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Volumn , Issue 50TH ANN. SYMP., 1997, Pages 3-18

Actin-binding membrane proteins identified by F-actin blot overlays

Author keywords

[No Author keywords available]

Indexed keywords

F ACTIN; MEMBRANE PROTEIN; ACTIN; ACTIN BINDING PROTEIN; DIAGNOSTIC AGENT; DODECYL SULFATE SODIUM; DREBRINS; NEUROPEPTIDE; RADIOACTIVE IODINE;

EID: 12644296969     PISSN: 00221295     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Conference Paper
Times cited : (20)

References (85)
  • 1
    • 0027393093 scopus 로고
    • Ezrin contains cytoskeleton and membrane binding domains accounting for its proposed role as a membrane-cytoskeletal linker
    • Algrain, M., O. Turunen, A. Vaheri, D. Louvard, and M. Arpin. 1993. Ezrin contains cytoskeleton and membrane binding domains accounting for its proposed role as a membrane-cytoskeletal linker. J. Cell Biol. 120:129-139.
    • (1993) J. Cell Biol. , vol.120 , pp. 129-139
    • Algrain, M.1    Turunen, O.2    Vaheri, A.3    Louvard, D.4    Arpin, M.5
  • 3
    • 0015830249 scopus 로고
    • HeLa cell plasma membranes
    • Atkinson, P.H. 1973. HeLa cell plasma membranes. Methods Cell Biol. 7:157-188.
    • (1973) Methods Cell Biol. , vol.7 , pp. 157-188
    • Atkinson, P.H.1
  • 4
    • 0022547743 scopus 로고
    • A 50 kDa, actin-binding protein in plasma membranes of rat hepatocytes and of rat liver tumors
    • Bärmann, M., J. Wadsack, and M. Frimmer. 1986. A 50 kDa, actin-binding protein in plasma membranes of rat hepatocytes and of rat liver tumors. Biochim. Biophys. Acta. 859:110-116.
    • (1986) Biochim. Biophys. Acta. , vol.859 , pp. 110-116
    • Bärmann, M.1    Wadsack, J.2    Frimmer, M.3
  • 6
    • 0028821843 scopus 로고
    • Ezrin oligomers are major cytoskeletal components of placental microvilli: A proposal for their involvement in cortical morphogenesis
    • Berryman, M., R. Gary, and A. Bretscher. 1995. Ezrin oligomers are major cytoskeletal components of placental microvilli: a proposal for their involvement in cortical morphogenesis. J. Cell Biol. 131:1231-1242.
    • (1995) J. Cell Biol. , vol.131 , pp. 1231-1242
    • Berryman, M.1    Gary, R.2    Bretscher, A.3
  • 7
    • 0020804117 scopus 로고
    • Purification of an 80,000-dalton protein that is a component of the isolated microvillus cytoskeleton, and its localization in nonmuscle cells
    • Bretscher, A. 1983. Purification of an 80,000-dalton protein that is a component of the isolated microvillus cytoskeleton, and its localization in nonmuscle cells. J. Cell Biol. 97:425-432.
    • (1983) J. Cell Biol. , vol.97 , pp. 425-432
    • Bretscher, A.1
  • 8
    • 0027640146 scopus 로고
    • Microfilaments and membranes
    • Bretscher, A. 1993. Microfilaments and membranes. Curr. Opin. Cell Biol. 5:653-660.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 653-660
    • Bretscher, A.1
  • 9
    • 0029609581 scopus 로고
    • Soluble ezrin purified from placenta exists as stable monomers and elongated dimers with masked C-terminal ezrin-radixin-moesin association domains
    • Bretscher, A., R. Gary, and M. Berryman. 1995. Soluble ezrin purified from placenta exists as stable monomers and elongated dimers with masked C-terminal ezrin-radixin-moesin association domains. Biochemistry. 34:16830-16837.
    • (1995) Biochemistry , vol.34 , pp. 16830-16837
    • Bretscher, A.1    Gary, R.2    Berryman, M.3
  • 10
    • 0028810956 scopus 로고
    • Synaptic structure and function: Dynamic organization yields architectural precision
    • Burns, M.E., and G.J. Augustine. 1995. Synaptic structure and function: dynamic organization yields architectural precision. Cell. 83:187-194.
    • (1995) Cell , vol.83 , pp. 187-194
    • Burns, M.E.1    Augustine, G.J.2
  • 11
    • 0028914964 scopus 로고
    • Three muscular dystrophies: Loss of cytoskeleton-extracellular matrix linkage
    • Campbell, K.P. 1995. Three muscular dystrophies: loss of cytoskeleton-extracellular matrix linkage. Cell. 80:675-679.
    • (1995) Cell , vol.80 , pp. 675-679
    • Campbell, K.P.1
  • 13
    • 0026026620 scopus 로고
    • Direct binding of F-actin to ponticulin, an integral plasma membrane glycoprotein
    • Chia, C.P., A.L. Hitt, and E.J. Luna. 1991. Direct binding of F-actin to ponticulin, an integral plasma membrane glycoprotein. Cell Motil. Cytoskeleton. 18:164-179.
    • (1991) Cell Motil. Cytoskeleton , vol.18 , pp. 164-179
    • Chia, C.P.1    Hitt, A.L.2    Luna, E.J.3
  • 14
    • 0027476154 scopus 로고
    • The integral membrane protein, ponticulin, acts as a monomer in nucleating actin assembly
    • Chia, C.P., A. Shariff, S.A. Savage, and E.J. Luna. 1993. The integral membrane protein, ponticulin, acts as a monomer in nucleating actin assembly. J. Cell Biol. 120:909-922.
    • (1993) J. Cell Biol. , vol.120 , pp. 909-922
    • Chia, C.P.1    Shariff, A.2    Savage, S.A.3    Luna, E.J.4
  • 15
    • 0023188303 scopus 로고
    • r 80,000 and participate in cell-cell contact formation in Dictyostelium discoideum
    • r 80,000 and participate in cell-cell contact formation in Dictyostelium discoideum. J. Cell Biol. 104:1375-1387.
    • (1987) J. Cell Biol. , vol.104 , pp. 1375-1387
    • Choi, A.H.C.1    Siu, C.-H.2
  • 16
    • 0014782521 scopus 로고
    • RNA in cytoplasmic and nuclear fractions of cellular slime mold amoebas
    • Cocucci, S.M., and M. Sussman. 1970. RNA in cytoplasmic and nuclear fractions of cellular slime mold amoebas. J. Cell Biol. 45:399-407.
    • (1970) J. Cell Biol. , vol.45 , pp. 399-407
    • Cocucci, S.M.1    Sussman, M.2
  • 17
    • 0027333420 scopus 로고
    • Life at the leading edge: The formation of cell protrusions
    • Condeelis, J. 1993. Life at the leading edge: the formation of cell protrusions. Anna. Rev. Cell Biol. 9:411-444.
    • (1993) Anna. Rev. Cell Biol. , vol.9 , pp. 411-444
    • Condeelis, J.1
  • 19
    • 0027196725 scopus 로고
    • The ezrin-like family of tyrosine kinase substrates: Receptor-specific pattern of tyrosine phosphorylation and relationship to malignant transformation
    • Fazioli, F., W.T. Wong, S.J. Ullrich, K. Sakaguchi, E. Appella, and P.P. Di Fiore. 1993. The ezrin-like family of tyrosine kinase substrates: receptor-specific pattern of tyrosine phosphorylation and relationship to malignant transformation. Oncogene. 8:1335-1345.
    • (1993) Oncogene , vol.8 , pp. 1335-1345
    • Fazioli, F.1    Wong, W.T.2    Ullrich, S.J.3    Sakaguchi, K.4    Appella, E.5    Di Fiore, P.P.6
  • 20
    • 0023188266 scopus 로고
    • The Dictyostelium discoideum 30,000-dalton protein is an actin filament-bundling protein that is selectively present in filopodia
    • Fechheimer, M. 1987. The Dictyostelium discoideum 30,000-dalton protein is an actin filament-bundling protein that is selectively present in filopodia. J. Cell Biol. 104:1539-1551.
    • (1987) J. Cell Biol. , vol.104 , pp. 1539-1551
    • Fechheimer, M.1
  • 21
    • 0028022792 scopus 로고
    • Association of the Dictyostelium 30,000 Mr actin bundling protein with contact regions
    • Fechheimer, M., H.M. Ingalls, R. Furukawa, and E.J. Luna. 1994. Association of the Dictyostelium 30,000 Mr actin bundling protein with contact regions. J. Cell Sci. 107:2393-2401.
    • (1994) J. Cell Sci. , vol.107 , pp. 2393-2401
    • Fechheimer, M.1    Ingalls, H.M.2    Furukawa, R.3    Luna, E.J.4
  • 22
    • 0025727170 scopus 로고
    • Isolation and sequencing of cDNA clones encoding the Dictyostelium discoideum 30,000-dalton actin-bundling protein
    • Fechheimer, M., D. Murdock, M. Carney, and C.V.C. Glover. 1991. Isolation and sequencing of cDNA clones encoding the Dictyostelium discoideum 30,000-dalton actin-bundling protein. J. Biol. Chem. 266:2883-2889.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2883-2889
    • Fechheimer, M.1    Murdock, D.2    Carney, M.3    Glover, C.V.C.4
  • 23
    • 0027397491 scopus 로고
    • +2-regulated actin cross-linking but lacks bundling activity
    • +2-regulated actin cross-linking but lacks bundling activity. J. Cell Biol. 120:1169-1176.
    • (1993) J. Cell Biol. , vol.120 , pp. 1169-1176
    • Fechheimer, M.1    Furukawa, R.2
  • 24
    • 0021759450 scopus 로고
    • Isolation and characterization of a 30,000-dalton calcium-sensitive actin cross-Unking protein from Dictyostelium discoideum
    • Fechheimer, M., and D.L. Taylor. 1984. Isolation and characterization of a 30,000-dalton calcium-sensitive actin cross-Unking 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
  • 25
    • 0027709195 scopus 로고
    • Regulation of platelet function by the cytoskeleton
    • K.S. Authi, et al., editor. Plenum Press, New York
    • Fox, J.E.B. 1993. Regulation of platelet function by the cytoskeleton. In Mechanisms of Platelet Activation and Control. K.S. Authi, et al., editor. Plenum Press, New York. 175-185.
    • (1993) Mechanisms of Platelet Activation and Control , pp. 175-185
    • Fox, J.E.B.1
  • 26
    • 0026594072 scopus 로고
    • Moesin, a new cytoskeletal protein and constituent of filopodia: Its role in cellular functions
    • Furthmayr, H., W. Lankes, and M. Amieva. 1992. Moesin, a new cytoskeletal protein and constituent of filopodia: its role in cellular functions. Kidney Int. 41:665-670.
    • (1992) Kidney Int. , vol.41 , pp. 665-670
    • Furthmayr, H.1    Lankes, W.2    Amieva, M.3
  • 27
    • 0002036804 scopus 로고
    • The Dictyostelium discoideum 30,000 dalton protein contributes to phagocytosis
    • Furukawa, R., S. Butz, E. Fleischmann, and M. Fechheimer. 1992. The Dictyostelium discoideum 30,000 dalton protein contributes to phagocytosis. Protoplasma. 169:18-27.
    • (1992) Protoplasma , vol.169 , pp. 18-27
    • Furukawa, R.1    Butz, S.2    Fleischmann, E.3    Fechheimer, M.4
  • 28
    • 0028169756 scopus 로고
    • Differential localization of α-actinin and the 30 kD actin-bundling protein in the cleavage furrow, phagocytic cup, and contractile vacuole of Dictyostelium discoideum
    • Furukawa, R., and M. Fechheimer. 1994. Differential localization of α-actinin and the 30 kD actin-bundling protein in the cleavage furrow, phagocytic cup, and contractile vacuole of Dictyostelium discoideum. Cell Motil. Cytoskeleton. 29:46-56.
    • (1994) Cell Motil. Cytoskeleton , vol.29 , pp. 46-56
    • Furukawa, R.1    Fechheimer, M.2
  • 29
    • 0030014981 scopus 로고    scopus 로고
    • Role of the Dictyostelium 30 kDa protein in actin bundle formation
    • Furukawa, R., and M. Fechheimer. 1996. Role of the Dictyostelium 30 kDa protein in actin bundle formation. Biochemistry. 35:7224-7232.
    • (1996) Biochemistry , vol.35 , pp. 7224-7232
    • Furukawa, R.1    Fechheimer, M.2
  • 30
    • 0029121577 scopus 로고
    • Ezrin self-association involves binding of an N-terminal domain to a normally masked C-terminal domain that includes the F-actin binding site
    • Gary, R., and A. Bretscher. 1995. Ezrin self-association involves binding of an N-terminal domain to a normally masked C-terminal domain that includes the F-actin binding site. Mol. Biol. Cell. 6:1061-1075.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1061-1075
    • Gary, R.1    Bretscher, A.2
  • 31
    • 0023078051 scopus 로고
    • Purification and characterization of Dictyostelium discoideum plasma membranes
    • Goodloe-Holland, C.M., and E.J. Luna. 1987. Purification and characterization of Dictyostelium discoideum plasma membranes. Methods Cell Biol. 28:103-128.
    • (1987) Methods Cell Biol. , vol.28 , pp. 103-128
    • Goodloe-Holland, C.M.1    Luna, E.J.2
  • 32
    • 0029895005 scopus 로고    scopus 로고
    • Vertebrate unconventional myosins
    • Hasson, T., and M.S. Mooseker. 1996. Vertebrate unconventional myosins. J. Biol. Chem. 271:16431-16434.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16431-16434
    • Hasson, T.1    Mooseker, M.S.2
  • 33
    • 0029033133 scopus 로고
    • Molecular dissection of radixin: Distinct and interdependent functions of the amino- and carboxy-terminal domains
    • Henry, M.D., C.G. Agosti, and F. Solomon. 1995. Molecular dissection of radixin: distinct and interdependent functions of the amino- and carboxy-terminal domains. J. Cell Biol. 129:1007-1022.
    • (1995) J. Cell Biol. , vol.129 , pp. 1007-1022
    • Henry, M.D.1    Agosti, C.G.2    Solomon, F.3
  • 34
    • 0027993569 scopus 로고
    • Ponticulin is the major high-affinity link between the plasma membrane and the cortical actin network in Dictyostelium
    • Hitt, A.L., J.H. Hartwig, and E.J. Luna. 1994a. Ponticulin is the major high-affinity link between the plasma membrane and the cortical actin network in Dictyostelium. J. Cell Biol. 126:1433-1444.
    • (1994) J. Cell Biol. , vol.126 , pp. 1433-1444
    • Hitt, A.L.1    Hartwig, J.H.2    Luna, E.J.3
  • 35
    • 0027933857 scopus 로고
    • Ponticulin is an atypical membrane protein
    • Hitt, A.L., T.H. Lu, and E.J. Luna. 1994b. Ponticulin is an atypical membrane protein. J. Cell Biol. 126:1421-1431.
    • (1994) J. Cell Biol. , vol.126 , pp. 1421-1431
    • Hitt, A.L.1    Lu, T.H.2    Luna, E.J.3
  • 36
    • 0028036369 scopus 로고
    • Membrane interactions with the actin cytoskeleton
    • Hitt, A.L., and E.J. Luna. 1994. Membrane interactions with the actin cytoskeleton. Curr. Opin. Cell Biol. 6:120-130.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 120-130
    • Hitt, A.L.1    Luna, E.J.2
  • 37
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes, R.O. 1992. Integrins: versatility, modulation, and signaling in cell adhesion. Cell. 69:11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 38
    • 0026503656 scopus 로고
    • Contact and adhesive specificities in the associations, migrations, and targeting of cells and axons
    • Hynes, R.O., and A.D. Lander. 1992. Contact and adhesive specificities in the associations, migrations, and targeting of cells and axons. Cell. 68:303-322.
    • (1992) Cell , vol.68 , pp. 303-322
    • Hynes, R.O.1    Lander, A.D.2
  • 39
    • 0029046119 scopus 로고
    • Effect of a neuron-specific actin-binding protein, drebrin A, on cell-substratum adhesion
    • Ikeda, K., T. Shirao, M. Toda, H. Asada, S. Toya, and K. Uyemura. 1995. Effect of a neuron-specific actin-binding protein, drebrin A, on cell-substratum adhesion. Neurosci. Lett. 194:197-200.
    • (1995) Neurosci. Lett. , vol.194 , pp. 197-200
    • Ikeda, K.1    Shirao, T.2    Toda, M.3    Asada, H.4    Toya, S.5    Uyemura, K.6
  • 40
    • 0022741831 scopus 로고
    • Junctional plasma membrane domains isolated from aggregating Dictyostelium discoideum amebae
    • Ingalls, H.M., C.M. Goodloe-Holland, and E.J. Luna. 1986. Junctional plasma membrane domains isolated from aggregating Dictyostelium discoideum amebae. Proc. Natl. Acad. Sci USA. 83:4779-4783.
    • (1986) Proc. Natl. Acad. Sci USA , vol.83 , pp. 4779-4783
    • Ingalls, H.M.1    Goodloe-Holland, C.M.2    Luna, E.J.3
  • 41
    • 0030222341 scopus 로고    scopus 로고
    • Crosstalk between cell adhesion molecules: Vinculin as a paradigm for regulation by conformation
    • Jockusch, B.M., and M. Rüdiger. 1996. Crosstalk between cell adhesion molecules: vinculin as a paradigm for regulation by conformation. Trends Cell Biol. 6:311-315.
    • (1996) Trends Cell Biol. , vol.6 , pp. 311-315
    • Jockusch, B.M.1    Rüdiger, M.2
  • 42
    • 0023742179 scopus 로고
    • Colocalization of F-actin and 34-kilodalton actin bundling protein in Dictyostelium amoebae and cultured fibroblasts
    • Johns, J.A., A.M. Brock, and J.D. Pardee. 1988. Colocalization of F-actin and 34-kilodalton actin bundling protein in Dictyostelium amoebae and cultured fibroblasts. Cell Motil. Cytoskeleton. 9:205-218.
    • (1988) Cell Motil. Cytoskeleton , vol.9 , pp. 205-218
    • Johns, J.A.1    Brock, A.M.2    Pardee, J.D.3
  • 43
    • 0027289194 scopus 로고
    • Molecular cloning of a developmentally regulated brain protein, chicken drebrin A and its expression by alternative splicing of the drebrin gene
    • Kojima, N., T. Shirao, and K. Obata. 1993. Molecular cloning of a developmentally regulated brain protein, chicken drebrin A and its expression by alternative splicing of the drebrin gene. Mol. Brain Res. 19:101-114.
    • (1993) Mol. Brain Res. , vol.19 , pp. 101-114
    • Kojima, N.1    Shirao, T.2    Obata, K.3
  • 44
    • 0026760578 scopus 로고
    • Identification of the two major epidermal growth factorinduced tyrosine phosphorylation sites in the microvillar core protein ezrin
    • Krieg, J., and T. Hunter. 1992. Identification of the two major epidermal growth factorinduced tyrosine phosphorylation sites in the microvillar core protein ezrin. J. Biol. Chem. 267:19258-19265.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19258-19265
    • Krieg, J.1    Hunter, T.2
  • 45
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond.). 227:680-685.
    • (1970) Nature (Lond.) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 46
    • 0027745661 scopus 로고
    • Cloning and sequencing of porcine moesin and radixin cDNA and identification of highly conserved domains
    • Lankes, W.T., R. Schwartz-Albiez, and H. Furthmayr. 1993. Cloning and sequencing of porcine moesin and radixin cDNA and identification of highly conserved domains. Biochim. Biophys. Acta. 1216:479-482.
    • (1993) Biochim. Biophys. Acta. , vol.1216 , pp. 479-482
    • Lankes, W.T.1    Schwartz-Albiez, R.2    Furthmayr, H.3
  • 47
    • 0028261815 scopus 로고
    • Adhesion and its role in the virulence of enteropathogenic Escherichia coli
    • Law, D. 1994. Adhesion and its role in the virulence of enteropathogenic Escherichia coli. Clin. Microbiol. Rev. 7:152-173.
    • (1994) Clin. Microbiol. Rev. , vol.7 , pp. 152-173
    • Law, D.1
  • 48
    • 0026497661 scopus 로고
    • Cytoskeleton-plasma membrane interactions
    • Luna, E.J., and A.L. Hitt. 1992. Cytoskeleton-plasma membrane interactions. Science. 258:955-964.
    • (1992) Science , vol.258 , pp. 955-964
    • Luna, E.J.1    Hitt, A.L.2
  • 50
    • 0003147477 scopus 로고
    • Disorders of the red cell membrane
    • R.I. Handin, S.E. Lux, and T.P. Stossel, editors. J.B. Lippincott Company, Philadelphia
    • Lux, S.E., and J. Palek. 1995. Disorders of the red cell membrane. In Blood: Principles and Practice of Hematology. R.I. Handin, S.E. Lux, and T.P. Stossel, editors. J.B. Lippincott Company, Philadelphia. 1701-1818.
    • (1995) Blood: Principles and Practice of Hematology , pp. 1701-1818
    • Lux, S.E.1    Palek, J.2
  • 52
    • 0028126085 scopus 로고
    • Organization and function of the cytoskeleton in polarized epithelial cells: A component of the protein sorting machinery
    • Mays, R.W., K.A. Beck, and W.J. Nelson. 1994. Organization and function of the cytoskeleton in polarized epithelial cells: a component of the protein sorting machinery. Curr. Opin. Cell Biol. 6:16-24.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 16-24
    • Mays, R.W.1    Beck, K.A.2    Nelson, W.J.3
  • 53
    • 0024707419 scopus 로고
    • F-actin affinity chromatography: Technique for isolating previously unidentified actin-binding proteins
    • Miller, K.G., and B.M. Alberts. 1989. F-actin affinity chromatography: technique for isolating previously unidentified actin-binding proteins. Proc. Natl Acad. Sci. USA. 86:4808-4812.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 4808-4812
    • Miller, K.G.1    Alberts, B.M.2
  • 54
    • 0022921831 scopus 로고
    • Localisation of light chain and actin binding sites on myosin
    • Mitchell, E.J., R. Jakes, and J. Kendrick-Jones. 1986. Localisation of light chain and actin binding sites on myosin. Eur. J. Biochem. 161:25-35.
    • (1986) Eur. J. Biochem. , vol.161 , pp. 25-35
    • Mitchell, E.J.1    Jakes, R.2    Kendrick-Jones, J.3
  • 55
    • 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
  • 57
    • 0022172245 scopus 로고
    • Organization, chemistry, and assembly of the cytoskeletal apparatus of the intestinal brush border
    • Mooseker, M.S. 1985. Organization, chemistry, and assembly of the cytoskeletal apparatus of the intestinal brush border. Annu. Rev. Cell Biol. 1:209-241.
    • (1985) Annu. Rev. Cell Biol. , vol.1 , pp. 209-241
    • Mooseker, M.S.1
  • 59
    • 0021326943 scopus 로고
    • Isolation and partial renaturation of proteolytic fragments of the myosin head
    • Muhlrad, A., and M.F. Morales. 1984. Isolation and partial renaturation of proteolytic fragments of the myosin head. Proc. Natl. Acad. Sci. USA. 81:1003-1007.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 1003-1007
    • Muhlrad, A.1    Morales, M.F.2
  • 60
    • 0015387411 scopus 로고
    • Chromatin structure and the cell cycle
    • Pederson, T. 1972. Chromatin structure and the cell cycle. Proc. Natl. Acad. Sci. USA. 69:2224-2228.
    • (1972) Proc. Natl. Acad. Sci. USA , vol.69 , pp. 2224-2228
    • Pederson, T.1
  • 62
    • 0025939215 scopus 로고
    • The neutrophil selectin LECAM-1 presents carbohydrate ligands to the vascular selectins ELAM-1 and GMP-140
    • Picker, L.J., R.A. Warnock, A.R. Burns, C.M. Doerschuk, E.L. Berg, and E.G. Butcher. 1991. The neutrophil selectin LECAM-1 presents carbohydrate ligands to the vascular selectins ELAM-1 and GMP-140. Cell. 66:921-933.
    • (1991) Cell , vol.66 , pp. 921-933
    • Picker, L.J.1    Warnock, R.A.2    Burns, A.R.3    Doerschuk, C.M.4    Berg, E.L.5    Butcher, E.G.6
  • 63
    • 12044259376 scopus 로고
    • Membrane ruffling and signal transduction
    • Ridley, A.J. 1994. Membrane ruffling and signal transduction. Bio Essays. 16:321-327.
    • (1994) Bio Essays , vol.16 , pp. 321-327
    • Ridley, A.J.1
  • 64
    • 0029828736 scopus 로고    scopus 로고
    • Dictyostelium discoideum cells lacking the 34,000 dalton actin binding protein can grow, locomote, and develop, but exhibit defects in regulation of cell structure and movement: A case of partial redundancy
    • Rivero, F., R. Furukawa, A.A. Noegel, and M. Fechheimer. 1996. Dictyostelium discoideum cells lacking the 34,000 dalton actin binding protein can grow, locomote, and develop, but exhibit defects in regulation of cell structure and movement: a case of partial redundancy. J. Cell Biol. 135:965-980.
    • (1996) J. Cell Biol. , vol.135 , pp. 965-980
    • Rivero, F.1    Furukawa, R.2    Noegel, A.A.3    Fechheimer, M.4
  • 65
    • 0001604571 scopus 로고
    • New actin-binding proteins from Dictyostelium discoideum
    • Schleicher, M., G. Gerisch, and G. Isenberg. 1984. New actin-binding proteins from Dictyostelium discoideum. EMBO J. 3:2095-2100.
    • (1984) EMBO J. , vol.3 , pp. 2095-2100
    • Schleicher, M.1    Gerisch, G.2    Isenberg, G.3
  • 66
    • 0025343106 scopus 로고
    • Dictyostelium discoideum plasma membranes contain an actin-nucleating activity that requires ponticulin, an integral membrane glycoprotein
    • Shariff, A., and E.J. Luna. 1990. Dictyostelium discoideum plasma membranes contain an actin-nucleating activity that requires ponticulin, an integral membrane glycoprotein. J. Cell Biol. 110:681-692.
    • (1990) J. Cell Biol. , vol.110 , pp. 681-692
    • Shariff, A.1    Luna, E.J.2
  • 67
    • 85047673845 scopus 로고
    • The roles of microfilament-associated proteins, drebrins, in brain morphogenesis: A review
    • Shirao, T. 1995. The roles of microfilament-associated proteins, drebrins, in brain morphogenesis: a review. J Biochem. 117:231-236.
    • (1995) J Biochem. , vol.117 , pp. 231-236
    • Shirao, T.1
  • 68
    • 0026512294 scopus 로고
    • Cloning of drebrin A and induction of neurite-like processes in drebrin-transfected cells
    • Shirao, T., N. Kojima, and K. Obata. 1992. Cloning of drebrin A and induction of neurite-like processes in drebrin-transfected cells. NeuroReport. 3:109-112.
    • (1992) NeuroReport , vol.3 , pp. 109-112
    • Shirao, T.1    Kojima, N.2    Obata, K.3
  • 69
    • 0028898820 scopus 로고
    • Indirect association of ezrin with F-actin: Isoform specificity and calcium sensitivity
    • Shuster, C.B., and I.M. Herman. 1995. Indirect association of ezrin with F-actin: isoform specificity and calcium sensitivity. J. Cell Biol. 128:837-848.
    • (1995) J. Cell Biol. , vol.128 , pp. 837-848
    • Shuster, C.B.1    Herman, I.M.2
  • 71
    • 0020775302 scopus 로고
    • Identification of G actin-binding proteins in rat tissues using a gel overlay technique
    • Snabes, M.C., A.E. Boyd, III, and J. Bryan. 1983. Identification of G actin-binding proteins in rat tissues using a gel overlay technique. Exp. Cell Res. 146:63-70.
    • (1983) Exp. Cell Res. , vol.146 , pp. 63-70
    • Snabes, M.C.1    Boyd III, A.E.2    Bryan, J.3
  • 72
    • 0027299745 scopus 로고
    • On the crawling of animal cells
    • Stossel, T.P. 1993. On the crawling of animal cells. Science. 260:1086-1094.
    • (1993) Science , vol.260 , pp. 1086-1094
    • Stossel, T.P.1
  • 73
    • 0021928968 scopus 로고
    • Isolation of an actin-binding protein from membranes of Dictyostelium discoideum
    • Stratford, C.A., and S. Brown. 1985. Isolation of an actin-binding protein from membranes of Dictyostelium discoideum. J. Cell Biol. 100:727-735.
    • (1985) J. Cell Biol. , vol.100 , pp. 727-735
    • Stratford, C.A.1    Brown, S.2
  • 75
    • 0028226406 scopus 로고
    • Axonal transport of actin and actin-binding proteins in the rat sciatic nerve
    • Tanaka, K., T. Tashiro, S. Sekimoto, and Y. Komiya. 1994. Axonal transport of actin and actin-binding proteins in the rat sciatic nerve. Neurosci. Res. 19:295-302.
    • (1994) Neurosci. Res. , vol.19 , pp. 295-302
    • Tanaka, K.1    Tashiro, T.2    Sekimoto, S.3    Komiya, Y.4
  • 76
    • 0026318162 scopus 로고
    • Force transmission across muscle cell membranes
    • Tidball, J.G. 1991. Force transmission across muscle cell membranes. J. Biomechanics. 24:4352.
    • (1991) J. Biomechanics , vol.24 , pp. 4352
    • Tidball, J.G.1
  • 77
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Stahelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA. 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Stahelin, T.2    Gordon, J.3
  • 78
    • 0027380638 scopus 로고
    • Submembranous junctional plaque proteins include potential tumor suppressor molecules
    • Tsukita, S., M. Itoh, A. Nagafuchi, S. Yonemura, and S. Tsukita. 1993. Submembranous junctional plaque proteins include potential tumor suppressor molecules. J. Cell Biol. 123:1049-1053.
    • (1993) J. Cell Biol. , vol.123 , pp. 1049-1053
    • Tsukita, S.1    Itoh, M.2    Nagafuchi, A.3    Yonemura, S.4    Tsukita, S.5
  • 79
    • 0027933858 scopus 로고
    • Ezrin has a COOH-terminal actin-binding site that is conserved in the ezrin protein family
    • Turunen, O., T. Wahlström, and A. Vaheri. 1994. Ezrin has a COOH-terminal actin-binding site that is conserved in the ezrin protein family. J. Cell Biol. 126:1445-1453.
    • (1994) J. Cell Biol. , vol.126 , pp. 1445-1453
    • Turunen, O.1    Wahlström, T.2    Vaheri, A.3
  • 80
    • 0021508527 scopus 로고
    • 1, associated with acetylcholine receptor containing membrane fragments is an actin-binding protein
    • 1, associated with acetylcholine receptor containing membrane fragments is an actin-binding protein. EMBO J. 3:2287-2290.
    • (1984) EMBO J. , vol.3 , pp. 2287-2290
    • Walker, J.H.1    Boustead, C.M.2    Witzemann, V.3
  • 81
    • 0027361181 scopus 로고
    • The actin-binding protein comitin (p24) is a component of the Golgi apparatus
    • Weiner, O.H., J. Murphy, G. Griffiths, M. Schleicher, and A.A. Noegel. 1993. The actin-binding protein comitin (p24) is a component of the Golgi apparatus. J. Cell Biol. 123:23-34.
    • (1993) J. Cell Biol. , vol.123 , pp. 23-34
    • Weiner, O.H.1    Murphy, J.2    Griffiths, G.3    Schleicher, M.4    Noegel, A.A.5
  • 82
    • 0024377431 scopus 로고
    • Immunofluorescence localization of ponticulin in motile cells
    • Wuestehube, L.J., C.P. Chia, and E.J. Luna. 1989. Immunofluorescence localization of ponticulin in motile cells. Cell Motil. Cytoskeleton. 13:245-263.
    • (1989) Cell Motil. Cytoskeleton , vol.13 , pp. 245-263
    • Wuestehube, L.J.1    Chia, C.P.2    Luna, E.J.3
  • 83
    • 0023425214 scopus 로고
    • F-actin binds to the cytoplasmic surface of ponticulin, a 17-kD integral glycoprotein from Dictyostelium discoideum
    • Wuestehube, L.J., and E.J. Luna. 1987. F-actin binds to the cytoplasmic surface of ponticulin, a 17-kD integral glycoprotein from Dictyostelium discoideum. J. Cell Biol. 105:1741-1751.
    • (1987) J. Cell Biol. , vol.105 , pp. 1741-1751
    • Wuestehube, L.J.1    Luna, E.J.2
  • 84
    • 0029862987 scopus 로고    scopus 로고
    • Biochemical characterization of ezrin-actin interaction
    • Yao, X., L. Cheng, and J.G. Forte. 1996. Biochemical characterization of ezrin-actin interaction. J. Biol. Chem. 271:7224-7229.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7224-7229
    • Yao, X.1    Cheng, L.2    Forte, J.G.3
  • 85
    • 0026645917 scopus 로고
    • Inhibition of actin filament depolymerization by the Dictyostelium 30,000-D actin-bundling protein
    • Zigmond, S.H., R. Furukawa, and M. Fechheimer. 1992. Inhibition of actin filament depolymerization by the Dictyostelium 30,000-D actin-bundling protein. J. Cell Biol. 119:559-567.
    • (1992) J. Cell Biol. , vol.119 , pp. 559-567
    • Zigmond, S.H.1    Furukawa, R.2    Fechheimer, M.3


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