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Volumn 15, Issue 1, 2015, Pages 41-48

Fascin-1 as a biomarker and prospective therapeutic target in colorectal cancer

Author keywords

Actin; adenocarcinoma; adenoma; cell migration; filopodia; focal adhesion; invasion; KRAS; metastasis

Indexed keywords

BIOLOGICAL MARKER; FASCIN; ACTIN BINDING PROTEIN; CARRIER PROTEIN; FSCN1 PROTEIN, HUMAN; TUMOR MARKER;

EID: 84919933906     PISSN: 14737159     EISSN: 17448352     Source Type: Journal    
DOI: 10.1586/14737159.2015.976557     Document Type: Article
Times cited : (26)

References (69)
  • 3
    • 84919925408 scopus 로고    scopus 로고
    • Colon cancer survival rates UK. Available from: www.wcrf.org/int/cancer-facts-figures/data-specific-cancers/colorectal-cancerstatistics
    • Colon Cancer Survival Rates UK
  • 6
    • 0033784843 scopus 로고    scopus 로고
    • The transcription factor Snail controls epithelial-mesenchymal transitions by repressing E-cadherin expression
    • Cano A, Mirna A, Pérez-Moreno MA, et al. The transcription factor Snail controls epithelial-mesenchymal transitions by repressing E-cadherin expression. Nature Cell Biol 2000;2:76-83
    • (2000) Nature Cell Biol , vol.2 , pp. 76-83
    • Cano, A.1    Mirna, A.2    Pérez-Moreno, M.A.3
  • 7
    • 84901789420 scopus 로고    scopus 로고
    • Epithelial-to-mesenchymal transition and the cancer stem cell phenotype: Insights from cancer biology with therapeutic implications for colorectal cancer
    • Findlay VJ, Wang C, Watson DK, Camp ER. Epithelial-to-mesenchymal transition and the cancer stem cell phenotype: insights from cancer biology with therapeutic implications for colorectal cancer. Cancer Gene Ther 2014;21:181-7
    • (2014) Cancer Gene Ther , vol.21 , pp. 181-187
    • Findlay, V.J.1    Wang, C.2    Watson, D.K.3    Camp, E.R.4
  • 8
    • 84870940346 scopus 로고    scopus 로고
    • Developmental pathways in colon cancer: Crosstalk between WNT, BMP, Hedgehog and Notch
    • Bertrand FE, Angus CW, Partis WJ, Sigounas G. Developmental pathways in colon cancer: crosstalk between WNT, BMP, Hedgehog and Notch. Cell Cycle 2012;11:4344-51
    • (2012) Cell Cycle , vol.11 , pp. 4344-4351
    • Bertrand, F.E.1    Angus, C.W.2    Partis, W.J.3    Sigounas, G.4
  • 9
    • 11144279340 scopus 로고    scopus 로고
    • Actinin-4 increases cell motility and promotes lymph node metastasis of colorectal cancer
    • Honda K, Yamada T, Hayashida Y, et al. Actinin-4 increases cell motility and promotes lymph node metastasis of colorectal cancer. Gastroenterology 2005;128:51-62
    • (2005) Gastroenterology , vol.128 , pp. 51-62
    • Honda, K.1    Yamada, T.2    Hayashida, Y.3
  • 10
    • 50949126005 scopus 로고    scopus 로고
    • In colon carcinogenesis, the cytoskeletal protein gelsolin is down-regulated during the transition from adenoma to carcinoma
    • Gay F, Estornes Y, Saurin JC, et al. In colon carcinogenesis, the cytoskeletal protein gelsolin is down-regulated during the transition from adenoma to carcinoma. Hum Pathol 2008;39:1420-30
    • (2008) Hum Pathol , vol.39 , pp. 1420-1430
    • Gay, F.1    Estornes, Y.2    Saurin, J.C.3
  • 11
    • 69249134997 scopus 로고    scopus 로고
    • Association of the actin-binding protein transgelin with lymph node metastasis in human colorectal cancer
    • Lin Y, Buckhaults PJ, Lee JR, et al. Association of the actin-binding protein transgelin with lymph node metastasis in human colorectal cancer. Neoplasia 2009;11:864-73
    • (2009) Neoplasia , vol.11 , pp. 864-873
    • Lin, Y.1    Buckhaults, P.J.2    Lee, J.R.3
  • 12
    • 80955177507 scopus 로고    scopus 로고
    • The roles of fascins in health and disease
    • Hashimoto Y, Kim DJ, Adams JC. The roles of fascins in health and disease. J Pathol 2011;224:289-00
    • (2011) J Pathol , vol.224 , pp. 289-300
    • Hashimoto, Y.1    Kim, D.J.2    Adams, J.C.3
  • 13
    • 0028799146 scopus 로고
    • Fascins, a family of actin bundling proteins
    • Edwards RA, Bryan J. Fascins, a family of actin bundling proteins. Cell Motil Cytoskeleton 1995;32:1-9
    • (1995) Cell Motil Cytoskeleton , vol.32 , pp. 1-9
    • Edwards, R.A.1    Bryan, J.2
  • 14
    • 0030785343 scopus 로고    scopus 로고
    • Characterisation of cell-matrix adhesion requirements for the formation of fascin microspikes
    • Adams JC. Characterisation of cell-matrix adhesion requirements for the formation of fascin microspikes. Mol Biol Cell 1997;8: 2345-63
    • (1997) Mol Biol Cell , vol.8 , pp. 2345-2363
    • Adams, J.C.1
  • 15
    • 84904055991 scopus 로고    scopus 로고
    • Fascin plays a role in stress fiber organization and focal adhesion disassembly
    • Elkhatib N, Neu MB, Zensen C, et al. Fascin plays a role in stress fiber organization and focal adhesion disassembly. Curr Biol 2014;24:1492-9
    • (2014) Curr Biol , vol.24 , pp. 1492-1499
    • Elkhatib, N.1    Neu, M.B.2    Zensen, C.3
  • 16
    • 0037415574 scopus 로고    scopus 로고
    • Mechanism of filopodia initiation by reorganization of a dendritic network
    • Svitkina TM, Bulanova EA, Chaga OY, et al. Mechanism of filopodia initiation by reorganization of a dendritic network. J Cell Biol 2003;160:409-21
    • (2003) J Cell Biol , vol.160 , pp. 409-421
    • Svitkina, T.M.1    Bulanova, E.A.2    Chaga, O.Y.3
  • 17
    • 54849437256 scopus 로고    scopus 로고
    • The filamentous actin crosslinking/bundling activity of mammalian formins
    • Esue O, Harris ES, Higgs HN, et al. The filamentous actin crosslinking/bundling activity of mammalian formins. J Mol Biol 2008;384:324-34
    • (2008) J Mol Biol , vol.384 , pp. 324-334
    • Esue, O.1    Harris, E.S.2    Higgs, H.N.3
  • 18
    • 77956537388 scopus 로고    scopus 로고
    • Self-assembly of filopodia-like structures on supported lipid bilayers
    • Lee K, Gallop JL, Rambani K, et al. Self-assembly of filopodia-like structures on supported lipid bilayers. Science 2010;329: 1341-5
    • (2010) Science , vol.329 , pp. 1341-1345
    • Lee, K.1    Gallop, J.L.2    Rambani, K.3
  • 19
    • 84880698305 scopus 로고    scopus 로고
    • The formin Daam1 and fascin directly collaborate to promote filopodia formation
    • Jaiswal R, Breitsprecher D, Collins A, et al. The formin Daam1 and fascin directly collaborate to promote filopodia formation. Curr Biol 2013;23:1373-9
    • (2013) Curr Biol , vol.23 , pp. 1373-1379
    • Jaiswal, R.1    Breitsprecher, D.2    Collins, A.3
  • 20
    • 84896519018 scopus 로고    scopus 로고
    • Ena/VASP Enabled is a highly processive actin polymerase tailored to self-assemble parallel-bundled F-actin networks with fascin
    • Winkelman JD, Bilancia CG, Peifer M, Kovar DR. Ena/VASP Enabled is a highly processive actin polymerase tailored to self-assemble parallel-bundled F-actin networks with fascin. Proc Natl Acad Sci USA 2014;111:4121-6
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 4121-4126
    • Winkelman, J.D.1    Bilancia, C.G.2    Peifer, M.3    Kovar, D.R.4
  • 21
    • 84873255855 scopus 로고    scopus 로고
    • Myosin VI has a one track mind versus myosin Va when moving on actin bundles or at an intersection
    • Ali MY, Previs SB, Trybus KM, et al. Myosin VI has a one track mind versus myosin Va when moving on actin bundles or at an intersection. Traffic 2013;14:70-81
    • (2013) Traffic , vol.14 , pp. 70-81
    • Ali, M.Y.1    Previs, S.B.2    Trybus, K.M.3
  • 22
    • 84881573878 scopus 로고    scopus 로고
    • Directional transport by nonprocessive motor proteins on fascin-cross-linked actin arrays
    • Lee Y, Famouri P. Directional transport by nonprocessive motor proteins on fascin-cross-linked actin arrays. Nano Lett 2013;13:3775-82
    • (2013) Nano Lett , vol.13 , pp. 3775-3782
    • Lee, Y.1    Famouri, P.2
  • 23
    • 84884394287 scopus 로고    scopus 로고
    • Actin structure-dependent stepping of myosin 5a and 10 during processive movement
    • Bao J, Huck D, Gunther LK, et al. Actin structure-dependent stepping of myosin 5a and 10 during processive movement. PLoS One 2013;8:e74936
    • (2013) PLoS One , vol.8 , pp. e74936
    • Bao, J.1    Huck, D.2    Gunther, L.K.3
  • 24
    • 67349229819 scopus 로고    scopus 로고
    • A novel form of motility in filopodia revealed by imaging myosin-X at the single-molecule level
    • Kerber ML, Jacobs DT, Campagnola L, et al. A novel form of motility in filopodia revealed by imaging myosin-X at the single-molecule level. Curr Biol 2009;19: 967-73
    • (2009) Curr Biol , vol.19 , pp. 967-973
    • Kerber, M.L.1    Jacobs, D.T.2    Campagnola, L.3
  • 25
    • 80054023872 scopus 로고    scopus 로고
    • Cofilin cooperates with fascin to disassemble filopodial actin filaments
    • Breitsprecher D, Koestler SA, Chizhov I, et al. Cofilin cooperates with fascin to disassemble filopodial actin filaments. J Cell Sci 2011;124:3305-18
    • (2011) J Cell Sci , vol.124 , pp. 3305-3318
    • Breitsprecher, D.1    Koestler, S.A.2    Chizhov, I.3
  • 26
    • 77951116071 scopus 로고    scopus 로고
    • Migrastatin analogues target fascin to block tumour metastasis
    • Chen L, Yang S, Jakoncic J, et al. Migrastatin analogues target fascin to block tumour metastasis. Nature 2010;464:1062-6.
    • (2010) Nature , vol.464 , pp. 1062-1066
    • Chen, L.1    Yang, S.2    Jakoncic, J.3
  • 27
    • 80051696938 scopus 로고    scopus 로고
    • Erratum in Nature 2011;476:240
    • (2011) Erratum in Nature , vol.476 , pp. 240
  • 28
    • 77954386574 scopus 로고    scopus 로고
    • Structure, evolutionary conservation, and conformational dynamics of Homo sapiens fascin-1, an F-actin crosslinking protein
    • Sedeh RS, Fedorov AA, Fedorov EV, et al. Structure, evolutionary conservation, and conformational dynamics of Homo sapiens fascin-1, an F-actin crosslinking protein. J Mol Biol 2010;400:589-04
    • (2010) J Mol Biol , vol.400 , pp. 589-604
    • Sedeh, R.S.1    Fedorov, A.A.2    Fedorov, E.V.3
  • 29
    • 80051952497 scopus 로고    scopus 로고
    • Mechanism of actin filament bundling by fascin
    • Jansen S, Collins A, Yang C, et al. Mechanism of actin filament bundling by fascin. J Biol Chem 2011;286:30087-96
    • (2011) J Biol Chem , vol.286 , pp. 30087-30096
    • Jansen, S.1    Collins, A.2    Yang, C.3
  • 30
    • 84872091686 scopus 로고    scopus 로고
    • Molecular mechanism of fascin function in filopodial formation
    • Yang S, Huang FK, Huang J, et al. Molecular mechanism of fascin function in filopodial formation. J Biol Chem 2013;288:274-84
    • (2013) J Biol Chem , vol.288 , pp. 274-284
    • Yang, S.1    Huang, F.K.2    Huang, J.3
  • 31
    • 0142073731 scopus 로고    scopus 로고
    • Interaction of fascin and protein kinase Calpha: A novel intersection in cell adhesion and motility
    • Anilkumar N, Parsons M, Monk R, et al. Interaction of fascin and protein kinase Calpha: a novel intersection in cell adhesion and motility. EMBO J 2003;22:5390-02
    • (2003) EMBO J , vol.22 , pp. 5390-5402
    • Anilkumar, N.1    Parsons, M.2    Monk, R.3
  • 32
    • 84862622680 scopus 로고    scopus 로고
    • Fascin promotes filopodia formation independent of its role in actin bundling
    • Zanet J, Jayo A, Plaza S, et al. Fascin promotes filopodia formation independent of its role in actin bundling. J Cell Biol 2012;197:477-86
    • (2012) J Cell Biol , vol.197 , pp. 477-486
    • Zanet, J.1    Jayo, A.2    Plaza, S.3
  • 33
    • 35848950225 scopus 로고    scopus 로고
    • Dual actin-bundling and protein kinase C-binding activities of fascin regulate carcinoma cell migration downstream of Rac and contribute to metastasis
    • Hashimoto Y, Parsons M, Adams JC. Dual actin-bundling and protein kinase C-binding activities of fascin regulate carcinoma cell migration downstream of Rac and contribute to metastasis. Mol Biol Cell 2007;18:4591-02
    • (2007) Mol Biol Cell , vol.18 , pp. 4591-4602
    • Hashimoto, Y.1    Parsons, M.2    Adams, J.C.3
  • 34
    • 53349097707 scopus 로고    scopus 로고
    • Rac regulates the interaction of fascin with protein kinase C in cell migration
    • Parsons M, Adams JC. Rac regulates the interaction of fascin with protein kinase C in cell migration. J Cell Sci 2008;121: 2805-13
    • (2008) J Cell Sci , vol.121 , pp. 2805-2813
    • Parsons, M.1    Adams, J.C.2
  • 35
    • 84864821892 scopus 로고    scopus 로고
    • A novel Rho-dependent pathway that drives interaction of fascin-1 with p-Lin-11/Isl-1/Mec-3 kinase (LIMK) 1/2 to promote fascin-1/actin binding and filopodia stability
    • Jayo A, Parsons M, Adams JC. A novel Rho-dependent pathway that drives interaction of fascin-1 with p-Lin-11/Isl-1/Mec-3 kinase (LIMK) 1/2 to promote fascin-1/actin binding and filopodia stability. BMC Biol 2012;10:72
    • (2012) BMC Biol , vol.10 , pp. 72
    • Jayo, A.1    Parsons, M.2    Adams, J.C.3
  • 36
    • 0037221974 scopus 로고    scopus 로고
    • Fascin, an actin-bundling protein, modulates colonic epithelial cell invasiveness and differentiation in vitro
    • Jawhari AU, Buda A, Jenkins M, et al. Fascin, an actin-bundling protein, modulates colonic epithelial cell invasiveness and differentiation in vitro. Am J Pathol 2003;162:69-80
    • (2003) Am J Pathol , vol.162 , pp. 69-80
    • Jawhari, A.U.1    Buda, A.2    Jenkins, M.3
  • 37
    • 34547101481 scopus 로고    scopus 로고
    • Fascin, a novel target of beta-catenin-TCF signaling, is expressed at the invasive front of human colon cancer
    • Vignjevic D, Schoumacher M, Gavert N. Fascin, a novel target of beta-catenin-TCF signaling, is expressed at the invasive front of human colon cancer. Cancer Res 2007;67:6844-53
    • (2007) Cancer Res , vol.67 , pp. 6844-6853
    • Vignjevic, D.1    Schoumacher, M.2    Gavert, N.3
  • 38
    • 77951771838 scopus 로고    scopus 로고
    • Actin, microtubules, and vimentin intermediate filaments cooperate for elongation of invadopodia
    • Schoumacher M, Goldman RD, Louvard D, Vignjevic DM. Actin, microtubules, and vimentin intermediate filaments cooperate for elongation of invadopodia. J Cell Biol 2010;189:541-56
    • (2010) J Cell Biol , vol.189 , pp. 541-556
    • Schoumacher, M.1    Goldman, R.D.2    Louvard, D.3    Vignjevic, D.M.4
  • 39
    • 0034698675 scopus 로고    scopus 로고
    • Stimulation of fascin microspikes by thrombospondin-1 is mediated by the GTPases Rac and Cdc 42
    • Adams JC, Schwartz MA. Stimulation of fascin microspikes by thrombospondin-1 is mediated by the GTPases Rac and Cdc 42. J Cell Biol 2000;150:807-22
    • (2000) J Cell Biol , vol.150 , pp. 807-822
    • Adams, J.C.1    Schwartz, M.A.2
  • 40
    • 64549140740 scopus 로고    scopus 로고
    • Fascin-1 promoter activity is regulated by CREB and the aryl hydrocarbon receptor in human carcinoma cells
    • Hashimoto Y, Loftis DW, Adams JC. Fascin-1 promoter activity is regulated by CREB and the aryl hydrocarbon receptor in human carcinoma cells. PLoS ONE 2009;4: e5130
    • (2009) PLoS ONE , vol.4 , pp. e5130
    • Hashimoto, Y.1    Loftis, D.W.2    Adams, J.C.3
  • 41
    • 84887443298 scopus 로고    scopus 로고
    • The prometastatic ribosomal S6 kinase 2-cAMP response element-binding protein (RSK2-CREB) signaling pathway up-regulates the actin-binding protein fascin-1 to promote tumor metastasis
    • Li D, Jin L, Alesi GN, et al. The prometastatic ribosomal S6 kinase 2-cAMP response element-binding protein (RSK2-CREB) signaling pathway up-regulates the actin-binding protein fascin-1 to promote tumor metastasis. J Biol Chem 2013;288: 32528-38
    • (2013) J Biol Chem , vol.288 , pp. 32528-32538
    • Li, D.1    Jin, L.2    Alesi, G.N.3
  • 42
    • 84898838516 scopus 로고    scopus 로고
    • Stress-induced cleavage of Myc promotes cancer cell survival
    • Conacci-Sorrell M, Ngouenet C, Anderson S, et al. Stress-induced cleavage of Myc promotes cancer cell survival. Genes Dev 2014;28:689-07
    • (2014) Genes Dev , vol.28 , pp. 689-707
    • Conacci-Sorrell, M.1    Ngouenet, C.2    Anderson, S.3
  • 43
    • 84899931775 scopus 로고    scopus 로고
    • Micro RNA-145 inhibits tumour growth and metastasis in colorectal cancer by targeting fascin-1
    • Feng Y, Zhu J, Ou C, et al. MicroRNA-145 inhibits tumour growth and metastasis in colorectal cancer by targeting fascin-1. Br J Cancer 2014;110:2300-9
    • (2014) Br J Cancer , vol.110 , pp. 2300-2309
    • Feng, Y.1    Zhu, J.2    Ou, C.3
  • 44
    • 84874213712 scopus 로고    scopus 로고
    • Association of fascin-1 with mortality, disease progression and metastasis in carcinomas: A systematic review and meta-analysis
    • Tan VY, Lewis SJ, Adams JC, Martin RM. Association of fascin-1 with mortality, disease progression and metastasis in carcinomas: a systematic review and meta-analysis. BMC Med 2013;11:5
    • (2013) BMC Med , vol.11 , pp. 5
    • Tan, V.Y.1    Lewis, S.J.2    Adams, J.C.3    Martin, R.M.4
  • 45
    • 84874214606 scopus 로고    scopus 로고
    • Fascin-1 is a novel biomarker of aggressiveness in some carcinomas
    • Kulasingam V, Diamandis EP. Fascin-1 is a novel biomarker of aggressiveness in some carcinomas. BMC Med 2013;11:53
    • (2013) BMC Med , vol.11 , pp. 53
    • Kulasingam, V.1    Diamandis, E.P.2
  • 46
    • 33750627650 scopus 로고    scopus 로고
    • Prognostic significance of fascin expression in advanced colorectal cancer: An immunohistochemical study of colorectal adenomas and adenocarcinomas
    • Hashimoto Y, Skacel M, Lavery IC, et al. Prognostic significance of fascin expression in advanced colorectal cancer: an immunohistochemical study of colorectal adenomas and adenocarcinomas. BMC Cancer 2006;6:241
    • (2006) BMC Cancer , vol.6 , pp. 241
    • Hashimoto, Y.1    Skacel, M.2    Lavery, I.C.3
  • 47
    • 70349666743 scopus 로고    scopus 로고
    • The actin-bundling protein fascin is overexpressed in colorectal adenomas and promotes motility in adenoma cells in vitro
    • Qualtrough D, Singh K, Banu N, et al. The actin-bundling protein fascin is overexpressed in colorectal adenomas and promotes motility in adenoma cells in vitro. Br J Cancer 2009;101:1124-9
    • (2009) Br J Cancer , vol.101 , pp. 1124-1129
    • Qualtrough, D.1    Singh, K.2    Banu, N.3
  • 48
    • 34247266530 scopus 로고    scopus 로고
    • Independent prognostic value of fascin immunoreactivity in stage III-IV colonic adenocarcinoma
    • Puppa G, Maisonneuve P, Sonzogni A, et al. Independent prognostic value of fascin immunoreactivity in stage III-IV colonic adenocarcinoma. Br J Cancer 2007;96: 1118-26
    • (2007) Br J Cancer , vol.96 , pp. 1118-1126
    • Puppa, G.1    Maisonneuve, P.2    Sonzogni, A.3
  • 49
    • 4844228230 scopus 로고    scopus 로고
    • Colorectal carcinoma and inflammatory bowel disease
    • Eaden J. Colorectal carcinoma and inflammatory bowel disease. Aliment Pharmacol Ther 2004;20(S4):24-30
    • (2004) Aliment Pharmacol Ther , vol.20 , Issue.S4 , pp. 24-30
    • Eaden, J.1
  • 50
    • 79951850798 scopus 로고    scopus 로고
    • The actin-bundling protein fascin is overexpressed in inflammatory bowel disease and may be important in tissue repair
    • Qualtrough D, Smallwood K, Littlejohns D, Pignatelli M. The actin-bundling protein fascin is overexpressed in inflammatory bowel disease and may be important in tissue repair. BMC Gastroenterol 2011;11:14
    • (2011) BMC Gastroenterol , vol.11 , pp. 14
    • Qualtrough, D.1    Smallwood, K.2    Littlejohns, D.3    Pignatelli, M.4
  • 51
    • 84898651848 scopus 로고    scopus 로고
    • Fascin regulates chronic inflammation-related human colon carcinogenesis by inhibiting cell anoikis
    • Kanda Y, Kawaguchi T, Kuramitsu Y, et al. Fascin regulates chronic inflammation-related human colon carcinogenesis by inhibiting cell anoikis. Proteomics 2014;14:1031-41
    • (2014) Proteomics , vol.14 , pp. 1031-1041
    • Kanda, Y.1    Kawaguchi, T.2    Kuramitsu, Y.3
  • 52
    • 84880834586 scopus 로고    scopus 로고
    • Rifaximin-mediated changes to the epithelial cell proteome: 2-D gel analysis
    • Schrodt C, McHugh EE, Gawinowicz MA, et al. Rifaximin-mediated changes to the epithelial cell proteome: 2-D gel analysis. PLoS One 2013;8(7):e68550
    • (2013) PLoS One , vol.8 , Issue.7 , pp. e68550
    • Schrodt, C.1    McHugh, E.E.2    Gawinowicz, M.A.3
  • 53
    • 84887101163 scopus 로고    scopus 로고
    • Micro RNAs and other non-coding RNAs as targets for anticancer drug development
    • Ling H, Fabbri M, Calin GA. Micro RNAs and other non-coding RNAs as targets for anticancer drug development. Nat Rev Drug Discov 2013;12:847-65
    • (2013) Nat Rev Drug Discov , vol.12 , pp. 847-865
    • Ling, H.1    Fabbri, M.2    Calin, G.A.3
  • 54
    • 80053084120 scopus 로고    scopus 로고
    • Emergence of potent inhibitors of metastasis in lung cancer via syntheses based on migrastatin
    • Lecomte N, Njardarson JT, Nagorny P, et al. Emergence of potent inhibitors of metastasis in lung cancer via syntheses based on migrastatin. Proc Natl Acad Sci USA 2011;108:15074-8
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 15074-15078
    • Lecomte, N.1    Njardarson, J.T.2    Nagorny, P.3
  • 55
    • 84903727936 scopus 로고    scopus 로고
    • Synthesis of migrastatin and its macroketone analogue and in vivo frap analysis of the macroketone on E-cadherin dynamics
    • Lo Re D, Zhou Y, Nobis M, et al. Synthesis of migrastatin and its macroketone analogue and in vivo frap analysis of the macroketone on E-cadherin dynamics. ChemBioChem 2014;15:1459-64
    • (2014) Chem Bio Chem , vol.15 , pp. 1459-1464
    • Lo Re, D.1    Zhou, Y.2    Nobis, M.3
  • 56
    • 84872068693 scopus 로고    scopus 로고
    • A cell-based fascin bioassay identifies compounds with potential anti-metastasis or cognition-enhancing functions
    • Kraft R, Kahn A, Medina-Franco JL, et al. A cell-based fascin bioassay identifies compounds with potential anti-metastasis or cognition-enhancing functions. Dis Model Mech 2013;6:217-35
    • (2013) Dis Model Mech , vol.6 , pp. 217-235
    • Kraft, R.1    Kahn, A.2    Medina-Franco, J.L.3
  • 57
    • 84906085238 scopus 로고    scopus 로고
    • Modification and biological evaluation of thiazole derivatives as novel inhibitors of metastatic cancer cell migration and invasion
    • Zheng S, Zhong Q, Xi Y, et al. Modification and biological evaluation of thiazole derivatives as novel inhibitors of metastatic cancer cell migration and invasion. J Med Chem 2014;57(15): 6653-67
    • (2014) J Med Chem , vol.57 , Issue.15 , pp. 6653-6667
    • Zheng, S.1    Zhong, Q.2    Xi, Y.3
  • 58
    • 0027310612 scopus 로고
    • Naturally occurring antibodies devoid of light chains
    • Hamers-Casterman C, Atarhouch T, Muyldermans S, et al. Naturally occurring antibodies devoid of light chains. Nature 1993;363:446-8
    • (1993) Nature , vol.363 , pp. 446-448
    • Hamers-Casterman, C.1    Atarhouch, T.2    Muyldermans, S.3
  • 59
    • 84901022975 scopus 로고    scopus 로고
    • Stratifying fascin and cortactin function in invadopodium formation using inhibitory nanobodies and targeted subcellular delocalization
    • Van Audenhove I, Boucherie C, Pieters L, et al. Stratifying fascin and cortactin function in invadopodium formation using inhibitory nanobodies and targeted subcellular delocalization. FASEB J 2014;28: 1805-18
    • (2014) FASEB J , vol.28 , pp. 1805-1818
    • Van Audenhove, I.1    Boucherie, C.2    Pieters, L.3
  • 60
    • 84902547698 scopus 로고    scopus 로고
    • Is availability of anti-EGFR therapy for the colorectal adenocarcinomas showing fascin expression limited
    • Koçer NE, Kayaselçuk F. Is availability of anti-EGFR therapy for the colorectal adenocarcinomas showing fascin expression limited Target Oncol 2014;9:171-5
    • (2014) Target Oncol , vol.9 , pp. 171-175
    • Koçer, N.E.1    Kayaselçuk, F.2
  • 61
    • 72249093615 scopus 로고    scopus 로고
    • Tumor self-seeding by circulating cancer cells
    • Kim MY, Oskarsson T, Acharyya S, et al. Tumor self-seeding by circulating cancer cells. Cell 2009;139:1315-26
    • (2009) Cell , vol.139 , pp. 1315-1326
    • Kim, M.Y.1    Oskarsson, T.2    Acharyya, S.3
  • 62
    • 84875813640 scopus 로고    scopus 로고
    • What are the best routes to effectively model human colorectal cancer
    • Young M, Ordonez L, Clarke AR. What are the best routes to effectively model human colorectal cancer Mol Oncol 2013;7: 178-89
    • (2013) Mol Oncol , vol.7 , pp. 178-189
    • Young, M.1    Ordonez, L.2    Clarke, A.R.3
  • 63
    • 84898420195 scopus 로고    scopus 로고
    • Colon-specific tumorigenesis in mice driven by Cre-mediated inactivation of Apc and activation of mutant Kras
    • Byun AJ, Hung KE, Fleet JC, et al. Colon-specific tumorigenesis in mice driven by Cre-mediated inactivation of Apc and activation of mutant Kras. Cancer Lett 2014;347:191-5
    • (2014) Cancer Lett , vol.347 , pp. 191-195
    • Byun, A.J.1    Hung, K.E.2    Fleet, J.C.3
  • 64
    • 84898596713 scopus 로고    scopus 로고
    • PTEN loss and KRAS activation leads to the formation of serrated adenomas and metastatic carcinoma in the mouse intestine
    • Davies EJ, Marsh Durban V, Meniel V, et al. PTEN loss and KRAS activation leads to the formation of serrated adenomas and metastatic carcinoma in the mouse intestine. J Pathol 2014;233:27-38
    • (2014) J Pathol , vol.233 , pp. 27-38
    • Davies, E.J.1    Marsh Durban, V.2    Meniel, V.3
  • 65
    • 34249905439 scopus 로고    scopus 로고
    • Overexpression of fascin-1 in advanced colorectal adenocarcinoma: Tissue microarray analysis of immunostaining scores with clinicopathological parameters
    • Tsai WC, Chao YC, Sheu LF, et al. Overexpression of fascin-1 in advanced colorectal adenocarcinoma: tissue microarray analysis of immunostaining scores with clinicopathological parameters. Dis Markers 2007;23:153-60
    • (2007) Dis Markers , vol.23 , pp. 153-160
    • Tsai, W.C.1    Chao, Y.C.2    Sheu, L.F.3
  • 66
    • 77951875068 scopus 로고    scopus 로고
    • Fascin expression predicts survival after potentially curative resection of node-positive colon cancer
    • Chan C, Jankova L, Fung CL, et al. Fascin expression predicts survival after potentially curative resection of node-positive colon cancer. Am J Surg Pathol 2010;34:656-66
    • (2010) Am J Surg Pathol , vol.34 , pp. 656-666
    • Chan, C.1    Jankova, L.2    Fung, C.L.3
  • 68
    • 79952964018 scopus 로고    scopus 로고
    • Clinicopathologic significance of fascin, extracellular matrix metalloproteinase inducer, and ezrin expressions in colorectal adenocarcinoma
    • Jung EJ, Lee JH, Min BW, et al. Clinicopathologic significance of fascin, extracellular matrix metalloproteinase inducer, and ezrin expressions in colorectal adenocarcinoma. Indian J Pathol Microbiol 2011;54:32-6
    • (2011) Indian J Pathol Microbiol , vol.54 , pp. 32-36
    • Jung, E.J.1    Lee, J.H.2    Min, B.W.3
  • 69
    • 82955164423 scopus 로고    scopus 로고
    • Prognostic impact of fascin-1 expression is more significant in advanced colorectal cancer
    • Oh SY, Kim YB, Suh KW, et al. Prognostic impact of fascin-1 expression is more significant in advanced colorectal cancer. J Surg Res 2012;172:102-8
    • (2012) J Surg Res , vol.172 , pp. 102-108
    • Oh, S.Y.1    Kim, Y.B.2    Suh, K.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.