Mammalian exchangers and co-transporters
    • Reithmeier, R.A., 1994. Mammalian exchangers and co-transporters. Curr. Opin. Cell Biol. 6, 583-594.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 583-594
    • Reithmeier, R.A.1
  • 46
    • 0035239215 scopus 로고    scopus 로고
    • Approaches to determining membrane protein structures to high resolution: Do selections of subpopulations occur?
    • Rosenbusch, J.P., Lustig, A., Grabo, M., Zulauf, M., Regenass, M., 2001. Approaches to determining membrane protein structures to high resolution: Do selections of subpopulations occur? Micron 32, 75-90.
    • (2001) Micron , vol.32 , pp. 75-90
    • Rosenbusch, J.P.1    Lustig, A.2    Grabo, M.3    Zulauf, M.4    Regenass, M.5
  • 47
    • 0030741753 scopus 로고    scopus 로고
    • Gel filtration chromatographic studies of the isolated membrane domain of band 3
    • Salhany, J.M., Cordes, K.A., Sloan, R.L., 1997. Gel filtration chromatographic studies of the isolated membrane domain of band 3. Mol Membr Biol 14, 71-79.
    • (1997) Mol. Membr. Biol. , vol.14 , pp. 71-79
    • Salhany, J.M.1    Cordes, K.A.2    Sloan, R.L.3
  • 48
    • 0026540522 scopus 로고
    • Structural stability of the erythrocyte anion transporter, band 3, in native membranes and in detergent micelles
    • Sami, M., Malik, S., Watts, A., 1992. Structural stability of the erythrocyte anion transporter, band 3, in native membranes and in detergent micelles. Biochim. Biophys. Acta 1105, 148-154.
    • (1992) Biochim. Biophys. Acta , vol.1105 , pp. 148-154
    • Sami, M.1    Malik, S.2    Watts, A.3
  • 49
    • 0027062891 scopus 로고
    • Factors determining the conformation and quaternary structure of isolated human erythrocyte band 3 in detergent solution
    • Schopfer, L.M., Salhany, J.M., 1992. Factors determining the conformation and quaternary structure of isolated human erythrocyte band 3 in detergent solution. Biochemistry 31, 12610-12617.
    • (1992) Biochemistry , vol.31 , pp. 12610-12617
    • Schopfer, L.M.1    Salhany, J.M.2
  • 50
    • 0023695201 scopus 로고
    • The relationships between oligomeric structure and function of band 3 protein from human erythrocyte membranes: Present knowledge and suggestions for further experiments
    • Schubert, D., 1988. The relationships between oligomeric structure and function of band 3 protein from human erythrocyte membranes: Present knowledge and suggestions for further experiments. Mol. Aspects Med. 10, 233-237.
    • (1988) Mol. Aspects Med. , vol.10 , pp. 233-237
    • Schubert, D.1
  • 51
    • 0029151926 scopus 로고
    • High level expression, partial purification, and functional reconstitution of the human AE1 anion exchanger in Saccharomyces cerevisiae
    • Sekler, I., Kopito, R., Casey, J.R., 1995. High level expression, partial purification, and functional reconstitution of the human AE1 anion exchanger in Saccharomyces cerevisiae. J. Biol. Chem. 270, 21028-21034.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21028-21034
    • Sekler, I.1    Kopito, R.2    Casey, J.R.3
  • 52
    • 0033827754 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic analysis of water channel AQP1
    • Sui, H., Walian, P.J., Tang, G., Oh, A., Jap, B.K., 2000. Crystallization and preliminary X-ray crystallographic analysis of water channel AQP1. Acta Crystallogr D Biol Crystallogr 56, 1198-1200.
    • (2000) Acta Crystallogr. D Biol. Crystallogr. , vol.56 , pp. 1198-1200
    • Sui, H.1    Walian, P.J.2    Tang, G.3    Oh, A.4    Jap, B.K.5
  • 53
    • 0027301429 scopus 로고
    • The major integral proteins of the human red cell
    • Tanner, M.J., 1993. The major integral proteins of the human red cell. Baillieres Clin Haematol 6, 333-356.
    • (1993) Baillieres Clin. Haematol. , vol.6 , pp. 333-356
    • Tanner, M.J.1
  • 54
    • 0345062333 scopus 로고    scopus 로고
    • Binding properties of the stilbene disulfonate sites on human erythrocyte AE1: Kinetic, thermodynamic, and solid state deuterium NMR analyses
    • Taylor, A.M., Grobner, G., Williamson, P.T., Watts, A., 1999. Binding properties of the stilbene disulfonate sites on human erythrocyte AE1: Kinetic, thermodynamic, and solid state deuterium NMR analyses. Biochemistry 38, 11172-11179.
    • (1999) Biochemistry , vol.38 , pp. 11172-11179
    • Taylor, A.M.1    Grobner, G.2    Williamson, P.T.3    Watts, A.4
  • 55
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution
    • Toyoshima, C., Nakasako, M., Nomura, H., Ogawa, H., 2000. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution. Nature 405, 647-655.
    • (2000) Nature , vol.405 , pp. 647-655
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 56
    • 0027957369 scopus 로고
    • Calorimetric evidence for allosteric subunit interactions associated with inhibitor binding to band 3 transporter
    • Van Dort, H.M., Low, P.S., Cordes, K.A., Schopfer, L.M., Salhany, J.M., 1994. Calorimetric evidence for allosteric subunit interactions associated with inhibitor binding to band 3 transporter. J. Biol. Chem. 269, 59-61.
    • (1994) J. Biol. Chem. , vol.269 , pp. 59-61
    • Van Dort, H.M.1    Low, P.S.2    Cordes, K.A.3    Schopfer, L.M.4    Salhany, J.M.5
  • 57
    • 0030966941 scopus 로고    scopus 로고
    • Self-association of Band 3, the human erythrocyte anion exchanger, in detergent solution
    • Vince, J.W., Sarabia, V.E., Reithmeier, R.A., 1997. Self-association of Band 3, the human erythrocyte anion exchanger, in detergent solution. Biochim. Biophys. Acta 1326, 295-306.
    • (1997) Biochim. Biophys. Acta , vol.1326 , pp. 295-306
    • Vince, J.W.1    Sarabia, V.E.2    Reithmeier, R.A.3
  • 58
    • 0028298801 scopus 로고
    • Band 3 protein: Structure, flexibility and function
    • Wang, D.N., 1994. Band 3 protein: Structure, flexibility and function. FEBS Lett. 346, 26-31.
    • (1994) FEBS Lett. , vol.346 , pp. 26-31
    • Wang, D.N.1
  • 59
    • 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., Kühlbrandt, W., Sarabia, V.E., Reithmeier, R.A., 1993. Two-dimensional structure of the membrane domain of human band 3, the anion transport protein of the erythrocyte membrane. EMBO J. 12, 2233-2239.
    • (1993) EMBO J. , vol.12 , pp. 2233-2239
    • Wang, D.N.1    Kühlbrandt, W.2    Sarabia, V.E.3    Reithmeier, R.A.4
  • 60
    • 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, A.F., Kühlbrandt, W., 1994. Three-dimensional map of the dimeric membrane domain of the human erythrocyte anion exchanger, Band 3. EMBO J. 13, 3230-3235.
    • (1994) EMBO J. , vol.13 , pp. 3230-3235
    • Wang, D.N.1    Sarabia, V.E.2    Reithmeier, A.F.3    Kühlbrandt, W.4
  • 61
    • 0022358166 scopus 로고
    • Molecular characterization of the human erythrocyte anion transport protein in octyl glucoside
    • Werner, P.K., Reithmeier, R.A., 1985. Molecular characterization of the human erythrocyte anion transport protein in octyl glucoside. Biochemistry 24, 6375-6381.
    • (1985) Biochemistry , vol.24 , pp. 6375-6381
    • Werner, P.K.1    Reithmeier, R.A.2
  • 62
    • 0030592179 scopus 로고    scopus 로고
    • Crystallization and preliminary structure of beef heart mitochondrial cytochrome-bc1 complex
    • Yu, C.A., Xia, J.Z., Kachurin, A.M., Yu, L., Xia, D., Kim, H., Deisenhofer, J., 1996. Crystallization and preliminary structure of beef heart mitochondrial cytochrome-bc1 complex. Biochim. Biophys. Acta 1275, 47-53.
    • (1996) Biochim. Biophys. Acta , vol.1275 , pp. 47-53
    • Yu, C.A.1    Xia, J.Z.2    Kachurin, A.M.3    Yu, L.4    Xia, D.5    Kim, H.6    Deisenhofer, J.7
  • 63
    • 0034329189 scopus 로고    scopus 로고
    • Crystallographic structure and functional interpretation of the cytoplasmic domain of erythrocyte membrane band 3
    • Zhang, D., Kiyatkin, A., Bolin, J.T., Low, P.S., 2000. Crystallographic structure and functional interpretation of the cytoplasmic domain of erythrocyte membrane band 3. Blood 96, 2925-2933.
    • (2000) Blood , vol.96 , pp. 2925-2933
    • Zhang, D.1    Kiyatkin, A.2    Bolin, J.T.3    Low, P.S.4
  • 64
    • 0034814948 scopus 로고    scopus 로고
    • Expression and characterization of the anion transporter homologue YNL275w in Saccharomyces cerevisiae
    • Zhao, R., Reithmeier, R.A., 2001. Expression and characterization of the anion transporter homologue YNL275w in Saccharomyces cerevisiae. Am. J. Physiol. Cell Physiol. 281, C33-45.
    • (2001) Am. J. Physiol. Cell Physiol. , vol.281
    • Zhao, R.1    Reithmeier, R.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.