메뉴 건너뛰기




Volumn 89, Issue 2, 2011, Pages 200-215

Modelling the structure of the red cell membrane

Author keywords

Band 3 macrocomplex; Erythrocyte; Lipid bilayer; Protein 4.1 junctional complex; Protein modeling

Indexed keywords

BAND 3 MACROCOMPLEX; BLOOD GROUP ANTIGEN; CYTOSKELETAL; CYTOSKELETONS; DISTANCE PARAMETER; ERYTHROCYTE; GAS EXCHANGE; HOMOLOGY MODELLING; MICROVASCULAR; MULTI-PROTEIN COMPLEX; OLIGOMERIC STATE; PROTEIN MODELING; PROTEIN STRUCTURES; RED CELLS; TENTATIVE MODELS;

EID: 79953737352     PISSN: 08298211     EISSN: 12086002     Source Type: Journal    
DOI: 10.1139/O10-154     Document Type: Review
Times cited : (72)

References (89)
  • 1
    • 23244437029 scopus 로고    scopus 로고
    • Identification and functional characterization of protein 4.1R and actin-binding sites in erythrocyte β spectrin: Regulation of the interactions by phosphatidylinositol-4,5-bisphosphate
    • DOI 10.1021/bi047331z
    • An, X., Debnath, G., Guo, X., Liu, S., Lux, S.E., Baines, A., et al. 2005. Identification and functional characterization of protein 4.1R and actin-binding sites in erythrocyte b spectrin: regulation of the interactions by phosphatidylinositol-4, 5-bisphosphate. Biochemistry, 44(31): 10681-10688. doi:10.1021/bi047331z. PMID:16060676. (Pubitemid 41098244)
    • (2005) Biochemistry , vol.44 , Issue.31 , pp. 10681-10688
    • An, X.1    Debnath, G.2    Guo, X.3    Liu, S.4    Lux, S.E.5    Baines, A.6    Gratzer, W.7    Mohandas, N.8
  • 2
    • 42049115740 scopus 로고    scopus 로고
    • Disorders of red cell membrane
    • DOI 10.1111/j.1365-2141.2008.07091.x
    • An, X., and Mohandas, N. 2008. Disorders of red cell membrane. Br. J. Haematol. 141(3): 367-375. PMID:18341630. (Pubitemid 351521152)
    • (2008) British Journal of Haematology , vol.141 , Issue.3 , pp. 367-375
    • An, X.1    Mohandas, N.2
  • 3
    • 70349254604 scopus 로고    scopus 로고
    • Adducin forms a bridge between the erythrocyte membrane and its cytoskeleton and regulates membrane cohesion
    • doi:10.1182/blood-2009-02-203216. PMID: 19567882
    • Anong, W.A., Franco, T., Chu, H., Weis, T.L., Devlin, E.E., Bodine, D.M., et al. 2009. Adducin forms a bridge between the erythrocyte membrane and its cytoskeleton and regulates membrane cohesion. Blood, 114(9): 1904-1912. doi:10.1182/blood-2009-02-203216. PMID:19567882.
    • (2009) Blood , vol.114 , Issue.9 , pp. 1904-1912
    • Anong, W.A.1    Franco, T.2    Chu, H.3    Weis, T.L.4    Devlin, E.E.5    Bodine, D.M.6
  • 4
    • 0021253013 scopus 로고
    • Individuals lacking the Gerbich blood-group antigen have alterations in the human erythrocyte membrane sialoglycoproteins β and γ
    • Anstee, D.J., Ridgwell, K., Tanner, M.J., Daniels, G.L., and Parsons, S.F. 1984. Individuals lacking the Gerbich blood-group antigen have alterations in the human erythrocyte membrane sialoglycoproteins b and g. Biochem. J. 221(1): 97-104. PMID: 6466322. (Pubitemid 14082296)
    • (1984) Biochemical Journal , vol.221 , Issue.1 , pp. 97-104
    • Anstee, D.J.1    Ridgwell, K.2    Tanner, M.J.A.3
  • 5
    • 0023883219 scopus 로고
    • Blood group antigen deficiencies associated with abnormal red cell shape
    • doi:10.1016/0268-960X(88)90033-1. PMID: 3135867
    • Anstee, D.J., and Tanner, M.J. 1988. Blood group antigen deficiencies associated with abnormal red cell shape. Blood Rev. 2(2): 115-120. doi:10.1016/0268-960X(88)90033-1. PMID:3135867.
    • (1988) Blood Rev , vol.2 , Issue.2 , pp. 115-120
    • Anstee, D.J.1    Tanner, M.J.2
  • 6
    • 0025946882 scopus 로고
    • New monoclonal antibodies in CD44 and CD58: Their use to quantify CD44 and CD58 on normal human erythrocytes and to compare the distribution of CD44 and CD58 in human tissues
    • PMID:1721039
    • Anstee, D.J., Gardner, B., Spring, F.A., Holmes, C.H., Simpson, K.L., Parsons, S.F., et al. 1991. New monoclonal antibodies in CD44 and CD58: their use to quantify CD44 and CD58 on normal human erythrocytes and to compare the distribution of CD44 and CD58 in human tissues. Immunology, 74(2): 197-205. PMID:1721039.
    • (1991) Immunology , vol.74 , Issue.2 , pp. 197-205
    • Anstee, D.J.1    Gardner, B.2    Spring, F.A.3    Holmes, C.H.4    Simpson, K.L.5    Parsons, S.F.6
  • 7
    • 0025084457 scopus 로고
    • Radiolabel-transfer cross-linking demonstrates that protein 4.1 binds to the N-terminal region of β spectrin and to actin in binary interactions
    • Becker, P.S., Schwartz, M.A., Morrow, J.S., and Lux, S.E. 1990. Radiolabel-transfer cross-linking demonstrates that protein 4.1 binds to the N-terminal region of b spectrin and to actin in binary interactions. Eur. J. Biochem. 193(3): 827-836. doi:10.1111/j.1432-1033.1990.tb19406.x. PMID:2249696. (Pubitemid 20381715)
    • (1990) European Journal of Biochemistry , vol.193 , Issue.3 , pp. 827-836
    • Becker, P.S.1    Schwartz, M.A.2    Morrow, J.S.3    Lux, S.E.4
  • 8
    • 0028909047 scopus 로고
    • Changes in the blood group Wright antigens are associated with a mutation at amino acid 658 in human erythrocyte band 3: A site of interaction between band 3 and glycophorin A under certain conditions
    • PMID:7812009
    • Bruce, L.J., Ring, S.M., Anstee, D.J., Reid, M.E., Wilkinson, S., and Tanner, M.J. 1995. Changes in the blood group Wright antigens are associated with a mutation at amino acid 658 in human erythrocyte band 3: a site of interaction between band 3 and glycophorin A under certain conditions. Blood, 85(2): 541-547. PMID:7812009.
    • (1995) Blood , vol.85 , Issue.2 , 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.6
  • 9
    • 0038157322 scopus 로고    scopus 로고
    • A band 3-based macrocomplex of integral and peripheral proteins in the RBC membrane
    • doi:10.1182/blood-2002-09-2824. PMID: 12531814
    • Bruce, L.J., Beckmann, R., Ribeiro, M.L., Peters, L.L., Chasis, J.A., Delaunay, J., et al. 2003. A band 3-based macrocomplex of integral and peripheral proteins in the RBC membrane. Blood, 101(10): 4180-U88. doi:10.1182/blood-2002-09-2824. PMID:12531814.
    • (2003) Blood , vol.101 , Issue.10
    • Bruce, L.J.1    Beckmann, R.2    Ribeiro, M.L.3    Peters, L.L.4    Chasis, J.A.5    Delaunay, J.6
  • 10
    • 41949136941 scopus 로고    scopus 로고
    • Red cell membrane transport abnormalities
    • DOI 10.1097/MOH.0b013e3282f97b0a, PII 0006275220080500000006
    • Bruce, L.J. 2008. Red cell membrane transport abnormalities. Curr. Opin. Hematol. 15(3): 184-190. doi:10.1097/MOH. 0b013e3282f97b0a. PMID:18391782. (Pubitemid 351509346)
    • (2008) Current Opinion in Hematology , vol.15 , Issue.3 , pp. 184-190
    • Bruce, L.J.1
  • 11
    • 55149125101 scopus 로고    scopus 로고
    • Structure, function and significance of Rh proteins in red cells
    • doi:10.1097/MOH.0b013e328311f422. PMID: 18832935
    • Burton, N.M., and Anstee, D.J. 2008. Structure, function and significance of Rh proteins in red cells. Curr. Opin. Hematol. 15(6): 625-630. doi:10.1097/MOH.0b013e328311f422. PMID: 18832935.
    • (2008) Curr. Opin. Hematol , vol.15 , Issue.6 , pp. 625-630
    • Burton, N.M.1    Anstee, D.J.2
  • 12
    • 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., and 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(24): 15726-15737. PMID:1874731. (Pubitemid 21907719)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.24 , pp. 15726-15737
    • Casey, J.R.1    Reithmeier, R.A.F.2
  • 14
    • 0022641996 scopus 로고
    • A family demonstrating inheritance of the Leach phenotype: A Gerbich-negative phenotype associated with elliptocytosis
    • Daniels, G.L., Shaw, M.A., Judson, P.A., Reid, M.E., Anstee, D.J., Colpitts, P., et al. 1986. A family demonstrating inheritance of the Leach phenotype: a Gerbich-negative phenotype associated with elliptocytosis. Vox Sang. 50(2): 117-121. doi:10.1111/j.1423-0410.1986.tb04860.x. PMID:3962280. (Pubitemid 16170375)
    • (1986) Vox Sanguinis , vol.50 , Issue.2 , pp. 117-121
    • Daniels, G.L.1    Shaw, M.-A.2    Judson, P.A.3
  • 15
    • 0003519583 scopus 로고
    • Blackwell Scientific Publications, Oxford, UK
    • Daniels, G. 1995. Human blood groups. Blackwell Scientific Publications, Oxford, UK.
    • (1995) Human Blood Groups
    • Daniels, G.1
  • 16
    • 0014804933 scopus 로고
    • Membrane splitting in freezeetching. Covalently bound ferritin as a membrane marker
    • doi:10.1083/jcb.45.3.598. PMID: 4918216
    • da Silva, P.P., and Branton, D. 1970. Membrane splitting in freezeetching. Covalently bound ferritin as a membrane marker. J. Cell Biol. 45(3): 598-605. doi:10.1083/jcb.45.3.598. PMID: 4918216.
    • (1970) J. Cell Biol , vol.45 , Issue.3 , pp. 598-605
    • Da Silva, P.P.1    Branton, D.2
  • 17
    • 33846274937 scopus 로고    scopus 로고
    • The molecular basis of hereditary red cell membrane disorders
    • DOI 10.1016/j.blre.2006.03.005, PII S0268960X06000257
    • Delaunay, J. 2007. The molecular basis of hereditary red cell membrane disorders. Blood Rev. 21(1): 1-20. doi:10.1016/j.blre. 2006.03.005. PMID:16730867. (Pubitemid 46110925)
    • (2007) Blood Reviews , vol.21 , Issue.1 , pp. 1-20
    • Delaunay, J.1
  • 18
    • 0014980851 scopus 로고
    • Maternal anti-LW
    • doi:10.1111/j. 1537-2995.1971.tb04372.x. PMID:5313203
    • DeVeber, L.L., Clark, G.W., Hunking, M., and Stroup, M. 1971. Maternal anti-LW. Transfusion, 11(1): 33-35. doi:10.1111/j. 1537-2995.1971.tb04372.x. PMID:5313203.
    • (1971) Transfusion , vol.11 , Issue.1 , pp. 33-35
    • Deveber, L.L.1    Clark, G.W.2    Hunking, M.3    Stroup, M.4
  • 19
    • 0037122805 scopus 로고    scopus 로고
    • X-ray structure of a CIC chloride channel at 3.0 A reveals the molecular basis of anion selectivity
    • DOI 10.1038/415287a
    • Dutzler, R., Campbell, E.B., Cadene, M., Chait, B.T., and MacKinnon, R. 2002. X-ray structure of a ClC chloride channel at 3.0 A reveals the molecular basis of anion selectivity. Nature, 415(6869): 287-294. doi:10.1038/415287a. PMID:11796999. (Pubitemid 34087544)
    • (2002) Nature , vol.415 , Issue.6869 , pp. 287-294
    • Dutzler, R.1    Campbell, E.B.2    Cadene, M.3    Chait, B.T.4    MacKinnon, R.5
  • 20
    • 0028336757 scopus 로고
    • Topology and organization of human Rh (rhesus) blood group-related polypeptides
    • Eyers, S.A., Ridgwell, K., Mawby, W.J., and Tanner, M.J. 1994. Topology and organization of human Rh (rhesus) blood grouprelated polypeptides. J. Biol. Chem. 269(9): 6417-6423. PMID: 8119991. (Pubitemid 24191014)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.9 , pp. 6417-6423
    • Eyers, S.A.C.1    Ridgwell, K.2    Mawby, W.J.3    Tanner, M.J.A.4
  • 21
    • 0026554403 scopus 로고
    • New monoclonal antibodies in CD59: Use for the analysis of peripheral blood cells from paroxysmal nocturnal haemoglobinuria (PNH) patients and for the quantitation of CD59 on normal and decay accelerating factor (DAF)deficient erythrocytes
    • PMID: 1374058
    • Fletcher, A., Bryant, J.A., Gardner, B., Judson, P.A., Spring, F.A., Parsons, S.F., et al. 1992. New monoclonal antibodies in CD59: use for the analysis of peripheral blood cells from paroxysmal nocturnal haemoglobinuria (PNH) patients and for the quantitation of CD59 on normal and decay accelerating factor (DAF)deficient erythrocytes. Immunology, 75(3): 507-512. PMID: 1374058.
    • (1992) Immunology , vol.75 , Issue.3 , pp. 507-512
    • Fletcher, A.1    Bryant, J.A.2    Gardner, B.3    Judson, P.A.4    Spring, F.A.5    Parsons, S.F.6
  • 22
    • 1942445176 scopus 로고    scopus 로고
    • Hereditary elliptocytosis: Spectrin and protein 4
    • doi:10.1053/j. seminhematol.2004.01.003. PMID:15071791
    • Gallagher, P.G. 2004. Hereditary elliptocytosis: spectrin and protein 4.R. Semin. Hematol. 41(2): 142-164. doi:10.1053/j. seminhematol.2004.01.003. PMID:15071791.
    • (2004) R. Semin. Hematol , vol.41 , Issue.2 , pp. 142-164
    • Gallagher, P.G.1
  • 23
    • 0024433989 scopus 로고
    • Epitopes on sialoglycoprotein α: Evidence for heterogeneity in the molecule
    • Gardner, B., Parsons, S.F., Merry, A.H., and Anstee, D.J. 1989. Epitopes on sialoglycoprotein a: evidence for heterogeneity in the molecule. Immunology, 68(2): 283-289. PMID:2478454. (Pubitemid 19246575)
    • (1989) Immunology , vol.68 , Issue.2 , pp. 283-289
    • Gardner, B.1    Parsons, S.F.2    Merry, A.H.3    Anstee, D.J.4
  • 24
    • 0026181869 scopus 로고
    • The abundance and organization of polypeptides associated with antigens of the Rh blood group system
    • doi:10.1111/j.1365-3148.1991.tb00013.x. PMID: 9259831
    • Gardner, B., Anstee, D.J., Mawby, W.J., Tanner, M.J., and von dem Borne, A.E. 1991. The abundance and organization of polypeptides associated with antigens of the Rh blood group system. Transfus. Med. 1(2): 77-85. doi:10.1111/j.1365-3148.1991.tb00013.x. PMID:9259831.
    • (1991) Transfus. Med , vol.1 , Issue.2 , pp. 77-85
    • Gardner, B.1    Anstee, D.J.2    Mawby, W.J.3    Tanner, M.J.4    Von Dem Borne, A.E.5
  • 25
    • 0020490532 scopus 로고
    • Erythrocyte membrane skeletal protein bands 4.1 a and b are sequence-related phosphoproteins
    • PMID:7068651
    • Goodman, S.R., Yu, J., Whitfield, C.F., Culp, E.N., and Posnak, E.J. 1982. Erythrocyte membrane skeletal protein bands 4.1 a and b are sequence-related phosphoproteins. J. Biol. Chem. 257(8): 4564-4569. PMID:7068651.
    • (1982) J. Biol. Chem , vol.257 , Issue.8 , pp. 4564-4569
    • Goodman, S.R.1    Yu, J.2    Whitfield, C.F.3    Culp, E.N.4    Posnak, E.J.5
  • 26
    • 0029903197 scopus 로고    scopus 로고
    • Electron-crystallographic refinement of the structure of bacteriorhodopsin
    • DOI 10.1006/jmbi.1996.0328
    • Grigorieff, N., Ceska, T.A., Downing, K.H., Baldwin, J.M., and Henderson, R. 1996. Electron-crystallographic refinement of the structure of bacteriorhodopsin. J. Mol. Biol. 259(3): 393-421. doi:10.1006/jmbi.1996.0328. PMID:8676377. (Pubitemid 26179019)
    • (1996) Journal of Molecular Biology , vol.259 , Issue.3 , pp. 393-421
    • Grigorieff, N.1    Ceska, T.A.2    Downing, K.H.3    Baldwin, J.M.4    Henderson, R.5
  • 27
    • 0026499518 scopus 로고
    • Glycophorin A facilitates the expression of human band 3-mediated anion transport in Xenopus oocytes
    • PMID: 1385395
    • Groves, J.D., and Tanner, M.J. 1992. Glycophorin A facilitates the expression of human band 3-mediated anion transport in Xenopus oocytes. J. Biol. Chem. 267(31): 22163-22170. PMID: 1385395.
    • (1992) J. Biol. Chem , vol.267 , Issue.31 , pp. 22163-22170
    • Groves, J.D.1    Tanner, M.J.2
  • 28
    • 77953097228 scopus 로고    scopus 로고
    • Function of human Rh based on structure of RhCG at 2.1 A
    • doi:10.1073/pnas.1003587107. PMID: 20457942
    • Gruswitz, F., Chaudhary, S., Ho, J.D., Schlessinger, A., Pezeshki, B., Ho, C.M., et al. 2010. Function of human Rh based on structure of RhCG at 2.1 A. Proc. Natl. Acad. Sci. U.S.A. 107(21): 9638-9643. doi:10.1073/pnas.1003587107. PMID:20457942.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , Issue.21 , pp. 9638-9643
    • Gruswitz, F.1    Chaudhary, S.2    Ho, J.D.3    Schlessinger, A.4    Pezeshki, B.5    Ho, C.M.6
  • 29
    • 0033790239 scopus 로고    scopus 로고
    • Protein 4.1R core domain structure and insights into regulation of cytoskeletal organization
    • doi:10.1038/82819. PMID: 11017195
    • Han, B.-G., Nunomura, W., Takakuwa, Y., Mohandas, N., and Jap, B.K. 2000. Protein 4.1R core domain structure and insights into regulation of cytoskeletal organization. Nat. Struct. Biol. 7(10): 871-875. doi:10.1038/82819. PMID:11017195.
    • (2000) Nat. Struct. Biol , vol.7 , Issue.10 , pp. 871-875
    • Han, B.-G.1    Nunomura, W.2    Takakuwa, Y.3    Mohandas, N.4    Jap, B.K.5
  • 30
    • 47349105855 scopus 로고    scopus 로고
    • Paired Receptor Specificity Explained by Structures of Signal Regulatory Proteins Alone and Complexed with CD47
    • DOI 10.1016/j.molcel.2008.05.026, PII S1097276508004346
    • Hatherley, D., Graham, S.C., Turner, J., Harlos, K., Stuart, D.I., and Barclay, A.N. 2008. Paired receptor specificity explained by structures of signal regulatory proteins alone and complexed with CD47. Mol. Cell, 31(2): 266-277. doi:10.1016/j.molcel. 2008.05.026. PMID:18657508. (Pubitemid 352001399)
    • (2008) Molecular Cell , vol.31 , Issue.2 , pp. 266-277
    • Hatherley, D.1    Graham, S.C.2    Turner, J.3    Harlos, K.4    Stuart, D.I.5    Barclay, A.N.6
  • 31
    • 0028944110 scopus 로고
    • Identification of the membrane attachment sites for protein 4.1 in the human erythrocyte
    • doi:10.1074/jbc.270.10.5360. PMID: 7890649
    • Hemming, N.J., Anstee, D.J., Staricoff, M.A., Tanner, M.J., and Mohandas, N. 1995. Identification of the membrane attachment sites for protein 4.1 in the human erythrocyte. J. Biol. Chem. 270(10): 5360-5366. doi:10.1074/jbc.270.10. 5360. PMID: 7890649.
    • (1995) J. Biol. Chem , vol.270 , Issue.10 , pp. 5360-5366
    • Hemming, N.J.1    Anstee, D.J.2    Staricoff, M.A.3    Tanner, M.J.4    Mohandas, N.5
  • 32
    • 0025075839 scopus 로고
    • Atomic model of the actin filament
    • doi:10.1038/347044a0. PMID:2395461
    • Holmes, K.C., Popp, D., Gebhard, W., and Kabsch, W. 1990. Atomic model of the actin filament. Nature, 347(6288): 44-49. doi:10.1038/347044a0. PMID:2395461.
    • (1990) Nature , vol.347 , Issue.6288 , pp. 44-49
    • Holmes, K.C.1    Popp, D.2    Gebhard, W.3    Kabsch, W.4
  • 33
    • 0029022939 scopus 로고
    • Adducin: A physical model with implications for function in assembly of spectrin-actin complexes
    • doi:10.1074/ jbc.270.32.18990. PMID:7642559
    • Hughes, C.A., and Bennett, V. 1995. Adducin: a physical model with implications for function in assembly of spectrin-actin complexes. J. Biol. Chem. 270(32): 18990-18996. doi:10.1074/ jbc.270.32.18990. PMID:7642559.
    • (1995) J. Biol. Chem , vol.270 , Issue.32 , pp. 18990-18996
    • Hughes, C.A.1    Bennett, V.2
  • 34
    • 62549129569 scopus 로고    scopus 로고
    • Structures of the spectrin-ankyrin interaction binding domains
    • doi:10.1182/blood-2008-10-184358. PMID: 19141864
    • Ipsaro, J.J., Huang, L., and Mondragon, A. 2009. Structures of the spectrin-ankyrin interaction binding domains. Blood, 113(22): 5385-5393. doi:10.1182/blood-2008-10-184358. PMID: 19141864.
    • (2009) Blood , vol.113 , Issue.22 , pp. 5385-5393
    • Ipsaro, J.J.1    Huang, L.2    Mondragon, A.3
  • 35
    • 0022555859 scopus 로고
    • Structural aspects of the red cell anion exchange protein
    • Jay, D., and Cantley, L. 1986. Structural aspects of the red cell anion exchange protein. Annu. Rev. Biochem. 55(1): 511-538. doi:10.1146/annurev.bi.55. 070186.002455. PMID:3527050. (Pubitemid 16070779)
    • (1986) Annual Review of Biochemistry , vol.VOL. 55 , pp. 511-538
    • Jay, D.1    Cantley, L.2
  • 36
    • 32044451299 scopus 로고    scopus 로고
    • A phosphorylation-induced conformation change in dematin headpiece
    • DOI 10.1016/j.str.2005.11.007, PII S0969212606000347
    • Jiang, Z.G., and McKnight, C.J. 2006. A phosphorylation-induced conformation change in dematin headpiece. Structure, 14(2): 379-387. doi:10.1016/j.str.2005.11.007. PMID:16472756. (Pubitemid 43202026)
    • (2006) Structure , vol.14 , Issue.2 , pp. 379-387
    • Jiang, Z.G.1    McKnight, C.J.2
  • 37
    • 78650324021 scopus 로고    scopus 로고
    • KASH (KEL34): A novel high incidence antigen in the Kell blood group system
    • Abstract
    • Karamatic Crew, V., Poole, J., Watson, T., Bullock, T., Burton, N., and Daniels, G. 2010. KASH (KEL34): A novel high incidence antigen in the Kell blood group system. Vox Sang. 99(Suppl. 1): 357. [Abstract.
    • (2010) Vox Sang , Issue.99 SUPPL. 1 , pp. 357
    • Karamatic Crew, V.1    Poole, J.2    Watson, T.3    Bullock, T.4    Burton, N.5    Daniels, G.6
  • 38
    • 0034113611 scopus 로고    scopus 로고
    • Molecular genetic analysis of the Japanese amorph Rh(null) phenotype [5]
    • DOI 10.1046/j.1537-2995.2000.40050617.x
    • Kato-Yamazaki, M., Okuda, H., Kawano, M., Omi, T., Iwamoto, T., Ishimori, T., et al. 2000. Molecular genetic analysis of the Japanese amorph Rhnull phenotype. Transfusion, 40(5): 617-618. doi:10.1046/j.1537-2995.2000.40050617.x. PMID: 10827273. (Pubitemid 30333895)
    • (2000) Transfusion , vol.40 , Issue.5 , pp. 617-618
    • Kato-Yamazaki, M.1    Okuda, H.2    Kawano, M.3    Omi, T.4    Iwamoto, T.5    Ishimori, T.6    Hasekura, H.7    Kajii, E.8
  • 39
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: A case study using the Phyre server
    • doi:10.1038/nprot.2009.2. PMID: 19247286
    • Kelley, L.A., and Sternberg, M.J.E. 2009. Protein structure prediction on the Web: a case study using the Phyre server. Nat. Pro-toc. 4(3): 363-371. doi:10.1038/nprot.2009.2. PMID:19247286.
    • (2009) Nat. Pro-toc , vol.4 , Issue.3 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.E.2
  • 40
    • 47249139953 scopus 로고    scopus 로고
    • Dematin and adducin provide a novel link between the spectrin cytoskeleton and human erythrocyte membrane by directly interacting with glucose transporter-1
    • doi:10.1074/jbc.M707818200. PMID: 18347014
    • Khan, A.A., Hanada, T., Mohseni, M., Jeong, J.J., Zeng, L., Gaetani, M., et al. 2008. Dematin and adducin provide a novel link between the spectrin cytoskeleton and human erythrocyte membrane by directly interacting with glucose transporter-1. J. Biol. Chem. 283(21): 14600-14609. doi:10.1074/jbc.M707818200. PMID:18347014.
    • (2008) J. Biol. Chem , vol.283 , Issue.21 , pp. 14600-14609
    • Khan, A.A.1    Hanada, T.2    Mohseni, M.3    Jeong, J.J.4    Zeng, L.5    Gaetani, M.6
  • 41
    • 58149193233 scopus 로고    scopus 로고
    • The SWISS-MODEL Repository and associated resources
    • doi:10. 1093/nar/gkn750. PMID:18931379
    • Kiefer, F., Arnold, K., KUnzli, M., Bordoli, L., and Schwede, T. 2009. The SWISS-MODEL Repository and associated resources. Nucleic Acids Res. 37(Database issue): D387-D392. doi:10. 1093/nar/gkn750. PMID:18931379.
    • (2009) Nucleic Acids Res , vol.37 , Issue.DATABASE ISSUE
    • Kiefer, F.1    Arnold, K.2    Kunzli, M.3    Bordoli, L.4    Schwede, T.5
  • 43
    • 77955837990 scopus 로고    scopus 로고
    • Analysis of the kinetics of band 3 diffusion in human erythroblasts during assembly of the erythrocyte membrane skeleton
    • doi:10.1111/j.1365-2141.2010.08268.x. PMID: 20553270
    • Kodippili, G.C., Spector, J., Kang, G.E., Liu, H., Wickrema, A., Ritchie, K., and Low, P.S. 2010. Analysis of the kinetics of band 3 diffusion in human erythroblasts during assembly of the erythrocyte membrane skeleton. Br. J. Haematol. 150(5): 592-600. doi:10.1111/j.1365-2141.2010.08268.x. PMID:20553270.
    • (2010) Br. J. Haematol , vol.150 , Issue.5 , pp. 592-600
    • Kodippili, G.C.1    Spector, J.2    Kang, G.E.3    Liu, H.4    Wickrema, A.5    Ritchie, K.6    Low, P.S.7
  • 44
    • 77951167838 scopus 로고    scopus 로고
    • Protein 4.2 binds to the carboxyl-terminal EF-hands of erythroid a-spectrin in a calciumand calmodulin-dependent manner
    • doi:10.1074/jbc.M109.056200. PMID: 20007969
    • Korsgren, C., Peters, L.L., and Lux, S.E. 2010. Protein 4.2 binds to the carboxyl-terminal EF-hands of erythroid a-spectrin in a calciumand calmodulin-dependent manner. J. Biol. Chem. 285(7): 4757-4770. doi:10.1074/jbc.M109.056200. PMID:20007969.
    • (2010) J. Biol. Chem. , vol.285 , Issue.7 , pp. 4757-4770
    • Korsgren, C.1    Peters, L.L.2    Lux, S.E.3
  • 45
    • 34250615914 scopus 로고    scopus 로고
    • Structural insight into the interaction between the p55 PDZ domain and glycophorin C
    • DOI 10.1016/j.bbrc.2007.05.215, PII S0006291X07012119
    • Kusunoki, H., and Kohno, T. 2007. Structural insight into the interaction between the p55 PDZ domain and glycophorin C. Biochem. Biophys. Res. Commun. 359(4): 972-978. doi:10.1016/j. bbrc.2007.05.215. PMID:17572384. (Pubitemid 46946913)
    • (2007) Biochemical and Biophysical Research Communications , vol.359 , Issue.4 , pp. 972-978
    • Kusunoki, H.1    Kohno, T.2
  • 46
    • 76749133529 scopus 로고    scopus 로고
    • Ankyrin recognizes both surface character and shape of the 14-15 di-repeat of b-spectrin
    • doi:10.1016/j.bbrc.2010.01.046. PMID: 20079712
    • La-Borde, P.J., Stabach, P.R., Simonovic, I., Morrow, J.S., and Simonovic, M. 2010. Ankyrin recognizes both surface character and shape of the 14-15 di-repeat of b-spectrin. Biochem. Bio-phys. Res. Commun. 392(4): 490-194. doi:10.1016/j.bbrc.2010.01.046. PMID:20079712.
    • (2010) Biochem. Bio-phys. Res. Commun , vol.392 , Issue.4 , pp. 490-194
    • La-Borde, P.J.1    Stabach, P.R.2    Simonovic, I.3    Morrow, J.S.4    Simonovic, M.5
  • 48
    • 0030586030 scopus 로고    scopus 로고
    • The first step in sugar transport: Crystal structure of the amino terminal domain of enzyme I of the E. coli PEP: Sugar phosphotransferase system and a model of the phosphotransfer complex with HPr
    • DOI 10.1016/S0969-2126(96)00092-5
    • Liao, D.I., Silverton, E., Seok, Y.J., Lee, B.R., Peterkofsky, A., and Davies, D.R. 1996. The first step in sugar transport: crystal structure of the amino terminal domain of enzyme I of the E. coli PEP: sugar phosphotransferase system and a model of the phosphotransfer complex with HPr. Structure, 4(7): 861-872. doi:10.1016/S0969-2126(96)00092-5. PMID:8805571. (Pubitemid 26312369)
    • (1996) Structure , vol.4 , Issue.7 , pp. 861-872
    • Liao, D.-I.1    Silverton, E.2    Seok, Y.-J.3    Lee, B.R.4    Peterkofsky, A.5    Davies, D.R.6
  • 49
    • 0023150141 scopus 로고
    • Visualization of the hexagonal lattice in the erythrocyte membrane skeleton
    • DOI 10.1083/jcb.104.3.527
    • Liu, S.C., Derick, L.H., and Palek, J. 1987. Visualization of the hexagonal lattice in the erythrocyte membrane skeleton. J. Cell Biol. 104(3): 527-536. doi:10.1083/jcb.104.3.527. PMID: 2434513. (Pubitemid 17024707)
    • (1987) Journal of Cell Biology , vol.104 , Issue.3 , pp. 527-536
    • Liu, S.-C.1    Derick, L.H.2    Palek, J.3
  • 50
    • 0029029602 scopus 로고
    • Molecular basis of altered red blood cell membrane properties in Southeast Asian ovalocytosis: Role of the mutant band 3 protein in band 3 oligomerization and retention by the membrane skeleton
    • PMID:7795244
    • Liu, S.C., Palek, J., Yi, S.J., Nichols, P.E., Derick, L.H., Chiou, S.S., et al. 1995. Molecular basis of altered red blood cell membrane properties in Southeast Asian ovalocytosis: role of the mutant band 3 protein in band 3 oligomerization and retention by the membrane skeleton. Blood, 86(1): 349-358. PMID:7795244.
    • (1995) Blood , vol.86 , Issue.1 , 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
  • 51
    • 72149092404 scopus 로고    scopus 로고
    • Blood-related proteomics
    • doi:10. 1016/j.jprot.2009.06.010. PMID:19567275
    • Liumbruno, G., D'Alessandro, A., Grazzini, G., and Zolla, L. 2010. Blood-related proteomics. J. Proteomics, 73(3): 483-507. doi:10. 1016/j.jprot.2009.06.010. PMID:19567275.
    • (2010) J. Proteomics , vol.73 , Issue.3 , pp. 483-507
    • Liumbruno, G.1    D'Alessandro, A.2    Grazzini, G.3    Zolla, L.4
  • 53
    • 0030932407 scopus 로고    scopus 로고
    • Transmembrane helix dimer: Structure and implications
    • DOI 10.1126/science.276.5309.131
    • MacKenzie, K.R., Prestegard, J.H., and Engelman, D.M. 1997. A transmembrane helix dimer: structure and implications. Science, 276(5309): 131-133. doi:10.1126/science.276.5309.131. PMID: 9082985. (Pubitemid 27161261)
    • (1997) Science , vol.276 , Issue.5309 , pp. 131-133
    • MacKenzie, K.R.1    Prestegard, J.H.2    Engelman, D.M.3
  • 54
    • 0027403576 scopus 로고
    • Estimate of the number of urea transport sites in erythrocyte ghosts using a hydrophobic mercurial
    • Mannuzzu, L.M., Moronne, M.M., and Macey, R.I. 1993. Estimate of the number of urea transport sites in erythrocyte ghosts using a hydrophobic mercurial. J. Membr. Biol. 133(1): 85-97. PMID: 8391582. (Pubitemid 23116350)
    • (1993) Journal of Membrane Biology , vol.133 , Issue.1 , pp. 85-97
    • Mannuzzu, L.M.1    Moronne, M.M.2    Macey, R.I.3
  • 55
    • 0014411415 scopus 로고
    • Selective solubilization of a protein component of the red cell membrane
    • doi:10.1126/science.159.3811.203. PMID: 5634911
    • Marchesi, V.T., and Steers, E., Jr. 1968. Selective solubilization of a protein component of the red cell membrane. Science, 159(3811): 203-204. doi:10.1126/science.159.3811.203. PMID: 5634911.
    • (1968) Science , vol.159 , Issue.3811 , pp. 203-204
    • Marchesi, V.T.1    Steers Jr., E.2
  • 56
    • 0023269408 scopus 로고
    • b on human erythrocytes
    • Merry, A.H., Gardner, B., Parsons, S.F., and Anstee, D.J. 1987. Estimation of the number of binding sites for a murine monoclonal anti-Lub on human erythrocytes. Vox Sang. 53(1): 57-60. doi:10.1111/j.1423-0410.1987. tb04915.x. PMID:3660770. (Pubitemid 17098394)
    • (1987) Vox Sanguinis , vol.53 , Issue.1 , pp. 57-60
    • Merry, A.H.1    Gardner, B.2    Parsons, S.F.3    Anstee, D.J.4
  • 57
    • 0029150191 scopus 로고
    • The ANK repeats of erythrocyte ankyrin form two distinct but cooperative binding sites for the erythrocyte anion exchanger
    • doi:10.1074/jbc.270.37.22050. PMID: 7665627
    • Michaely, P., and Bennett, V. 1995. The ANK repeats of erythrocyte ankyrin form two distinct but cooperative binding sites for the erythrocyte anion exchanger. J. Biol. Chem. 270(37): 22050-22057. doi:10.1074/jbc.270.37. 22050. PMID:7665627.
    • (1995) J. Biol. Chem , vol.270 , Issue.37 , pp. 22050-22057
    • Michaely, P.1    Bennett, V.2
  • 58
    • 0037011104 scopus 로고    scopus 로고
    • Crystal structure of a 12 ANK repeat stack from human ankyrinR
    • DOI 10.1093/emboj/cdf651
    • Michaely, P., Tomchick, D.R., Machius, M., and Anderson, R.G. 2002. Crystal structure of a 12 ANK repeat stack from human ankyrinR. EMBO J. 21(23): 6387-6396. doi:10.1093/emboj/cdf651. PMID:12456646. (Pubitemid 35448417)
    • (2002) EMBO Journal , vol.21 , Issue.23 , pp. 6387-6396
    • Michaely, P.1    Tomchick, D.R.2    Machius, M.3    Anderson, R.G.W.4
  • 59
    • 33645320817 scopus 로고    scopus 로고
    • + symport in LacY
    • doi:10.1038/sj.emboj.7601028. PMID: 16525509
    • Mirza, O., Guan, L., Verner, G., Iwata, S., and Kaback, H.R. 2006. Structural evidence for induced fit and a mechanism for sugar/ H+ symport in LacY. EMBO J. 25(6): 1177-1183. doi:10.1038/sj.emboj.7601028. PMID:16525509.
    • (2006) EMBO J , vol.25 , Issue.6 , pp. 1177-1183
    • Mirza, O.1    Guan, L.2    Verner, G.3    Iwata, S.4    Kaback, H.R.5
  • 60
    • 0023600841 scopus 로고
    • Erythrocyte adducin: A calmodulin-regulated actin-bundling protein that stimulates spectrin-actin binding
    • DOI 10.1083/jcb.105.6.2837
    • Mische, S.M., Mooseker, M.S., and Morrow, J.S. 1987. Erythrocyte adducin: a calmodulin-regulated actin-bundling protein that stimulates spectrin-actin binding. J. Cell Biol. 105(6): 2837-2845. doi:10.1083/jcb.105.6.2837. PMID:3693401. (Pubitemid 18017714)
    • (1987) Journal of Cell Biology , vol.105 , Issue.6 , pp. 2837-2845
    • Mische, S.M.1    Mooseker, M.S.2    Morrow, J.S.3
  • 62
    • 33646163010 scopus 로고    scopus 로고
    • Extending a spectrin repeat unit. I: Linear force-extension response
    • doi:10.1529/biophysj.105. 066969. PMID:16227506
    • Paramore, S., Ayton, G.S., Mirijanian, D.T., and Voth, G.A. 2006., Extending a spectrin repeat unit. I: linear force-extension response. Biophys. J. 90(1): 92-100. doi:10.1529/biophysj.105. 066969. PMID:16227506.
    • (2006) Biophys. J , vol.90 , Issue.1 , pp. 92-100
    • Paramore, S.1    Ayton, G.S.2    Mirijanian, D.T.3    Voth, G.A.4
  • 63
    • 0027616610 scopus 로고
    • Monoclonal antibodies against Kell glycoprotein: Serology, immunochemistry and quantification of antigen sites
    • doi:10.1111/j.1365-3148.1993.tb00051.x. PMID: 7690639
    • Parsons, S.F., Gardner, B., and Anstee, D.J. 1993. Monoclonal antibodies against Kell glycoprotein: serology, immunochemistry and quantification of antigen sites. Transfus. Med. 3(2): 137-142. doi:10.1111/j.1365-3148.1993. tb00051.x. PMID:7690639.
    • (1993) Transfus. Med , vol.3 , Issue.2 , pp. 137-142
    • Parsons, S.F.1    Gardner, B.2    Anstee, D.J.3
  • 64
    • 0028088012 scopus 로고
    • Mutations in aquaporin-1 in phenotypically normal humans without functional CHIP water channels
    • Preston, G.M., Smith, B.L., Zeidel, M.L., Moulds, J.J., and Agre, P. 1994. Mutations in aquaporin-1 in phenotypically normal humans without functional CHIP water channels. Science, 265(5178): 1585-1587. doi:10.1126/science.7521540. PMID: 7521540. (Pubitemid 24308974)
    • (1994) Science , vol.265 , Issue.5178 , pp. 1585-1587
    • Preston, G.M.1    Smith, B.L.2    Zeidel, M.L.3    Moulds, J.J.4    Agre, P.5
  • 68
    • 0028287321 scopus 로고
    • Studies on the glycoprotein associated with Rh (rhesus) blood group antigen expression in the human red blood cell membrane
    • Ridgwell, K., Eyers, S.A., Mawby, W.J., Anstee, D.J., and Tanner, M.J. 1994. Studies on the glycoprotein associated with Rh (rhesus) blood group antigen expression in the human red blood cell membrane. J. Biol. Chem. 269(9): 6410-6416. PMID: 7509803. (Pubitemid 24191013)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.9 , pp. 6410-6416
    • Ridgwell, K.1    Eyers, S.A.C.2    Mawby, W.J.3    Anstee, D.J.4    Tanner, M.J.A.5
  • 70
    • 0027982771 scopus 로고
    • Production of a new murine monoclonal antibody with Fy6 specificity and characterization of the immunopurified N-glycosylated Duffy-active molecule
    • Riwom, S., Janvier, D., Navenot, J.M., Benbunan, M., Muller, J.Y., and Blanchard, D. 1994. Production of a new murine monoclonal antibody with Fy6 specificity and characterization of the immunopurified N-glycosylated Duffy-active molecule. Vox Sang. 66(1): 61-67. doi:10.1111/j.1423-0410.1994. tb00279.x. PMID: 8146985. (Pubitemid 24017160)
    • (1994) Vox Sanguinis , vol.66 , Issue.1 , pp. 61-67
    • Riwom, S.1    Janvier, D.2    Navenot, J.M.3    Benbunan, M.4    Muller, J.Y.5    Blanchard, D.6
  • 71
    • 12344321851 scopus 로고    scopus 로고
    • Predicting the three-dimensional structure of the human facilitative glucose transporter Glut1 by a novel evolutionary homology strategy: Insights on the molecular mechanism of substrate migration, and binding for glucose and inhibitory molecules
    • DOI 10.1529/biophysj.104.047886
    • Salas-Burgos, A., Iserovich, P., Zuniga, F., Vera, J.C., and Fischbarg, J. 2004. Predicting the three-dimensional structure of the human facilitative glucose transporter glut1 by a novel evolutionary homology strategy: insights on the molecular mechanism of substrate migration, and binding sites for glucose and inhibitory molecules. Biophys. J. 87(5): 2990-2999. doi:10.1529/ biophysj.104.047886. PMID:15326030. (Pubitemid 40468559)
    • (2004) Biophysical Journal , vol.87 , Issue.5 , pp. 2990-2999
    • Salas-Burgos, A.1    Iserovich, P.2    Zuniga, F.3    Vera, J.C.4    Fischbarg, J.5
  • 73
    • 64649092658 scopus 로고    scopus 로고
    • Protein 4.2: A complex linker
    • doi:10.1016/j.bcmd.2009.01.005. PMID: 19269200
    • Satchwell, T.J., Shoemark, D.K., Sessions, R.B., and Toye, A.M. 2009. Protein 4.2: a complex linker. Blood Cells Mol. Dis. 42(3): 201-210. doi:10.1016/j.bcmd.2009.01.005. PMID: 19269200.
    • (2009) Blood Cells Mol. Dis , vol.42 , Issue.3 , pp. 201-210
    • Satchwell, T.J.1    Shoemark, D.K.2    Sessions, R.B.3    Toye, A.M.4
  • 74
    • 8244249135 scopus 로고
    • Studies of the metabolism of human erythrocyte membranes
    • doi:10.1172/ JCI104768. PMID:13987053
    • Schrier, S.L. 1963. Studies of the metabolism of human erythrocyte membranes. J. Clin. Invest. 42(6): 756-766. doi:10.1172/ JCI104768. PMID:13987053.
    • (1963) J. Clin. Invest , vol.42 , Issue.6 , pp. 756-766
    • Schrier, S.L.1
  • 75
    • 0018742616 scopus 로고
    • The molecular structure of human erythrocyte spectrin. Biophysical and electron microscopic studies
    • DOI 10.1016/0022-2836(79)90078-0
    • Shotton, D.M., Burke, B.E., and Branton, D. 1979. The molecular structure of human erythrocyte spectrin. Biophysical and electron microscopic studies. J. Mol. Biol. 131(2): 303-329. doi:10.1016/0022-2836(79)90078-0. PMID:490648. (Pubitemid 9230185)
    • (1979) Journal of Molecular Biology , vol.131 , Issue.2 , pp. 303-329
    • Shotton, D.M.1    Burke, B.E.2    Branton, D.3
  • 76
    • 0028348960 scopus 로고
    • Quantitation of the number of molecules of glycophorins C and D on normal red blood cells using radioiodinated Fab fragments of monoclonal antibodies
    • Smythe, J., Gardner, B., and Anstee, D.J. 1994. Quantitation of the number of molecules of glycophorins C and D on normal red blood cells using radioiodinated Fab fragments of monoclonal antibodies. Blood, 83(6): 1668-1672. PMID:8123859. (Pubitemid 24081584)
    • (1994) Blood , vol.83 , Issue.6 , pp. 1668-1672
    • Smythe, J.1    Gardner, B.2    Anstee, D.J.3
  • 77
    • 0035880255 scopus 로고    scopus 로고
    • Intercellular adhesion molecule-4 binds a4b1 and aV-family integrins through novel integrin-binding mechanisms
    • doi:10. 1182/blood.V98.2.458. PMID:11435317
    • Spring, F.A., Parsons, S.F., Ortlepp, S., Olsson, M.L., Sessions, R., Brady, R.L., and Anstee, D.J. 2001. Intercellular adhesion molecule-4 binds a4b1 and aV-family integrins through novel integrin-binding mechanisms. Blood, 98(2): 458-466. doi:10. 1182/blood.V98.2.458. PMID:11435317.
    • (2001) Blood , vol.98 , Issue.2 , pp. 458-466
    • Spring, F.A.1    Parsons, S.F.2    Ortlepp, S.3    Olsson, M.L.4    Sessions, R.5    Brady, R.L.6    Anstee, D.J.7
  • 78
    • 67049164963 scopus 로고    scopus 로고
    • The structure of the ankyrin-binding site of b-spectrin reveals how tandem spectrin-repeats generate unique ligand-binding properties
    • doi:10.1182/blood-2008-10-184291. PMID: 19168783
    • Stabach, P.R., Simonovic, I., Ranieri, M.A., Aboodi, M.S., Steitz, T.A., Simonovic;, M., and Morrow, J.S. 2009. The structure of the ankyrin-binding site of b-spectrin reveals how tandem spectrin-repeats generate unique ligand-binding properties. Blood, 113(22): 5377-5384. doi:10.1182/blood-2008-10- 184291. PMID:19168783.
    • (2009) Blood , vol.113 , Issue.22 , pp. 5377-5384
    • Stabach, P.R.1    Simonovic, I.2    Ranieri, M.A.3    Aboodi, M.S.4    Steitz, T.A.5    Simonovic, M.6    Morrow, J.S.7
  • 79
    • 0030796451 scopus 로고    scopus 로고
    • Structural basis for cyclic terpene biosynthesis by tobacco 5-epi- aristolochene synthase
    • DOI 10.1126/science.277.5333.1815
    • Starks, C.M., Back, K., Chappell, J., and Noel, J.P. 1997. Structural basis for cyclic terpene biosynthesis by tobacco 5-epi-aristolochene synthase. Science, 277(5333): 1815-1820. doi:10. 1126/science.277.5333.1815. PMID:9295271. (Pubitemid 27449192)
    • (1997) Science , vol.277 , Issue.5333 , pp. 1815-1820
    • Starks, C.M.1    Back, K.2    Chappell, J.3    Noel, J.P.4
  • 80
    • 0018118531 scopus 로고
    • The band 3 protein of the human red cell membrane: A review
    • Steck, T.L. 1978. The band 3 protein of the human red cell membrane: A review. J. Supramol. Struct. 8(3): 311-324. doi:10.1002/jss.400080309. PMID:364194. (Pubitemid 9034695)
    • (1978) Journal of Supramolecular and Cellular Biochemistry , vol.8 , Issue.3 , pp. 311-324
    • Steck, T.L.1
  • 81
    • 0014939405 scopus 로고
    • Inside-out red cell membrane vesicles: Preparation and purification
    • doi:10.1126/science.168. 3928.255. PMID:5418644
    • Steck, T.L., Weinstein, R.S., Straus, J.H., and Wallach, D.F. 1970. Inside-out red cell membrane vesicles: preparation and purification. Science, 168(3928): 255-257. doi:10.1126/science.168. 3928.255. PMID:5418644.
    • (1970) Science , vol.168 , Issue.3928 , pp. 255-257
    • Steck, T.L.1    Weinstein, R.S.2    Straus, J.H.3    Wallach, D.F.4
  • 82
    • 0035930581 scopus 로고    scopus 로고
    • A transport metabolon. Functional interaction of carbonic anhydrase II and chloride/bicarbonate exchangers
    • PMID:11606574
    • Sterling, D., Reithmeier, R.A., and Casey, J.R. 2001. A transport metabolon. Functional interaction of carbonic anhydrase II and chloride/bicarbonate exchangers. J. Biol. Chem. 276(51): 47886-47894. PMID:11606574.
    • (2001) J. Biol. Chem , vol.276 , Issue.51 , pp. 47886-47894
    • Sterling, D.1    Reithmeier, R.A.2    Casey, J.R.3
  • 83
    • 0024996679 scopus 로고
    • Kinetics and regulation of the ankyrin- band 3 interaction of the human red blood cell membrane
    • PMID:2144526
    • Thevenin, B.J., and Low, P.S. 1990. Kinetics and regulation of the ankyrin-band 3 interaction of the human red blood cell membrane. J. Biol. Chem. 265(27): 16166-16172. PMID:2144526.
    • (1990) J. Biol. Chem , vol.265 , Issue.27 , pp. 16166-16172
    • Thevenin, B.J.1    Low, P.S.2
  • 84
    • 77949916296 scopus 로고    scopus 로고
    • Understanding protein non- folding
    • PMID: 20117254
    • Uversky, V.N., and Dunker, A.K. 2010. Understanding protein non- folding. Biochim. Biophys. Acta, 1804(6): 1231-1264. PMID: 20117254.
    • (2010) Biochim. Biophys. Acta , vol.1804 , Issue.6 , pp. 1231-1264
    • Uversky, V.N.1    Dunker, A.K.2
  • 86
    • 0028099996 scopus 로고
    • Tropomodulin caps the pointed ends of actin filaments
    • DOI 10.1083/jcb.127.6.1627
    • Weber, A., Pennise, C.R., Babcock, G.G., and Fowler, V.M. 1994. Tropomodulin caps the pointed ends of actin filaments. J. Cell Biol. 127(6): 1627-1635. doi:10.1083/jcb.127.6.1627. PMID: 7798317. (Pubitemid 24380901)
    • (1994) Journal of Cell Biology , vol.127 , Issue.6 , pp. 1627-1635
    • Weber, A.1    Pennise, C.R.2    Babcock, G.G.3    Fowler, V.M.4
  • 87
    • 77249153631 scopus 로고    scopus 로고
    • Structure of the membrane domain of human erythrocyte anion exchanger 1 revealed by electron crystallography
    • doi:10.1016/j.jmb. 2010.01.027. PMID:20100494
    • Yamaguchi, T., Ikeda, Y., Abe, Y., Kuma, H., Kang, D., Hamasaki, N., and Hirai, T. 2010. Structure of the membrane domain of human erythrocyte anion exchanger 1 revealed by electron crystallography. J. Mol. Biol. 397(1): 179-189. doi:10.1016/j.jmb. 2010.01.027. PMID:20100494.
    • (2010) J. Mol. Biol. , vol.397 , Issue.1 , pp. 179-189
    • Yamaguchi, T.1    Ikeda, Y.2    Abe, Y.3    Kuma, H.4    Kang, D.5    Hamasaki, N.6    Hirai, T.7
  • 89
    • 0034329189 scopus 로고    scopus 로고
    • Crystal-lographic structure and functional interpretation of the cytoplasmic domain of erythrocyte membrane band 3
    • PMID:11049968
    • Zhang, D., Kiyatkin, A., Bolin, J.T., and Low, P.S. 2000. Crystal-lographic structure and functional interpretation of the cytoplasmic domain of erythrocyte membrane band 3. Blood, 96(9): 2925-2933. PMID:11049968.
    • (2000) Blood , vol.96 , Issue.9 , pp. 2925-2933
    • Zhang, D.1    Kiyatkin, A.2    Bolin, J.T.3    Low, P.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.