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Volumn 110, Issue 16, 1997, Pages 1893-1906

Structural and functional similarities between the human cytoskeletal protein zyxin and the ActA protein of Listeria monocytogenes

Author keywords

ActA; Actin; Cell motility; Listeria; Zyxin

Indexed keywords

BACTERIAL PROTEIN; CYTOSKELETON PROTEIN;

EID: 0030828053     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (73)

References (78)
  • 1
    • 0029954225 scopus 로고    scopus 로고
    • Coordinated regulation of platelet actin filament barbed ends by gelsolin and capping protein
    • Barkalow, K., Witke, W., Kwiatkowski, D. J. and Hartwig, J. H. (1996). Coordinated regulation of platelet actin filament barbed ends by gelsolin and capping protein. J. Cell Biol. 134, 389-399.
    • (1996) J. Cell Biol. , vol.134 , pp. 389-399
    • Barkalow, K.1    Witke, W.2    Kwiatkowski, D.J.3    Hartwig, J.H.4
  • 2
    • 0023000443 scopus 로고
    • Identification of a new protein localized at sites of cell-substrate adhesion
    • Beckerle, M. C. (1986). Identification of a new protein localized at sites of cell-substrate adhesion. J. Cell Biol. 103, 1679-1687.
    • (1986) J. Cell Biol. , vol.103 , pp. 1679-1687
    • Beckerle, M.C.1
  • 3
    • 0029761645 scopus 로고    scopus 로고
    • The focal-adhesion vasodilator-stimulated phosphoprotein (VASP) binds tu the proline-rich domain in vinculin
    • Brindle, N. P., Holt, M. R., Davies, J. E., Price, C. J. and Critchely, D. R. (1996). The focal-adhesion vasodilator-stimulated phosphoprotein (VASP) binds tu the proline-rich domain in vinculin. Biochem. J. 318, 753-757.
    • (1996) Biochem. J. , vol.318 , pp. 753-757
    • Brindle, N.P.1    Holt, M.R.2    Davies, J.E.3    Price, C.J.4    Critchely, D.R.5
  • 4
    • 0019551730 scopus 로고
    • 'Western blotting' : Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A
    • Burnette, W. N. (1981). 'Western blotting' : electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal. Biochem. 112, 195-203.
    • (1981) Anal. Biochem. , vol.112 , pp. 195-203
    • Burnette, W.N.1
  • 5
    • 0026045382 scopus 로고
    • Kinetic analysis of F-actin depolymerization in polymorphonuclear leukocyte lysates indicates that chemoattractant stimulation increases actin filament length distribution
    • Cano, M. L., Lauffenburger, D. A. and Zigmond, S. H. (1991). Kinetic analysis of F-actin depolymerization in polymorphonuclear leukocyte lysates indicates that chemoattractant stimulation increases actin filament length distribution. J. Cell Biol. 115, 677-687.
    • (1991) J. Cell Biol. , vol.115 , pp. 677-687
    • Cano, M.L.1    Lauffenburger, D.A.2    Zigmond, S.H.3
  • 6
    • 0028933782 scopus 로고
    • A focal adhesion factor directly linking intracellularly motile Listeria monocytogenes and Listeria ivanovii to the actin-based cytoskeleton of mammalian cells
    • Chakraborty, T., Ebel, F., Domann, E., Niebuhr, K., Gerstel, B., Pistor, S., Temm-Grove, C. J., Jockusch, B. M., Reinhard, M., Walter, U. and Wehland, J. (1995). A focal adhesion factor directly linking intracellularly motile Listeria monocytogenes and Listeria ivanovii to the actin-based cytoskeleton of mammalian cells. EMRO J. 14, 1314-1321.
    • (1995) EMRO J. , vol.14 , pp. 1314-1321
    • Chakraborty, T.1    Ebel, F.2    Domann, E.3    Niebuhr, K.4    Gerstel, B.5    Pistor, S.6    Temm-Grove, C.J.7    Jockusch, B.M.8    Reinhard, M.9    Walter, U.10    Wehland, J.11
  • 7
    • 0017782474 scopus 로고
    • Continuous growth and differentiation of human myeloid leukaemic cells in suspension culture
    • Coliins, S. J., Gallo, R. C. and Gallagher, R. E. (1977). Continuous growth and differentiation of human myeloid leukaemic cells in suspension culture. Nature 270, 347-349.
    • (1977) Nature , vol.270 , pp. 347-349
    • Coliins, S.J.1    Gallo, R.C.2    Gallagher, R.E.3
  • 8
    • 0026075528 scopus 로고
    • Purification and characterization of zyxin, an 82,000-Dalton component of adherens junctions
    • Crawford, A. W. and Beckerle, M. C. (1991). Purification and characterization of zyxin, an 82,000-Dalton component of adherens junctions. J. Biol. Chem. 266m 5847-5853.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5847-5853
    • Crawford, A.W.1    Beckerle, M.C.2
  • 9
    • 0026586856 scopus 로고
    • An interaction between zyxin and alpha-actinin
    • Crawford, A. W., Michelsen, J. W. and Beckerle, M. C. (1992). An interaction between zyxin and alpha-actinin. J. Cell Biol. 116, 1381-1393.
    • (1992) J. Cell Biol. , vol.116 , pp. 1381-1393
    • Crawford, A.W.1    Michelsen, J.W.2    Beckerle, M.C.3
  • 10
    • 0028866712 scopus 로고
    • Actin-based motility of vaccinia virus
    • Cudmore, S., Cossart, P., Griffiths, G. and Way, M. (1995). Actin-based motility of vaccinia virus. Nature 378, 636-638.
    • (1995) Nature , vol.378 , pp. 636-638
    • Cudmore, S.1    Cossart, P.2    Griffiths, G.3    Way, M.4
  • 11
    • 0029020632 scopus 로고
    • Actin polymerization and intracellular solvent flow in cell surface blebbing
    • Cunningham, C. C. (1995). Actin polymerization and intracellular solvent flow in cell surface blebbing. J. Cell Biol. 129, 1589-1599.
    • (1995) J. Cell Biol. , vol.129 , pp. 1589-1599
    • Cunningham, C.C.1
  • 12
    • 0025081821 scopus 로고
    • Listeria monocytogenes moves rapidly through the host-cell cytoplasm by inducing directional actin assembly
    • Dabiri, G. A., Sanger, J. M., Portnoy, D. A. and Southwick, F. S. (1990). Listeria monocytogenes moves rapidly through the host-cell cytoplasm by inducing directional actin assembly. Proc. Nat. Acad. Sci. USA 87, 6068-6072.
    • (1990) Proc. Nat. Acad. Sci. USA , vol.87 , pp. 6068-6072
    • Dabiri, G.A.1    Sanger, J.M.2    Portnoy, D.A.3    Southwick, F.S.4
  • 13
    • 0026577663 scopus 로고
    • A novel bacterial virulence gene in Listeria monocytogenes required for host cell microfilament interaction with homology to the proline-rich region of vinculin
    • Domann, E., Wehland, J., Rohde, M., Pistor, S., Hartl, M., Goebel, W., Leimeister- Wächter, M., Wuenschner, M. and Chakraborty, T. (1992). A novel bacterial virulence gene in Listeria monocytogenes required for host cell microfilament interaction with homology to the proline-rich region of vinculin. EMBO J. 11. 1981-1990.
    • (1992) EMBO J. , vol.11 , pp. 1981-1990
    • Domann, E.1    Wehland, J.2    Rohde, M.3    Pistor, S.4    Hartl, M.5    Goebel, W.6    Leimeister-Wächter, M.7    Wuenschner, M.8    Chakraborty, T.9
  • 14
    • 0022340978 scopus 로고
    • Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product
    • Evan, G. I., Lewis, G., Ramsay, G. and Bishop, J. M. (1985). Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product. Mol. Cell. Biol. 5. 3610-3616.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 3610-3616
    • Evan, G.I.1    Lewis, G.2    Ramsay, G.3    Bishop, J.M.4
  • 15
    • 0027968554 scopus 로고
    • Purification. characterization and crystalization of human platelet profilin expressed in Escherichia coli
    • Fedorov, A. A., Pollard, T. D. and Almo, S. C. (1994) Purification. characterization and crystalization of human platelet profilin expressed in Escherichia coli. J. Mol. Biol. 241, 480-482.
    • (1994) J. Mol. Biol. , vol.241 , pp. 480-482
    • Fedorov, A.A.1    Pollard, T.D.2    Almo, S.C.3
  • 16
    • 0024095187 scopus 로고
    • Actions of cytochalasins on the organisation of actin filaments and microtubules in a neuronal growth cone
    • Forscher, P. and Smith, S. J. (1988). Actions of cytochalasins on the organisation of actin filaments and microtubules in a neuronal growth cone. J. Cell Biol. 107, 1505-1516.
    • (1988) J. Cell Biol. , vol.107 , pp. 1505-1516
    • Forscher, P.1    Smith, S.J.2
  • 17
    • 0025328511 scopus 로고
    • Novel cysteine-rich motif and homeodomain in the product of the Caenorhabditis elegans cell lineage gene lin 11
    • Freyd, G., Kim, S. K. and Horvitzm H. R. (1990) Novel cysteine-rich motif and homeodomain in the product of the Caenorhabditis elegans cell lineage gene lin 11. Nature 344, 876-879.
    • (1990) Nature , vol.344 , pp. 876-879
    • Freyd, G.1    Kim, S.K.2    Horvitzm, H.R.3
  • 18
    • 0024317269 scopus 로고
    • Villin induces microvilli growth and actin redistribution in transfected fibroblasts
    • Friederich, E., Huet, C., Arpin, M. and Louvard, D. (1989). Villin induces microvilli growth and actin redistribution in transfected fibroblasts. Cell 59, 461-475.
    • (1989) Cell , vol.59 , pp. 461-475
    • Friederich, E.1    Huet, C.2    Arpin, M.3    Louvard, D.4
  • 19
    • 0029079119 scopus 로고
    • Targeting of Listeria monocytogenes ActA protein to the plasma membrane as a tool to dissect both actin-based cell morphogenesis and ActA function
    • Friederich, E., Gouin, E., Hellio, R., Koeks, C., Cossart, P. and Louvard, D. (1995). Targeting of Listeria monocytogenes ActA protein to the plasma membrane as a tool to dissect both actin-based cell morphogenesis and ActA function. EMBO J. 14, 2731-2744.
    • (1995) EMBO J. , vol.14 , pp. 2731-2744
    • Friederich, E.1    Gouin, E.2    Hellio, R.3    Koeks, C.4    Cossart, P.5    Louvard, D.6
  • 20
    • 0030006456 scopus 로고    scopus 로고
    • The ActA polypeptides of Listeria ivanovii and Listeria monocytogenes harbor related binding sites for host microfilament proteins
    • Gerstel, B., Gröbe, L., Pistor, S., Chakraborty, T. and Wehland, J. (1996). The ActA polypeptides of Listeria ivanovii and Listeria monocytogenes harbor related binding sites for host microfilament proteins. Infect. Immun. 64, 1929-1936.
    • (1996) Infect. Immun. , vol.64 , pp. 1929-1936
    • Gerstel, B.1    Gröbe, L.2    Pistor, S.3    Chakraborty, T.4    Wehland, J.5
  • 21
    • 0030592559 scopus 로고    scopus 로고
    • Mena, a relative of VASP and Drosophila enabled, is implicated in the control of microfilament dynamics
    • Gertler, F. B., Niebuhr, K., Reinhard, M., Wehland, J. and Soriano, P. (1996). Mena, a relative of VASP and Drosophila enabled, is implicated in the control of microfilament dynamics. Cell 87, 227-239.
    • (1996) Cell , vol.87 , pp. 227-239
    • Gertler, F.B.1    Niebuhr, K.2    Reinhard, M.3    Wehland, J.4    Soriano, P.5
  • 22
    • 0026720075 scopus 로고
    • Tight control of gene expression in mammalian cells by tetracycline-responsive promoters
    • Gossen, M. and Bujard, H. (1992). Tight control of gene expression in mammalian cells by tetracycline-responsive promoters. Proc. Nat. Acad. Sci. USA 89, 5547-5551.
    • (1992) Proc. Nat. Acad. Sci. USA , vol.89 , pp. 5547-5551
    • Gossen, M.1    Bujard, H.2
  • 23
    • 0029011237 scopus 로고
    • IactA of Listeria ivanovii, although distantly related to Listeria monocytogenes act A, restores actin tail formation in an L. monocytogenes actA mutant
    • Gouin, E., Dehoux, P., Mengaud, J., Kocks, C. and Cossart, P. (1995) iactA of Listeria ivanovii, although distantly related to Listeria monocytogenes act A, restores actin tail formation in an L. monocytogenes actA mutant. Infect. Immun. 63, 2729-2737.
    • (1995) Infect. Immun. , vol.63 , pp. 2729-2737
    • Gouin, E.1    Dehoux, P.2    Mengaud, J.3    Kocks, C.4    Cossart, P.5
  • 24
    • 0024445576 scopus 로고
    • Purification of a vasodilator-regulated phosphoprotein from human platelets
    • Halbrügge, M. and Walter, U. (1989). Purification of a vasodilator-regulated phosphoprotein from human platelets, Eur. J. Biochem. 185, 41-51.
    • (1989) Eur. J. Biochem. , vol.185 , pp. 41-51
    • Halbrügge, M.1    Walter, U.2
  • 25
    • 0025013547 scopus 로고
    • A polybasic domain or palmitoylation is required in addition to the CAAX motif to localize p21ras to the plasma membrane
    • Hancock, J. F., Paterson, H. and Marshall, C. J. (1990). A polybasic domain or palmitoylation is required in addition to the CAAX motif to localize p21ras to the plasma membrane. Cell 63, 133-139.
    • (1990) Cell , vol.63 , pp. 133-139
    • Hancock, J.F.1    Paterson, H.2    Marshall, C.J.3
  • 26
    • 0026037624 scopus 로고
    • A CAAX or a CAAL motif and a second signal are sufficient for plasma membrane targeting of ras proteins
    • Hancock, J. F., Cadwallader, K., Paterson, H. and Marshall, C. J. (1991). A CAAX or a CAAL motif and a second signal are sufficient for plasma membrane targeting of ras proteins. EMBO J. 10, 4033-4039.
    • (1991) EMBO J. , vol.10 , pp. 4033-4039
    • Hancock, J.F.1    Cadwallader, K.2    Paterson, H.3    Marshall, C.J.4
  • 28
    • 0029117595 scopus 로고
    • Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets
    • Hartwig, J. H., Bokoch, G. M., Carpenter, C. L., Janmey, P. A., Taylor, L. A., Toker, A. and Stossel, T. P. (1995). Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets. Cell 82, 643-653.
    • (1995) Cell , vol.82 , pp. 643-653
    • Hartwig, J.H.1    Bokoch, G.M.2    Carpenter, C.L.3    Janmey, P.A.4    Taylor, L.A.5    Toker, A.6    Stossel, T.P.7
  • 29
    • 0031042322 scopus 로고    scopus 로고
    • Actin and cell pathogenesis. Curr
    • Higley, S. and Way, M. (1997). Actin and cell pathogenesis. Curr. Opin. Cell Biol. 9, 62-69.
    • (1997) Opin. Cell Biol. , vol.9 , pp. 62-69
    • Higley, S.1    Way, M.2
  • 30
    • 0029985426 scopus 로고    scopus 로고
    • SH3 domain-dependent interaction of the proto-oncogene product Vav with the focal contact protein zyxin
    • Hubert, O., Schilling, J. W., Berkerle, M. C., Ulrich, A. and Jallal, B. (1996). SH3 domain-dependent interaction of the proto-oncogene product Vav with the focal contact protein zyxin. Oncogene 12, 1577-1581.
    • (1996) Oncogene , vol.12 , pp. 1577-1581
    • Hubert, O.1    Schilling, J.W.2    Berkerle, M.C.3    Ulrich, A.4    Jallal, B.5
  • 31
    • 0026515440 scopus 로고
    • L. monocytogenes-induced actin assembly requires the actA gene product, a surface protein
    • Kocks, C., Gouin, K., Tabouret, M., Berche, P., Ohayon, H. and Cossart, P. (1992). L. monocytogenes-induced actin assembly requires the actA gene product, a surface protein. Cell 68, 521-531.
    • (1992) Cell , vol.68 , pp. 521-531
    • Kocks, C.1    Gouin, K.2    Tabouret, M.3    Berche, P.4    Ohayon, H.5    Cossart, P.6
  • 32
    • 0029591170 scopus 로고
    • The unrelated surface proteins ActA of Listeria monocytogenes and IcsA of Shigella flexneri are sufficient to confer actin-based motility on Listeria innocula and Escherichia coli respectively
    • Kocks, C., Marchand, J. B., Gouin, G., d'Hauteville, H., Sansonetti, P. J., Carlier, M. F. and Cossart, P. (1995). The unrelated surface proteins ActA of Listeria monocytogenes and IcsA of Shigella flexneri are sufficient to confer actin-based motility on Listeria innocula and Escherichia coli respectively. Mol. Microbiol 18, 413-423.
    • (1995) Mol. Microbiol , vol.18 , pp. 413-423
    • Kocks, C.1    Marchand, J.B.2    Gouin, G.3    D'Hauteville, H.4    Sansonetti, P.J.5    Carlier, M.F.6    Cossart, P.7
  • 34
    • 0028985135 scopus 로고
    • The actin polymerization protein from Listeria ivanovii is a large repeat protein which shows only limited amino-acid sequence homology to ActA from Listeria monocytogenes
    • Kreft, J., Dumbsky, M. and Theiss, S. (1995). The actin polymerization protein from Listeria ivanovii is a large repeat protein which shows only limited amino-acid sequence homology to ActA from Listeria monocytogenes. FEMS Microbiol. Lett. 126, 113-122.
    • (1995) FEMS Microbiol. Lett. , vol.126 , pp. 113-122
    • Kreft, J.1    Dumbsky, M.2    Theiss, S.3
  • 35
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of haeteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of haeteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 36
    • 0029609261 scopus 로고
    • The amino-terminal part of ActA is critical for the actin-based motility of Listeria monocytogenes; the central proline-rich region acts as a stimulator
    • Lasa, I., David, V., Gouin, E., Marchand, J. P. and Cossart, P. (1995). The amino-terminal part of ActA is critical for the actin-based motility of Listeria monocytogenes; the central proline-rich region acts as a stimulator. Mol. Microbiol. 18, 425-426.
    • (1995) Mol. Microbiol. , vol.18 , pp. 425-426
    • Lasa, I.1    David, V.2    Gouin, E.3    Marchand, J.P.4    Cossart, P.5
  • 37
    • 0030024449 scopus 로고    scopus 로고
    • Actin-based bacterial motility: Towards a definition of the minimal requirements
    • Lasa, I. and Cossart, P. (1996). Actin-based bacterial motility: Towards a definition of the minimal requirements. Trends Cell Biol. 6, 109-114.
    • (1996) Trends Cell Biol. , vol.6 , pp. 109-114
    • Lasa, I.1    Cossart, P.2
  • 38
    • 0030900504 scopus 로고    scopus 로고
    • Identification of two regions in the amino terminal domain of ActA involved in the-actin comet tail formation by Listeria monocytogenes
    • Lasa, I., Gouin, E., Goethals, M., Vancompernolle, K., David, V., Vandekerckhove, J. and Cossart, P. (1997). Identification of two regions in the amino terminal domain of ActA involved in the-actin comet tail formation by Listeria monocytogenes. EMBO J. 16, 1531-1540.
    • (1997) EMBO J. , vol.16 , pp. 1531-1540
    • Lasa, I.1    Gouin, E.2    Goethals, M.3    Vancompernolle, K.4    David, V.5    Vandekerckhove, J.6    Cossart, P.7
  • 39
    • 0030045346 scopus 로고    scopus 로고
    • Cell migration: A physically integrated molecular process
    • Lauflenburger, D. A. and Horwitz, A. F. (1996). Cell migration: A physically integrated molecular process. Cell 84, 359-369.
    • (1996) Cell , vol.84 , pp. 359-369
    • Lauflenburger, D.A.1    Horwitz, A.F.2
  • 41
    • 0014115428 scopus 로고
    • Production of free light chains of immunoglobulin by a hematopoietic cell line derived from a patient with multiple myeloma
    • Matsuoka, Y., Moore, G. F., Yagi, Y. and Pressman, D. (1967) Production of free light chains of immunoglobulin by a hematopoietic cell line derived from a patient with multiple myeloma. Proc. Soc. Exp. Biol. Med. 125, 1246-1250.
    • (1967) Proc. Soc. Exp. Biol. Med. , vol.125 , pp. 1246-1250
    • Matsuoka, Y.1    Moore, G.F.2    Yagi, Y.3    Pressman, D.4
  • 42
    • 0020339969 scopus 로고
    • Transient expression of the chicken lysozyme gene after transfer into human cells
    • Matthias, P. D., Renkawitz, R., Grez, M. and Schutz, G. (1982). Transient expression of the chicken lysozyme gene after transfer into human cells. EMBO J. 1, 1207-1212.
    • (1982) EMBO J. , vol.1 , pp. 1207-1212
    • Matthias, P.D.1    Renkawitz, R.2    Grez, M.3    Schutz, G.4
  • 43
    • 0028961293 scopus 로고
    • Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia. and filopodia
    • Nobes, C. D. and Hall, A. (1995). Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia. and filopodia. Cell 81, 53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 44
    • 0017696571 scopus 로고
    • High resolution two-dimensional electrophoresis of basic as well as acidic proteins
    • O'Karrell, P. Z., Goodman, H. M. and O'Farrell, P. H. (1977). High resolution two-dimensional electrophoresis of basic as well as acidic proteins. Cell 12, 1133-1142.
    • (1977) Cell , vol.12 , pp. 1133-1142
    • O'Karrell, P.Z.1    Goodman, H.M.2    O'Farrell, P.H.3
  • 45
    • 0024426297 scopus 로고
    • Incorporation and turnover of biotin-labeled actin microinjected into fibroblastic cells: An immunoelectron microscopic study
    • Okabe, S. and Hirokawa, N. (1989). Incorporation and turnover of biotin-labeled actin microinjected into fibroblastic cells: An immunoelectron microscopic study. J. Cell Biol. 109, 1581-1595.
    • (1989) J. Cell Biol. , vol.109 , pp. 1581-1595
    • Okabe, S.1    Hirokawa, N.2
  • 46
    • 0027772556 scopus 로고
    • How profilm promotes actin filament assembly in the presence of thymosinß4
    • Pantaloni, D. and Carlier, M.-F. (1993). How profilm promotes actin filament assembly in the presence of thymosinß4. Cell 75, 1007-1014.
    • (1993) Cell , vol.75 , pp. 1007-1014
    • Pantaloni, D.1    Carlier, M.-F.2
  • 48
    • 0030586909 scopus 로고    scopus 로고
    • LPP, the preferred fusion partner gene of HMGIC in lipomas, is a novel member of the LIM protein gene family
    • Petit, M. M., Mols, R., Schoenmakers, E. F., Mandahl, N. and Van De Ven, W. J. (1996). LPP, the preferred fusion partner gene of HMGIC in lipomas, is a novel member of the LIM protein gene family. Genomic 36, 118-129.
    • (1996) Genomic , vol.36 , pp. 118-129
    • Petit, M.M.1    Mols, R.2    Schoenmakers, E.F.3    Mandahl, N.4    Van De Ven, W.J.5
  • 49
    • 0029294733 scopus 로고
    • The bacterial actin nucleator protein ActA of Listeria monocytogenes contains multiple binding sites for host microfilament proteins
    • Pistor, S., Chakraborty, T., Walter, U. and Wehland, J. (1995). The bacterial actin nucleator protein ActA of Listeria monocytogenes contains multiple binding sites for host microfilament proteins. Curr. Biol. 5, 517-525.
    • (1995) Curr. Biol. , vol.5 , pp. 517-525
    • Pistor, S.1    Chakraborty, T.2    Walter, U.3    Wehland, J.4
  • 50
    • 0026563095 scopus 로고
    • The 46/50 kDa phosphoprotein VASP purified from human platelets is a novel protein associated with actin filaments and focal contacts
    • Reinhard, M., Halbrügge, M., Scheer, U., Wiegand, C., Jockusch, B. M. and Walter, U. (1992). The 46/50 kDa phosphoprotein VASP purified from human platelets is a novel protein associated with actin filaments and focal contacts. EMBO J. 11, 2063-2070.
    • (1992) EMBO J. , vol.11 , pp. 2063-2070
    • Reinhard, M.1    Halbrügge, M.2    Scheer, U.3    Wiegand, C.4    Jockusch, B.M.5    Walter, U.6
  • 51
    • 0029025248 scopus 로고
    • The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilins
    • Reinhard, M., Giehl, C., Abel, K., Haffner, C., Jarchau, T., Hoppe, V., Jockusch, B. M. and Walter, U. (1995a). The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilins. EMBO J. 14, 1583-1589.
    • (1995) EMBO J. , vol.14 , pp. 1583-1589
    • Reinhard, M.1    Giehl, C.2    Abel, K.3    Haffner, C.4    Jarchau, T.5    Hoppe, V.6    Jockusch, B.M.7    Walter, U.8
  • 52
    • 0029157584 scopus 로고
    • Identification, purification, and characterization of a zyxin-related protein that binds the focal adhesion and microfilament protein VASP (vasodilator-stimulated phosphoprotein)
    • Reinhard, M., Jouvenal, K., Tripier, D. and Walter, U. (1995b). Identification, purification, and characterization of a zyxin-related protein that binds the focal adhesion and microfilament protein VASP (vasodilator-stimulated phosphoprotein). Proc. Nat. Acad. Sci. USA 92, 7956-7960.
    • (1995) Proc. Nat. Acad. Sci. USA , vol.92 , pp. 7956-7960
    • Reinhard, M.1    Jouvenal, K.2    Tripier, D.3    Walter, U.4
  • 53
    • 0030577348 scopus 로고    scopus 로고
    • VASP interaction with vinculin: A recurring theme of interactions with proline-rich motifs
    • Reinhard, M., Rudiger, M., Jockusch, B. M. and Walter, U. (1996) VASP interaction with vinculin: a recurring theme of interactions with proline-rich motifs. FEBS Let. 399, 103-107.
    • (1996) FEBS Let. , vol.399 , pp. 103-107
    • Reinhard, M.1    Rudiger, M.2    Jockusch, B.M.3    Walter, U.4
  • 54
    • 0027258614 scopus 로고
    • Regulatory sequences on the human villin gene trigger the expression of a reporter gene in a differentiating HT29 intestinal cell line
    • Robine, S., Sahuquillo-Merino, C., Louvard, D. and Pringault, E. (1993). Regulatory sequences on the human villin gene trigger the expression of a reporter gene in a differentiating HT29 intestinal cell line. J. Biol. Chem. 268, 11426-11434.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11426-11434
    • Robine, S.1    Sahuquillo-Merino, C.2    Louvard, D.3    Pringault, E.4
  • 55
    • 0026512793 scopus 로고
    • Human papillonmvirus type 1 E4 proteins differing by their N-terminal ends have distinct cellular localizations when transiently expressed in vitro
    • Rogel-Gaillard, C., Breitburd, F. and Orth, G. (1992). Human papillonmvirus type 1 E4 proteins differing by their N-terminal ends have distinct cellular localizations when transiently expressed in vitro. J. Virol. 66, 816-823.
    • (1992) J. Virol. , vol.66 , pp. 816-823
    • Rogel-Gaillard, C.1    Breitburd, F.2    Orth, G.3
  • 56
    • 0027080110 scopus 로고
    • Zyxin and cCRP: Two interactive LIM domain proteins associated with the cytoskeleton
    • Sadler, I., Crawford, A. W., Michelsen, J. W. and Beckerle, M. C. (1992). Zyxin and cCRP: Two interactive LIM domain proteins associated with the cytoskeleton. J. Cell Biol 119, 1573-1587.
    • (1992) J. Cell Biol , vol.119 , pp. 1573-1587
    • Sadler, I.1    Crawford, A.W.2    Michelsen, J.W.3    Beckerle, M.C.4
  • 58
    • 0029795850 scopus 로고    scopus 로고
    • Dynamics of capping protein and actin assembly in vitro: Uncapping barbed ends by polyphosphoinositides
    • Schafer, D. A., Jennings, P. B. and Cooper, J. A. (1996) Dynamics of capping protein and actin assembly in vitro: Uncapping barbed ends by polyphosphoinositides. J. Cell. Biol. 135, 169-179.
    • (1996) J. Cell. Biol. , vol.135 , pp. 169-179
    • Schafer, D.A.1    Jennings, P.B.2    Cooper, J.A.3
  • 59
    • 0028134697 scopus 로고
    • The LIM domain is a modular protein-binding interface
    • Schmeichel, K. L. and Beckerle, M. C. (1994). The LIM domain is a modular protein-binding interface. Cell 79, 211-219.
    • (1994) Cell , vol.79 , pp. 211-219
    • Schmeichel, K.L.1    Beckerle, M.C.2
  • 60
    • 0031017595 scopus 로고    scopus 로고
    • Molecular dissection of a LIM domain
    • Schmeichel, K. L. and Beckerle, M. C. (1997). Molecular dissection of a LIM domain. Mol. Biol. Cell 8, 219-230.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 219-230
    • Schmeichel, K.L.1    Beckerle, M.C.2
  • 61
    • 0027297369 scopus 로고
    • Protein localisation to the nucleolus: A search for targeting domains in nucleolin
    • Schmidt-Zachmann, M. S. and Nigg, E. A. (1993). Protein localisation to the nucleolus: a search for targeting domains in nucleolin. J. Cell Sci. 105, 799-806.
    • (1993) J. Cell Sci. , vol.105 , pp. 799-806
    • Schmidt-Zachmann, M.S.1    Nigg, E.A.2
  • 63
    • 0017802361 scopus 로고
    • Polarity of actin at the leading edge of cultured cells
    • Small, J. V., Isenberg, G. and Celis, J. E. (1978), Polarity of actin at the leading edge of cultured cells. Nature 272, 638-639.
    • (1978) Nature , vol.272 , pp. 638-639
    • Small, J.V.1    Isenberg, G.2    Celis, J.E.3
  • 64
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichm coli as fusions with glutathione S-transferase
    • Smith, D. B. and Johnson, K. S. (1988). Single-step purification of polypeptides expressed in Escherichm coli as fusions with glutathione S-transferase. Gene 67, 31-41.
    • (1988) Gene , vol.67 , pp. 31-41
    • Smith, D.B.1    Johnson, K.S.2
  • 65
    • 0028837734 scopus 로고
    • Asymmetric distribution of the Listeria monocytogenes ActA protein is required and sufficient to direct actin-based motility
    • Smith, G. A., Portnoy, D. A. and Theriot, J. A. (1995). Asymmetric distribution of the Listeria monocytogenes ActA protein is required and sufficient to direct actin-based motility. Mol. Microbiol. 17, 945-951.
    • (1995) Mol. Microbiol. , vol.17 , pp. 945-951
    • Smith, G.A.1    Portnoy, D.A.2    Theriot, J.A.3
  • 66
    • 0029807736 scopus 로고    scopus 로고
    • The tandem repeat domain in the Listeria monocytogenes ActA protein controls the rate of actin-based motility, the percentage ot mining bacteria, and the localization of vasodilator-stimulated phosphoprotein and profilin
    • Smith, G. A., Theriot, J. A. and Portnoy, D. A. (1996). The tandem repeat domain in the Listeria monocytogenes ActA protein controls the rate of actin-based motility, the percentage ot mining bacteria, and the localization of vasodilator-stimulated phosphoprotein and profilin. J. Cell Biol. 135, 647-660.
    • (1996) J. Cell Biol. , vol.135 , pp. 647-660
    • Smith, G.A.1    Theriot, J.A.2    Portnoy, D.A.3
  • 67
    • 0028276812 scopus 로고
    • Arrest of Listeria movement in host cells by a bacteria actA analogue: Implications for actin-based motility
    • Southwick, F. S. and Purich, D. L. (1994). Arrest of Listeria movement in host cells by a bacteria actA analogue: Implications for actin-based motility. Proc Nat. Acad. Sci. USA 91, 5168-5172.
    • (1994) Proc Nat. Acad. Sci. USA , vol.91 , pp. 5168-5172
    • Southwick, F.S.1    Purich, D.L.2
  • 68
    • 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
  • 69
    • 0029589267 scopus 로고
    • The cell biology of infection by intracellular bacterial pathogens
    • ed. J. A. Spudich. Annual Reviews Inc.. Palo Alto. Ca.
    • Theriot, J. A. (1995). The cell biology of infection by intracellular bacterial pathogens. In Annual Review of Cell and Developmental Biology (ed. J. A. Spudich). pp. 213-239. Annual Reviews Inc.. Palo Alto. Ca.
    • (1995) Annual Review of Cell and Developmental Biology , pp. 213-239
    • Theriot, J.A.1
  • 70
    • 0025740949 scopus 로고
    • Actin microfilament dynamics in locomoting cells
    • Theriot, J. A. and Mitchison, T. J. (1991). Actin microfilament dynamics in locomoting cells. Nature 352, 126-131.
    • (1991) Nature , vol.352 , pp. 126-131
    • Theriot, J.A.1    Mitchison, T.J.2
  • 71
    • 0024741693 scopus 로고
    • Actin filaments and the growth. movement, and spread of the intracellular bacterial parasite. Listeria monocytogenes
    • Tilney. L. G. and Portnoy, D. A. (1989). Actin filaments and the growth. movement, and spread of the intracellular bacterial parasite. Listeria monocytogenes. J. Cell Biol. 109, l597-1608.
    • (1989) J. Cell Biol. , vol.109
    • Tilney, L.G.1    Portnoy, D.A.2
  • 72
    • 0025606399 scopus 로고
    • Actin filament nucleation by the bacterial pathogen Listeria monocytogenes
    • Tilney, L. G., Connelly, P. S. and Portnoy, D. A. (1990). Actin filament nucleation by the bacterial pathogen Listeria monocytogenes. J. Cell Biol. 111, 2979-2988.
    • (1990) J. Cell Biol. , vol.111 , pp. 2979-2988
    • Tilney, L.G.1    Connelly, P.S.2    Portnoy, D.A.3
  • 73
    • 0026719663 scopus 로고
    • How Listeria exploits host cell actin to form its own cytoskeleton. I. Formation of a tail and how that tail might he involved in movement
    • Tilney, L. G., DeRosier, D. J. and Tilney, M.S. (1992a). How Listeria exploits host cell actin to form its own cytoskeleton. I. Formation of a tail and how that tail might he involved in movement. J. Cell Biol. 118, 71-81.
    • (1992) J. Cell Biol. , vol.118 , pp. 71-81
    • Tilney, L.G.1    Derosier, D.J.2    Tilney, M.S.3
  • 74
    • 0026659493 scopus 로고
    • How Listeria exploits host cell actin to form its own cytoskeleton. II. Nucleation, act in filament polarity, filament assembly, and evidence for a pointed end capper
    • Tilney, L. G., DeRosier, D. J., Weber, A. and Tilney, M. S. (1992b). How Listeria exploits host cell actin to form its own cytoskeleton. II. Nucleation, act in filament polarity, filament assembly, and evidence for a pointed end capper. J. Cell Biol. 118, 83-93.
    • (1992) J. Cell Biol. , vol.118 , pp. 83-93
    • Tilney, L.G.1    DeRosier, D.J.2    Weber, A.3    Tilney, M.S.4
  • 75
    • 0022390903 scopus 로고
    • Exchange of actin subunits at the leading edge of living fibroblasts: Possible role of treadmilling
    • Wang, Y.-L. (1985). Exchange of actin subunits at the leading edge of living fibroblasts: Possible role of treadmilling. J. Cell Biol. 101, 597-602.
    • (1985) J. Cell Biol. , vol.101 , pp. 597-602
    • Wang, Y.-L.1
  • 76
    • 0031021153 scopus 로고    scopus 로고
    • Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes
    • Welch, M. D., Iwamatsu, A. and Mitchison, T. J. (1997) Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes. Nature 385, 265-269.
    • (1997) Nature , vol.385 , pp. 265-269
    • Welch, M.D.1    Iwamatsu, A.2    Mitchison, T.J.3
  • 77
    • 0028061406 scopus 로고
    • LIM domain recognition of a tyrosine-containing tight turn
    • Wu, R. V. and Gill, G. N. (1994). LIM domain recognition of a tyrosine-containing tight turn. J. Biol. Chem. 269, 25085-25090.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25085-25090
    • Wu, R.V.1    Gill, G.N.2
  • 78
    • 0029858630 scopus 로고    scopus 로고
    • A zyxin-related protein whose synthesis is reduced in virally transformed fibroblast
    • Zumbrunn, J. and Trueb, B. (1996). A zyxin-related protein whose synthesis is reduced in virally transformed fibroblast. Eur. J. Biochem. 241, 657-663.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 657-663
    • Zumbrunn, J.1    Trueb, B.2


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