메뉴 건너뛰기




Volumn 86, Issue 4, 1996, Pages 631-642

Cortexillins, major determinants of cell shape and size, are actin- bundling proteins with a parallel coiled-coil tail

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN BINDING PROTEIN;

EID: 16044367114     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)80136-1     Document Type: Article
Times cited : (150)

References (68)
  • 1
    • 0023419545 scopus 로고
    • A glow discharge unit to render electron microscope grids and other surfaces hydrophilic
    • Aebi, U., and Pollard, T.D. (1987). A glow discharge unit to render electron microscope grids and other surfaces hydrophilic. J. Electron Microsc. Tech. 7, 29-33.
    • (1987) J. Electron Microsc. Tech. , vol.7 , pp. 29-33
    • Aebi, U.1    Pollard, T.D.2
  • 3
    • 0028987269 scopus 로고
    • Coiled-coil regions in the carboxy-terminal domains of dystrophin and related proteins: Potentials for protein-protein interactions
    • Blake, D.J., Tinsley, J.M., Davies, K.E., Knight, A.E., Winder, S.J., and Kendrick-Jones, J. (1995). Coiled-coil regions in the carboxy-terminal domains of dystrophin and related proteins: potentials for protein-protein interactions. Trends Biochem. Sci. 20, 133-135.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 133-135
    • Blake, D.J.1    Tinsley, J.M.2    Davies, K.E.3    Knight, A.E.4    Winder, S.J.5    Kendrick-Jones, J.6
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantification of microgram quantities of protein utilizing the principle of protein dye-binding
    • Bradford, M.M. (1976). A rapid and sensitive method for quantification of microgram quantities of protein utilizing the principle of protein dye-binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0028046781 scopus 로고
    • Towards atomic interpretation of F-actin filament three-dimensional reconstruction
    • Bremer, A., Henn, C., Goldie, K.N., Engel, A., Smith, P.R., and Aebi, U. (1994). Towards atomic interpretation of F-actin filament three-dimensional reconstruction. J. Mol. Biol. 242, 683-700.
    • (1994) J. Mol. Biol. , vol.242 , pp. 683-700
    • Bremer, A.1    Henn, C.2    Goldie, K.N.3    Engel, A.4    Smith, P.R.5    Aebi, U.6
  • 6
    • 0019313223 scopus 로고
    • Fimbrin, a new microfilament-associated protein present in microvilli and other cell surface structures
    • Bretscher, A., and Weber, K. (1980). Fimbrin, a new microfilament-associated protein present in microvilli and other cell surface structures. J. Cell Biol. 86, 335-340.
    • (1980) J. Cell Biol. , vol.86 , pp. 335-340
    • Bretscher, A.1    Weber, K.2
  • 8
    • 0001340764 scopus 로고
    • Electron microscopic mapping of monoclonal antibodies on the tail region of dictyostelium myosin
    • Claviez, M., Pagh, K., Maruta, H., Baltes, W., Fisher, P., and Gerisch, G. (1982). Electron microscopic mapping of monoclonal antibodies on the tail region of Dictyostelium myosin. EMBO J. 1, 1017-1022.
    • (1982) EMBO J. , vol.1 , pp. 1017-1022
    • Claviez, M.1    Pagh, K.2    Maruta, H.3    Baltes, W.4    Fisher, P.5    Gerisch, G.6
  • 9
    • 0022833372 scopus 로고
    • Cytoskeletons from a mutant of Dictyostelium discoideum with flattened cells
    • Claviez, M., Brink, M., and Gerisch, G. (1986). Cytoskeletons from a mutant of Dictyostelium discoideum with flattened cells. J. Cell Sci. 86, 69-82.
    • (1986) J. Cell Sci. , vol.86 , pp. 69-82
    • Claviez, M.1    Brink, M.2    Gerisch, G.3
  • 10
    • 0025272940 scopus 로고
    • α-Helical coiled-coils: How to design an α-helical protein
    • Cohen, C., and Parry, D.A.D. (1990). α-Helical coiled-coils: how to design an α-helical protein. Proteins 7, 1-15.
    • (1990) Proteins , vol.7 , pp. 1-15
    • Cohen, C.1    Parry, D.A.D.2
  • 11
    • 0028293441 scopus 로고
    • α-Helical coiled-coils: More facts and better prediction
    • Cohen, C., and Parry, D.A.D. (1994). α-Helical coiled-coils: more facts and better prediction. Science 265, 488-489.
    • (1994) Science , vol.265 , pp. 488-489
    • Cohen, C.1    Parry, D.A.D.2
  • 12
    • 0026570396 scopus 로고
    • Targeted disruption of the ABP-120 gene leads to cells with altered motility
    • Cox, D., Condeelis, J., Wessels, D., Soll, D., Kern, H., and Knecht, D.A. (1992). Targeted disruption of the ABP-120 gene leads to cells with altered motility. J. Cell Biol. 116, 943-955.
    • (1992) J. Cell Biol. , vol.116 , pp. 943-955
    • Cox, D.1    Condeelis, J.2    Wessels, D.3    Soll, D.4    Kern, H.5    Knecht, D.A.6
  • 13
    • 0025091625 scopus 로고
    • Fimbrin is a homologue of the cytoplasmatic phosphoprotein plastin and has domains homologous with calmodulin and actin gelation proteins
    • DeArruda, M.V., Watson, S., Lin, C.-S., Leavitt, J., and Matsudaira, P. (1990). Fimbrin is a homologue of the cytoplasmatic phosphoprotein plastin and has domains homologous with calmodulin and actin gelation proteins. J. Cell Biol. 111, 1069-1079.
    • (1990) J. Cell Biol. , vol.111 , pp. 1069-1079
    • DeArruda, M.V.1    Watson, S.2    Lin, C.-S.3    Leavitt, J.4    Matsudaira, P.5
  • 14
    • 0023250545 scopus 로고
    • Disruption of the Dictyostelium heavy chain gene by homologous recombination
    • DeLozanne, A., and Spudich, J.A. (1987). Disruption of the Dictyostelium heavy chain gene by homologous recombination. Science 236, 1086-1091.
    • (1987) Science , vol.236 , pp. 1086-1091
    • DeLozanne, A.1    Spudich, J.A.2
  • 15
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux, J., Haeberli, P., and Smithies, O. (1984). A comprehensive set of sequence analysis programs for the VAX. Nucl. Acids Res. 12, 387-395.
    • (1984) Nucl. Acids Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 16
    • 0011757380 scopus 로고
    • Analytical ultracentrifugation
    • D. Rickwood, ed. (Oxford and Washington, D.C.: IRL Press)
    • Eason, R. (1986). Analytical ultracentrifugation. In Centrifugation, A Practical Approach, Second Edition, D. Rickwood, ed. (Oxford and Washington, D.C.: IRL Press), pp. 251-286.
    • (1986) Centrifugation, a Practical Approach, Second Edition , pp. 251-286
    • Eason, R.1
  • 17
    • 0023792823 scopus 로고
    • A new siliconized-glass fiber as support for protein-chemical analysis of electroblotted proteins
    • Eckerskorn, C., Mewes, W., Goretzki, H., and Lottspeich, F. (1988). A new siliconized-glass fiber as support for protein-chemical analysis of electroblotted proteins. Eur. J. Biochem. 176, 509-519.
    • (1988) Eur. J. Biochem. , vol.176 , pp. 509-519
    • Eckerskorn, C.1    Mewes, W.2    Goretzki, H.3    Lottspeich, F.4
  • 18
    • 0021759450 scopus 로고
    • Isolation and characterization of a 30,000 dalton calcium sensitive actin cross-linking protein from Dictyostelium discoideum
    • Fechheimer, M., and Taylor, D.L. (1984). Isolation and characterization of a 30,000 dalton calcium sensitive actin cross-linking protein from Dictyostelium discoideum. J. Biol. Chem. 259, 4514-4520.
    • (1984) J. Biol. Chem. , vol.259 , pp. 4514-4520
    • Fechheimer, M.1    Taylor, D.L.2
  • 19
    • 0017619556 scopus 로고
    • Theory of protein molecule self-organization. II. A comparison of calculated thermodynamic parameters of local secondary structures with experiments
    • Finkelstein, A.V., Ptitsyn, O.B., and Kozitsyn, S.A. (1977). Theory of protein molecule self-organization. II. A comparison of calculated thermodynamic parameters of local secondary structures with experiments. Biopolymers 16, 497-524.
    • (1977) Biopolymers , vol.16 , pp. 497-524
    • Finkelstein, A.V.1    Ptitsyn, O.B.2    Kozitsyn, S.A.3
  • 20
    • 0020960602 scopus 로고
    • Preparations of single molecules and supramolecular complexes for high-resolution metal shadowing
    • Fowler, W.E., and Aebi, U. (1983). Preparations of single molecules and supramolecular complexes for high-resolution metal shadowing. J. Ultrastruct. Res. 83, 319-334.
    • (1983) J. Ultrastruct. Res. , vol.83 , pp. 319-334
    • Fowler, W.E.1    Aebi, U.2
  • 21
    • 0024366590 scopus 로고
    • Functional domains of the Drosophila melanogaster muscle myosin heavy-chain gene are encoded by alternatively spliced exons
    • George, E.L., Ober, M.B., and Emerson, C.P., Jr. (1989). Functional domains of the Drosophila melanogaster muscle myosin heavy-chain gene are encoded by alternatively spliced exons. Mol. Cell. Biol. 9, 2957-2974.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 2957-2974
    • George, E.L.1    Ober, M.B.2    Emerson C.P., Jr.3
  • 22
    • 0028894384 scopus 로고
    • Crystal structure of the heterodimeric bZIP transcription factor c-Fos-c-Jun bound to DNA
    • Glover, J.N.M., and Harrison, S.C. (1995). Crystal structure of the heterodimeric bZIP transcription factor c-Fos-c-Jun bound to DNA. Nature 373, 257-261.
    • (1995) Nature , vol.373 , pp. 257-261
    • Glover, J.N.M.1    Harrison, S.C.2
  • 24
    • 0027756896 scopus 로고
    • A switch between two, three and four stranded coiled-coils in GCN4 leucine zipper mutants
    • Harbury, P.B., Zhang, T., Kim, P.S., and Alber, T. (1993). A switch between two, three and four stranded coiled-coils in GCN4 leucine zipper mutants. Science 262, 1401-1407.
    • (1993) Science , vol.262 , pp. 1401-1407
    • Harbury, P.B.1    Zhang, T.2    Kim, P.S.3    Alber, T.4
  • 25
    • 0027934571 scopus 로고
    • Crystal structure of an isoleucine-zipper trimer
    • Harbury, P.B., Kim, P.S., and Alber, T. (1994). Crystal structure of an isoleucine-zipper trimer. Nature 371, 80-83.
    • (1994) Nature , vol.371 , pp. 80-83
    • Harbury, P.B.1    Kim, P.S.2    Alber, T.3
  • 28
    • 0027244276 scopus 로고
    • The 100 kDa F-actin capping protein of Dictyostelium amoebae is a villin prototype ("protovillin")
    • Hofmann, A., Noegel, A.A., Bomblies, L., Lottspeich, F., and Schleicher, M. (1993). The 100 kDa F-actin capping protein of Dictyostelium amoebae is a villin prototype ("protovillin"). FEBS Lett. 328, 71-76.
    • (1993) FEBS Lett. , vol.328 , pp. 71-76
    • Hofmann, A.1    Noegel, A.A.2    Bomblies, L.3    Lottspeich, F.4    Schleicher, M.5
  • 29
    • 0026732691 scopus 로고
    • Characterization of human brain cDNA encoding the general isoform of β-spectrin
    • Hu, R.J., Watanabe, M., and Bennett, V. (1992). Characterization of human brain cDNA encoding the general isoform of β-spectrin. J. Biol. Chem. 267, 18715-18722.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18715-18722
    • Hu, R.J.1    Watanabe, M.2    Bennett, V.3
  • 30
    • 0026918335 scopus 로고
    • A preparation protocol for postembedding immunoelectron microscopy of Dictyostelium discoideum with monoclonal antibodies
    • Humbel, B.M., and Biegelmann, E. (1992). A preparation protocol for postembedding immunoelectron microscopy of Dictyostelium discoideum with monoclonal antibodies. Scanning Microsc. 6, 817-825.
    • (1992) Scanning Microsc. , vol.6 , pp. 817-825
    • Humbel, B.M.1    Biegelmann, E.2
  • 31
    • 0023157142 scopus 로고
    • Modulation of gelsolin function by phosphatidylinositol 4,5-bisphosphate
    • Janmey, P.A., and Stossel, T.P. (1987). Modulation of gelsolin function by phosphatidylinositol 4,5-bisphosphate. Nature 325, 362-364.
    • (1987) Nature , vol.325 , pp. 362-364
    • Janmey, P.A.1    Stossel, T.P.2
  • 32
    • 0026724890 scopus 로고
    • Phosphoinositide-binding peptides derived from the sequences of gelsolin and villin
    • Janmey, P.A., Lamb, J., Allen, P.G., and Matsudaira, P.T. (1992). Phosphoinositide-binding peptides derived from the sequences of gelsolin and villin. J. Biol. Chem. 267, 11818-11823.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11818-11823
    • Janmey, P.A.1    Lamb, J.2    Allen, P.G.3    Matsudaira, P.T.4
  • 33
    • 0020265993 scopus 로고
    • Rat monoclonal antibodies derived by using a new nonsecreting rat cell line
    • Kilmartin, J.V., Wright, B., and Milstein, C. (1982). Rat monoclonal antibodies derived by using a new nonsecreting rat cell line. J. Cell Biol. 93, 576-582.
    • (1982) J. Cell Biol. , vol.93 , pp. 576-582
    • Kilmartin, J.V.1    Wright, B.2    Milstein, C.3
  • 34
    • 0023189474 scopus 로고
    • Antisense RNA inactivation of myosin heavy chain expression in Dictyostelium discoideum
    • Knecht, D.A., and Loomis, W.F. (1987). Antisense RNA inactivation of myosin heavy chain expression in Dictyostelium discoideum. Science 236, 1081-1086.
    • (1987) Science , vol.236 , pp. 1081-1086
    • Knecht, D.A.1    Loomis, W.F.2
  • 35
    • 0028303384 scopus 로고
    • A thermodynamic scale for leucine zipper stability and dimerization specificity: E and g interhelical interactions
    • Krylov, D., Mikhailenko, I., and Vinson, C. (1994). A thermodynamic scale for leucine zipper stability and dimerization specificity: e and g interhelical interactions. EMBO J. 13, 2849-2861.
    • (1994) EMBO J. , vol.13 , pp. 2849-2861
    • Krylov, D.1    Mikhailenko, I.2    Vinson, C.3
  • 36
    • 0025696701 scopus 로고
    • Actin-associated proteins in Dictyostelium discoideum
    • Luna, E.J., and Condeelis, J.S. (1990). Actin-associated proteins in Dictyostelium discoideum. Dev. Genet. 11, 328-332.
    • (1990) Dev. Genet. , vol.11 , pp. 328-332
    • Luna, E.J.1    Condeelis, J.S.2
  • 37
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas, A., Van Dyke, M., and Stock, J. (1991). Predicting coiled coils from protein sequences. Science 252, 1162-1164.
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 38
    • 0018934798 scopus 로고
    • Viscometric analysis of the gelation of Acanthamoeba extracts and purification of two gelation factors
    • MacLean-Fletcher, S.D., and Pollard, T.D. (1980). Viscometric analysis of the gelation of Acanthamoeba extracts and purification of two gelation factors. J. Cell Biol. 85, 414-428.
    • (1980) J. Cell Biol. , vol.85 , pp. 414-428
    • MacLean-Fletcher, S.D.1    Pollard, T.D.2
  • 39
    • 0024634880 scopus 로고
    • Gene replacement in Dictyostelium: Generation of myosin null mutants
    • Manstein, D.J., Titus, M.A., DeLozanne, A., and Spudich, J.A. (1989). Gene replacement in Dictyostelium: generation of myosin null mutants. EMBO J. 8, 923-932.
    • (1989) EMBO J. , vol.8 , pp. 923-932
    • Manstein, D.J.1    Titus, M.A.2    DeLozanne, A.3    Spudich, J.A.4
  • 40
    • 0026034515 scopus 로고
    • Modular organization of actin crosslinking proteins
    • Matsudaira, P. (1991). Modular organization of actin crosslinking proteins. Trends Biochem. Sci. 16, 87-92.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 87-92
    • Matsudaira, P.1
  • 41
    • 0016774265 scopus 로고
    • Tropomyosin coiled-coil interactions: Evidence for an unstaggered structure
    • McLachlan, A.D., and Stewart, M. (1975). Tropomyosin coiled-coil interactions: evidence for an unstaggered structure. J. Mol. Biol. 98, 293-304.
    • (1975) J. Mol. Biol. , vol.98 , pp. 293-304
    • McLachlan, A.D.1    Stewart, M.2
  • 42
    • 0025339009 scopus 로고
    • Bundling of actin filaments by α-actinin depends on its molecular length
    • Meyer, R.K., and Aebi, U. (1990). Bundling of actin filaments by α-actinin depends on its molecular length. J. Cell Biol. 110, 2013-2024.
    • (1990) J. Cell Biol. , vol.110 , pp. 2013-2024
    • Meyer, R.K.1    Aebi, U.2
  • 43
    • 0028330850 scopus 로고
    • Electrostatic interactions control the parallel and antiparallel orientation of α-helical chains in two stranded α-helical coiled-coil
    • Monera, O.D., Khy, C., and Hodges, R.S. (1994). Electrostatic interactions control the parallel and antiparallel orientation of α-helical chains in two stranded α-helical coiled-coil. Biochemistry 33, 3862-3872.
    • (1994) Biochemistry , vol.33 , pp. 3862-3872
    • Monera, O.D.1    Khy, C.2    Hodges, R.S.3
  • 44
    • 0021737746 scopus 로고
    • DNA-mediated transformation of Dictyostelium discoideum: Regulated expression of an actin gene fusion
    • Nellen, W., Silan, C., and Firtel, R.A. (1984). DNA-mediated transformation of Dictyostelium discoideum: regulated expression of an actin gene fusion. Mol. Cell. Biol. 4, 2890-2898.
    • (1984) Mol. Cell. Biol. , vol.4 , pp. 2890-2898
    • Nellen, W.1    Silan, C.2    Firtel, R.A.3
  • 46
    • 0026355413 scopus 로고
    • Protein kinase phosphorylation site sequences and consensus specificity motifs: Tabulations
    • Pearson, R.B., and Kemp, B.E. (1991). Protein kinase phosphorylation site sequences and consensus specificity motifs: tabulations. Meth. Enzymol. 200, 62-81.
    • (1991) Meth. Enzymol. , vol.200 , pp. 62-81
    • Pearson, R.B.1    Kemp, B.E.2
  • 47
    • 0022555884 scopus 로고
    • Actin and actin-binding proteins: A critical evaluation of mechanisms and functions
    • Pollard, T.D., and Cooper, J.A. (1986). Actin and actin-binding proteins: a critical evaluation of mechanisms and functions. Annu. Rev. Biochem. 55, 987-1035.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 987-1035
    • Pollard, T.D.1    Cooper, J.A.2
  • 49
    • 0027215373 scopus 로고
    • Isolation and characterization of a myosin heavy chain gene (mhcA) from the human parasitic pathogen Entamoeba histolytica
    • Raymond-Denise, A., Sansonetti, P.J., and Guillen, N. (1993). Isolation and characterization of a myosin heavy chain gene (mhcA) from the human parasitic pathogen Entamoeba histolytica. Mol. Biochem. Parasitol. 59, 123-131.
    • (1993) Mol. Biochem. Parasitol. , vol.59 , pp. 123-131
    • Raymond-Denise, A.1    Sansonetti, P.J.2    Guillen, N.3
  • 50
    • 0014199107 scopus 로고
    • Studies on the isolation and molecular properties of homogeneous globular actin: Evidence for a single polypeptide chain
    • Rees, M.K., and Young, M. (1967). Studies on the isolation and molecular properties of homogeneous globular actin: evidence for a single polypeptide chain. J. Biol. Chem. 242, 4449-4458.
    • (1967) J. Biol. Chem. , vol.242 , pp. 4449-4458
    • Rees, M.K.1    Young, M.2
  • 51
    • 0028929442 scopus 로고
    • Cell-substrate interactions and locomotion of Dictyostelium wild-type and mutants defective in three cytoskeletal proteins: A study using quantitative reflection interference contrast microscopy
    • Schindl, M., Wallraff, E., Deubzer, B., Witke, W., Gerisch, G., and Sackmann, E. (1995). Cell-substrate interactions and locomotion of Dictyostelium wild-type and mutants defective in three cytoskeletal proteins: a study using quantitative reflection interference contrast microscopy. Biophys. J. 68, 1177-1190.
    • (1995) Biophys. J. , vol.68 , pp. 1177-1190
    • Schindl, M.1    Wallraff, E.2    Deubzer, B.3    Witke, W.4    Gerisch, G.5    Sackmann, E.6
  • 52
    • 0026860948 scopus 로고
    • Dynamics of the dictyostelium cytoskeleton during chemotaxis
    • Schleicher, M., and Noegel, A.A. (1992). Dynamics of the Dictyostelium cytoskeleton during chemotaxis. New Biol. 4, 461-472.
    • (1992) New Biol. , vol.4 , pp. 461-472
    • Schleicher, M.1    Noegel, A.A.2
  • 53
    • 0027278479 scopus 로고
    • Two developmentally regulated mRNAs encoding actin-binding proteins in Physarum polycephalum
    • St-Pierre, B., Couture, C., Laroche, A., and Pallotta, D. (1993). Two developmentally regulated mRNAs encoding actin-binding proteins in Physarum polycephalum. Biochim. Biophys. Acta 1173, 107-110.
    • (1993) Biochim. Biophys. Acta , vol.1173 , pp. 107-110
    • St-Pierre, B.1    Couture, C.2    Laroche, A.3    Pallotta, D.4
  • 54
    • 0027217068 scopus 로고
    • A transformation vector for Dictyostelium discoideum with a new selectable marker, bsr
    • Sutoh, K. (1993). A transformation vector for Dictyostelium discoideum with a new selectable marker, bsr. Plasmid 30, 150-154.
    • (1993) Plasmid , vol.30 , pp. 150-154
    • Sutoh, K.1
  • 55
    • 0028181758 scopus 로고
    • Reversible random coil β-sheet transitions of the Alzheimer β-amyloid fragment (25-35)
    • Terzi, E., Hölzemann, G., and Seelig, J. (1994). Reversible random coil β-sheet transitions of the Alzheimer β-amyloid fragment (25-35). Biochemistry 33, 1345-1350.
    • (1994) Biochemistry , vol.33 , pp. 1345-1350
    • Terzi, E.1    Hölzemann, G.2    Seelig, J.3
  • 56
    • 0025735685 scopus 로고
    • Screening of Dictyostelium mutants defective in cytoskeletal proteins by colony immunoblotting
    • Wallraff, E., and Gerisch, G. (1991). Screening of Dictyostelium mutants defective in cytoskeletal proteins by colony immunoblotting. Meth. Enzymol. 196, 334-348.
    • (1991) Meth. Enzymol. , vol.196 , pp. 334-348
    • Wallraff, E.1    Gerisch, G.2
  • 57
    • 0022603987 scopus 로고
    • Selection of Dictyostelium mutants defective in cytoskeletal proteins: Use of an antibody that binds to the ends of α-actinin rods
    • Wallraff, E., Schleicher, M., Modersitzki, M., Rieger, D., Isenberg, G., and Gerisch, G. (1986). Selection of Dictyostelium mutants defective in cytoskeletal proteins: use of an antibody that binds to the ends of α-actinin rods. EMBO J. 5, 61-67.
    • (1986) EMBO J. , vol.5 , pp. 61-67
    • Wallraff, E.1    Schleicher, M.2    Modersitzki, M.3    Rieger, D.4    Isenberg, G.5    Gerisch, G.6
  • 58
    • 0028916228 scopus 로고
    • Motility and substratum adhesion of Dictyostelium wild-type and cytoskeletal mutant cells: A study by RICM/bright-field double-view image analysis
    • Weber, I., Wallraff, E., Albrecht, R., and Gerisch, G. (1995). Motility and substratum adhesion of Dictyostelium wild-type and cytoskeletal mutant cells: a study by RICM/bright-field double-view image analysis. J. Cell Sci. 108, 1519-1530.
    • (1995) J. Cell Sci. , vol.108 , pp. 1519-1530
    • Weber, I.1    Wallraff, E.2    Albrecht, R.3    Gerisch, G.4
  • 59
    • 0017176529 scopus 로고
    • Head to tail polymerisation of actin
    • Wegner, A. (1976). Head to tail polymerisation of actin. J. Mol. Biol. 108, 139-150.
    • (1976) J. Mol. Biol. , vol.108 , pp. 139-150
    • Wegner, A.1
  • 60
    • 0021646592 scopus 로고
    • A revision of the Dictyostelium discoideum cell cycle
    • Weijer, C.J., Duschl, G., and David, C.N. (1984). A revision of the Dictyostelium discoideum cell cycle. J. Cell Sci. 70, 111-131.
    • (1984) J. Cell Sci. , vol.70 , pp. 111-131
    • Weijer, C.J.1    Duschl, G.2    David, C.N.3
  • 61
    • 0026593102 scopus 로고
    • Redundancy in the microfilament system: Abnormal development of Dictyostelium cells lacking two F-actin cross-linking proteins
    • Witke, W., Schleicher, M., and Noegel, A.A. (1992). Redundancy in the microfilament system: abnormal development of Dictyostelium cells lacking two F-actin cross-linking proteins. Cell 68, 53-62.
    • (1992) Cell , vol.68 , pp. 53-62
    • Witke, W.1    Schleicher, M.2    Noegel, A.A.3
  • 63
    • 0014328849 scopus 로고
    • The lattice spacing of crystalline catalase as an internal standard of length in electron microscopy
    • Wrigley, N.G. (1968). The lattice spacing of crystalline catalase as an internal standard of length in electron microscopy. J. Ultrastruct. Res. 24, 454-464.
    • (1968) J. Ultrastruct. Res. , vol.24 , pp. 454-464
    • Wrigley, N.G.1
  • 65
    • 0025346081 scopus 로고
    • Cloning and chromosomal localization of human cytoskeletal α-actinin gene reveals linkage to the β-spectrin gene
    • Youssoufian, H., McAfee, M., and Kwiatkowski, D.J. (1990). Cloning and chromosomal localization of human cytoskeletal α-actinin gene reveals linkage to the β-spectrin gene. Am. J. Hum. Genet. 47, 62-71.
    • (1990) Am. J. Hum. Genet. , vol.47 , pp. 62-71
    • Youssoufian, H.1    McAfee, M.2    Kwiatkowski, D.J.3
  • 66
    • 0025651999 scopus 로고
    • gCap39, a calcium ion- and polyphosphoinositide-regulated actin capping protein
    • Yu, F.-X., Johnston, P.A., Suedhof, T.C., and Yin, H.L. (1990). gCap39, a calcium ion- and polyphosphoinositide-regulated actin capping protein. Science 250, 1413-1415.
    • (1990) Science , vol.250 , pp. 1413-1415
    • Yu, F.-X.1    Johnston, P.A.2    Suedhof, T.C.3    Yin, H.L.4
  • 67
    • 0027949381 scopus 로고
    • The net energetic contribution of interhelical electrostatic attractions to coiled-coil stability
    • Zhou, N.E., Khy, C., and Hodges, R.S. (1994a). The net energetic contribution of interhelical electrostatic attractions to coiled-coil stability. Protein Eng. 7, 1365-1372.
    • (1994) Protein Eng. , vol.7 , pp. 1365-1372
    • Zhou, N.E.1    Khy, C.2    Hodges, R.S.3
  • 68
    • 0028364239 scopus 로고
    • The role of interhelical ionic interactions in controlling protein folding and stability: De novo designed synthetic two-stranded α-helical coiled-coils
    • Zhou, N.E., Khy, C., and Hodges, R.S. (1994b). The role of interhelical ionic interactions in controlling protein folding and stability: de novo designed synthetic two-stranded α-helical coiled-coils. J. Mol. Biol. 237, 500-512.
    • (1994) J. Mol. Biol. , vol.237 , pp. 500-512
    • Zhou, N.E.1    Khy, C.2    Hodges, R.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.