메뉴 건너뛰기




Volumn 79, Issue 6, 2000, Pages 2987-3000

Actin protofilament orientation in deformation of the erythrocyte membrane skeleton

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; MEMBRANE PROTEIN; SPECTRIN;

EID: 0033638280     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(00)76535-0     Document Type: Article
Times cited : (36)

References (31)
  • 1
    • 0027291592 scopus 로고
    • Evidence that red blood cell protein p55 may participate in the skeleton-membrane linkage that involves protein 4.1 and glycophorin C
    • Alloisio, N., N. Dalla Venezia, A. Rana, K. Andrabi, P. Texier, F. Gilsanz, J. P. Cartron, J. Delaunay, and A. H. Chishti. 1993. Evidence that red blood cell protein p55 may participate in the skeleton-membrane linkage that involves protein 4.1 and glycophorin C. Blood. 82:1323-1327.
    • (1993) Blood , vol.82 , pp. 1323-1327
    • Alloisio, N.1    Dalla Venezia, N.2    Rana, A.3    Andrabi, K.4    Texier, P.5    Gilsanz, F.6    Cartron, J.P.7    Delaunay, J.8    Chishti, A.H.9
  • 2
    • 0018389150 scopus 로고
    • Carbocyanine dye orientation in red cell membrane studied by microscopic fluorescence polarization
    • Axelrod, D. 1979. Carbocyanine dye orientation in red cell membrane studied by microscopic fluorescence polarization. Biophys. J. 26: 557-574.
    • (1979) Biophys. J. , vol.26 , pp. 557-574
    • Axelrod, D.1
  • 3
    • 0018759538 scopus 로고
    • The membrane attachment protein for spectrin is associated with band 3 in human erythrocyte membranes
    • Bennett, V., and P. J. Stenbuck. 1979. The membrane attachment protein for spectrin is associated with band 3 in human erythrocyte membranes. Nature. 280:468-473.
    • (1979) Nature , vol.280 , pp. 468-473
    • Bennett, V.1    Stenbuck, P.J.2
  • 4
    • 0029885486 scopus 로고    scopus 로고
    • The orientation of eosin-5-maleimide on human erythrocyte band 3 measured by fluorescence polarization microscopy
    • Blackman, S. M., C. E. Cobb, A. H. Beth, and D. W. Piston. 1996. The orientation of eosin-5-maleimide on human erythrocyte band 3 measured by fluorescence polarization microscopy. Biophys. J. 71:194-208.
    • (1996) Biophys. J. , vol.71 , pp. 194-208
    • Blackman, S.M.1    Cobb, C.E.2    Beth, A.H.3    Piston, D.W.4
  • 5
    • 0031708414 scopus 로고    scopus 로고
    • Simulations of the erythrocyte cytoskeleton at large deformation I: Microscopic models
    • Boey, S. K., D. H. Boal, and D. E. Discher. 1998. Simulations of the erythrocyte cytoskeleton at large deformation I: microscopic models. Biophys. J. 75:1573-1583.
    • (1998) Biophys. J. , vol.75 , pp. 1573-1583
    • Boey, S.K.1    Boal, D.H.2    Discher, D.E.3
  • 6
    • 0022344550 scopus 로고
    • Visualization of the protein associations in the erythrocyte membrane skeleton
    • Byers, T. J., and D. Branton. 1985. Visualization of the protein associations in the erythrocyte membrane skeleton. Proc. Natl. Acad. Sci. USA. 82:6153-6157.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 6153-6157
    • Byers, T.J.1    Branton, D.2
  • 7
    • 0031705402 scopus 로고    scopus 로고
    • Simulations of the erythrocyte cytoskeleton at large deformation II: Micropipette aspiration
    • Discher, D. E., D. H. Boal, and S. K. Boey. 1998. Simulations of the erythrocyte cytoskeleton at large deformation II: micropipette aspiration. Biophys. J. 75:1584-1597.
    • (1998) Biophys. J. , vol.75 , pp. 1584-1597
    • Discher, D.E.1    Boal, D.H.2    Boey, S.K.3
  • 8
    • 0029818016 scopus 로고    scopus 로고
    • Kinematics of red cell aspiration by fluorescence-imaged microdeformation
    • Discher, D. E., and N. Mohandas. 1996. Kinematics of red cell aspiration by fluorescence-imaged microdeformation. Biophys. J. 71:1680-1694.
    • (1996) Biophys. J. , vol.71 , pp. 1680-1694
    • Discher, D.E.1    Mohandas, N.2
  • 9
    • 0027938023 scopus 로고
    • Molecular maps of red cell deformation: Hidden elasticity and in situ connectivity
    • Discher, D. E., N. Mohandas, and E. A. Evans. 1994. Molecular maps of red cell deformation: hidden elasticity and in situ connectivity. Science. 266:1032-1035.
    • (1994) Science , vol.266 , pp. 1032-1035
    • Discher, D.E.1    Mohandas, N.2    Evans, E.A.3
  • 10
    • 0029162126 scopus 로고
    • Mechanochemistry of protein 4.1's spectrinactin binding domain: Ternary complex interactions, membrane binding, network integration, structural strengthening
    • Discher, D. E., R. Winardi, P. O. Schischmanoff, M. Parra, J. G. Conboy, and N. Mohandas. 1995. Mechanochemistry of protein 4.1's spectrinactin binding domain: ternary complex interactions, membrane binding, network integration, structural strengthening. J. Cell Biol. 130:897-907.
    • (1995) J. Cell Biol. , vol.130 , pp. 897-907
    • Discher, D.E.1    Winardi, R.2    Schischmanoff, P.O.3    Parra, M.4    Conboy, J.G.5    Mohandas, N.6
  • 11
    • 0015894192 scopus 로고
    • New membrane concept applied to the analysis of fluid shear- and micropipette-deformed red blood cells
    • Evans, E. A. 1973. New membrane concept applied to the analysis of fluid shear- and micropipette-deformed red blood cells. Biophys. J. 13: 941-954.
    • (1973) Biophys. J. , vol.13 , pp. 941-954
    • Evans, E.A.1
  • 13
    • 0030021105 scopus 로고    scopus 로고
    • Regulation of actin filament length in erythrocytes and striated muscle
    • Fowler, V. M. 1996. Regulation of actin filament length in erythrocytes and striated muscle. Curr. Opin. Cell Biol. 8:86-96.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 86-96
    • Fowler, V.M.1
  • 14
    • 0034206061 scopus 로고    scopus 로고
    • Potts fully frustrated model: Thermodynamics, percolation, and dynamics in two dimensions
    • Franzese, G. 2000. Potts fully frustrated model: thermodynamics, percolation, and dynamics in two dimensions. Phys. Rev. E. 61:6383-6391.
    • (2000) Phys. Rev. E , vol.61 , pp. 6383-6391
    • Franzese, G.1
  • 15
    • 0023642534 scopus 로고
    • The use of a charge-coupled device for quantitative optical microscopy of biological structures
    • Hiraoka, Y., J. W. Sedat, and D. A. Agard. 1987. The use of a charge-coupled device for quantitative optical microscopy of biological structures. Science. 238:36-41.
    • (1987) Science , vol.238 , pp. 36-41
    • Hiraoka, Y.1    Sedat, J.W.2    Agard, D.A.3
  • 16
    • 0025336497 scopus 로고
    • Spectrin, actin and the structure of the cortical lattice in mammalian cochlear outer hair cells
    • Holley, M. C., and J. F. Ashmore. 1990. Spectrin, actin and the structure of the cortical lattice in mammalian cochlear outer hair cells. J. Cell Sci. 96:283-291.
    • (1990) J. Cell Sci. , vol.96 , pp. 283-291
    • Holley, M.C.1    Ashmore, J.F.2
  • 17
    • 0030025568 scopus 로고    scopus 로고
    • F-actin, a model polymer for semiflexible chains in dilute, semidilute, and liquid crystalline solutions
    • Kas, J., H. Strey, J. X. Tang, D. Finger, R. Ezzell, E. Sackmann, and P. A. Janmey. 1996. F-actin, a model polymer for semiflexible chains in dilute, semidilute, and liquid crystalline solutions. Biophys. J. 70: 609-625.
    • (1996) Biophys. J. , vol.70 , pp. 609-625
    • Kas, J.1    Strey, H.2    Tang, J.X.3    Finger, D.4    Ezzell, R.5    Sackmann, E.6    Janmey, P.A.7
  • 18
    • 0023919181 scopus 로고
    • Force measurements by micromanipulation of a single actin filament by glass needles
    • Kishino, A., and T. Yanagida. 1988. Force measurements by micromanipulation of a single actin filament by glass needles. Nature. 334:74-76.
    • (1988) Nature , vol.334 , pp. 74-76
    • Kishino, A.1    Yanagida, T.2
  • 20
    • 0032774448 scopus 로고    scopus 로고
    • Direct measures of large, anisotropic strains in deformation of the erythrocyte cytoskeleton
    • Lee, J. C.-M., D. Wong, and D. E. Discher. 1999. Direct measures of large, anisotropic strains in deformation of the erythrocyte cytoskeleton. Biophys. J. 77:853-864.
    • (1999) Biophys. J. , vol.77 , pp. 853-864
    • Lee, J.C.-M.1    Wong, D.2    Discher, D.E.3
  • 21
    • 0028263839 scopus 로고
    • Mechanical properties of the red cell membrane in relation to molecular structure and genetic defects
    • Mohandas, N., and E. Evans. 1994. Mechanical properties of the red cell membrane in relation to molecular structure and genetic defects. Annu. Rev. Biophys. Biomol. Struct. 23:787-818.
    • (1994) Annu. Rev. Biophys. Biomol. Struct. , vol.23 , pp. 787-818
    • Mohandas, N.1    Evans, E.2
  • 22
    • 0032568650 scopus 로고    scopus 로고
    • The interaction of Arp2/3 complex with actin: Nucleation, high affinity pointed end capping, and formation of branching networks of filaments
    • Mullins, R. D., J. A. Heuser, and T. D. Pollard. 1998. The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments. Proc. Natl. Acad. Sci. USA. 95:6181-6186.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6181-6186
    • Mullins, R.D.1    Heuser, J.A.2    Pollard, T.D.3
  • 23
    • 0031984179 scopus 로고    scopus 로고
    • Fluorescence-imaged microdeformation of the outer hair cell lateral wall
    • Oghalai, J. S., and A. A. Patel, T. Nakagawa, and W. E. Brownell. 1998. Fluorescence-imaged microdeformation of the outer hair cell lateral wall. J. Neurosci. 18:48-58.
    • (1998) J. Neurosci. , vol.18 , pp. 48-58
    • Oghalai, J.S.1    Patel, A.A.2    Nakagawa, T.3    Brownell, W.E.4
  • 24
    • 0032774449 scopus 로고    scopus 로고
    • Actin protofilament orientation at the erythrocyte membrane
    • Picart, C., and D. E. Discher. 1999. Actin protofilament orientation at the erythrocyte membrane. Biophys. J. 77:865-878.
    • (1999) Biophys. J. , vol.77 , pp. 865-878
    • Picart, C.1    Discher, D.E.2
  • 25
    • 0025354418 scopus 로고
    • Glycophorin C content of human erythrocyte membrane is regulated by protein 4.1
    • Reid, M. E., Y. Takakuwa, J. Conboy, G. Tchernia, and N. Mohandas. 1990. Glycophorin C content of human erythrocyte membrane is regulated by protein 4.1. Blood. 75:2229-2234.
    • (1990) Blood , vol.75 , pp. 2229-2234
    • Reid, M.E.1    Takakuwa, Y.2    Conboy, J.3    Tchernia, G.4    Mohandas, N.5
  • 26
    • 0033582763 scopus 로고    scopus 로고
    • Single molecule force spectroscopy of spectrin repeats: Low unfolding forces in helix bundles
    • Rief, M., J. Pascual, M. Saraste, and H. E. Gaub. 1999. Single molecule force spectroscopy of spectrin repeats: low unfolding forces in helix bundles. J. Mol. Biol. 286:553-561.
    • (1999) J. Mol. Biol. , vol.286 , pp. 553-561
    • Rief, M.1    Pascual, J.2    Saraste, M.3    Gaub, H.E.4
  • 27
    • 0022486512 scopus 로고
    • Ultrastructure of the intact skeleton of the human erythrocyte membrane
    • Shen, B. W., R. Josephs, and T. L. Steck. 1986. Ultrastructure of the intact skeleton of the human erythrocyte membrane. J. Cell. Biol. 102: 997-1006.
    • (1986) J. Cell. Biol. , vol.102 , pp. 997-1006
    • Shen, B.W.1    Josephs, R.2    Steck, T.L.3
  • 28
    • 0023688017 scopus 로고
    • Regulation of band 3 mobilities in erythrocyte ghost membranes by protein association and cytoskeletal meshwork
    • Tsuji, A., K. Kawasaki, S. Ohnishi, H. Merkle, and A. Kusumi A. 1988. Regulation of band 3 mobilities in erythrocyte ghost membranes by protein association and cytoskeletal meshwork. Biochemistry. 27:7447-7452.
    • (1988) Biochemistry , vol.27 , pp. 7447-7452
    • Tsuji, A.1    Kawasaki, K.2    Ohnishi, S.3    Merkle, H.4    A. Kusumi, A.5
  • 29
    • 0028246498 scopus 로고
    • Immunolocalization of tropomodulin, tropomyosin and actin in spread human erythrocyte skeletons
    • Ursitti, J. A., and V. M. Fowler. 1994. Immunolocalization of tropomodulin, tropomyosin and actin in spread human erythrocyte skeletons. J. Cell. Sci. 107:1633-1639.
    • (1994) J. Cell. Sci. , vol.107 , pp. 1633-1639
    • Ursitti, J.A.1    Fowler, V.M.2
  • 30
    • 0023915893 scopus 로고
    • Reductions of erythrocyte membrane viscoelastic coefficients reflect spectrin deficiencies in hereditary spherocytosis
    • Waugh, R. E., and P. Agre. 1988. Reductions of erythrocyte membrane viscoelastic coefficients reflect spectrin deficiencies in hereditary spherocytosis. J. Clin. Invest. 81:133-141.
    • (1988) J. Clin. Invest. , vol.81 , pp. 133-141
    • Waugh, R.E.1    Agre, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.