메뉴 건너뛰기




Volumn 36, Issue 10, 2004, Pages 1890-1909

The actin cytoskeleton in normal and pathological cell motility

Author keywords

actin related protein; Arp; BCR; breakpoint cluster region; DAD; diaphanous autoregulatory domain; Diaphanous related formins; DRFs; EGFR; Ena; Ena VASP like; Ena VASP homology; enabled; epidermal growth factor receptor; EVH; EVL; F actin; FH; filamentous actin

Indexed keywords

ACTIN FILAMENT; ACTIN POLYMERIZATION; CELL FUNCTION; CELL MOTILITY; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN METABOLISM; PROTEIN PHOSPHORYLATION; REVIEW; SIGNAL TRANSDUCTION; STRUCTURAL HOMOLOGY;

EID: 2942564379     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biocel.2004.01.024     Document Type: Review
Times cited : (190)

References (152)
  • 1
    • 0034697303 scopus 로고    scopus 로고
    • Regulation of microfilament reorganization and invasiveness of breast cancer cells by kinase dead p21-activated kinase-1
    • Adam L., Vadlamudi R., Mandal M., Chernoff J., Kumar R. Regulation of microfilament reorganization and invasiveness of breast cancer cells by kinase dead p21-activated kinase-1. Journal of Biological Chemistry. 275:2000;12041-12050
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 12041-12050
    • Adam, L.1    Vadlamudi, R.2    Mandal, M.3    Chernoff, J.4    Kumar, R.5
  • 2
    • 0035951824 scopus 로고    scopus 로고
    • Identification of a carboxyl-terminal diaphanous-related formin homology protein autoregulatory domain
    • Alberts A.S. Identification of a carboxyl-terminal diaphanous-related formin homology protein autoregulatory domain. Journal of Biological Chemistry. 276:2001;2824-2830
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 2824-2830
    • Alberts, A.S.1
  • 3
  • 4
    • 0033280237 scopus 로고    scopus 로고
    • Proteins of the ADF/cofilin family: Essential regulators of actin dynamics
    • Bamburg J.R. Proteins of the ADF/cofilin family: essential regulators of actin dynamics. Annual Review of Cell and Developmental Biology. 15:1999;185-230
    • (1999) Annual Review of Cell and Developmental Biology , vol.15 , pp. 185-230
    • Bamburg, J.R.1
  • 5
    • 0029802607 scopus 로고    scopus 로고
    • Thymosin beta 15: A novel regulator of tumor cell motility upregulated in metastatic prostate cancer
    • Bao L., Loda M., Janmey P.A., Stewart R., Anand-Apte B., Zetter B.R. Thymosin beta 15: a novel regulator of tumor cell motility upregulated in metastatic prostate cancer. Nature medicine. 2:1996;1322-1328
    • (1996) Nature Medicine , vol.2 , pp. 1322-1328
    • Bao, L.1    Loda, M.2    Janmey, P.A.3    Stewart, R.4    Anand-Apte, B.5    Zetter, B.R.6
  • 7
    • 18444389953 scopus 로고    scopus 로고
    • Antagonism between Ena/VASP proteins and actin filament capping regulates fibroblast motility
    • Bear J.E., Svitkina T.M., Krause M., Schafer D.A., Loureiro J.J., Strasser G.A., et al. Antagonism between Ena/VASP proteins and actin filament capping regulates fibroblast motility. Cell. 109:2002;509-521
    • (2002) Cell , vol.109 , pp. 509-521
    • Bear, J.E.1    Svitkina, T.M.2    Krause, M.3    Schafer, D.A.4    Loureiro, J.J.5    Strasser, G.A.6
  • 8
    • 0034664732 scopus 로고    scopus 로고
    • Ciboulot regulates actin assembly during Drosophila brain metamorphosis
    • Boquet I., Boujemaa R., Carlier M.F., Preat T. Ciboulot regulates actin assembly during Drosophila brain metamorphosis. Cell. 102:2000;797-808
    • (2000) Cell , vol.102 , pp. 797-808
    • Boquet, I.1    Boujemaa, R.2    Carlier, M.F.3    Preat, T.4
  • 10
    • 84886632310 scopus 로고
    • Actin polymerizability is influenced by profilin, a low molecular weight protein in non-muscle cells
    • Carlsson L., Nystrom L.E., Sundkvist I., Markey F., Lindberg U. Actin polymerizability is influenced by profilin, a low molecular weight protein in non-muscle cells. Journal of Molecular Biology. 115:1977;465-483
    • (1977) Journal of Molecular Biology , vol.115 , pp. 465-483
    • Carlsson, L.1    Nystrom, L.E.2    Sundkvist, I.3    Markey, F.4    Lindberg, U.5
  • 11
    • 0034614942 scopus 로고    scopus 로고
    • Role of cofilin in epidermal growth factor-stimulated actin polymerization and lamellipod protrusion
    • Chan A.Y., Bailly M., Zebda N., Segall J.E., Condeelis J.S. Role of cofilin in epidermal growth factor-stimulated actin polymerization and lamellipod protrusion. Journal of Cell Biology. 148:2000;531-542
    • (2000) Journal of Cell Biology , vol.148 , pp. 531-542
    • Chan, A.Y.1    Bailly, M.2    Zebda, N.3    Segall, J.E.4    Condeelis, J.S.5
  • 13
    • 0033853425 scopus 로고    scopus 로고
    • Imaging of cancer invasion and metastasis using green fluorescent protein
    • Condeelis J.S., Wyckoff J., Segall J.E. Imaging of cancer invasion and metastasis using green fluorescent protein. European Journal of Cancer. 36:2000;1671-1680
    • (2000) European Journal of Cancer , vol.36 , pp. 1671-1680
    • Condeelis, J.S.1    Wyckoff, J.2    Segall, J.E.3
  • 16
    • 0032898117 scopus 로고    scopus 로고
    • Identification of Tyr438 as the major in vitro c-Src phosphorylation site in human gelsolin: A mass spectrometric approach
    • De Corte V., Demol H., Goethals M., Van Damme J., Gettemans J., Vandekerckhove J. Identification of Tyr438 as the major in vitro c-Src phosphorylation site in human gelsolin: a mass spectrometric approach. Protein Sciences. 8:1999;234-241
    • (1999) Protein Sciences , vol.8 , pp. 234-241
    • De Corte, V.1    Demol, H.2    Goethals, M.3    Van Damme, J.4    Gettemans, J.5    Vandekerckhove, J.6
  • 18
    • 0036154207 scopus 로고    scopus 로고
    • Clamped-filament elongation model for actin-based motors
    • Dickinson R.B., Purich D.L. Clamped-filament elongation model for actin-based motors. Biophysics Journal. 82:2002;605-617
    • (2002) Biophysics Journal , vol.82 , pp. 605-617
    • Dickinson, R.B.1    Purich, D.L.2
  • 19
    • 0037102301 scopus 로고    scopus 로고
    • Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck
    • Eden S., Rohatgi R., Podtelejnikov A.V., Mann M., Kirschner M.W. Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck. Nature. 418:2002;790-793
    • (2002) Nature , vol.418 , pp. 790-793
    • Eden, S.1    Rohatgi, R.2    Podtelejnikov, A.V.3    Mann, M.4    Kirschner, M.W.5
  • 20
    • 0037069690 scopus 로고    scopus 로고
    • Rho GTPases in cell biology
    • Etienne-Manneville S., Hall A. Rho GTPases in cell biology. Nature. 420:2002;629-635
    • (2002) Nature , vol.420 , pp. 629-635
    • Etienne-Manneville, S.1    Hall, A.2
  • 21
    • 0032959561 scopus 로고    scopus 로고
    • Regulation of p190 Rho-GAP by v-Src is linked to cytoskeletal disruption during transformation
    • Fincham V.J., Chudleigh A., Frame M.C. Regulation of p190 Rho-GAP by v-Src is linked to cytoskeletal disruption during transformation. Journal of Cell Science. 112:1999;947-956
    • (1999) Journal of Cell Science , vol.112 , pp. 947-956
    • Fincham, V.J.1    Chudleigh, A.2    Frame, M.C.3
  • 22
    • 0033952145 scopus 로고    scopus 로고
    • The biology of cell locomotion within three-dimensional extracellular matrix
    • Friedl P., Brocker E.B. The biology of cell locomotion within three-dimensional extracellular matrix. Cellular and Molecular Life Sciences. 57:2000;41-64
    • (2000) Cellular and Molecular Life Sciences , vol.57 , pp. 41-64
    • Friedl, P.1    Brocker, E.B.2
  • 23
    • 0028866016 scopus 로고
    • Migration of coordinated cell clusters in mesenchymal and epithelial cancer explants in vitro
    • Friedl P., Noble P.B., Walton P.A., Laird D.W., Chauvin P.J., Tabah R.J., et al. Migration of coordinated cell clusters in mesenchymal and epithelial cancer explants in vitro. Cancer Research. 55:1995;4557-4560
    • (1995) Cancer Research , vol.55 , pp. 4557-4560
    • Friedl, P.1    Noble, P.B.2    Walton, P.A.3    Laird, D.W.4    Chauvin, P.J.5    Tabah, R.J.6
  • 24
    • 0034792774 scopus 로고    scopus 로고
    • Amoeboid leukocyte crawling through extracellular matrix: Lessons from the Dictyostelium paradigm of cell movement
    • Friedl P., Borgmann S., Brocker E.B. Amoeboid leukocyte crawling through extracellular matrix: lessons from the Dictyostelium paradigm of cell movement. Journal of Leukocyte Biology. 70:2001;491-509
    • (2001) Journal of Leukocyte Biology , vol.70 , pp. 491-509
    • Friedl, P.1    Borgmann, S.2    Brocker, E.B.3
  • 26
    • 0035809163 scopus 로고    scopus 로고
    • A novel neural Wiskott-Aldrich syndrome protein (N-WASP) binding protein, WISH, induces Arp2/3 complex activation independent of Cdc42
    • Fukuoka M., Suetsugu S., Miki H., Fukami K., Endo T., Takenawa T. A novel neural Wiskott-Aldrich syndrome protein (N-WASP) binding protein, WISH, induces Arp2/3 complex activation independent of Cdc42. Journal of Cell Biology. 152:2001;471-482
    • (2001) Journal of Cell Biology , vol.152 , pp. 471-482
    • Fukuoka, M.1    Suetsugu, S.2    Miki, H.3    Fukami, K.4    Endo, T.5    Takenawa, T.6
  • 27
    • 0035479910 scopus 로고    scopus 로고
    • Assembly and mechanosensory function of focal contacts
    • Geiger B., Bershadsky A. Assembly and mechanosensory function of focal contacts. Current Opinion in Cell Biology. 13:2001;584-592
    • (2001) Current Opinion in Cell Biology , vol.13 , pp. 584-592
    • Geiger, B.1    Bershadsky, A.2
  • 28
    • 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., Soriano P. Mena, a relative of VASP and Drosophila enabled, is implicated in the control of microfilament dynamics. Cell. 87:1996;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
  • 29
    • 0037007130 scopus 로고    scopus 로고
    • Ena/VASP proteins regulate cortical neuronal positioning
    • Goh K.L., Cai L., Cepko C.L., Gertler F.B. Ena/VASP proteins regulate cortical neuronal positioning. Current Biology. 12:2002;565-569
    • (2002) Current Biology , vol.12 , pp. 565-569
    • Goh, K.L.1    Cai, L.2    Cepko, C.L.3    Gertler, F.B.4
  • 30
    • 0035199154 scopus 로고    scopus 로고
    • Actin-based motility of intracellular microbial pathogens
    • table
    • Goldberg M.B. Actin-based motility of intracellular microbial pathogens. Microbiology and Molecular Biology Reviews. 65:2001;595-626. table
    • (2001) Microbiology and Molecular Biology Reviews , vol.65 , pp. 595-626
    • Goldberg, M.B.1
  • 31
    • 0027104517 scopus 로고
    • The control of actin nucleotide exchange by thymosin beta 4 and profilin. A potential regulatory mechanism for actin polymerization in cells
    • Goldschmidt-Clermont P.J., Furman M.I., Wachsstock D., Safer D., Nachmias V.T., Pollard T.D. The control of actin nucleotide exchange by thymosin beta 4 and profilin. A potential regulatory mechanism for actin polymerization in cells. Molecular Biology of the Cell. 3:1992;1015-1024
    • (1992) Molecular Biology of the Cell , vol.3 , pp. 1015-1024
    • Goldschmidt-Clermont, P.J.1    Furman, M.I.2    Wachsstock, D.3    Safer, D.4    Nachmias, V.T.5    Pollard, T.D.6
  • 32
    • 0033055077 scopus 로고    scopus 로고
    • A comparative study of the actin-based motilities of the pathogenic bacteria Listeria monocytogenes, Shigella flexneri and Rickettsia conorii
    • Gouin E., Gantelet H., Egile C., Lasa I., Ohayon H., Villiers V., et al. A comparative study of the actin-based motilities of the pathogenic bacteria Listeria monocytogenes, Shigella flexneri and Rickettsia conorii. Journal of Cell Sciences. 112(Pt 11):1999;1697-1708
    • (1999) Journal of Cell Sciences , vol.112 , Issue.11 PART , pp. 1697-1708
    • Gouin, E.1    Gantelet, H.2    Egile, C.3    Lasa, I.4    Ohayon, H.5    Villiers, V.6
  • 33
    • 0024445576 scopus 로고
    • Purification of a vasodilator-regulated phosphoprotein from human platelets
    • Halbrugge M., Walter U. Purification of a vasodilator-regulated phosphoprotein from human platelets. European Journal of Biochemistry. 185:1989;41-50
    • (1989) European Journal of Biochemistry , vol.185 , pp. 41-50
    • Halbrugge, M.1    Walter, U.2
  • 35
    • 0032702259 scopus 로고    scopus 로고
    • Regulation of actin polymerization by Arp2/3 complex and WASp/Scar proteins
    • Higgs H.N., Pollard T.D. Regulation of actin polymerization by Arp2/3 complex and WASp/Scar proteins. Journal of Biological Chemistry. 274:1999;32531-32534
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 32531-32534
    • Higgs, H.N.1    Pollard, T.D.2
  • 36
    • 0033601076 scopus 로고    scopus 로고
    • Shroom, a PDZ domain-containing actin-binding protein, is required for neural tube morphogenesis in mice
    • Hildebrand J.D., Soriano P. Shroom, a PDZ domain-containing actin-binding protein, is required for neural tube morphogenesis in mice. Cell. 99:1999;485-497
    • (1999) Cell , vol.99 , pp. 485-497
    • Hildebrand, J.D.1    Soriano, P.2
  • 37
    • 0034635434 scopus 로고    scopus 로고
    • Specific requirement for the p85-p110alpha phosphatidylinositol 3-kinase during epidermal growth factor-stimulated actin nucleation in breast cancer cells
    • Hill K., Welti S., Yu J., Murray J.T., Yip S.C., Condeelis J.S., et al. Specific requirement for the p85-p110alpha phosphatidylinositol 3-kinase during epidermal growth factor-stimulated actin nucleation in breast cancer cells. Journal of Biological Chemistry. 275:2000;3741-3744
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 3741-3744
    • Hill, K.1    Welti, S.2    Yu, J.3    Murray, J.T.4    Yip, S.C.5    Condeelis, J.S.6
  • 38
    • 0034944962 scopus 로고    scopus 로고
    • Molecular cloning and characterization of profilin-3: A novel cytoskeleton-associated gene expressed in rat kidney and testes
    • Hu E., Chen Z., Fredrickson T., Zhu Y. Molecular cloning and characterization of profilin-3: a novel cytoskeleton-associated gene expressed in rat kidney and testes. Experimental Nephrology. 9:2001;265-274
    • (2001) Experimental Nephrology , vol.9 , pp. 265-274
    • Hu, E.1    Chen, Z.2    Fredrickson, T.3    Zhu, Y.4
  • 39
    • 0039701142 scopus 로고    scopus 로고
    • Characterization of the actin binding properties of the vasodilator-stimulated phosphoprotein VASP
    • Huttelmaier S., Harbeck B., Steffens O., Messerschmidt T., Illenberger B.M. Characterization of the actin binding properties of the vasodilator-stimulated phosphoprotein VASP. FEBS Letters. 451:1999;68-74
    • (1999) FEBS Letters , vol.451 , pp. 68-74
    • Huttelmaier, S.1    Harbeck, B.2    Steffens, O.3    Messerschmidt, T.4    Illenberger, B.M.5
  • 40
    • 0032992123 scopus 로고    scopus 로고
    • Cooperation of two actin-binding proteins, cofilin and Aip1, in Saccharomyces cerevisiae
    • Iida K., Yahara I. Cooperation of two actin-binding proteins, cofilin and Aip1, in Saccharomyces cerevisiae. Genes Cells. 4:1999;21-32
    • (1999) Genes Cells , vol.4 , pp. 21-32
    • Iida, K.1    Yahara, I.2
  • 42
    • 0036643661 scopus 로고    scopus 로고
    • Reduced expression of the insulin-induced protein 1 and p41 Arp2/3 complex genes in human gastric cancers
    • Kaneda A., Kaminishi M., Nakanishi Y., Sugimura T., Ushijima J. Reduced expression of the insulin-induced protein 1 and p41 Arp2/3 complex genes in human gastric cancers. International Journal of Cancer. 100:2002;57-62
    • (2002) International Journal of Cancer , vol.100 , pp. 57-62
    • Kaneda, A.1    Kaminishi, M.2    Nakanishi, Y.3    Sugimura, T.4    Ushijima, J.5
  • 43
    • 0033601258 scopus 로고    scopus 로고
    • Profilin promotes barbed-end actin filament assembly without lowering the critical concentration
    • Kang F., Purich D.L., Southwick F.S. Profilin promotes barbed-end actin filament assembly without lowering the critical concentration. Journal of Biological Chemistry. 274:1999;36963-36972
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 36963-36972
    • Kang, F.1    Purich, D.L.2    Southwick, F.S.3
  • 47
    • 0032813571 scopus 로고    scopus 로고
    • Cell adhesion molecules in the pathogenesis of and host defence against microbial infection
    • Kerr J.R. Cell adhesion molecules in the pathogenesis of and host defence against microbial infection. Molecular Pathology. 52:1999;220-230
    • (1999) Molecular Pathology , vol.52 , pp. 220-230
    • Kerr, J.R.1
  • 50
    • 0034599541 scopus 로고    scopus 로고
    • Fyn-binding protein (Fyb)/SLP-76-associated protein (SLAP), Ena/vasodilator-stimulated phosphoprotein (VASP) proteins and the Arp2/3 complex link T cell receptor (TCR) signaling to the actin cytoskeleton
    • Krause M., Sechi A.S., Konradt M., Monner D., Gertler F.B., Wehland J. Fyn-binding protein (Fyb)/SLP-76-associated protein (SLAP), Ena/vasodilator- stimulated phosphoprotein (VASP) proteins and the Arp2/3 complex link T cell receptor (TCR) signaling to the actin cytoskeleton. Journal of Cell Biology. 149:2000;181-194
    • (2000) Journal of Cell Biology , vol.149 , pp. 181-194
    • Krause, M.1    Sechi, A.S.2    Konradt, M.3    Monner, D.4    Gertler, F.B.5    Wehland, J.6
  • 51
    • 0023878565 scopus 로고
    • Human profilin. Molecular cloning, sequence comparison, and chromosomal analysis
    • Kwiatkowski D.J., Bruns G.A. Human profilin. Molecular cloning, sequence comparison, and chromosomal analysis. Journal of Biological Chemistry. 263:1988;5910-5915
    • (1988) Journal of Biological Chemistry , vol.263 , pp. 5910-5915
    • Kwiatkowski, D.J.1    Bruns, G.A.2
  • 52
    • 0029011187 scopus 로고
    • Purification and characterization of bovine profilin II. Actin, poly(L-proline) and inositolphospholipid binding
    • Lambrechts A., Van Damme J., Goethals M., Vandekerckhove J., Ampe C. Purification and characterization of bovine profilin II. Actin, poly(L-proline) and inositolphospholipid binding. European Journal of Biochemistry. 230:1995;281-286
    • (1995) European Journal of Biochemistry , vol.230 , pp. 281-286
    • Lambrechts, A.1    Van Damme, J.2    Goethals, M.3    Vandekerckhove, J.4    Ampe, C.5
  • 54
    • 0034680938 scopus 로고    scopus 로고
    • CAMP-dependent protein kinase phosphorylation of EVL, a Mena/VASP Relative, Regulates its interaction with Actin and SH3 domains
    • Lambrechts A., Kwiatkowski A.V., Lanier L.M., Bear J.E., Vandekerckhove J., Ampe C., et al. cAMP-dependent protein kinase phosphorylation of EVL, a Mena/VASP Relative, Regulates its interaction with Actin and SH3 domains. Journal of Biological Chemistry. 275:2000;36143-36151
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 36143-36151
    • Lambrechts, A.1    Kwiatkowski, A.V.2    Lanier, L.M.3    Bear, J.E.4    Vandekerckhove, J.5    Ampe, C.6
  • 55
    • 0033781583 scopus 로고    scopus 로고
    • Profilin II is alternatively spliced, resulting in profilin isoforms that are differentially expressed and have distinct biochemical properties
    • Lambrechts A., Braun A., Jonckheere V., Aszodi A., Lanier L.M., Robbens J., et al. Profilin II is alternatively spliced, resulting in profilin isoforms that are differentially expressed and have distinct biochemical properties. Molecular and Cellular Biology. 20:2000;8209-8219
    • (2000) Molecular and Cellular Biology , vol.20 , pp. 8209-8219
    • Lambrechts, A.1    Braun, A.2    Jonckheere, V.3    Aszodi, A.4    Lanier, L.M.5    Robbens, J.6
  • 57
    • 0021919105 scopus 로고
    • Specific interaction between phosphatidylinositol 4,5-bisphosphate and profilactin
    • Lassing I., Lindberg U. Specific interaction between phosphatidylinositol 4, 5-bisphosphate and profilactin. Nature. 314:1985;472-474
    • (1985) Nature , vol.314 , pp. 472-474
    • Lassing, I.1    Lindberg, U.2
  • 58
    • 0030045346 scopus 로고    scopus 로고
    • Cell migration: A physically integrated molecular process
    • Lauffenburger, D. A., & Horwitz, A. F. (1996). Cell migration: a physically integrated molecular process, Cell, 359-369.
    • (1996) Cell , pp. 359-369
    • Lauffenburger, D.A.1    Horwitz, A.F.2
  • 60
    • 0023376140 scopus 로고
    • Expression of transfected mutant beta-actin genes: Transitions toward the stable tumorigenic state
    • Leavitt J., Ng S.Y., Varma M., Latter G., Burbeck S., Gunning P., et al. Expression of transfected mutant beta-actin genes: transitions toward the stable tumorigenic state. Molecular and Cellular Biology. 7:1987;2467-2476
    • (1987) Molecular and Cellular Biology , vol.7 , pp. 2467-2476
    • Leavitt, J.1    Ng, S.Y.2    Varma, M.3    Latter, G.4    Burbeck, S.5    Gunning, P.6
  • 61
    • 0033564171 scopus 로고    scopus 로고
    • Downregulated gelsolin expression in hyperplastic and neoplastic lesions of the prostate
    • Lee H.K., Driscoll D., Asch H., Asch B., Zhang P.J. Downregulated gelsolin expression in hyperplastic and neoplastic lesions of the prostate. Prostate. 40:1999;14-19
    • (1999) Prostate , vol.40 , pp. 14-19
    • Lee, H.K.1    Driscoll, D.2    Asch, H.3    Asch, B.4    Zhang, P.J.5
  • 62
    • 0035845856 scopus 로고    scopus 로고
    • Overexpression of the thymosin beta-10 gene in human ovarian cancer cells disrupts F-actin stress fiber and leads to apoptosis
    • Lee S.H., Zhang W., Choi J.J., Cho Y.S., Oh S.H., Kim J.W., et al. Overexpression of the thymosin beta-10 gene in human ovarian cancer cells disrupts F-actin stress fiber and leads to apoptosis. Oncogene. 20:2001;6700-6706
    • (2001) Oncogene , vol.20 , pp. 6700-6706
    • Lee, S.H.1    Zhang, W.2    Choi, J.J.3    Cho, Y.S.4    Oh, S.H.5    Kim, J.W.6
  • 63
    • 0036020201 scopus 로고    scopus 로고
    • MIM, a potential metastasis suppressor gene in bladder cancer
    • Lee Y.G., Macoska J.A., Korenchuk S., Pienta K.J. MIM, a potential metastasis suppressor gene in bladder cancer. Neoplasia. 4:2002;291-294
    • (2002) Neoplasia , vol.4 , pp. 291-294
    • Lee, Y.G.1    MacOska, J.A.2    Korenchuk, S.3    Pienta, K.J.4
  • 64
    • 0043202969 scopus 로고    scopus 로고
    • The mouse Formin mDia1 is a potent actin nucleation factor regulated by autoinhibition
    • Li F., Higgs H.N. The mouse Formin mDia1 is a potent actin nucleation factor regulated by autoinhibition. Current Biology. 13:2003;1335-1340
    • (2003) Current Biology , vol.13 , pp. 1335-1340
    • Li, F.1    Higgs, H.N.2
  • 65
    • 0030936323 scopus 로고    scopus 로고
    • PTEN, a putative protein tyrosine phosphatase gene mutated in human brain, breast, and prostate cancer
    • Li J., Yen C., Liaw D., Podsypanina K., Bose S., Wang S.I., et al. PTEN, a putative protein tyrosine phosphatase gene mutated in human brain, breast, and prostate cancer. Science. 275:1997;1943-1947
    • (1997) Science , vol.275 , pp. 1943-1947
    • Li, J.1    Yen, C.2    Liaw, D.3    Podsypanina, K.4    Bose, S.5    Wang, S.I.6
  • 66
    • 0343183328 scopus 로고    scopus 로고
    • Genetic deletion of the Pten tumor suppressor gene promotes cell motility by activation of Rac1 and Cdc42 GTPases
    • Liliental J., Moon S.Y., Lesche R., Mamillapalli R., Li D., Zheng Y., et al. Genetic deletion of the Pten tumor suppressor gene promotes cell motility by activation of Rac1 and Cdc42 GTPases. Current Biology. 10:2000;401-404
    • (2000) Current Biology , vol.10 , pp. 401-404
    • Liliental, J.1    Moon, S.Y.2    Lesche, R.3    Mamillapalli, R.4    Li, D.5    Zheng, Y.6
  • 67
    • 0036441201 scopus 로고    scopus 로고
    • Actin cytoskeleton regulation in neuronal morphogenesis and structural plasticity
    • Luo L. Actin cytoskeleton regulation in neuronal morphogenesis and structural plasticity. Annual Review of Cell and Developmental Biology. 18:2002;601-635
    • (2002) Annual Review of Cell and Developmental Biology , vol.18 , pp. 601-635
    • Luo, L.1
  • 68
    • 0028136434 scopus 로고
    • Purification of a cortical complex containing two unconventional actins from Acanthamoeba by affinity chromatography on profilin-agarose
    • Machesky L.M., Atkinson S.J., Ampe C., Vandekerckhove J., Pollard T.D. Purification of a cortical complex containing two unconventional actins from Acanthamoeba by affinity chromatography on profilin-agarose. Journal of Cell Biology. 127:1994;107-115
    • (1994) Journal of Cell Biology , vol.127 , pp. 107-115
    • MacHesky, L.M.1    Atkinson, S.J.2    Ampe, C.3    Vandekerckhove, J.4    Pollard, T.D.5
  • 69
    • 0034279330 scopus 로고    scopus 로고
    • Changes in tumorigenesis- and angiogenesis-related gene transcript abundance profiles in ovarian cancer detected by tailored high density cDNA arrays
    • Martoglio A.M., Tom B.D., Starkey M., Corps A.N., Charnock-Jones D.S., Smith S.K. Changes in tumorigenesis- and angiogenesis-related gene transcript abundance profiles in ovarian cancer detected by tailored high density cDNA arrays. Molecular Medicine. 6:2000;750-765
    • (2000) Molecular Medicine , vol.6 , pp. 750-765
    • Martoglio, A.M.1    Tom, B.D.2    Starkey, M.3    Corps, A.N.4    Charnock-Jones, D.S.5    Smith, S.K.6
  • 71
    • 0027536793 scopus 로고
    • An actin-binding function contributes to transformation by the Bcr-Abl oncoprotein of Philadelphia chromosome-positive human leukemias
    • McWhirter J.R., Wang J.Y. An actin-binding function contributes to transformation by the Bcr-Abl oncoprotein of Philadelphia chromosome-positive human leukemias. The EMBO Journal. 12:1993;1533-1546
    • (1993) The EMBO Journal , vol.12 , pp. 1533-1546
    • McWhirter, J.R.1    Wang, J.Y.2
  • 72
    • 0032531960 scopus 로고    scopus 로고
    • Gelsolin and functionally similar actin-binding proteins are regulated by lysophosphatidic acid
    • Meerschaert K., De Corte V., De Ville Y., Vandekerckhove J., Gettemans J. Gelsolin and functionally similar actin-binding proteins are regulated by lysophosphatidic acid. The EMBO Journal. 17:1998;5923-5932
    • (1998) The EMBO Journal , vol.17 , pp. 5923-5932
    • Meerschaert, K.1    De Corte, V.2    De Ville, Y.3    Vandekerckhove, J.4    Gettemans, J.5
  • 73
    • 18444372636 scopus 로고    scopus 로고
    • Abnormal spine morphology and enhanced LTP in LIMK-1 knockout mice
    • Meng Y., Zhang Y., Tregoubov V., Janus C., Cruz L., Jackson M., et al. Abnormal spine morphology and enhanced LTP in LIMK-1 knockout mice. Neuron. 35:2002;121-133
    • (2002) Neuron , vol.35 , pp. 121-133
    • Meng, Y.1    Zhang, Y.2    Tregoubov, V.3    Janus, C.4    Cruz, L.5    Jackson, M.6
  • 74
    • 0041327718 scopus 로고    scopus 로고
    • Leading the way: Directional sensing through phosphatidylinositol 3-kinase and other signaling pathways
    • Merlot S., Firtel R.A. Leading the way: directional sensing through phosphatidylinositol 3-kinase and other signaling pathways. Journal of Cell Science. 116:2003;3471-3478
    • (2003) Journal of Cell Science , vol.116 , pp. 3471-3478
    • Merlot, S.1    Firtel, R.A.2
  • 75
    • 0030049170 scopus 로고    scopus 로고
    • Actin-based cell motility and cell locomotion
    • Mitchison T.J., Cramer L.P. Actin-based cell motility and cell locomotion. Cell. 84:1996;371-379
    • (1996) Cell , vol.84 , pp. 371-379
    • Mitchison, T.J.1    Cramer, L.P.2
  • 76
  • 77
    • 0032784388 scopus 로고    scopus 로고
    • Distinct actions and cooperative roles of ROCK and mDia in Rho small G protein-induced reorganization of the actin cytoskeleton in Madin-Darby canine kidney cells
    • Nakano K., Takaishi K., Kodama A., Mammoto A., Shiozaki H., Monden M., et al. Distinct actions and cooperative roles of ROCK and mDia in Rho small G protein-induced reorganization of the actin cytoskeleton in Madin-Darby canine kidney cells. Molecular Biology of the Cell. 10:1999;2481-2491
    • (1999) Molecular Biology of the Cell , vol.10 , pp. 2481-2491
    • Nakano, K.1    Takaishi, K.2    Kodama, A.3    Mammoto, A.4    Shiozaki, H.5    Monden, M.6
  • 78
    • 0030864520 scopus 로고    scopus 로고
    • A novel proline-rich motif present in ActA of Listeria monocytogenes and cytoskeletal proteins is the ligand for the EVH1 domain, a protein module present in the Ena/VASP family
    • Niebuhr K., Ebel F., Frank R., Reinhard M., Domann E., Carl U.D., et al. A novel proline-rich motif present in ActA of Listeria monocytogenes and cytoskeletal proteins is the ligand for the EVH1 domain, a protein module present in the Ena/VASP family. The EMBO Journal. 16:1997;5433-5444
    • (1997) The EMBO Journal , vol.16 , pp. 5433-5444
    • Niebuhr, K.1    Ebel, F.2    Frank, R.3    Reinhard, M.4    Domann, E.5    Carl, U.D.6
  • 79
    • 0141629510 scopus 로고    scopus 로고
    • Wiskott-Aldrich Syndrome: A model for defective actin reorganization, cell trafficking and synapse formation
    • Notarangelo L.D., Ochs H.D. Wiskott-Aldrich Syndrome: a model for defective actin reorganization, cell trafficking and synapse formation. Current Opinion on Immunolgy. 15:2003;585-591
    • (2003) Current Opinion on Immunolgy , vol.15 , pp. 585-591
    • Notarangelo, L.D.1    Ochs, H.D.2
  • 82
    • 0037469079 scopus 로고    scopus 로고
    • Ras superfamily monomeric G proteins in carcinoma cell motility
    • Oxford G., Theodorescu D. Ras superfamily monomeric G proteins in carcinoma cell motility. Cancer Letters. 189:2003;117-128
    • (2003) Cancer Letters , vol.189 , pp. 117-128
    • Oxford, G.1    Theodorescu, D.2
  • 84
    • 0027772556 scopus 로고
    • How profilin promotes actin filament assembly in the presence of thymosin beta 4
    • Pantaloni D., Carlier M.F. How profilin promotes actin filament assembly in the presence of thymosin beta 4. Cell. 75:1993;1007-1014
    • (1993) Cell , vol.75 , pp. 1007-1014
    • Pantaloni, D.1    Carlier, M.F.2
  • 86
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard T.D., Borisy G.G. Cellular motility driven by assembly and disassembly of actin filaments. Cell. 112:2003;453-465
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 87
    • 0034721696 scopus 로고    scopus 로고
    • Integration of multiple signals through cooperative regulation of the N-WASP-Arp2/3 complex
    • Prehoda K.E., Scott J.A., Mullins R.D., Lim W.A. Integration of multiple signals through cooperative regulation of the N-WASP-Arp2/3 complex. Science. 290:2000;801-806
    • (2000) Science , vol.290 , pp. 801-806
    • Prehoda, K.E.1    Scott, J.A.2    Mullins, R.D.3    Lim, W.A.4
  • 88
    • 0036368684 scopus 로고    scopus 로고
    • Targeting actin remodeling profiles for the detection and management of urothelial cancers - A perspective for bladder cancer research
    • Rao J. Targeting actin remodeling profiles for the detection and management of urothelial cancers - a perspective for bladder cancer research. Front Bioscience. 1:2002;1-8
    • (2002) Front Bioscience , vol.1 , pp. 1-8
    • Rao, J.1
  • 89
    • 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., Halbrugge M., Scheer U., Wiegand C., Jockusch B.M., Walter U. The 46/50 kDa phosphoprotein VASP purified from human platelets is a novel protein associated with actin filaments and focal contacts. The EMBO Journal. 11:1992;2063-2070
    • (1992) The EMBO Journal , vol.11 , pp. 2063-2070
    • Reinhard, M.1    Halbrugge, M.2    Scheer, U.3    Wiegand, C.4    Jockusch, B.M.5    Walter, U.6
  • 90
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley A.J., Hall A. The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell. 70:1992;389-399
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 91
    • 0026654125 scopus 로고
    • The small GTP-binding protein rac regulates growth factor-induced membrane ruffling
    • Ridley A.J., Paterson H.F., Johnston C.L., Diekmann D., Hall A. The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell. 70:1992;401-410
    • (1992) Cell , vol.70 , pp. 401-410
    • Ridley, A.J.1    Paterson, H.F.2    Johnston, C.L.3    Diekmann, D.4    Hall, A.5
  • 92
    • 0031857349 scopus 로고    scopus 로고
    • Murine adseverin (D5), a novel member of the gelsolin family, and murine adseverin are induced by interleukin-9 in T-helper lymphocytes
    • Robbens J., Louahed J., De Pestel K., Van Colen I., Ampe C., Vandekerckhove J., et al. Murine adseverin (D5), a novel member of the gelsolin family, and murine adseverin are induced by interleukin-9 in T-helper lymphocytes. Molecular and Cellular Biology. 18:1998;4589-4596
    • (1998) Molecular and Cellular Biology , vol.18 , pp. 4589-4596
    • Robbens, J.1    Louahed, J.2    De Pestel, K.3    Van Colen, I.4    Ampe, C.5    Vandekerckhove, J.6
  • 94
    • 0033870355 scopus 로고    scopus 로고
    • EMS1 gene amplification correlates with poor prognosis in squamous cell carcinomas of the head and neck
    • Rodrigo J.P., Garcia L.A., Ramos S., Lazo P.S., Suarez C. EMS1 gene amplification correlates with poor prognosis in squamous cell carcinomas of the head and neck. Clinical Cancer Research. 6:2000;3177-3182
    • (2000) Clinical Cancer Research , vol.6 , pp. 3177-3182
    • Rodrigo, J.P.1    Garcia, L.A.2    Ramos, S.3    Lazo, P.S.4    Suarez, C.5
  • 95
    • 0034683746 scopus 로고    scopus 로고
    • Mechanism of N-WASP activation by CDC42 and phosphatidylinositol 4, 5-bisphosphate
    • Rohatgi R., Ho H.Y., Kirschner M.W. Mechanism of N-WASP activation by CDC42 and phosphatidylinositol 4, 5-bisphosphate. Journal of Cell Biology. 150:2000;1299-1310
    • (2000) Journal of Cell Biology , vol.150 , pp. 1299-1310
    • Rohatgi, R.1    Ho, H.Y.2    Kirschner, M.W.3
  • 97
    • 0037463318 scopus 로고    scopus 로고
    • Gelsolin suppresses tumorigenicity through inhibiting PKC activation in a human lung cancer cell line, PC10
    • Sagawa N., Fujita H., Banno Y., Nozawa Y., Katoh H., Kuzumaki N. Gelsolin suppresses tumorigenicity through inhibiting PKC activation in a human lung cancer cell line, PC10. British Journal of Cancer. 88:2003;606-612
    • (2003) British Journal of Cancer , vol.88 , pp. 606-612
    • Sagawa, N.1    Fujita, H.2    Banno, Y.3    Nozawa, Y.4    Katoh, H.5    Kuzumaki, N.6
  • 98
    • 0042354574 scopus 로고    scopus 로고
    • Differing modes of tumour cell invasion have distinct requirements for Rho/ROCK signalling and extracellular proteolysis
    • Sahai E., Marshall C.J. Differing modes of tumour cell invasion have distinct requirements for Rho/ROCK signalling and extracellular proteolysis. Nature Cell Biology. 5:2003;711-719
    • (2003) Nature Cell Biology , vol.5 , pp. 711-719
    • Sahai, E.1    Marshall, C.J.2
  • 102
    • 0033515062 scopus 로고    scopus 로고
    • Impact of profilin on actin-bound nucleotide exchange and actin polymerization dynamics
    • Selden L.A., Kinosian H.J., Estes J.E., Gershman L.C. Impact of profilin on actin-bound nucleotide exchange and actin polymerization dynamics. Biochemistry. 38:1999;2769-2778
    • (1999) Biochemistry , vol.38 , pp. 2769-2778
    • Selden, L.A.1    Kinosian, H.J.2    Estes, J.E.3    Gershman, L.C.4
  • 103
    • 0032893518 scopus 로고    scopus 로고
    • Cell motility as a prognostic factor in Stage I nonsmall cell lung carcinoma: The role of gelsolin expression
    • Shieh D.B., Godleski J., Herndon J.E. Jr., Azuma T., Mercer H., Sugarbaker D.L., et al. Cell motility as a prognostic factor in Stage I nonsmall cell lung carcinoma: the role of gelsolin expression. Cancer. 85:1999;47-57
    • (1999) Cancer , vol.85 , pp. 47-57
    • Shieh, D.B.1    Godleski, J.2    Herndon Jr., J.E.3    Azuma, T.4    Mercer, H.5    Sugarbaker, D.L.6
  • 104
    • 0028450653 scopus 로고
    • Lamellipodia architecture: Actin filament turnover and the lateral flow of actin filaments during motility
    • Small J.V. Lamellipodia architecture: actin filament turnover and the lateral flow of actin filaments during motility. Seminars in Cell Biology. 5:1994;157-163
    • (1994) Seminars in Cell Biology , vol.5 , pp. 157-163
    • Small, J.V.1
  • 109
    • 0035097592 scopus 로고    scopus 로고
    • The cell biology of neuronal navigation
    • Song H., Poo M. The cell biology of neuronal navigation. Nature Cell Biology. 3:2001;E81-E88
    • (2001) Nature Cell Biology , vol.3 , pp. 81-E88
    • Song, H.1    Poo, M.2
  • 110
    • 0037194581 scopus 로고    scopus 로고
    • WAVE3, an actin-polymerization gene, is truncated and inactivated as a result of a constitutional t(1;13)(q21;q12) chromosome translocation in a patient with ganglioneuroblastoma
    • Sossey-Alaoui K., Su G., Malaj E., Roe B., Cowell J.K. WAVE3, an actin-polymerization gene, is truncated and inactivated as a result of a constitutional t(1;13)(q21;q12) chromosome translocation in a patient with ganglioneuroblastoma. Oncogene. 21:2002;5967-5974
    • (2002) Oncogene , vol.21 , pp. 5967-5974
    • Sossey-Alaoui, K.1    Su, G.2    Malaj, E.3    Roe, B.4    Cowell, J.K.5
  • 111
    • 17144436629 scopus 로고    scopus 로고
    • Identification of a candidate tumour suppressor gene, MMAC1, at chromosome 10q23.3 that is mutated in multiple advanced cancers
    • Steck P.A., Pershouse M.A., Jasser S.A., Yung W.K., Lin H., Ligon A.H., et al. Identification of a candidate tumour suppressor gene, MMAC1, at chromosome 10q23.3 that is mutated in multiple advanced cancers. Nature Genetics. 15:1997;356-362
    • (1997) Nature Genetics , vol.15 , pp. 356-362
    • Steck, P.A.1    Pershouse, M.A.2    Jasser, S.A.3    Yung, W.K.4    Lin, H.5    Ligon, A.H.6
  • 112
    • 0037107132 scopus 로고    scopus 로고
    • Three functionally distinct adhesions in filopodia: Shaft adhesions control lamellar extension
    • Steketee M.B., Tosney K.W. Three functionally distinct adhesions in filopodia: shaft adhesions control lamellar extension. Journal of Neurosciences. 22:2002;8071-8083
    • (2002) Journal of Neurosciences , vol.22 , pp. 8071-8083
    • Steketee, M.B.1    Tosney, K.W.2
  • 113
    • 0036850180 scopus 로고    scopus 로고
    • Sustained activation of N-WASP through phosphorylation is essential for neurite extension
    • Suetsugu S., Hattori M., Miki H., Tezuka T., Yamamoto T., Mikoshiba K., et al. Sustained activation of N-WASP through phosphorylation is essential for neurite extension. Development of Cell. 3:2002;645-658
    • (2002) Development of Cell , vol.3 , pp. 645-658
    • Suetsugu, S.1    Hattori, M.2    Miki, H.3    Tezuka, T.4    Yamamoto, T.5    Mikoshiba, K.6
  • 114
    • 0032423797 scopus 로고    scopus 로고
    • N-WASP is an important protein for the actin-based motility of Shigella flexneri in the infected epithelial cells
    • Suzuki T., Sasakawa C. N-WASP is an important protein for the actin-based motility of Shigella flexneri in the infected epithelial cells. Japanese Journal of Medicinal Sciences and Biology. 51:1998;S63-68
    • (1998) Japanese Journal of Medicinal Sciences and Biology , vol.51 , pp. 63-68
    • Suzuki, T.1    Sasakawa, C.2
  • 115
    • 0033620689 scopus 로고    scopus 로고
    • Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia
    • Svitkina T.M., Borisy G.G. Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia. Journal of Cell Biology. 145:1999;1009-1026
    • (1999) Journal of Cell Biology , vol.145 , pp. 1009-1026
    • Svitkina, T.M.1    Borisy, G.G.2
  • 118
    • 0034983715 scopus 로고    scopus 로고
    • WASP and WAVE family proteins: Key molecules for rapid rearrangement of cortical actin filaments and cell movement
    • Takenawa T., Miki H. WASP and WAVE family proteins: key molecules for rapid rearrangement of cortical actin filaments and cell movement. Journal of Cell Sciences. 114:2001;1801-1809
    • (2001) Journal of Cell Sciences , vol.114 , pp. 1801-1809
    • Takenawa, T.1    Miki, H.2
  • 120
    • 0034892806 scopus 로고    scopus 로고
    • Gelsolin as a negative prognostic factor and effector of motility in erbB-2-positive epidermal growth factor receptor-positive breast cancers
    • Thor A.D., Edgerton S.M., Liu S., Moore D.H. 2nd, Kwiatkowski D.J. Gelsolin as a negative prognostic factor and effector of motility in erbB-2-positive epidermal growth factor receptor-positive breast cancers. Clinical Cancer Research. 7:2001;2415-2424
    • (2001) Clinical Cancer Research , vol.7 , pp. 2415-2424
    • Thor, A.D.1    Edgerton, S.M.2    Liu, S.3    Moore II, D.H.4    Kwiatkowski, D.J.5
  • 122
    • 0035171699 scopus 로고    scopus 로고
    • Cofilin phosphorylation by protein kinase testicular protein kinase 1 and its role in integrin-mediated actin reorganization and focal adhesion formation
    • Toshima J., Toshima J.Y., Amano T., Yang N., Narumiya S., Mizuno K. Cofilin phosphorylation by protein kinase testicular protein kinase 1 and its role in integrin-mediated actin reorganization and focal adhesion formation. Molecular Biology of the Cell. 12:2001;1131-1145
    • (2001) Molecular Biology of the Cell , vol.12 , pp. 1131-1145
    • Toshima, J.1    Toshima, J.Y.2    Amano, T.3    Yang, N.4    Narumiya, S.5    Mizuno, K.6
  • 123
    • 0033914895 scopus 로고    scopus 로고
    • Ultrastructure of Rickettsia rickettsii actin tails and localization of cytoskeletal proteins
    • Van Kirk L.S., Hayes S.F., Heinzen R.A. Ultrastructure of Rickettsia rickettsii actin tails and localization of cytoskeletal proteins. Infection and Immunity. 68:2000;4706-4713
    • (2000) Infection and Immunity , vol.68 , pp. 4706-4713
    • Van Kirk, L.S.1    Hayes, S.F.2    Heinzen, R.A.3
  • 126
    • 0034633937 scopus 로고    scopus 로고
    • The competitive interaction of actin and PIP2 with actophorin is based on overlapping target sites: Design of a gain-of-function mutant
    • Van Troys M., Dewitte D., Verschelde J.L., Goethals M., Vandekerckhove J., Ampe C. The competitive interaction of actin and PIP2 with actophorin is based on overlapping target sites: design of a gain-of-function mutant. Biochemistry. 39:2000;12181-12189
    • (2000) Biochemistry , vol.39 , pp. 12181-12189
    • Van Troys, M.1    Dewitte, D.2    Verschelde, J.L.3    Goethals, M.4    Vandekerckhove, J.5    Ampe, C.6
  • 127
    • 0019125204 scopus 로고
    • Coexpression of a mutant beta-actin and the two normal beta- and gamma-cytoplasmic actins in a stably transformed human cell line
    • Vandekerckhove J., Leavitt J., Kakunaga T., Weber K. Coexpression of a mutant beta-actin and the two normal beta- and gamma-cytoplasmic actins in a stably transformed human cell line. Cell. 22:1980;893-899
    • (1980) Cell , vol.22 , pp. 893-899
    • Vandekerckhove, J.1    Leavitt, J.2    Kakunaga, T.3    Weber, K.4
  • 128
    • 0034695656 scopus 로고    scopus 로고
    • Directed actin polymerization is the driving force for epithelial cell-cell adhesion
    • Vasioukhin V., Bauer C., Yin M., Fuchs E. Directed actin polymerization is the driving force for epithelial cell-cell adhesion. Cell. 100:2000;209-219
    • (2000) Cell , vol.100 , pp. 209-219
    • Vasioukhin, V.1    Bauer, C.2    Yin, M.3    Fuchs, E.4
  • 130
    • 0037048683 scopus 로고    scopus 로고
    • The vasodilator-stimulated phosphoprotein promotes actin polymerisation through direct binding to monomeric actin
    • Walders-Harbeck B., Khaitlina S.Y., Hinssen H., Jockusch B.M., Illenberger S. The vasodilator-stimulated phosphoprotein promotes actin polymerisation through direct binding to monomeric actin. FEBS Letters. 529:2002;275-280
    • (2002) FEBS Letters , vol.529 , pp. 275-280
    • Walders-Harbeck, B.1    Khaitlina, S.Y.2    Hinssen, H.3    Jockusch, B.M.4    Illenberger, S.5
  • 133
    • 0017176529 scopus 로고
    • Head to tail polymerization of actin
    • Wegner A. Head to tail polymerization of actin. Journal of Molecular Biology. 108:1976;139-150
    • (1976) Journal of Molecular Biology , vol.108 , pp. 139-150
    • Wegner, A.1
  • 137
    • 0036968347 scopus 로고    scopus 로고
    • Activation of the PI3K/Akt pathway and chemotherapeutic resistance
    • West K.A., Castillo S.S., Dennis P.A. Activation of the PI3K/Akt pathway and chemotherapeutic resistance. Drug Resistence Update. 5:2002;234-248
    • (2002) Drug Resistence Update , vol.5 , pp. 234-248
    • West, K.A.1    Castillo, S.S.2    Dennis, P.A.3
  • 139
    • 0028914814 scopus 로고
    • Hemostatic, inflammatory, and fibroblast responses are blunted in mice lacking gelsolin
    • Witke W., Sharpe A.H., Hartwig J.H., Azuma T., Stossel T.P., Kwiatkowski D.J. Hemostatic, inflammatory, and fibroblast responses are blunted in mice lacking gelsolin. Cell. 81:1995;41-51
    • (1995) Cell , vol.81 , pp. 41-51
    • Witke, W.1    Sharpe, A.H.2    Hartwig, J.H.3    Azuma, T.4    Stossel, T.P.5    Kwiatkowski, D.J.6
  • 140
    • 0037455576 scopus 로고    scopus 로고
    • Compensation mechanism in tumor cell migration: Mesenchymal-amoeboid transition after blocking of pericellular proteolysis
    • Wolf K., Mazo I., Leung H., Engelke K., von Andrian U.H., Deryugina E.I., et al. Compensation mechanism in tumor cell migration: mesenchymal-amoeboid transition after blocking of pericellular proteolysis. Journal of Cell Biology. 160:2003;267-277
    • (2003) Journal of Cell Biology , vol.160 , pp. 267-277
    • Wolf, K.1    Mazo, I.2    Leung, H.3    Engelke, K.4    Von Andrian, U.H.5    Deryugina, E.I.6
  • 141
    • 0016826292 scopus 로고
    • Evidence for biased bidirectional polymerization of actin filaments using heavy meromyosin prepared by an improved method
    • Woodrum D.T., Rich S.A., Pollard T.D. Evidence for biased bidirectional polymerization of actin filaments using heavy meromyosin prepared by an improved method. Journal of Cell Biology. 67:1975;231-237
    • (1975) Journal of Cell Biology , vol.67 , pp. 231-237
    • Woodrum, D.T.1    Rich, S.A.2    Pollard, T.D.3
  • 142
    • 0343185927 scopus 로고    scopus 로고
    • Activation-dependent changes in soluble fibronectin binding and expression of beta1 integrin activation epitopes in T cells: Relationship to T cell adhesion and migration
    • Woods M.L., Cabanas C., Shimizu Y. Activation-dependent changes in soluble fibronectin binding and expression of beta1 integrin activation epitopes in T cells: relationship to T cell adhesion and migration. European Journal of Immunology. 30:2000;38-49
    • (2000) European Journal of Immunology , vol.30 , pp. 38-49
    • Woods, M.L.1    Cabanas, C.2    Shimizu, Y.3
  • 143
    • 0027419589 scopus 로고
    • Cortactin, an 80/85-kilodalton pp60src substrate, is a filamentous actin-binding protein enriched in the cell cortex
    • Wu H., Parsons J.T. Cortactin, an 80/85-kilodalton pp60src substrate, is a filamentous actin-binding protein enriched in the cell cortex. Journal of Cell Biology. 120:1993;1417-1426
    • (1993) Journal of Cell Biology , vol.120 , pp. 1417-1426
    • Wu, H.1    Parsons, J.T.2
  • 144
    • 0031929760 scopus 로고    scopus 로고
    • Vinculin knockout results in heart and brain defects during embryonic development
    • Xu W., Baribault H., Adamson E.D. Vinculin knockout results in heart and brain defects during embryonic development. Development. 125:1998;327-337
    • (1998) Development , vol.125 , pp. 327-337
    • Xu, W.1    Baribault, H.2    Adamson, E.D.3
  • 146
    • 0042815094 scopus 로고    scopus 로고
    • WAVE2 deficiency reveals distinct roles in embryogenesis and Rac-mediated actin-based motility
    • Yan C., Martinez-Quiles N., Eden S., Shibata T., Takeshima F., Shinkura R., et al. WAVE2 deficiency reveals distinct roles in embryogenesis and Rac-mediated actin-based motility. The EMBO Journal. 22:2003;3602-3612
    • (2003) The EMBO Journal , vol.22 , pp. 3602-3612
    • Yan, C.1    Martinez-Quiles, N.2    Eden, S.3    Shibata, T.4    Takeshima, F.5    Shinkura, R.6
  • 147
    • 0034769874 scopus 로고    scopus 로고
    • Genome-wide screening of genes showing altered expression in liver metastases of human colorectal cancers by cDNA microarray
    • Yanagawa R., Furukawa Y., Tsunoda T., Kitahara O., Kameyama M., Murata K., et al. Genome-wide screening of genes showing altered expression in liver metastases of human colorectal cancers by cDNA microarray. Neoplasia. 3:2001;395-401
    • (2001) Neoplasia , vol.3 , pp. 395-401
    • Yanagawa, R.1    Furukawa, Y.2    Tsunoda, T.3    Kitahara, O.4    Kameyama, M.5    Murata, K.6
  • 148
    • 0032565769 scopus 로고    scopus 로고
    • Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization
    • Yang N., Higuchi O., Ohashi K., Nagata K., Wada A., Kangawa K., et al. Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization. Nature. 393:1998;809-812
    • (1998) Nature , vol.393 , pp. 809-812
    • Yang, N.1    Higuchi, O.2    Ohashi, K.3    Nagata, K.4    Wada, A.5    Kangawa, K.6
  • 149
    • 0038311944 scopus 로고    scopus 로고
    • Phosphoinositide regulation of the actin cytoskeleton
    • Yin H.L., Janmey P.A. Phosphoinositide regulation of the actin cytoskeleton. Annual Revison of Physiolgy. 65:2003;761-789
    • (2003) Annual Revison of Physiolgy , vol.65 , pp. 761-789
    • Yin, H.L.1    Janmey, P.A.2
  • 150
    • 0024837180 scopus 로고
    • Calcium and polyphosphoinositide regulation of actin network structure by gelsolin
    • Yin H.L. Calcium and polyphosphoinositide regulation of actin network structure by gelsolin. Advances in Experimental Medicine and Biology. 255:1989;315-323
    • (1989) Advances in Experimental Medicine and Biology , vol.255 , pp. 315-323
    • Yin, H.L.1
  • 152
    • 0027293382 scopus 로고
    • Recent quantitative studies of actin filament turnover during cell locomotion
    • Zigmond S.H. Recent quantitative studies of actin filament turnover during cell locomotion. Cell Motility and the Cytoskeleton. 25:1993;309-316
    • (1993) Cell Motility and the Cytoskeleton , vol.25 , pp. 309-316
    • Zigmond, S.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.