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Volumn 289, Issue , 2011, Pages 117-147

Significance of talin in cancer progression and metastasis

Author keywords

Anoikis; Focal adhesions; Integrins; Invasion; Metastasis; Migration; Talin

Indexed keywords

ACTIN; ALPHA 1 ADRENERGIC RECEPTOR BLOCKING AGENT; ANDROGEN RECEPTOR; BETA1 INTEGRIN; BETA3 INTEGRIN; BEVACIZUMAB; BIOLOGICAL MARKER; CILENGITIDE; DOXAZOSIN; DZ 50; ESTROGEN RECEPTOR; ETARACIZUMAB; FOCAL ADHESION KINASE; INTEGRIN; INTETUMUMAB; MATRIX METALLOPROTEINASE; MUTANT PROTEIN; N ACETYLPROLYLHISTIDYLSERYLCYSTEINYLASPARAGINE AMIDE; PAXILLIN; PLATELET DERIVED GROWTH FACTOR BETA RECEPTOR; QUINAZOLINE DERIVATIVE; SILIBININ; SORAFENIB; SUNITINIB; TALIN; TALIN1; UNCLASSIFIED DRUG; UNINDEXED DRUG; VASCULOTROPIN A; VASCULOTROPIN RECEPTOR 2; VIMENTIN;

EID: 79960149427     PISSN: 19376448     EISSN: 19376448     Source Type: Book Series    
DOI: 10.1016/B978-0-12-386039-2.00004-3     Document Type: Chapter
Times cited : (78)

References (216)
  • 1
    • 36649025928 scopus 로고    scopus 로고
    • Inducible FGFR-1 activation leads to irreversible prostate adenocarcinoma and an epithelial-to-mesenchymal transition
    • Acevedo V.D., Gangula R.D., et al. Inducible FGFR-1 activation leads to irreversible prostate adenocarcinoma and an epithelial-to-mesenchymal transition. Cancer Cell 2007, 12:559-571.
    • (2007) Cancer Cell , vol.12 , pp. 559-571
    • Acevedo, V.D.1    Gangula, R.D.2
  • 2
    • 35548936833 scopus 로고    scopus 로고
    • Models, mechanisms and clinical evidence for cancer dormancy
    • Aguirre-Ghiso J.A. Models, mechanisms and clinical evidence for cancer dormancy. Nat. Rev. Cancer 2007, 7:834-846.
    • (2007) Nat. Rev. Cancer , vol.7 , pp. 834-846
    • Aguirre-Ghiso, J.A.1
  • 3
    • 0037379794 scopus 로고    scopus 로고
    • ERK(MAPK) activity as a determinant of tumor growth and dormancy; regulation by p38(SAPK)
    • Aguirre-Ghiso J.A., Estrada Y., et al. ERK(MAPK) activity as a determinant of tumor growth and dormancy; regulation by p38(SAPK). Cancer Res. 2003, 63:1684-1695.
    • (2003) Cancer Res. , vol.63 , pp. 1684-1695
    • Aguirre-Ghiso, J.A.1    Estrada, Y.2
  • 4
    • 0027395858 scopus 로고
    • Role of integrins and other cell adhesion molecules in tumor progression and metastasis
    • Albelda S.M. Role of integrins and other cell adhesion molecules in tumor progression and metastasis. Lab. Invest. 1993, 68:4-17.
    • (1993) Lab. Invest. , vol.68 , pp. 4-17
    • Albelda, S.M.1
  • 5
    • 33644821239 scopus 로고    scopus 로고
    • Doxazosin induces apoptosis in LNCaP prostate cancer cell line through DNA binding and DNA-dependent protein kinase down-regulation
    • Arencibia J.M., Del Rio M., et al. Doxazosin induces apoptosis in LNCaP prostate cancer cell line through DNA binding and DNA-dependent protein kinase down-regulation. Int. J. Oncol. 2005, 27:1617-1623.
    • (2005) Int. J. Oncol. , vol.27 , pp. 1617-1623
    • Arencibia, J.M.1    Del Rio, M.2
  • 6
    • 47949114114 scopus 로고    scopus 로고
    • Integrins in angiogenesis and lymphangiogenesis
    • Avraamides C.J., Garmy-Susini B., et al. Integrins in angiogenesis and lymphangiogenesis. Nat. Rev. Cancer 2008, 8:604-617.
    • (2008) Nat. Rev. Cancer , vol.8 , pp. 604-617
    • Avraamides, C.J.1    Garmy-Susini, B.2
  • 7
    • 0034711307 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase function is required for transforming growth factor beta-mediated epithelial to mesenchymal transition and cell migration
    • Bakin A.V., Tomlinson A.K., et al. Phosphatidylinositol 3-kinase function is required for transforming growth factor beta-mediated epithelial to mesenchymal transition and cell migration. J. Biol. Chem. 2000, 275:36803-36810.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36803-36810
    • Bakin, A.V.1    Tomlinson, A.K.2
  • 8
    • 0036674213 scopus 로고    scopus 로고
    • P38 mitogen-activated protein kinase is required for TGFbeta-mediated fibroblastic transdifferentiation and cell migration
    • Bakin A.V., Rinehart C., et al. p38 mitogen-activated protein kinase is required for TGFbeta-mediated fibroblastic transdifferentiation and cell migration. J. Cell Sci. 2002, 115:3193-3206.
    • (2002) J. Cell Sci. , vol.115 , pp. 3193-3206
    • Bakin, A.V.1    Rinehart, C.2
  • 9
    • 77950594400 scopus 로고    scopus 로고
    • Extracellular matrix: a gatekeeper in the transition from dormancy to metastatic growth
    • Barkan D., Green J.E., et al. Extracellular matrix: a gatekeeper in the transition from dormancy to metastatic growth. Eur. J. Cancer 2010, 46:1181-1188.
    • (2010) Eur. J. Cancer , vol.46 , pp. 1181-1188
    • Barkan, D.1    Green, J.E.2
  • 10
    • 0025238080 scopus 로고
    • The adhesion plaque protein, talin, is phosphorylated in vivo in chicken embryo fibroblasts exposed to a tumor-promoting phorbol ester
    • Beckerle M.C. The adhesion plaque protein, talin, is phosphorylated in vivo in chicken embryo fibroblasts exposed to a tumor-promoting phorbol ester. Cell Regul. 1990, 1:227-236.
    • (1990) Cell Regul. , vol.1 , pp. 227-236
    • Beckerle, M.C.1
  • 11
    • 0024846571 scopus 로고
    • Activation-dependent redistribution of the adhesion plaque protein, talin, in intact human platelets
    • Beckerle M.C., Miller D.E., et al. Activation-dependent redistribution of the adhesion plaque protein, talin, in intact human platelets. J. Cell Biol. 1989, 109:3333-3346.
    • (1989) J. Cell Biol. , vol.109 , pp. 3333-3346
    • Beckerle, M.C.1    Miller, D.E.2
  • 12
    • 33646859981 scopus 로고    scopus 로고
    • Phase II evaluations of cilengitide in asymptomatic patients with androgen-independent prostate cancer: scientific rationale and study design
    • Beekman K.W., Colevas A.D., et al. Phase II evaluations of cilengitide in asymptomatic patients with androgen-independent prostate cancer: scientific rationale and study design. Clin. Genitourin. Cancer 2006, 4:299-302.
    • (2006) Clin. Genitourin. Cancer , vol.4 , pp. 299-302
    • Beekman, K.W.1    Colevas, A.D.2
  • 13
    • 0037079614 scopus 로고    scopus 로고
    • Quinazoline-derived alpha1-adrenoceptor antagonists induce prostate cancer cell apoptosis via an alpha1-adrenoceptor-independent action
    • Benning C.M., Kyprianou N. Quinazoline-derived alpha1-adrenoceptor antagonists induce prostate cancer cell apoptosis via an alpha1-adrenoceptor-independent action. Cancer Res. 2002, 62:597-602.
    • (2002) Cancer Res. , vol.62 , pp. 597-602
    • Benning, C.M.1    Kyprianou, N.2
  • 14
    • 0035185853 scopus 로고    scopus 로고
    • Transforming growth factor-beta1 mediates epithelial to mesenchymal transdifferentiation through a RhoA-dependent mechanism
    • Bhowmick N.A., Ghiassi M., et al. Transforming growth factor-beta1 mediates epithelial to mesenchymal transdifferentiation through a RhoA-dependent mechanism. Mol. Biol. Cell 2001, 12:27-36.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 27-36
    • Bhowmick, N.A.1    Ghiassi, M.2
  • 16
    • 79955727135 scopus 로고    scopus 로고
    • The dual kinase complex FAK-Src as a promising therapeutic target in cancer
    • Bolos V., Gasent J.M., et al. The dual kinase complex FAK-Src as a promising therapeutic target in cancer. Onco. Targets Ther. 2010, 3:83-97.
    • (2010) Onco. Targets Ther. , vol.3 , pp. 83-97
    • Bolos, V.1    Gasent, J.M.2
  • 17
    • 44449148944 scopus 로고    scopus 로고
    • The N-terminal domains of talin cooperate with the phosphotyrosine binding-like domain to activate beta1 and beta3 integrins
    • Bouaouina M., Lad Y., et al. The N-terminal domains of talin cooperate with the phosphotyrosine binding-like domain to activate beta1 and beta3 integrins. J. Biol. Chem. 2008, 283:6118-6125.
    • (2008) J. Biol. Chem. , vol.283 , pp. 6118-6125
    • Bouaouina, M.1    Lad, Y.2
  • 18
    • 0036774751 scopus 로고    scopus 로고
    • Talin is essential for integrin function in Drosophila
    • Brown N.H., Gregory S.L., et al. Talin is essential for integrin function in Drosophila. Dev. Cell 2002, 3:569-579.
    • (2002) Dev. Cell , vol.3 , pp. 569-579
    • Brown, N.H.1    Gregory, S.L.2
  • 20
    • 3042609771 scopus 로고    scopus 로고
    • Talin controls integrin activation
    • Calderwood D.A. Talin controls integrin activation. Biochem. Soc. Trans. 2004, 32:434-437.
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 434-437
    • Calderwood, D.A.1
  • 21
    • 0033213922 scopus 로고    scopus 로고
    • The Talin head domain binds to integrin beta subunit cytoplasmic tails and regulates integrin activation
    • Calderwood D.A., Zent R., et al. The Talin head domain binds to integrin beta subunit cytoplasmic tails and regulates integrin activation. J. Biol. Chem. 1999, 274:28071-28074.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28071-28074
    • Calderwood, D.A.1    Zent, R.2
  • 22
    • 0037077282 scopus 로고    scopus 로고
    • The phosphotyrosine binding-like domain of talin activates integrins
    • Calderwood D.A., Yan B., et al. The phosphotyrosine binding-like domain of talin activates integrins. J. Biol. Chem. 2002, 277:21749-21758.
    • (2002) J. Biol. Chem. , vol.277 , pp. 21749-21758
    • Calderwood, D.A.1    Yan, B.2
  • 23
    • 1042267263 scopus 로고    scopus 로고
    • Cell adhesion and signalling by cadherins and Ig-CAMs in cancer
    • Cavallaro U., Christofori G. Cell adhesion and signalling by cadherins and Ig-CAMs in cancer. Nat. Rev. Cancer 2004, 4:118-132.
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 118-132
    • Cavallaro, U.1    Christofori, G.2
  • 24
    • 0036674501 scopus 로고    scopus 로고
    • Dissemination and growth of cancer cells in metastatic sites
    • Chambers A.F., Groom A.C., et al. Dissemination and growth of cancer cells in metastatic sites. Nat. Rev. Cancer 2002, 2:563-572.
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 563-572
    • Chambers, A.F.1    Groom, A.C.2
  • 25
    • 20144386127 scopus 로고    scopus 로고
    • Robustness, scalability, and integration of a wound-response gene expression signature in predicting breast cancer survival
    • Chang H.Y., Nuyten D.S., et al. Robustness, scalability, and integration of a wound-response gene expression signature in predicting breast cancer survival. Proc. Natl. Acad. Sci. USA 2005, 102:3738-3743.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 3738-3743
    • Chang, H.Y.1    Nuyten, D.S.2
  • 26
    • 27944509109 scopus 로고    scopus 로고
    • Differential effect of the focal adhesion kinase Y397F mutant on v-Src-stimulated cell invasion and tumor growth
    • Chang L.C., Huang C.H., et al. Differential effect of the focal adhesion kinase Y397F mutant on v-Src-stimulated cell invasion and tumor growth. J. Biomed. Sci. 2005, 12:571-585.
    • (2005) J. Biomed. Sci. , vol.12 , pp. 571-585
    • Chang, L.C.1    Huang, C.H.2
  • 27
    • 0029984390 scopus 로고    scopus 로고
    • The bombesin/GRP receptor transfected into Rat-1 fibroblasts couples to phospholipase C activation, tyrosine phosphorylation of p125FAK and paxillin and cell proliferation
    • Charlesworth A., Broad S., et al. The bombesin/GRP receptor transfected into Rat-1 fibroblasts couples to phospholipase C activation, tyrosine phosphorylation of p125FAK and paxillin and cell proliferation. Oncogene 1996, 12:1337-1345.
    • (1996) Oncogene , vol.12 , pp. 1337-1345
    • Charlesworth, A.1    Broad, S.2
  • 28
    • 55949128465 scopus 로고    scopus 로고
    • Anoikis: a necessary death program for anchorage-dependent cells
    • Chiarugi P., Giannoni E. Anoikis: a necessary death program for anchorage-dependent cells. Biochem. Pharmacol. 2008, 76:1352-1364.
    • (2008) Biochem. Pharmacol. , vol.76 , pp. 1352-1364
    • Chiarugi, P.1    Giannoni, E.2
  • 29
    • 33745297408 scopus 로고    scopus 로고
    • New signals from the invasive front
    • Christofori G. New signals from the invasive front. Nature 2006, 441:444-450.
    • (2006) Nature , vol.441 , pp. 444-450
    • Christofori, G.1
  • 30
    • 33745240059 scopus 로고    scopus 로고
    • Phase 1 trial of the antiangiogenic peptide ATN-161 (Ac-PHSCN-NH(2)), a beta integrin antagonist, in patients with solid tumours
    • Cianfrocca M.E., Kimmel K.A., et al. Phase 1 trial of the antiangiogenic peptide ATN-161 (Ac-PHSCN-NH(2)), a beta integrin antagonist, in patients with solid tumours. Br. J. Cancer 2006, 94:1621-1626.
    • (2006) Br. J. Cancer , vol.94 , pp. 1621-1626
    • Cianfrocca, M.E.1    Kimmel, K.A.2
  • 31
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: the road taken
    • Clark E.A., Brugge J.S. Integrins and signal transduction pathways: the road taken. Science 1995, 268:233-239.
    • (1995) Science , vol.268 , pp. 233-239
    • Clark, E.A.1    Brugge, J.S.2
  • 32
    • 78449281238 scopus 로고    scopus 로고
    • Cancer therapy beyond apoptosis: autophagy and anoikis as mechanisms of cell death
    • Coates J.M., Galante J.M., et al. Cancer therapy beyond apoptosis: autophagy and anoikis as mechanisms of cell death. J. Surg. Res. 2010, 164:301-308.
    • (2010) J. Surg. Res. , vol.164 , pp. 301-308
    • Coates, J.M.1    Galante, J.M.2
  • 33
    • 0037171468 scopus 로고    scopus 로고
    • Increased Bcl-xL expression mediates v-Src-induced resistance to anoikis in intestinal epithelial cells
    • Coll M.L., Rosen K., et al. Increased Bcl-xL expression mediates v-Src-induced resistance to anoikis in intestinal epithelial cells. Oncogene 2002, 21:2908-2913.
    • (2002) Oncogene , vol.21 , pp. 2908-2913
    • Coll, M.L.1    Rosen, K.2
  • 34
    • 0036191946 scopus 로고    scopus 로고
    • The regulation of prostate cancer cell adhesion to human bone marrow endothelial cell monolayers by androgen dihydrotestosterone and cytokines
    • Cooper C.R., Bhatia J.K., et al. The regulation of prostate cancer cell adhesion to human bone marrow endothelial cell monolayers by androgen dihydrotestosterone and cytokines. Clin. Exp. Metastasis 2002, 19:25-33.
    • (2002) Clin. Exp. Metastasis , vol.19 , pp. 25-33
    • Cooper, C.R.1    Bhatia, J.K.2
  • 35
    • 33748049409 scopus 로고    scopus 로고
    • Integrin-mediated cell-matrix interactions for prosurvival and antiapoptotic signaling after genotoxic injury
    • Cordes N. Integrin-mediated cell-matrix interactions for prosurvival and antiapoptotic signaling after genotoxic injury. Cancer Lett. 2006, 242:11-19.
    • (2006) Cancer Lett. , vol.242 , pp. 11-19
    • Cordes, N.1
  • 36
    • 33644778551 scopus 로고    scopus 로고
    • Beta1-integrin-mediated signaling essentially contributes to cell survival after radiation-induced genotoxic injury
    • Cordes N., Seidler J., et al. beta1-integrin-mediated signaling essentially contributes to cell survival after radiation-induced genotoxic injury. Oncogene 2006, 25:1378-1390.
    • (2006) Oncogene , vol.25 , pp. 1378-1390
    • Cordes, N.1    Seidler, J.2
  • 37
    • 0142106350 scopus 로고    scopus 로고
    • Talin loss-of-function uncovers roles in cell contractility and migration in C. elegans
    • Cram E.J., Clark S.G., et al. Talin loss-of-function uncovers roles in cell contractility and migration in C. elegans. J. Cell Sci. 2003, 116:3871-3878.
    • (2003) J. Cell Sci. , vol.116 , pp. 3871-3878
    • Cram, E.J.1    Clark, S.G.2
  • 39
    • 3042800591 scopus 로고    scopus 로고
    • Recruitment of focal adhesion kinase and paxillin to beta1 integrin promotes cancer cell migration via mitogen activated protein kinase activation
    • Crowe D.L., Ohannessian A. Recruitment of focal adhesion kinase and paxillin to beta1 integrin promotes cancer cell migration via mitogen activated protein kinase activation. BMC Cancer 2004, 4:18.
    • (2004) BMC Cancer , vol.4 , pp. 18
    • Crowe, D.L.1    Ohannessian, A.2
  • 40
    • 0035984238 scopus 로고    scopus 로고
    • Alpha1-adrenoceptor antagonists radiosensitize prostate cancer cells via apoptosis induction
    • Cuellar D.C., Rhee J., et al. Alpha1-adrenoceptor antagonists radiosensitize prostate cancer cells via apoptosis induction. Anticancer Res. 2002, 22:1673-1679.
    • (2002) Anticancer Res. , vol.22 , pp. 1673-1679
    • Cuellar, D.C.1    Rhee, J.2
  • 41
    • 0032530482 scopus 로고    scopus 로고
    • Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase
    • Delcommenne M., Tan C., et al. Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase. Proc. Natl. Acad. Sci. USA 1998, 95:11211-11216.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11211-11216
    • Delcommenne, M.1    Tan, C.2
  • 42
    • 67650021249 scopus 로고    scopus 로고
    • Intestinal epithelial cancer cell anoikis resistance: EGFR-mediated sustained activation of Src overrides Fak-dependent signaling to MEK/Erk and/or PI3-K/Akt-1
    • Demers M.J., Thibodeau S., et al. Intestinal epithelial cancer cell anoikis resistance: EGFR-mediated sustained activation of Src overrides Fak-dependent signaling to MEK/Erk and/or PI3-K/Akt-1. J. Cell. Biochem. 2009, 107:639-654.
    • (2009) J. Cell. Biochem. , vol.107 , pp. 639-654
    • Demers, M.J.1    Thibodeau, S.2
  • 43
    • 18644371169 scopus 로고    scopus 로고
    • Recruitment and regulation of phosphatidylinositol phosphate kinase type 1 gamma by the FERM domain of talin
    • Di Paolo G., Pellegrini L., et al. Recruitment and regulation of phosphatidylinositol phosphate kinase type 1 gamma by the FERM domain of talin. Nature 2002, 420:85-89.
    • (2002) Nature , vol.420 , pp. 85-89
    • Di Paolo, G.1    Pellegrini, L.2
  • 44
    • 4344627055 scopus 로고    scopus 로고
    • Suppression of anoikis and induction of metastasis by the neurotrophic receptor TrkB
    • Douma S., Van Laar T., et al. Suppression of anoikis and induction of metastasis by the neurotrophic receptor TrkB. Nature 2004, 430:1034-1039.
    • (2004) Nature , vol.430 , pp. 1034-1039
    • Douma, S.1    Van Laar, T.2
  • 45
    • 85006314494 scopus 로고    scopus 로고
    • A novel Epac-specific cAMP analogue demonstrates independent regulation of RAP1 and ERK
    • Enserink J.M., Christensen A.E., et al. A novel Epac-specific cAMP analogue demonstrates independent regulation of RAP1 and ERK. Nat. Cell Biol. 2002, 4:901-906.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 901-906
    • Enserink, J.M.1    Christensen, A.E.2
  • 46
    • 4043141477 scopus 로고    scopus 로고
    • Quantitative cancer proteomics: stable isotope labeling with amino acids in cell culture (SILAC) as a tool for prostate cancer research
    • Everley P.A., Krijgsveld J., et al. Quantitative cancer proteomics: stable isotope labeling with amino acids in cell culture (SILAC) as a tool for prostate cancer research. Mol. Cell. Proteomics 2004, 3:729-735.
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 729-735
    • Everley, P.A.1    Krijgsveld, J.2
  • 47
    • 77954563464 scopus 로고    scopus 로고
    • Hypoxia, inflammation, and the tumor microenvironment in metastatic disease
    • Finger E.C., Giaccia A.J. Hypoxia, inflammation, and the tumor microenvironment in metastatic disease. Cancer Metastasis Rev. 2010, 29:285-293.
    • (2010) Cancer Metastasis Rev. , vol.29 , pp. 285-293
    • Finger, E.C.1    Giaccia, A.J.2
  • 48
    • 0025141337 scopus 로고
    • What is the evidence that tumors are angiogenesis dependent?
    • Folkman J. What is the evidence that tumors are angiogenesis dependent?. J. Natl. Cancer Inst. 1990, 82:4-6.
    • (1990) J. Natl. Cancer Inst. , vol.82 , pp. 4-6
    • Folkman, J.1
  • 49
    • 85047687155 scopus 로고    scopus 로고
    • Expression of caveolin-1 and caveolin-2 in urothelial carcinoma of the urinary bladder correlates with tumor grade and squamous differentiation
    • Fong A., Garcia E., et al. Expression of caveolin-1 and caveolin-2 in urothelial carcinoma of the urinary bladder correlates with tumor grade and squamous differentiation. Am. J. Clin. Pathol. 2003, 120:93-100.
    • (2003) Am. J. Clin. Pathol. , vol.120 , pp. 93-100
    • Fong, A.1    Garcia, E.2
  • 50
    • 0035740002 scopus 로고    scopus 로고
    • Integrins and prostate cancer metastases
    • Fornaro M., Manes T., et al. Integrins and prostate cancer metastases. Cancer Metastasis Rev. 2001, 20:321-331.
    • (2001) Cancer Metastasis Rev. , vol.20 , pp. 321-331
    • Fornaro, M.1    Manes, T.2
  • 51
    • 51049114515 scopus 로고    scopus 로고
    • A tal(in) of cell spreading
    • Frame M., Norman J. A tal(in) of cell spreading. Nat. Cell Biol. 2008, 10:1017-1019.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 1017-1019
    • Frame, M.1    Norman, J.2
  • 52
    • 33846604223 scopus 로고    scopus 로고
    • A randomized multi-center phase II trial of the angiogenesis inhibitor Cilengitide (EMD 121974) and gemcitabine compared with gemcitabine alone in advanced unresectable pancreatic cancer
    • Friess H., Langrehr J.M., et al. A randomized multi-center phase II trial of the angiogenesis inhibitor Cilengitide (EMD 121974) and gemcitabine compared with gemcitabine alone in advanced unresectable pancreatic cancer. BMC Cancer 2006, 6:285.
    • (2006) BMC Cancer , vol.6 , pp. 285
    • Friess, H.1    Langrehr, J.M.2
  • 53
    • 0029739950 scopus 로고    scopus 로고
    • Control of adhesion-dependent cell survival by focal adhesion kinase
    • Frisch S.M., Vuori K., et al. Control of adhesion-dependent cell survival by focal adhesion kinase. J. Cell Biol. 1996, 134:793-799.
    • (1996) J. Cell Biol. , vol.134 , pp. 793-799
    • Frisch, S.M.1    Vuori, K.2
  • 54
    • 0036121308 scopus 로고    scopus 로고
    • Hakai, a c-Cbl-like protein, ubiquitinates and induces endocytosis of the E-cadherin complex
    • Fujita Y., Krause G., et al. Hakai, a c-Cbl-like protein, ubiquitinates and induces endocytosis of the E-cadherin complex. Nat. Cell Biol. 2002, 4:222-231.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 222-231
    • Fujita, Y.1    Krause, G.2
  • 55
    • 0037238844 scopus 로고    scopus 로고
    • Structural determinants of integrin recognition by talin
    • Garcia-Alvarez B., de Pereda J.M., et al. Structural determinants of integrin recognition by talin. Mol. Cell 2003, 11:49-58.
    • (2003) Mol. Cell , vol.11 , pp. 49-58
    • Garcia-Alvarez, B.1    de Pereda, J.M.2
  • 56
    • 31544446659 scopus 로고    scopus 로고
    • Doxazosin induces apoptosis of benign and malignant prostate cells via a death receptor-mediated pathway
    • Garrison J.B., Kyprianou N. Doxazosin induces apoptosis of benign and malignant prostate cells via a death receptor-mediated pathway. Cancer Res. 2006, 66:464-472.
    • (2006) Cancer Res. , vol.66 , pp. 464-472
    • Garrison, J.B.1    Kyprianou, N.2
  • 57
    • 37049031489 scopus 로고    scopus 로고
    • Novel quinazoline-based compounds impair prostate tumorigenesis by targeting tumor vascularity
    • Garrison J.B., Shaw Y.J., et al. Novel quinazoline-based compounds impair prostate tumorigenesis by targeting tumor vascularity. Cancer Res. 2007, 67:11344-11352.
    • (2007) Cancer Res. , vol.67 , pp. 11344-11352
    • Garrison, J.B.1    Shaw, Y.J.2
  • 58
    • 0033794569 scopus 로고    scopus 로고
    • Complexity and specificity of integrin signalling
    • Giancotti F.G. Complexity and specificity of integrin signalling. Nat. Cell Biol. 2000, 2:E13-E14.
    • (2000) Nat. Cell Biol. , vol.2
    • Giancotti, F.G.1
  • 59
  • 60
    • 0033373537 scopus 로고    scopus 로고
    • Vimentin contributes to human mammary epithelial cell migration
    • Gilles C., Polette M., et al. Vimentin contributes to human mammary epithelial cell migration. J. Cell Sci. 1999, 112:4615-4625.
    • (1999) J. Cell Sci. , vol.112 , pp. 4615-4625
    • Gilles, C.1    Polette, M.2
  • 61
    • 77956510396 scopus 로고    scopus 로고
    • The central region of talin has a unique fold that binds vinculin and actin
    • Gingras A.R., Bate N., et al. The central region of talin has a unique fold that binds vinculin and actin. J. Biol. Chem. 2010, 285:29577-29587.
    • (2010) J. Biol. Chem. , vol.285 , pp. 29577-29587
    • Gingras, A.R.1    Bate, N.2
  • 62
    • 3543127788 scopus 로고    scopus 로고
    • Selective modulation of type 1 insulin-like growth factor receptor signaling and functions by beta1 integrins
    • Goel H.L., Fornaro M., et al. Selective modulation of type 1 insulin-like growth factor receptor signaling and functions by beta1 integrins. J. Cell Biol. 2004, 166:407-418.
    • (2004) J. Cell Biol. , vol.166 , pp. 407-418
    • Goel, H.L.1    Fornaro, M.2
  • 63
    • 53849143245 scopus 로고    scopus 로고
    • Integrins in prostate cancer progression
    • Goel H.L., Li J., et al. Integrins in prostate cancer progression. Endocr. Relat. Cancer 2008, 15:657-664.
    • (2008) Endocr. Relat. Cancer , vol.15 , pp. 657-664
    • Goel, H.L.1    Li, J.2
  • 64
    • 46149093439 scopus 로고    scopus 로고
    • Structural basis for the autoinhibition of talin in regulating integrin activation
    • Goksoy E., Ma Y.Q., et al. Structural basis for the autoinhibition of talin in regulating integrin activation. Mol. Cell 2008, 31:124-133.
    • (2008) Mol. Cell , vol.31 , pp. 124-133
    • Goksoy, E.1    Ma, Y.Q.2
  • 65
    • 0028067413 scopus 로고
    • Native talin is a dumbbell-shaped homodimer when it interacts with actin
    • Goldmann W.H., Bremer A., et al. Native talin is a dumbbell-shaped homodimer when it interacts with actin. J. Struct. Biol. 1994, 112:3-10.
    • (1994) J. Struct. Biol. , vol.112 , pp. 3-10
    • Goldmann, W.H.1    Bremer, A.2
  • 66
    • 42049092980 scopus 로고    scopus 로고
    • Insulin-like growth factor-I-dependent up-regulation of ZEB1 drives epithelial-to-mesenchymal transition in human prostate cancer cells
    • Graham T.R., Zhau H.E., et al. Insulin-like growth factor-I-dependent up-regulation of ZEB1 drives epithelial-to-mesenchymal transition in human prostate cancer cells. Cancer Res. 2008, 68:2479-2488.
    • (2008) Cancer Res. , vol.68 , pp. 2479-2488
    • Graham, T.R.1    Zhau, H.E.2
  • 67
    • 75749103348 scopus 로고    scopus 로고
    • Src signaling in cancer invasion
    • Guarino M. Src signaling in cancer invasion. J. Cell. Physiol. 2010, 223:14-26.
    • (2010) J. Cell. Physiol. , vol.223 , pp. 14-26
    • Guarino, M.1
  • 68
    • 5044238876 scopus 로고    scopus 로고
    • Integrin signalling during tumour progression
    • Guo W., Giancotti F.G. Integrin signalling during tumour progression. Nat. Rev. Mol. Cell Biol. 2004, 5:816-826.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 816-826
    • Guo, W.1    Giancotti, F.G.2
  • 69
    • 33751252276 scopus 로고    scopus 로고
    • Cancer metastasis: building a framework
    • Gupta G.P., Massague J. Cancer metastasis: building a framework. Cell 2006, 127:679-695.
    • (2006) Cell , vol.127 , pp. 679-695
    • Gupta, G.P.1    Massague, J.2
  • 70
    • 0029803150 scopus 로고    scopus 로고
    • Cell adhesion molecules mediate radiation-induced leukocyte adhesion to the vascular endothelium
    • Hallahan D., Kuchibhotla J., et al. Cell adhesion molecules mediate radiation-induced leukocyte adhesion to the vascular endothelium. Cancer Res. 1996, 56:5150-5155.
    • (1996) Cancer Res. , vol.56 , pp. 5150-5155
    • Hallahan, D.1    Kuchibhotla, J.2
  • 71
    • 57549092526 scopus 로고    scopus 로고
    • The tumour microenvironment: a novel target for cancer therapy
    • Hanna E., Quick J., et al. The tumour microenvironment: a novel target for cancer therapy. Oral Dis. 2009, 15:8-17.
    • (2009) Oral Dis. , vol.15 , pp. 8-17
    • Hanna, E.1    Quick, J.2
  • 72
    • 35148888509 scopus 로고    scopus 로고
    • Effect of alpha1-adrenoceptor antagonist exposure on prostate cancer incidence: an observational cohort study
    • Harris A.M., Warner B.W., et al. Effect of alpha1-adrenoceptor antagonist exposure on prostate cancer incidence: an observational cohort study. J. Urol. 2007, 178:2176-2180.
    • (2007) J. Urol. , vol.178 , pp. 2176-2180
    • Harris, A.M.1    Warner, B.W.2
  • 73
    • 0031016323 scopus 로고    scopus 로고
    • Experimental co-expression of vimentin and keratin intermediate filaments in human breast cancer cells results in phenotypic interconversion and increased invasive behavior
    • Hendrix M.J., Seftor E.A., et al. Experimental co-expression of vimentin and keratin intermediate filaments in human breast cancer cells results in phenotypic interconversion and increased invasive behavior. Am. J. Pathol. 1997, 150:483-495.
    • (1997) Am. J. Pathol. , vol.150 , pp. 483-495
    • Hendrix, M.J.1    Seftor, E.A.2
  • 74
    • 0022534722 scopus 로고
    • Interaction of plasma membrane fibronectin receptor with talin-a transmembrane linkage
    • Horwitz A., Duggan K., et al. Interaction of plasma membrane fibronectin receptor with talin-a transmembrane linkage. Nature 1986, 320:531-533.
    • (1986) Nature , vol.320 , pp. 531-533
    • Horwitz, A.1    Duggan, K.2
  • 75
    • 24644480749 scopus 로고    scopus 로고
    • Molecular requirements for epithelial-mesenchymal transition during tumor progression
    • Huber M.A., Kraut N., et al. Molecular requirements for epithelial-mesenchymal transition during tumor progression. Curr. Opin. Cell Biol. 2005, 17:548-558.
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 548-558
    • Huber, M.A.1    Kraut, N.2
  • 76
    • 0023666065 scopus 로고
    • Integrins: a family of cell surface receptors
    • Hynes R.O. Integrins: a family of cell surface receptors. Cell 1987, 48:549-554.
    • (1987) Cell , vol.48 , pp. 549-554
    • Hynes, R.O.1
  • 77
    • 70849099495 scopus 로고    scopus 로고
    • The extracellular matrix: not just pretty fibrils
    • Hynes R.O. The extracellular matrix: not just pretty fibrils. Science 2009, 326:1216-1219.
    • (2009) Science , vol.326 , pp. 1216-1219
    • Hynes, R.O.1
  • 78
    • 0032725309 scopus 로고    scopus 로고
    • Divergent signaling pathways link focal adhesion kinase to mitogen-activated protein kinase cascades. Evidence for a role of paxillin in c-Jun NH(2)-terminal kinase activation
    • Igishi T., Fukuhara S., et al. Divergent signaling pathways link focal adhesion kinase to mitogen-activated protein kinase cascades. Evidence for a role of paxillin in c-Jun NH(2)-terminal kinase activation. J. Biol. Chem. 1999, 274:30738-30746.
    • (1999) J. Biol. Chem. , vol.274 , pp. 30738-30746
    • Igishi, T.1    Fukuhara, S.2
  • 79
    • 0031471321 scopus 로고    scopus 로고
    • Overexpression of normal c-Src in poorly metastatic human colon cancer cells enhances primary tumor growth but not metastatic potential
    • Irby R., Mao W., et al. Overexpression of normal c-Src in poorly metastatic human colon cancer cells enhances primary tumor growth but not metastatic potential. Cell Growth Differ. 1997, 8:1287-1295.
    • (1997) Cell Growth Differ. , vol.8 , pp. 1287-1295
    • Irby, R.1    Mao, W.2
  • 80
    • 39149121168 scopus 로고    scopus 로고
    • Paxillin is a target for somatic mutations in lung cancer: implications for cell growth and invasion
    • Jagadeeswaran R., Surawska H., et al. Paxillin is a target for somatic mutations in lung cancer: implications for cell growth and invasion. Cancer Res. 2008, 68:132-142.
    • (2008) Cancer Res. , vol.68 , pp. 132-142
    • Jagadeeswaran, R.1    Surawska, H.2
  • 81
    • 1542269303 scopus 로고    scopus 로고
    • Integrins: roles in cancer development and as treatment targets
    • Jin H., Varner J. Integrins: roles in cancer development and as treatment targets. Br. J. Cancer 2004, 90:561-565.
    • (2004) Br. J. Cancer , vol.90 , pp. 561-565
    • Jin, H.1    Varner, J.2
  • 82
    • 33646593786 scopus 로고    scopus 로고
    • Modifying the soil to affect the seed: role of stromal-derived matrix metalloproteinases in cancer progression
    • Jodele S., Blavier L., et al. Modifying the soil to affect the seed: role of stromal-derived matrix metalloproteinases in cancer progression. Cancer Metastasis Rev. 2006, 25:35-43.
    • (2006) Cancer Metastasis Rev. , vol.25 , pp. 35-43
    • Jodele, S.1    Blavier, L.2
  • 83
    • 3042658327 scopus 로고    scopus 로고
    • Integrin regulation of cell signalling and motility
    • Juliano R.L., Reddig P., et al. Integrin regulation of cell signalling and motility. Biochem. Soc. Trans. 2004, 32:443-446.
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 443-446
    • Juliano, R.L.1    Reddig, P.2
  • 84
    • 65549164757 scopus 로고    scopus 로고
    • Microtubule depolymerizing vascular disrupting agents: novel therapeutic agents for oncology and other pathologies
    • Kanthou C., Tozer G.M. Microtubule depolymerizing vascular disrupting agents: novel therapeutic agents for oncology and other pathologies. Int. J. Exp. Pathol. 2009, 903:284-294.
    • (2009) Int. J. Exp. Pathol. , vol.903 , pp. 284-294
    • Kanthou, C.1    Tozer, G.M.2
  • 85
    • 0034004457 scopus 로고    scopus 로고
    • RAP1 is a potent activation signal for leukocyte function-associated antigen 1 distinct from protein kinase C and phosphatidylinositol-3-OH kinase
    • Katagiri K., Hattori M., et al. RAP1 is a potent activation signal for leukocyte function-associated antigen 1 distinct from protein kinase C and phosphatidylinositol-3-OH kinase. Mol. Cell. Biol. 2000, 20:1956-1969.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1956-1969
    • Katagiri, K.1    Hattori, M.2
  • 86
    • 0036146452 scopus 로고    scopus 로고
    • RAP1 functions as a key regulator of T-cell and antigen-presenting cell interactions and modulates T-cell responses
    • Katagiri K., Hattori M., et al. RAP1 functions as a key regulator of T-cell and antigen-presenting cell interactions and modulates T-cell responses. Mol. Cell. Biol. 2002, 22:1001-1015.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1001-1015
    • Katagiri, K.1    Hattori, M.2
  • 87
    • 0033559617 scopus 로고    scopus 로고
    • Rapid induction of cytokine and E-selectin expression in the liver in response to metastatic tumor cells
    • Khatib A.M., Kontogiannea M., et al. Rapid induction of cytokine and E-selectin expression in the liver in response to metastatic tumor cells. Cancer Res. 1999, 59:1356-1361.
    • (1999) Cancer Res. , vol.59 , pp. 1356-1361
    • Khatib, A.M.1    Kontogiannea, M.2
  • 88
    • 0033566695 scopus 로고    scopus 로고
    • Cell cycle arrest and inhibition of anoikis by galectin-3 in human breast epithelial cells
    • Kim H.R., Lin H.M., et al. Cell cycle arrest and inhibition of anoikis by galectin-3 in human breast epithelial cells. Cancer Res. 1999, 59:4148-4154.
    • (1999) Cancer Res. , vol.59 , pp. 4148-4154
    • Kim, H.R.1    Lin, H.M.2
  • 89
    • 0042681786 scopus 로고    scopus 로고
    • Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins
    • Kim M., Carman C.V., et al. Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins. Science 2003, 301:1720-1725.
    • (2003) Science , vol.301 , pp. 1720-1725
    • Kim, M.1    Carman, C.V.2
  • 90
    • 70349758510 scopus 로고    scopus 로고
    • Src kinases as therapeutic targets for cancer
    • Kim L.C., Song L., et al. Src kinases as therapeutic targets for cancer. Nat. Rev. Clin. Oncol. 2009, 6:587-595.
    • (2009) Nat. Rev. Clin. Oncol. , vol.6 , pp. 587-595
    • Kim, L.C.1    Song, L.2
  • 92
    • 33748951893 scopus 로고    scopus 로고
    • The impact of cell adhesion changes on proliferation and survival during prostate cancer development and progression
    • Knudsen B.S., Miranti C.K. The impact of cell adhesion changes on proliferation and survival during prostate cancer development and progression. J. Cell. Biochem. 2006, 99:345-361.
    • (2006) J. Cell. Biochem. , vol.99 , pp. 345-361
    • Knudsen, B.S.1    Miranti, C.K.2
  • 93
    • 0036395953 scopus 로고    scopus 로고
    • Rearrangement of integrins in avidity regulation by leukocytes
    • Kucik D.F. Rearrangement of integrins in avidity regulation by leukocytes. Immunol. Res. 2002, 26:199-206.
    • (2002) Immunol. Res. , vol.26 , pp. 199-206
    • Kucik, D.F.1
  • 94
    • 0037376011 scopus 로고    scopus 로고
    • Doxazosin and terazosin suppress prostate growth by inducing apoptosis: clinical significance
    • Kyprianou N. Doxazosin and terazosin suppress prostate growth by inducing apoptosis: clinical significance. J. Urol. 2003, 169:1520-1525.
    • (2003) J. Urol. , vol.169 , pp. 1520-1525
    • Kyprianou, N.1
  • 95
    • 71349084602 scopus 로고    scopus 로고
    • Apoptosis induction by doxazosin and other quinazoline alpha1-adrenoceptor antagonists: a new mechanism for cancer treatment?
    • Kyprianou N., Vaughan T.B., et al. Apoptosis induction by doxazosin and other quinazoline alpha1-adrenoceptor antagonists: a new mechanism for cancer treatment?. Naunyn Schmiedebergs Arch. Pharmacol. 2009, 380:473-477.
    • (2009) Naunyn Schmiedebergs Arch. Pharmacol. , vol.380 , pp. 473-477
    • Kyprianou, N.1    Vaughan, T.B.2
  • 96
    • 5044241734 scopus 로고    scopus 로고
    • RIAM, an Ena/VASP and Profilin ligand, interacts with RAP1-GTP and mediates RAP1-induced adhesion
    • Lafuente E.M., van Puijenbroek A.A., et al. RIAM, an Ena/VASP and Profilin ligand, interacts with RAP1-GTP and mediates RAP1-induced adhesion. Dev. Cell 2004, 7:585-595.
    • (2004) Dev. Cell , vol.7 , pp. 585-595
    • Lafuente, E.M.1    van Puijenbroek, A.A.2
  • 97
    • 4143099262 scopus 로고    scopus 로고
    • Tumor galectinology: insights into the complex network of a family of endogenous lectins
    • Lahm H., Andre S., et al. Tumor galectinology: insights into the complex network of a family of endogenous lectins. Glycoconj. J. 2004, 20:227-238.
    • (2004) Glycoconj. J. , vol.20 , pp. 227-238
    • Lahm, H.1    Andre, S.2
  • 98
    • 57049169143 scopus 로고    scopus 로고
    • Kindlins: essential regulators of integrin signalling and cell-matrix adhesion
    • Larjava H., Plow E.F., et al. Kindlins: essential regulators of integrin signalling and cell-matrix adhesion. EMBO Rep. 2008, 9:1203-1208.
    • (2008) EMBO Rep. , vol.9 , pp. 1203-1208
    • Larjava, H.1    Plow, E.F.2
  • 99
    • 0029916875 scopus 로고    scopus 로고
    • Outside-in integrin signal transduction. Alpha IIb beta 3-(GP IIb IIIa) tyrosine phosphorylation induced by platelet aggregation
    • Law D.A., Nannizzi-Alaimo L., et al. Outside-in integrin signal transduction. Alpha IIb beta 3-(GP IIb IIIa) tyrosine phosphorylation induced by platelet aggregation. J. Biol. Chem. 1996, 271:10811-10815.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10811-10815
    • Law, D.A.1    Nannizzi-Alaimo, L.2
  • 100
    • 1642307942 scopus 로고    scopus 로고
    • Integrin-linked kinase function is required for transforming growth factor beta-mediated epithelial to mesenchymal transition
    • Lee Y.I., Kwon Y.J., et al. Integrin-linked kinase function is required for transforming growth factor beta-mediated epithelial to mesenchymal transition. Biochem. Biophys. Res. Commun. 2004, 316:997-1001.
    • (2004) Biochem. Biophys. Res. Commun. , vol.316 , pp. 997-1001
    • Lee, Y.I.1    Kwon, Y.J.2
  • 101
    • 64149100431 scopus 로고    scopus 로고
    • RIAM activates integrins by linking talin to ras GTPase membrane-targeting sequences
    • Lee H.S., Lim C.J., et al. RIAM activates integrins by linking talin to ras GTPase membrane-targeting sequences. J. Biol. Chem. 2009, 284:5119-5127.
    • (2009) J. Biol. Chem. , vol.284 , pp. 5119-5127
    • Lee, H.S.1    Lim, C.J.2
  • 102
    • 61449220945 scopus 로고    scopus 로고
    • Genetic and cell biological analysis of integrin outside-in signaling
    • Legate K.R., Wickstrom S.A., et al. Genetic and cell biological analysis of integrin outside-in signaling. Genes Dev. 2009, 23:397-418.
    • (2009) Genes Dev. , vol.23 , pp. 397-418
    • Legate, K.R.1    Wickstrom, S.A.2
  • 103
    • 0029054284 scopus 로고
    • Mapping in vivo associations of cytoplasmic proteins with integrin beta 1 cytoplasmic domain mutants
    • Lewis J.M., Schwartz M.A. Mapping in vivo associations of cytoplasmic proteins with integrin beta 1 cytoplasmic domain mutants. Mol. Biol. Cell 1995, 6:151-160.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 151-160
    • Lewis, J.M.1    Schwartz, M.A.2
  • 104
    • 0345491598 scopus 로고    scopus 로고
    • Caveolin-1 maintains activated Akt in prostate cancer cells through scaffolding domain binding site interactions with and inhibition of serine/threonine protein phosphatases PP1 and PP2A
    • Li L., Ren C.H., et al. Caveolin-1 maintains activated Akt in prostate cancer cells through scaffolding domain binding site interactions with and inhibition of serine/threonine protein phosphatases PP1 and PP2A. Mol. Cell. Biol. 2003, 23:9389-9404.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 9389-9404
    • Li, L.1    Ren, C.H.2
  • 105
    • 0038644597 scopus 로고    scopus 로고
    • Activation of integrin alphaIIbbeta3 by modulation of transmembrane helix associations
    • Li R., Mitra N., et al. Activation of integrin alphaIIbbeta3 by modulation of transmembrane helix associations. Science 2003, 300:795-798.
    • (2003) Science , vol.300 , pp. 795-798
    • Li, R.1    Mitra, N.2
  • 106
    • 76349090440 scopus 로고    scopus 로고
    • Fibronectin promotes tyrosine phosphorylation of paxillin and cell invasiveness in the gastric cancer cell line AGS
    • Li D., Ding J., et al. Fibronectin promotes tyrosine phosphorylation of paxillin and cell invasiveness in the gastric cancer cell line AGS. Tumori 2009, 95:769-779.
    • (2009) Tumori , vol.95 , pp. 769-779
    • Li, D.1    Ding, J.2
  • 107
    • 48849089827 scopus 로고    scopus 로고
    • FERM control of FAK function: implications for cancer therapy
    • Lim S.T., Mikolon D., et al. FERM control of FAK function: implications for cancer therapy. Cell Cycle 2008, 7:2306-2314.
    • (2008) Cell Cycle , vol.7 , pp. 2306-2314
    • Lim, S.T.1    Mikolon, D.2
  • 108
    • 0037038412 scopus 로고    scopus 로고
    • Type I gamma phosphatidylinositol phosphate kinase targets and regulates focal adhesions
    • Ling K., Doughman R.L., et al. Type I gamma phosphatidylinositol phosphate kinase targets and regulates focal adhesions. Nature 2002, 420:89-93.
    • (2002) Nature , vol.420 , pp. 89-93
    • Ling, K.1    Doughman, R.L.2
  • 109
    • 0347993703 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of type I gamma phosphatidylinositol phosphate kinase by Src regulates an integrin-talin switch
    • Ling K., Doughman R.L., et al. Tyrosine phosphorylation of type I gamma phosphatidylinositol phosphate kinase by Src regulates an integrin-talin switch. J. Cell Biol. 2003, 163:1339-1349.
    • (2003) J. Cell Biol. , vol.163 , pp. 1339-1349
    • Ling, K.1    Doughman, R.L.2
  • 110
    • 4344687434 scopus 로고    scopus 로고
    • Anoikis: cancer and the homeless cell
    • Liotta L.A., Kohn E. Anoikis: cancer and the homeless cell. Nature 2004, 430:973-974.
    • (2004) Nature , vol.430 , pp. 973-974
    • Liotta, L.A.1    Kohn, E.2
  • 111
    • 0033731119 scopus 로고    scopus 로고
    • Integrin cytoplasmic domain-binding proteins
    • Liu S., Calderwood D.A., et al. Integrin cytoplasmic domain-binding proteins. J. Cell Sci. 2000, 113:3563-3571.
    • (2000) J. Cell Sci. , vol.113 , pp. 3563-3571
    • Liu, S.1    Calderwood, D.A.2
  • 112
    • 35148832569 scopus 로고    scopus 로고
    • Epidermal growth factor receptor cooperates with signal transducer and activator of transcription 3 to induce epithelial-mesenchymal transition in cancer cells via up-regulation of TWIST gene expression
    • Lo H.W., Hsu S.C., et al. Epidermal growth factor receptor cooperates with signal transducer and activator of transcription 3 to induce epithelial-mesenchymal transition in cancer cells via up-regulation of TWIST gene expression. Cancer Res. 2007, 67:9066-9076.
    • (2007) Cancer Res. , vol.67 , pp. 9066-9076
    • Lo, H.W.1    Hsu, S.C.2
  • 113
    • 43149085289 scopus 로고    scopus 로고
    • Kindlin-2 (Mig-2): a co-activator of beta3 integrins
    • Ma Y.Q., Qin J., et al. Kindlin-2 (Mig-2): a co-activator of beta3 integrins. J. Cell Biol. 2008, 181:439-446.
    • (2008) J. Cell Biol. , vol.181 , pp. 439-446
    • Ma, Y.Q.1    Qin, J.2
  • 114
    • 0037076211 scopus 로고    scopus 로고
    • C. elegans PAT-4/ILK functions as an adaptor protein within integrin adhesion complexes
    • Mackinnon A.C., Qadota H., et al. C. elegans PAT-4/ILK functions as an adaptor protein within integrin adhesion complexes. Curr. Biol. 2002, 12:787-797.
    • (2002) Curr. Biol. , vol.12 , pp. 787-797
    • Mackinnon, A.C.1    Qadota, H.2
  • 115
    • 0035877656 scopus 로고    scopus 로고
    • Conformation, localization, and integrin binding of talin depend on its interaction with phosphoinositides
    • Martel V., Racaud-Sultan C., et al. Conformation, localization, and integrin binding of talin depend on its interaction with phosphoinositides. J. Biol. Chem. 2001, 276:21217-21227.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21217-21227
    • Martel, V.1    Racaud-Sultan, C.2
  • 116
    • 34548587031 scopus 로고    scopus 로고
    • A chemical screen identifies anisomycin as an anoikis sensitizer that functions by decreasing FLIP protein synthesis
    • Mawji I.A., Simpson C.D., et al. A chemical screen identifies anisomycin as an anoikis sensitizer that functions by decreasing FLIP protein synthesis. Cancer Res. 2007, 67:8307-8315.
    • (2007) Cancer Res. , vol.67 , pp. 8307-8315
    • Mawji, I.A.1    Simpson, C.D.2
  • 117
    • 34447275249 scopus 로고    scopus 로고
    • Critical role for Fas-associated death domain-like interleukin-1-converting enzyme-like inhibitory protein in anoikis resistance and distant tumor formation
    • Mawji I.A., Simpson C.D., et al. Critical role for Fas-associated death domain-like interleukin-1-converting enzyme-like inhibitory protein in anoikis resistance and distant tumor formation. J. Natl Cancer Inst. 2007, 99:811-822.
    • (2007) J. Natl Cancer Inst. , vol.99 , pp. 811-822
    • Mawji, I.A.1    Simpson, C.D.2
  • 118
    • 34249821363 scopus 로고    scopus 로고
    • Structure of the PTB domain of tensin1 and a model for its recruitment to fibrillar adhesions
    • Mccleverty C.J., Lin D.C., et al. Structure of the PTB domain of tensin1 and a model for its recruitment to fibrillar adhesions. Protein Sci. 2007, 16:1223-1229.
    • (2007) Protein Sci. , vol.16 , pp. 1223-1229
    • Mccleverty, C.J.1    Lin, D.C.2
  • 119
    • 27744563296 scopus 로고    scopus 로고
    • Phase I trial of a monoclonal antibody specific for alphavbeta3 integrin (MEDI-522) in patients with advanced malignancies, including an assessment of effect on tumor perfusion
    • McNeel D.G., Eickhoff J., et al. Phase I trial of a monoclonal antibody specific for alphavbeta3 integrin (MEDI-522) in patients with advanced malignancies, including an assessment of effect on tumor perfusion. Clin. Cancer Res. 2005, 11:7851-7860.
    • (2005) Clin. Cancer Res. , vol.11 , pp. 7851-7860
    • McNeel, D.G.1    Eickhoff, J.2
  • 120
    • 77953190164 scopus 로고    scopus 로고
    • The insulin-like growth factor receptor I promotes motility and invasion of bladder cancer cells through Akt- and mitogen-activated protein kinase-dependent activation of paxillin
    • Metalli D., Lovat F., et al. The insulin-like growth factor receptor I promotes motility and invasion of bladder cancer cells through Akt- and mitogen-activated protein kinase-dependent activation of paxillin. Am. J. Pathol. 2010, 176:2997-3006.
    • (2010) Am. J. Pathol. , vol.176 , pp. 2997-3006
    • Metalli, D.1    Lovat, F.2
  • 122
    • 44149105411 scopus 로고    scopus 로고
    • Kindlin-2 controls bidirectional signaling of integrins
    • Montanez E., Ussar S., et al. Kindlin-2 controls bidirectional signaling of integrins. Genes Dev. 2008, 22:1325-1330.
    • (2008) Genes Dev. , vol.22 , pp. 1325-1330
    • Montanez, E.1    Ussar, S.2
  • 124
    • 66149128873 scopus 로고    scopus 로고
    • The tail of integrins, talin, and kindlins
    • Moser M., Legate K.R., et al. The tail of integrins, talin, and kindlins. Science 2009, 324:895-899.
    • (2009) Science , vol.324 , pp. 895-899
    • Moser, M.1    Legate, K.R.2
  • 125
    • 34247504971 scopus 로고    scopus 로고
    • Phase I evaluation of a fully human anti-alphav integrin monoclonal antibody (CNTO 95) in patients with advanced solid tumors
    • Mullamitha S.A., Ton N.C., et al. Phase I evaluation of a fully human anti-alphav integrin monoclonal antibody (CNTO 95) in patients with advanced solid tumors. Clin. Cancer Res. 2007, 13:2128-2135.
    • (2007) Clin. Cancer Res. , vol.13 , pp. 2128-2135
    • Mullamitha, S.A.1    Ton, N.C.2
  • 126
    • 34249087162 scopus 로고    scopus 로고
    • Phase I and correlative biology study of cilengitide in patients with recurrent malignant glioma
    • Nabors L.B., Mikkelsen T., et al. Phase I and correlative biology study of cilengitide in patients with recurrent malignant glioma. J. Clin. Oncol. 2007, 25:1651-1657.
    • (2007) J. Clin. Oncol. , vol.25 , pp. 1651-1657
    • Nabors, L.B.1    Mikkelsen, T.2
  • 127
    • 0025881470 scopus 로고
    • Cloning of a complementary DNA for a protein-tyrosine kinase that specifically phosphorylates a negative regulatory site of p60c-src
    • Nada S., Okada M., et al. Cloning of a complementary DNA for a protein-tyrosine kinase that specifically phosphorylates a negative regulatory site of p60c-src. Nature 1991, 351:69-72.
    • (1991) Nature , vol.351 , pp. 69-72
    • Nada, S.1    Okada, M.2
  • 128
    • 0033888016 scopus 로고    scopus 로고
    • Galectin-3 induces endothelial cell morphogenesis and angiogenesis
    • Nangia-Makker P., Honjo Y., et al. Galectin-3 induces endothelial cell morphogenesis and angiogenesis. Am. J. Pathol. 2000, 156:899-909.
    • (2000) Am. J. Pathol. , vol.156 , pp. 899-909
    • Nangia-Makker, P.1    Honjo, Y.2
  • 129
    • 37549029679 scopus 로고    scopus 로고
    • Loss of talin1 in platelets abrogates integrin activation, platelet aggregation, and thrombus formation in vitro and in vivo
    • Nieswandt B., Moser M., et al. Loss of talin1 in platelets abrogates integrin activation, platelet aggregation, and thrombus formation in vitro and in vivo. J. Exp. Med. 2007, 204:3113-3118.
    • (2007) J. Exp. Med. , vol.204 , pp. 3113-3118
    • Nieswandt, B.1    Moser, M.2
  • 130
    • 3242791922 scopus 로고    scopus 로고
    • Galectins and urological cancer
    • Oka N., Takenaka Y., et al. Galectins and urological cancer. J. Cell. Biochem. 2004, 91:118-124.
    • (2004) J. Cell. Biochem. , vol.91 , pp. 118-124
    • Oka, N.1    Takenaka, Y.2
  • 131
    • 0035126590 scopus 로고    scopus 로고
    • Parvin, a 42kDa focal adhesion protein, related to the alpha-actinin superfamily
    • Olski T.M., Noegel A.A., et al. Parvin, a 42kDa focal adhesion protein, related to the alpha-actinin superfamily. J. Cell Sci. 2001, 114:525-538.
    • (2001) J. Cell Sci. , vol.114 , pp. 525-538
    • Olski, T.M.1    Noegel, A.A.2
  • 132
    • 0033598162 scopus 로고    scopus 로고
    • Exogenous expression of beta-catenin regulates contact inhibition, anchorage-independent growth, anoikis, and radiation-induced cell cycle arrest
    • Orford K., Orford C.C., et al. Exogenous expression of beta-catenin regulates contact inhibition, anchorage-independent growth, anoikis, and radiation-induced cell cycle arrest. J. Cell Biol. 1999, 146:855-868.
    • (1999) J. Cell Biol. , vol.146 , pp. 855-868
    • Orford, K.1    Orford, C.C.2
  • 133
    • 47549089080 scopus 로고    scopus 로고
    • Matrix metalloproteinases stimulate epithelial-mesenchymal transition during tumor development
    • Orlichenko L.S., Radisky D.C. Matrix metalloproteinases stimulate epithelial-mesenchymal transition during tumor development. Clin. Exp. Metastasis 2008, 25:593-600.
    • (2008) Clin. Exp. Metastasis , vol.25 , pp. 593-600
    • Orlichenko, L.S.1    Radisky, D.C.2
  • 134
    • 0026331047 scopus 로고
    • Modulation of the affinity of integrin alpha IIb beta 3 (GPIIb-IIIa) by the cytoplasmic domain of alpha IIb
    • O'toole T.E., Mandelman D., et al. Modulation of the affinity of integrin alpha IIb beta 3 (GPIIb-IIIa) by the cytoplasmic domain of alpha IIb. Science 1991, 254:845-847.
    • (1991) Science , vol.254 , pp. 845-847
    • O'toole, T.E.1    Mandelman, D.2
  • 135
    • 0028285015 scopus 로고
    • Integrin cytoplasmic domains mediate inside-out signal transduction
    • O'toole T.E., Katagiri Y., et al. Integrin cytoplasmic domains mediate inside-out signal transduction. J. Cell Biol. 1994, 124:1047-1059.
    • (1994) J. Cell Biol. , vol.124 , pp. 1047-1059
    • O'toole, T.E.1    Katagiri, Y.2
  • 136
    • 0033002997 scopus 로고    scopus 로고
    • Induced focal adhesion kinase (FAK) expression in FAK-null cells enhances cell spreading and migration requiring both auto- and activation loop phosphorylation sites and inhibits adhesion-dependent tyrosine phosphorylation of Pyk2
    • Owen J.D., Ruest P.J., et al. Induced focal adhesion kinase (FAK) expression in FAK-null cells enhances cell spreading and migration requiring both auto- and activation loop phosphorylation sites and inhibits adhesion-dependent tyrosine phosphorylation of Pyk2. Mol. Cell. Biol. 1999, 19:4806-4818.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4806-4818
    • Owen, J.D.1    Ruest, P.J.2
  • 137
    • 70350028199 scopus 로고    scopus 로고
    • Apoptosis commitment and activation of mitochondrial Bax during anoikis is regulated by p38MAPK
    • Owens T.W., Valentijn A.J., et al. Apoptosis commitment and activation of mitochondrial Bax during anoikis is regulated by p38MAPK. Cell Death Differ. 2009, 16:1551-1562.
    • (2009) Cell Death Differ. , vol.16 , pp. 1551-1562
    • Owens, T.W.1    Valentijn, A.J.2
  • 138
    • 41949131361 scopus 로고    scopus 로고
    • An integrin phosphorylation switch: the effect of beta3 integrin tail phosphorylation on Dok1 and talin binding
    • Oxley C.L., Anthis N.J., et al. An integrin phosphorylation switch: the effect of beta3 integrin tail phosphorylation on Dok1 and talin binding. J. Biol. Chem. 2008, 283:5420-5426.
    • (2008) J. Biol. Chem. , vol.283 , pp. 5420-5426
    • Oxley, C.L.1    Anthis, N.J.2
  • 139
    • 4143083987 scopus 로고    scopus 로고
    • Activation of a vinculin-binding site in the talin rod involves rearrangement of a five-helix bundle
    • Papagrigoriou E., Gingras A.R., et al. Activation of a vinculin-binding site in the talin rod involves rearrangement of a five-helix bundle. EMBO J. 2004, 23:2942-2951.
    • (2004) EMBO J. , vol.23 , pp. 2942-2951
    • Papagrigoriou, E.1    Gingras, A.R.2
  • 140
    • 0037509990 scopus 로고    scopus 로고
    • Focal adhesion kinase: the first ten years
    • Parsons J.T. Focal adhesion kinase: the first ten years. J. Cell Sci. 2003, 116:1409-1416.
    • (2003) J. Cell Sci. , vol.116 , pp. 1409-1416
    • Parsons, J.T.1
  • 141
    • 0038792746 scopus 로고    scopus 로고
    • Quinazoline-based alpha 1-adrenoceptor antagonists induce prostate cancer cell apoptosis via TGF-beta signalling and I kappa B alpha induction
    • Partin J.V., Anglin I.E., et al. Quinazoline-based alpha 1-adrenoceptor antagonists induce prostate cancer cell apoptosis via TGF-beta signalling and I kappa B alpha induction. Br. J. Cancer 2003, 88:1615-1621.
    • (2003) Br. J. Cancer , vol.88 , pp. 1615-1621
    • Partin, J.V.1    Anglin, I.E.2
  • 142
    • 0034997845 scopus 로고    scopus 로고
    • Mitogen-activated protein (MAP) kinase pathways: regulation and physiological functions
    • Pearson G., Robinson F., et al. Mitogen-activated protein (MAP) kinase pathways: regulation and physiological functions. Endocr. Rev. 2001, 22:153-183.
    • (2001) Endocr. Rev. , vol.22 , pp. 153-183
    • Pearson, G.1    Robinson, F.2
  • 143
    • 0032510494 scopus 로고    scopus 로고
    • A causal role for E-cadherin in the transition from adenoma to carcinoma
    • Perl A.K., Wilgenbus P., et al. A causal role for E-cadherin in the transition from adenoma to carcinoma. Nature 1998, 392:190-193.
    • (1998) Nature , vol.392 , pp. 190-193
    • Perl, A.K.1    Wilgenbus, P.2
  • 144
    • 0038724824 scopus 로고    scopus 로고
    • The role of integrin-linked kinase (ILK) in cancer progression
    • Persad S., Dedhar S. The role of integrin-linked kinase (ILK) in cancer progression. Cancer Metastasis Rev. 2003, 22:375-384.
    • (2003) Cancer Metastasis Rev. , vol.22 , pp. 375-384
    • Persad, S.1    Dedhar, S.2
  • 145
    • 0034724443 scopus 로고    scopus 로고
    • Inhibition of integrin-linked kinase (ILK) suppresses activation of protein kinase B/Akt and induces cell cycle arrest and apoptosis of PTEN-mutant prostate cancer cells
    • Persad S., Attwell S., et al. Inhibition of integrin-linked kinase (ILK) suppresses activation of protein kinase B/Akt and induces cell cycle arrest and apoptosis of PTEN-mutant prostate cancer cells. Proc. Natl. Acad. Sci. USA 2000, 97:3207-3212.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3207-3212
    • Persad, S.1    Attwell, S.2
  • 146
    • 37549064277 scopus 로고    scopus 로고
    • Talin is required for integrin-mediated platelet function in hemostasis and thrombosis
    • Petrich B.G., Marchese P., et al. Talin is required for integrin-mediated platelet function in hemostasis and thrombosis. J. Exp. Med. 2007, 204:3103-3111.
    • (2007) J. Exp. Med. , vol.204 , pp. 3103-3111
    • Petrich, B.G.1    Marchese, P.2
  • 147
    • 7944233251 scopus 로고    scopus 로고
    • The interplay between Src and integrins in normal and tumor biology
    • Playford M.P., Schaller M.D. The interplay between Src and integrins in normal and tumor biology. Oncogene 2004, 23:7928-7946.
    • (2004) Oncogene , vol.23 , pp. 7928-7946
    • Playford, M.P.1    Schaller, M.D.2
  • 148
    • 0031779565 scopus 로고    scopus 로고
    • Association of fibroblastoid features with the invasive phenotype in human bronchial cancer cell lines
    • Polette M., Gilles C., et al. Association of fibroblastoid features with the invasive phenotype in human bronchial cancer cell lines. Clin. Exp. Metastasis 1998, 16:105-112.
    • (1998) Clin. Exp. Metastasis , vol.16 , pp. 105-112
    • Polette, M.1    Gilles, C.2
  • 149
    • 34249309574 scopus 로고    scopus 로고
    • Matrix metalloproteinase-induced epithelial-mesenchymal transition: tumor progression at Snail's pace
    • Przybylo J.A., Radisky D.C. Matrix metalloproteinase-induced epithelial-mesenchymal transition: tumor progression at Snail's pace. Int. J. Biochem. Cell Biol. 2007, 39:1082-1088.
    • (2007) Int. J. Biochem. Cell Biol. , vol.39 , pp. 1082-1088
    • Przybylo, J.A.1    Radisky, D.C.2
  • 150
  • 151
    • 77954861244 scopus 로고    scopus 로고
    • Matrix metalloproteinase-induced epithelial-mesenchymal transition in breast cancer
    • Radisky E.S., Radisky D.C. Matrix metalloproteinase-induced epithelial-mesenchymal transition in breast cancer. J. Mammary Gland Biol. Neoplasia 2010, 15:201-212.
    • (2010) J. Mammary Gland Biol. Neoplasia , vol.15 , pp. 201-212
    • Radisky, E.S.1    Radisky, D.C.2
  • 152
    • 0035515318 scopus 로고    scopus 로고
    • Caveolin-1 expression is associated with high-grade bladder cancer
    • Rajjayabun P.H., Garg S., et al. Caveolin-1 expression is associated with high-grade bladder cancer. Urology 2001, 58:811-814.
    • (2001) Urology , vol.58 , pp. 811-814
    • Rajjayabun, P.H.1    Garg, S.2
  • 153
    • 36148992199 scopus 로고    scopus 로고
    • Integrin trafficking and its role in cancer metastasis
    • Ramsay A.G., Marshall J.F., et al. Integrin trafficking and its role in cancer metastasis. Cancer Metastasis Rev. 2007, 26:567-578.
    • (2007) Cancer Metastasis Rev. , vol.26 , pp. 567-578
    • Ramsay, A.G.1    Marshall, J.F.2
  • 154
    • 0029947181 scopus 로고    scopus 로고
    • Requirement for phosphatidylinositol 3'-kinase activity in platelet-derived growth factor-stimulated tyrosine phosphorylation of p125 focal adhesion kinase and paxillin
    • Rankin S., Hooshmand-Rad R., et al. Requirement for phosphatidylinositol 3'-kinase activity in platelet-derived growth factor-stimulated tyrosine phosphorylation of p125 focal adhesion kinase and paxillin. J. Biol. Chem. 1996, 271:7829-7834.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7829-7834
    • Rankin, S.1    Hooshmand-Rad, R.2
  • 156
    • 29244478619 scopus 로고    scopus 로고
    • Anoikis and survival connections in the tumor microenvironment: is there a role in prostate cancer metastasis?
    • Rennebeck G., Martelli M., et al. Anoikis and survival connections in the tumor microenvironment: is there a role in prostate cancer metastasis?. Cancer Res. 2005, 65:11230-11235.
    • (2005) Cancer Res. , vol.65 , pp. 11230-11235
    • Rennebeck, G.1    Martelli, M.2
  • 157
    • 0034632070 scopus 로고    scopus 로고
    • The UNC-112 gene in Caenorhabditis elegans encodes a novel component of cell-matrix adhesion structures required for integrin localization in the muscle cell membrane
    • Rogalski T.M., Mullen G.P., et al. The UNC-112 gene in Caenorhabditis elegans encodes a novel component of cell-matrix adhesion structures required for integrin localization in the muscle cell membrane. J. Cell Biol. 2000, 150:253-264.
    • (2000) J. Cell Biol. , vol.150 , pp. 253-264
    • Rogalski, T.M.1    Mullen, G.P.2
  • 158
    • 77957923161 scopus 로고    scopus 로고
    • Targeted therapies of cancer: angiogenesis inhibition seems not enough
    • Roodink I., Leenders W.P. Targeted therapies of cancer: angiogenesis inhibition seems not enough. Cancer Lett. 2010, 299:1-10.
    • (2010) Cancer Lett. , vol.299 , pp. 1-10
    • Roodink, I.1    Leenders, W.P.2
  • 159
    • 70349861793 scopus 로고    scopus 로고
    • Plexin D1 is ubiquitously expressed on tumor vessels and tumor cells in solid malignancies
    • Roodink I., Verrijp K., et al. Plexin D1 is ubiquitously expressed on tumor vessels and tumor cells in solid malignancies. BMC Cancer 2009, 9:297.
    • (2009) BMC Cancer , vol.9 , pp. 297
    • Roodink, I.1    Verrijp, K.2
  • 160
    • 0034678411 scopus 로고    scopus 로고
    • Activated Ras prevents downregulation of Bcl-X(L) triggered by detachment from the extracellular matrix. A mechanism Ras induced resistance anoikis intestinal epithelial cells
    • Rosen K., Rak J., et al. Activated Ras prevents downregulation of Bcl-X(L) triggered by detachment from the extracellular matrix. A mechanism Ras induced resistance anoikis intestinal epithelial cells. J. Cell Biol. 2000, 149:447-456.
    • (2000) J. Cell Biol. , vol.149 , pp. 447-456
    • Rosen, K.1    Rak, J.2
  • 161
    • 0037195923 scopus 로고    scopus 로고
    • Cell detachment triggers p38 mitogen-activated protein kinase-dependent overexpression of Fas ligand. A novel mechanism Anoikis intestinal epithelial cells
    • Rosen K., Shi W., et al. Cell detachment triggers p38 mitogen-activated protein kinase-dependent overexpression of Fas ligand. A novel mechanism Anoikis intestinal epithelial cells. J. Biol. Chem. 2002, 277:46123-46130.
    • (2002) J. Biol. Chem. , vol.277 , pp. 46123-46130
    • Rosen, K.1    Shi, W.2
  • 162
    • 61449222897 scopus 로고    scopus 로고
    • Cell surface heparan sulfate released by heparanase promotes melanoma cell migration and angiogenesis
    • Roy M., Marchetti D. Cell surface heparan sulfate released by heparanase promotes melanoma cell migration and angiogenesis. J. Cell. Biochem. 2009, 106:200-209.
    • (2009) J. Cell. Biochem. , vol.106 , pp. 200-209
    • Roy, M.1    Marchetti, D.2
  • 163
    • 77951480423 scopus 로고    scopus 로고
    • Targeting anoikis resistance in prostate cancer metastasis
    • Sakamoto S., Kyprianou N. Targeting anoikis resistance in prostate cancer metastasis. Mol. Aspects Med. 2010, 31:205-214.
    • (2010) Mol. Aspects Med. , vol.31 , pp. 205-214
    • Sakamoto, S.1    Kyprianou, N.2
  • 164
    • 77950203804 scopus 로고    scopus 로고
    • Talin1 promotes tumor invasion and metastasis via focal adhesion signaling and anoikis resistance
    • Sakamoto S., Mccann R.O., et al. Talin1 promotes tumor invasion and metastasis via focal adhesion signaling and anoikis resistance. Cancer Res. 2010, 70:1885-1895.
    • (2010) Cancer Res. , vol.70 , pp. 1885-1895
    • Sakamoto, S.1    Mccann, R.O.2
  • 165
    • 0028925737 scopus 로고
    • Molecular cloning of human paxillin, a focal adhesion protein phosphorylated by P210BCR/ABL
    • Salgia R., Li J.L., et al. Molecular cloning of human paxillin, a focal adhesion protein phosphorylated by P210BCR/ABL. J. Biol. Chem. 1995, 270:5039-5047.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5039-5047
    • Salgia, R.1    Li, J.L.2
  • 166
    • 0033531243 scopus 로고    scopus 로고
    • Expression of the focal adhesion protein paxillin in lung cancer and its relation to cell motility
    • Salgia R., Li J.L., et al. Expression of the focal adhesion protein paxillin in lung cancer and its relation to cell motility. Oncogene 1999, 18:67-77.
    • (1999) Oncogene , vol.18 , pp. 67-77
    • Salgia, R.1    Li, J.L.2
  • 167
    • 0037314650 scopus 로고    scopus 로고
    • Immunoscintigraphic detection of the ED-B domain of fibronectin, a marker of angiogenesis, in patients with cancer
    • Santimaria M., Moscatelli G., et al. Immunoscintigraphic detection of the ED-B domain of fibronectin, a marker of angiogenesis, in patients with cancer. Clin. Cancer Res. 2003, 9:571-579.
    • (2003) Clin. Cancer Res. , vol.9 , pp. 571-579
    • Santimaria, M.1    Moscatelli, G.2
  • 168
    • 0037369151 scopus 로고    scopus 로고
    • Caveolin-1 expression is a predictor of recurrence-free survival in pT2N0 prostate carcinoma diagnosed in Japanese patients
    • Satoh T., Yang G., et al. Caveolin-1 expression is a predictor of recurrence-free survival in pT2N0 prostate carcinoma diagnosed in Japanese patients. Cancer 2003, 97:1225-1233.
    • (2003) Cancer , vol.97 , pp. 1225-1233
    • Satoh, T.1    Yang, G.2
  • 169
    • 0028350859 scopus 로고
    • Autophosphorylation of the focal adhesion kinase, pp 125FAK, directs SH2-dependent binding of pp60src
    • Schaller M.D., Hildebrand J.D., et al. Autophosphorylation of the focal adhesion kinase, pp 125FAK, directs SH2-dependent binding of pp60src. Mol. Cell. Biol. 1994, 14:1680-1688.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1680-1688
    • Schaller, M.D.1    Hildebrand, J.D.2
  • 170
    • 0032859988 scopus 로고    scopus 로고
    • Complex formation with focal adhesion kinase: a mechanism to regulate activity and subcellular localization of Src kinases
    • Schaller M.D., Hildebrand J.D., et al. Complex formation with focal adhesion kinase: a mechanism to regulate activity and subcellular localization of Src kinases. Mol. Biol. Cell 1999, 10:3489-3505.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 3489-3505
    • Schaller, M.D.1    Hildebrand, J.D.2
  • 171
    • 3142521875 scopus 로고    scopus 로고
    • Control of motile and invasive cell phenotypes by focal adhesion kinase
    • Schlaepfer D.D., Mitra S.K., et al. Control of motile and invasive cell phenotypes by focal adhesion kinase. Biochim. Biophys. Acta 2004, 1692:77-102.
    • (2004) Biochim. Biophys. Acta , vol.1692 , pp. 77-102
    • Schlaepfer, D.D.1    Mitra, S.K.2
  • 172
    • 77956555910 scopus 로고    scopus 로고
    • Paxillin regulates androgen- and epidermal growth factor- induced MAPK signaling and cell proliferation in prostate cancer cells
    • Sen A., O'malley K., et al. Paxillin regulates androgen- and epidermal growth factor- induced MAPK signaling and cell proliferation in prostate cancer cells. J. Biol. Chem. 2010, 285:28787-28795.
    • (2010) J. Biol. Chem. , vol.285 , pp. 28787-28795
    • Sen, A.1    O'malley, K.2
  • 173
    • 10644221869 scopus 로고    scopus 로고
    • Intrasteric inhibition mediates the interaction of the I/LWEQ module proteins Talin1, Talin2, Hip1, and Hip12 with actin
    • Senetar M.A., Foster S.J., et al. Intrasteric inhibition mediates the interaction of the I/LWEQ module proteins Talin1, Talin2, Hip1, and Hip12 with actin. Biochemistry 2004, 43:15418-15428.
    • (2004) Biochemistry , vol.43 , pp. 15418-15428
    • Senetar, M.A.1    Foster, S.J.2
  • 174
    • 33847217997 scopus 로고    scopus 로고
    • Talin2 is induced during striated muscle differentiation and is targeted to stable adhesion complexes in mature muscle
    • Senetar M.A., Moncman C.L., et al. Talin2 is induced during striated muscle differentiation and is targeted to stable adhesion complexes in mature muscle. Cell Motil. Cytoskeleton 2007, 64:157-173.
    • (2007) Cell Motil. Cytoskeleton , vol.64 , pp. 157-173
    • Senetar, M.A.1    Moncman, C.L.2
  • 175
    • 0036499140 scopus 로고    scopus 로고
    • Adhesion-mediated intracellular redistribution of c-Fas-associated death domain-like IL-1-converting enzyme-like inhibitory protein-long confers resistance to CD95-induced apoptosis in hematopoietic cancer cell lines
    • Shain K.H., Landowski T.H., et al. Adhesion-mediated intracellular redistribution of c-Fas-associated death domain-like IL-1-converting enzyme-like inhibitory protein-long confers resistance to CD95-induced apoptosis in hematopoietic cancer cell lines. J. Immunol. 2002, 168:2544-2553.
    • (2002) J. Immunol. , vol.168 , pp. 2544-2553
    • Shain, K.H.1    Landowski, T.H.2
  • 176
    • 77949862490 scopus 로고    scopus 로고
    • The final steps of integrin activation: the end game
    • Shattil S.J., Kim C., et al. The final steps of integrin activation: the end game. Nat. Rev. Mol. Cell Biol. 2010, 11:288-300.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 288-300
    • Shattil, S.J.1    Kim, C.2
  • 177
    • 3042754728 scopus 로고    scopus 로고
    • Pharmacological exploitation of the alpha1-adrenoreceptor antagonist doxazosin to develop a novel class of antitumor agents that block intracellular protein kinase B/Akt activation
    • Shaw Y.J., Yang Y.T., et al. Pharmacological exploitation of the alpha1-adrenoreceptor antagonist doxazosin to develop a novel class of antitumor agents that block intracellular protein kinase B/Akt activation. J. Med. Chem. 2004, 47:4453-4462.
    • (2004) J. Med. Chem. , vol.47 , pp. 4453-4462
    • Shaw, Y.J.1    Yang, Y.T.2
  • 178
    • 37549053307 scopus 로고    scopus 로고
    • Collagen I promotes epithelial-to-mesenchymal transition in lung cancer cells via transforming growth factor-beta signaling
    • Shintani Y., Maeda M., et al. Collagen I promotes epithelial-to-mesenchymal transition in lung cancer cells via transforming growth factor-beta signaling. Am. J. Respir. Cell Mol. Biol. 2008, 38:95-104.
    • (2008) Am. J. Respir. Cell Mol. Biol. , vol.38 , pp. 95-104
    • Shintani, Y.1    Maeda, M.2
  • 179
    • 0038389789 scopus 로고    scopus 로고
    • Loss of kindlin-1, a human homolog of the Caenorhabditis elegans actin-extracellular-matrix linker protein UNC-112, causes Kindler syndrome
    • Siegel D.H., Ashton G.H., et al. Loss of kindlin-1, a human homolog of the Caenorhabditis elegans actin-extracellular-matrix linker protein UNC-112, causes Kindler syndrome. Am. J. Hum. Genet. 2003, 73:174-187.
    • (2003) Am. J. Hum. Genet. , vol.73 , pp. 174-187
    • Siegel, D.H.1    Ashton, G.H.2
  • 180
    • 34648819675 scopus 로고    scopus 로고
    • A C-terminal dimerization motif is required for focal adhesion targeting of Talin1 and the interaction of the Talin1 I/LWEQ module with F-actin
    • Smith S.J., Mccann R.O. A C-terminal dimerization motif is required for focal adhesion targeting of Talin1 and the interaction of the Talin1 I/LWEQ module with F-actin. Biochemistry 2007, 46:10886-10898.
    • (2007) Biochemistry , vol.46 , pp. 10886-10898
    • Smith, S.J.1    Mccann, R.O.2
  • 181
    • 0024371489 scopus 로고
    • Vimentin rather than keratin expression in some hormone-independent breast cancer cell lines and in oncogene-transformed mammary epithelial cells
    • Sommers C.L., Walker-Jones D., et al. Vimentin rather than keratin expression in some hormone-independent breast cancer cell lines and in oncogene-transformed mammary epithelial cells. Cancer Res. 1989, 49:4258-4263.
    • (1989) Cancer Res. , vol.49 , pp. 4258-4263
    • Sommers, C.L.1    Walker-Jones, D.2
  • 182
    • 0028138771 scopus 로고
    • Differentiation state and invasiveness of human breast cancer cell lines
    • Sommers C.L., Byers S.W., et al. Differentiation state and invasiveness of human breast cancer cell lines. Breast Cancer Res. Treat. 1994, 31:325-335.
    • (1994) Breast Cancer Res. Treat. , vol.31 , pp. 325-335
    • Sommers, C.L.1    Byers, S.W.2
  • 183
    • 0030970723 scopus 로고    scopus 로고
    • Decreased tumorigenicity of a human colon adenocarcinoma cell line by an antisense expression vector specific for c-Src
    • Staley C.A., Parikh N.U., et al. Decreased tumorigenicity of a human colon adenocarcinoma cell line by an antisense expression vector specific for c-Src. Cell Growth Differ. 1997, 8:269-274.
    • (1997) Cell Growth Differ. , vol.8 , pp. 269-274
    • Staley, C.A.1    Parikh, N.U.2
  • 184
    • 4344713411 scopus 로고    scopus 로고
    • Changes in extracellular matrix (ECM) and ECM-associated proteins in the metastatic progression of prostate cancer
    • Stewart D.A., Cooper C.R., et al. Changes in extracellular matrix (ECM) and ECM-associated proteins in the metastatic progression of prostate cancer. Reprod. Biol. Endocrinol. 2004, 2:2.
    • (2004) Reprod. Biol. Endocrinol. , vol.2 , pp. 2
    • Stewart, D.A.1    Cooper, C.R.2
  • 185
    • 0037457423 scopus 로고    scopus 로고
    • Inhibition of integrin alpha5beta1 function with a small peptide (ATN-161) plus continuous 5-FU infusion reduces colorectal liver metastases and improves survival in mice
    • Stoeltzing O., Liu W., et al. Inhibition of integrin alpha5beta1 function with a small peptide (ATN-161) plus continuous 5-FU infusion reduces colorectal liver metastases and improves survival in mice. Int. J. Cancer 2003, 104:496-503.
    • (2003) Int. J. Cancer , vol.104 , pp. 496-503
    • Stoeltzing, O.1    Liu, W.2
  • 186
    • 0141865705 scopus 로고    scopus 로고
    • Talin binding to integrin beta tails: a final common step in integrin activation
    • Tadokoro S., Shattil S.J., et al. Talin binding to integrin beta tails: a final common step in integrin activation. Science 2003, 302:103-106.
    • (2003) Science , vol.302 , pp. 103-106
    • Tadokoro, S.1    Shattil, S.J.2
  • 187
    • 15944425998 scopus 로고    scopus 로고
    • Dynamic process of prostate cancer metastasis to bone
    • Tantivejkul K., Kalikin L.M., et al. Dynamic process of prostate cancer metastasis to bone. J. Cell. Biochem. 2004, 91:706-717.
    • (2004) J. Cell. Biochem. , vol.91 , pp. 706-717
    • Tantivejkul, K.1    Kalikin, L.M.2
  • 188
    • 0036595629 scopus 로고    scopus 로고
    • Epithelial-mesenchymal transitions in tumour progression
    • Thiery J.P. Epithelial-mesenchymal transitions in tumour progression. Nat. Rev. Cancer 2002, 2:442-454.
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 442-454
    • Thiery, J.P.1
  • 189
    • 70450198396 scopus 로고    scopus 로고
    • Epithelial-mesenchymal transitions in development and disease
    • Thiery J.P., Acloque H., et al. Epithelial-mesenchymal transitions in development and disease. Cell 2009, 139:871-890.
    • (2009) Cell , vol.139 , pp. 871-890
    • Thiery, J.P.1    Acloque, H.2
  • 190
    • 0031439247 scopus 로고    scopus 로고
    • Cellular functions regulated by Src family kinases
    • Thomas S.M., Brugge J.S. Cellular functions regulated by Src family kinases. Annu. Rev. Cell Dev. Biol. 1997, 13:513-609.
    • (1997) Annu. Rev. Cell Dev. Biol. , vol.13 , pp. 513-609
    • Thomas, S.M.1    Brugge, J.S.2
  • 191
    • 0033579448 scopus 로고    scopus 로고
    • The role of focal adhesion kinase binding in the regulation of tyrosine phosphorylation of paxillin
    • Thomas J.W., Cooley M.A., et al. The role of focal adhesion kinase binding in the regulation of tyrosine phosphorylation of paxillin. J. Biol. Chem. 1999, 274:36684-36692.
    • (1999) J. Biol. Chem. , vol.274 , pp. 36684-36692
    • Thomas, J.W.1    Cooley, M.A.2
  • 192
    • 20344379950 scopus 로고    scopus 로고
    • Disrupting tumour blood vessels
    • Tozer G.M., Kanthou C., et al. Disrupting tumour blood vessels. Nat. Rev. Cancer 2005, 5:423-435.
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 423-435
    • Tozer, G.M.1    Kanthou, C.2
  • 193
    • 2442488748 scopus 로고    scopus 로고
    • CNTO 95, a fully human monoclonal antibody that inhibits alphav integrins, has antitumor and antiangiogenic activity in vivo
    • Trikha M., Zhou Z., et al. CNTO 95, a fully human monoclonal antibody that inhibits alphav integrins, has antitumor and antiangiogenic activity in vivo. Int. J. Cancer 2004, 110:326-335.
    • (2004) Int. J. Cancer , vol.110 , pp. 326-335
    • Trikha, M.1    Zhou, Z.2
  • 194
    • 0037418837 scopus 로고    scopus 로고
    • Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation
    • Tu Y., Wu S., et al. Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation. Cell 2003, 113:37-47.
    • (2003) Cell , vol.113 , pp. 37-47
    • Tu, Y.1    Wu, S.2
  • 195
    • 0024379267 scopus 로고
    • The role of phosphorylation and limited proteolytic cleavage of talin and vinculin in the disruption of focal adhesion integrity
    • Turner C.E., Pavalko F.M., et al. The role of phosphorylation and limited proteolytic cleavage of talin and vinculin in the disruption of focal adhesion integrity. J. Biol. Chem. 1989, 264:11938-11944.
    • (1989) J. Biol. Chem. , vol.264 , pp. 11938-11944
    • Turner, C.E.1    Pavalko, F.M.2
  • 196
    • 9644268238 scopus 로고    scopus 로고
    • Structural and evolutionary division of phosphotyrosine binding (PTB) domains
    • Uhlik M.T., Temple B., et al. Structural and evolutionary division of phosphotyrosine binding (PTB) domains. J. Mol. Biol. 2005, 345:1-20.
    • (2005) J. Mol. Biol. , vol.345 , pp. 1-20
    • Uhlik, M.T.1    Temple, B.2
  • 197
    • 33747877557 scopus 로고    scopus 로고
    • The Kindlins: subcellular localization and expression during murine development
    • Ussar S., Wang H.V., et al. The Kindlins: subcellular localization and expression during murine development. Exp. Cell Res. 2006, 312:3142-3151.
    • (2006) Exp. Cell Res. , vol.312 , pp. 3142-3151
    • Ussar, S.1    Wang, H.V.2
  • 198
    • 0034652205 scopus 로고    scopus 로고
    • A structural basis for integrin activation by the cytoplasmic tail of the alpha IIb-subunit
    • Vinogradova O., Haas T., et al. A structural basis for integrin activation by the cytoplasmic tail of the alpha IIb-subunit. Proc. Natl. Acad. Sci. USA 2000, 97:1450-1455.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 1450-1455
    • Vinogradova, O.1    Haas, T.2
  • 199
    • 0035999158 scopus 로고    scopus 로고
    • Mammalian heparanase: involvement in cancer metastasis, angiogenesis and normal development
    • Vlodavsky I., Goldshmidt O., et al. Mammalian heparanase: involvement in cancer metastasis, angiogenesis and normal development. Semin. Cancer Biol. 2002, 12:121-129.
    • (2002) Semin. Cancer Biol. , vol.12 , pp. 121-129
    • Vlodavsky, I.1    Goldshmidt, O.2
  • 200
    • 46249121793 scopus 로고    scopus 로고
    • Mechanisms and consequences of agonist-induced talin recruitment to platelet integrin alphaIIbbeta3
    • Watanabe N., Bodin L., et al. Mechanisms and consequences of agonist-induced talin recruitment to platelet integrin alphaIIbbeta3. J. Cell Biol. 2008, 181:1211-1222.
    • (2008) J. Cell Biol. , vol.181 , pp. 1211-1222
    • Watanabe, N.1    Bodin, L.2
  • 201
    • 0036222784 scopus 로고    scopus 로고
    • Adhesion assembly, disassembly and turnover in migrating cells-over and over and over again
    • Webb D.J., Parsons J.T., et al. Adhesion assembly, disassembly and turnover in migrating cells-over and over and over again. Nat. Cell Biol. 2002, 4:E97-E100.
    • (2002) Nat. Cell Biol. , vol.4
    • Webb, D.J.1    Parsons, J.T.2
  • 202
    • 33845987101 scopus 로고    scopus 로고
    • Structural basis of integrin activation by talin
    • Wegener K.L., Partridge A.W., et al. Structural basis of integrin activation by talin. Cell 2007, 128:171-182.
    • (2007) Cell , vol.128 , pp. 171-182
    • Wegener, K.L.1    Partridge, A.W.2
  • 203
    • 0033942173 scopus 로고    scopus 로고
    • The cytoplasmic tyrosines of integrin subunit beta1 are involved in focal adhesion kinase activation
    • Wennerberg K., Armulik A., et al. The cytoplasmic tyrosines of integrin subunit beta1 are involved in focal adhesion kinase activation. Mol. Cell. Biol. 2000, 20:5758-5765.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5758-5765
    • Wennerberg, K.1    Armulik, A.2
  • 204
    • 14944370105 scopus 로고    scopus 로고
    • Migfilin and its binding partners: from cell biology to human diseases
    • Wu C. Migfilin and its binding partners: from cell biology to human diseases. J. Cell Sci. 2005, 118:659-664.
    • (2005) J. Cell Sci. , vol.118 , pp. 659-664
    • Wu, C.1
  • 205
    • 68349113541 scopus 로고    scopus 로고
    • Silibinin inhibits prostate cancer invasion, motility and migration by suppressing vimentin and MMP-2 expression
    • Wu K.J., Zeng J., et al. Silibinin inhibits prostate cancer invasion, motility and migration by suppressing vimentin and MMP-2 expression. Acta Pharmacol. Sin. 2009, 30:1162-1168.
    • (2009) Acta Pharmacol. Sin. , vol.30 , pp. 1162-1168
    • Wu, K.J.1    Zeng, J.2
  • 206
    • 59449090107 scopus 로고    scopus 로고
    • TGF-beta-induced epithelial to mesenchymal transition
    • Xu J., Lamouille S., et al. TGF-beta-induced epithelial to mesenchymal transition. Cell Res. 2009, 19:156-172.
    • (2009) Cell Res. , vol.19 , pp. 156-172
    • Xu, J.1    Lamouille, S.2
  • 207
    • 49649109588 scopus 로고    scopus 로고
    • SRC directly phosphorylates Bif-1 and prevents its interaction with Bax and the initiation of anoikis
    • Yamaguchi H., Woods N.T., et al. SRC directly phosphorylates Bif-1 and prevents its interaction with Bax and the initiation of anoikis. J. Biol. Chem. 2008, 283:19112-19118.
    • (2008) J. Biol. Chem. , vol.283 , pp. 19112-19118
    • Yamaguchi, H.1    Woods, N.T.2
  • 208
    • 0035958967 scopus 로고    scopus 로고
    • Calpain cleavage promotes talin binding to the beta 3 integrin cytoplasmic domain
    • Yan B., Calderwood D.A., et al. Calpain cleavage promotes talin binding to the beta 3 integrin cytoplasmic domain. J. Biol. Chem. 2001, 276:28164-28170.
    • (2001) J. Biol. Chem. , vol.276 , pp. 28164-28170
    • Yan, B.1    Calderwood, D.A.2
  • 209
    • 65349132693 scopus 로고    scopus 로고
    • EMT, the cytoskeleton, and cancer cell invasion
    • Yilmaz M., Christofori G. EMT, the cytoskeleton, and cancer cell invasion. Cancer Metastasis Rev. 2009, 28:15-33.
    • (2009) Cancer Metastasis Rev. , vol.28 , pp. 15-33
    • Yilmaz, M.1    Christofori, G.2
  • 210
    • 24644487312 scopus 로고    scopus 로고
    • TGF-beta and epithelial-to-mesenchymal transitions
    • Zavadil J., Bottinger E.P. TGF-beta and epithelial-to-mesenchymal transitions. Oncogene 2005, 24:5764-5774.
    • (2005) Oncogene , vol.24 , pp. 5764-5774
    • Zavadil, J.1    Bottinger, E.P.2
  • 211
    • 1842524153 scopus 로고    scopus 로고
    • Integration of TGF-beta/Smad and Jagged1/Notch signalling in epithelial-to-mesenchymal transition
    • Zavadil J., Cermak L., et al. Integration of TGF-beta/Smad and Jagged1/Notch signalling in epithelial-to-mesenchymal transition. EMBO J. 2004, 23:1155-1165.
    • (2004) EMBO J. , vol.23 , pp. 1155-1165
    • Zavadil, J.1    Cermak, L.2
  • 212
    • 33750453376 scopus 로고    scopus 로고
    • Effects of a monoclonal anti-alphavbeta3 integrin antibody on blood vessels-a pharmacodynamic study
    • Zhang D., Pier T., et al. Effects of a monoclonal anti-alphavbeta3 integrin antibody on blood vessels-a pharmacodynamic study. Invest. New Drugs 2007, 25:49-55.
    • (2007) Invest. New Drugs , vol.25 , pp. 49-55
    • Zhang, D.1    Pier, T.2
  • 213
    • 51049100594 scopus 로고    scopus 로고
    • Talin depletion reveals independence of initial cell spreading from integrin activation and traction
    • Zhang X., Jiang G., et al. Talin depletion reveals independence of initial cell spreading from integrin activation and traction. Nat. Cell Biol. 2008, 10:1062-1068.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 1062-1068
    • Zhang, X.1    Jiang, G.2
  • 214
    • 67651085772 scopus 로고    scopus 로고
    • Signal transduction by focal adhesion kinase in cancer
    • Zhao J., Guan J.L. Signal transduction by focal adhesion kinase in cancer. Cancer Metastasis Rev. 2009, 28:35-49.
    • (2009) Cancer Metastasis Rev. , vol.28 , pp. 35-49
    • Zhao, J.1    Guan, J.L.2
  • 215
    • 48249128425 scopus 로고    scopus 로고
    • Vimentin affects the mobility and invasiveness of prostate cancer cells
    • Zhao Y., Yan Q., et al. Vimentin affects the mobility and invasiveness of prostate cancer cells. Cell Biochem. Funct. 2008, 26:571-577.
    • (2008) Cell Biochem. Funct. , vol.26 , pp. 571-577
    • Zhao, Y.1    Yan, Q.2
  • 216
    • 0242412978 scopus 로고    scopus 로고
    • Elevated hyaluronan production induces mesenchymal and transformed properties in epithelial cells
    • Zoltan-Jones A., Huang L., et al. Elevated hyaluronan production induces mesenchymal and transformed properties in epithelial cells. J. Biol. Chem. 2003, 278:45801-45810.
    • (2003) J. Biol. Chem. , vol.278 , pp. 45801-45810
    • Zoltan-Jones, A.1    Huang, L.2


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