메뉴 건너뛰기




Volumn 66, Issue 8, 2006, Pages 4273-4278

Caspase-8 promotes cell motility and calpain activity under nonapoptotic conditions

Author keywords

[No Author keywords available]

Indexed keywords

CALPAIN; CASPASE 8; RAC PROTEIN;

EID: 33646264300     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-05-4183     Document Type: Article
Times cited : (113)

References (57)
  • 1
    • 2442683110 scopus 로고    scopus 로고
    • Monitoring caspase activity in living cells using fluorescent proteins and How cytometry
    • He L, Wu X, Meylan F, et al. Monitoring caspase activity in living cells using fluorescent proteins and How cytometry. Am J Pathol 2004;164:1901-13.
    • (2004) Am J Pathol , vol.164 , pp. 1901-1913
    • He, L.1    Wu, X.2    Meylan, F.3
  • 2
    • 0142188706 scopus 로고    scopus 로고
    • Coexistence of high levels of apoptotic signaling and inhibitor of apoptosis proteins in human tumor cells: Implication for cancer specific therapy
    • Yang L, Cao Z, Yan H, Wood WC. Coexistence of high levels of apoptotic signaling and inhibitor of apoptosis proteins in human tumor cells: implication for cancer specific therapy. Cancer Res 2003;63:6815-24.
    • (2003) Cancer Res , vol.63 , pp. 6815-6824
    • Yang, L.1    Cao, Z.2    Yan, H.3    Wood, W.C.4
  • 3
    • 0031966318 scopus 로고    scopus 로고
    • Chemosensitivity of solid tumor cells in vitro is related to activation of the CD95 system
    • Fulda S, Los M, Friesen C, Debatin KM. Chemosensitivity of solid tumor cells in vitro is related to activation of the CD95 system. Int J Cancer 1998;76:105-14.
    • (1998) Int J Cancer , vol.76 , pp. 105-114
    • Fulda, S.1    Los, M.2    Friesen, C.3    Debatin, K.M.4
  • 5
    • 19544382901 scopus 로고    scopus 로고
    • The caspase-8 modulator c-FLIP
    • Kataoka T. The caspase-8 modulator c-FLIP. Crit Rev Immunol 2005;25:31-58.
    • (2005) Crit Rev Immunol , vol.25 , pp. 31-58
    • Kataoka, T.1
  • 8
    • 0038393124 scopus 로고    scopus 로고
    • The death effector domain protein family: Regulators of cellular homeostasis
    • Tibbetts MD, Zheng L, Lenardo MJ. The death effector domain protein family: regulators of cellular homeostasis. Nat Immunol 2003;4:404-9.
    • (2003) Nat Immunol , vol.4 , pp. 404-409
    • Tibbetts, M.D.1    Zheng, L.2    Lenardo, M.J.3
  • 9
    • 0034077189 scopus 로고    scopus 로고
    • Roles of caspases in apoptosis, development, and cytokine maturation revealed by homozygous gene deficiencies
    • Wang J, Lenardo MJ. Roles of caspases in apoptosis, development, and cytokine maturation revealed by homozygous gene deficiencies. J Cell Sci 2000;113:753-7.
    • (2000) J Cell Sci , vol.113 , pp. 753-757
    • Wang, J.1    Lenardo, M.J.2
  • 10
    • 85047689672 scopus 로고    scopus 로고
    • A crucial role of caspase-3 in osteogenic differentiation of bone marrow stromal stem cells
    • Miura M, Chen XD, Allen MR, et al. A crucial role of caspase-3 in osteogenic differentiation of bone marrow stromal stem cells. J Clin Invest 2004;114:1704-13.
    • (2004) J Clin Invest , vol.114 , pp. 1704-1713
    • Miura, M.1    Chen, X.D.2    Allen, M.R.3
  • 13
    • 3142598843 scopus 로고    scopus 로고
    • A role for Drosophila IAP1-mediated caspase inhibition in Rac-dependent cell migration
    • Geisbrecht ER, Montell DJ. A role for Drosophila IAP1-mediated caspase inhibition in Rac-dependent cell migration. Cell 2004;118:111-25.
    • (2004) Cell , vol.118 , pp. 111-125
    • Geisbrecht, E.R.1    Montell, D.J.2
  • 14
    • 0032143986 scopus 로고    scopus 로고
    • Targeted disruption of the mouse caspase 8 gene ablates cell death induction by the TNF receptors, Fas/Apo1, and DR3 and is lethal prenatally
    • Varfolomeev EE, Schuchmann M, Luria V, et al. Targeted disruption of the mouse caspase 8 gene ablates cell death induction by the TNF receptors, Fas/Apo1, and DR3 and is lethal prenatally. Immunity 1998;9:267-76.
    • (1998) Immunity , vol.9 , pp. 267-276
    • Varfolomeev, E.E.1    Schuchmann, M.2    Luria, V.3
  • 15
    • 4344560197 scopus 로고    scopus 로고
    • Caspase-8 serves both apoptotic and nonapoptotic roles
    • Kang TB, Ben-Moshe T, Varfolomeev EE, et al. Caspase-8 serves both apoptotic and nonapoptotic roles. J Immunol 2004;173:2976-84.
    • (2004) J Immunol , vol.173 , pp. 2976-2984
    • Kang, T.B.1    Ben-Moshe, T.2    Varfolomeev, E.E.3
  • 16
    • 0033532143 scopus 로고    scopus 로고
    • Dephosphorylation of focal adhesion kinase (FAK) and loss of focal contacts precede caspase-mediated cleavage of FAK during apoptosis in renal epithelial cells
    • van de Water B, Nagelkerke JF, Stevens JL. Dephosphorylation of focal adhesion kinase (FAK) and loss of focal contacts precede caspase-mediated cleavage of FAK during apoptosis in renal epithelial cells. J Biol Chem 1999;274:13328-37.
    • (1999) J Biol Chem , vol.274 , pp. 13328-13337
    • Van De Water, B.1    Nagelkerke, J.F.2    Stevens, J.L.3
  • 17
    • 0042167442 scopus 로고    scopus 로고
    • Identification of the primary caspase 3 cleavage site in α II-spectrin during apoptosis
    • Williams ST, Smith AN, Cianci CD, Morrow JS, Brown TL. Identification of the primary caspase 3 cleavage site in α II-spectrin during apoptosis. Apoptosis 2003;8:353-61.
    • (2003) Apoptosis , vol.8 , pp. 353-361
    • Williams, S.T.1    Smith, A.N.2    Cianci, C.D.3    Morrow, J.S.4    Brown, T.L.5
  • 18
    • 0037334827 scopus 로고    scopus 로고
    • Caspase-dependent cleavage of myosin light chain kinase (MLCK) is involved in TNF-α-mediated bovine pulmonary endothelial cell apoptosis
    • Petrache I, Birukov K, Zaiman AL, et al. Caspase-dependent cleavage of myosin light chain kinase (MLCK) is involved in TNF-α-mediated bovine pulmonary endothelial cell apoptosis. FASEB J 2003;17:407-16.
    • (2003) FASEB J , vol.17 , pp. 407-416
    • Petrache, I.1    Birukov, K.2    Zaiman, A.L.3
  • 19
    • 0033927556 scopus 로고    scopus 로고
    • Identification of the cytolinker plectin as a major early in vivo substrate for caspase 8 during CD95 and tumor necrosis factor receptor-mediated apoptosis
    • Stegh AH, Herrmann H, Lampel S, et al. Identification of the cytolinker plectin as a major early in vivo substrate for caspase 8 during CD95 and tumor necrosis factor receptor-mediated apoptosis. Mol Cell Biol 2000;20:5665-79.
    • (2000) Mol Cell Biol , vol.20 , pp. 5665-5679
    • Stegh, A.H.1    Herrmann, H.2    Lampel, S.3
  • 20
    • 0031954631 scopus 로고    scopus 로고
    • MEK kinase 1, a substrate for DEVD-directed caspases, is involved in genotoxin-induced apoptosis
    • Widmann C, Gerwins P, Johnson NL, Jarpe MB, Johnson GL. MEK kinase 1, a substrate for DEVD-directed caspases, is involved in genotoxin-induced apoptosis. Mol Cell Biol 1998;18:2416-29.
    • (1998) Mol Cell Biol , vol.18 , pp. 2416-2429
    • Widmann, C.1    Gerwins, P.2    Johnson, N.L.3    Jarpe, M.B.4    Johnson, G.L.5
  • 21
    • 0030755579 scopus 로고    scopus 로고
    • The regulation of anoikis: MEKK-1 activation requires cleavage by caspases
    • Cardone MH, Salvesen GS, Widmann C, Johnson G, Frisch SM. The regulation of anoikis: MEKK-1 activation requires cleavage by caspases. Cell 1997;90:315-23.
    • (1997) Cell , vol.90 , pp. 315-323
    • Cardone, M.H.1    Salvesen, G.S.2    Widmann, C.3    Johnson, G.4    Frisch, S.M.5
  • 22
    • 0032510794 scopus 로고    scopus 로고
    • Fas-induced proteolytic activation and intracellular redistribution of the stress-signaling kinase MEKK1
    • U S A
    • Deak JC, Cross JV, Lewis M, et al. Fas-induced proteolytic activation and intracellular redistribution of the stress-signaling kinase MEKK1. Proc Natl Acad Sci U S A 1998;95:5595-600.
    • (1998) Proc Natl Acad Sci , vol.95 , pp. 5595-5600
    • Deak, J.C.1    Cross, J.V.2    Lewis, M.3
  • 23
    • 15844409177 scopus 로고    scopus 로고
    • D4-GDI, a substrate of CPP32, is proteolyzed during Fas-induced apoptosis
    • Na S, Chuang TH, Cunningham A, et al. D4-GDI, a substrate of CPP32, is proteolyzed during Fas-induced apoptosis. J Biol Chem 1996;271:11209-13.
    • (1996) J Biol Chem , vol.271 , pp. 11209-11213
    • Na, S.1    Chuang, T.H.2    Cunningham, A.3
  • 24
    • 0032991861 scopus 로고    scopus 로고
    • Cleavage and nuclear translocation of the caspase 3 substrate Rho GDP-dissociation inhibitor, D4-GDI, during apoptosis
    • Krieser RJ, Eastman A. Cleavage and nuclear translocation of the caspase 3 substrate Rho GDP-dissociation inhibitor, D4-GDI, during apoptosis. Cell Death Differ 1999;6:412-9.
    • (1999) Cell Death Differ , vol.6 , pp. 412-419
    • Krieser, R.J.1    Eastman, A.2
  • 25
    • 0034011860 scopus 로고    scopus 로고
    • Caspases cleave the amino-terminal calpain inhibitory unit of calpastatin during apoptosis in human Jurkat T cells
    • Tokyo
    • Kato M, Nonaka T, Maki M, Kikuchi H, Imajoh-Ohmi S. Caspases cleave the amino-terminal calpain inhibitory unit of calpastatin during apoptosis in human Jurkat T cells. J Biochem (Tokyo) 2000;127:297-305.
    • (2000) J Biochem , vol.127 , pp. 297-305
    • Kato, M.1    Nonaka, T.2    Maki, M.3    Kikuchi, H.4    Imajoh-Ohmi, S.5
  • 26
    • 0041018181 scopus 로고    scopus 로고
    • Cleavage of the calpain inhibitor, calpastatin, during apoptosis
    • Porn-Ares MI, Samali A, Orrenius S. Cleavage of the calpain inhibitor, calpastatin, during apoptosis. Cell Death Differ 1998;5:1028-33.
    • (1998) Cell Death Differ , vol.5 , pp. 1028-1033
    • Porn-Ares, M.I.1    Samali, A.2    Orrenius, S.3
  • 27
    • 0032529621 scopus 로고    scopus 로고
    • Caspase-mediated fragmentation of calpain inhibitor protein calpastatin during apoptosis
    • Wang KK, Posmantur R, Nadimpalli R, et al. Caspase-mediated fragmentation of calpain inhibitor protein calpastatin during apoptosis. Arch Biochem Biophys 1998;356:187-96.
    • (1998) Arch Biochem Biophys , vol.356 , pp. 187-196
    • Wang, K.K.1    Posmantur, R.2    Nadimpalli, R.3
  • 28
    • 0037648485 scopus 로고    scopus 로고
    • Cross-talk between calpain and caspase proteolytic systems during neuronal apoptosis
    • Neumar RW, Xu YA, Gada H, Guttmann RP, Siman R. Cross-talk between calpain and caspase proteolytic systems during neuronal apoptosis. J Biol Chem 2003;278:14162-7.
    • (2003) J Biol Chem , vol.278 , pp. 14162-14167
    • Neumar, R.W.1    Xu, Y.A.2    Gada, H.3    Guttmann, R.P.4    Siman, R.5
  • 29
    • 0041631013 scopus 로고    scopus 로고
    • Caspase 3-mediated inactivation of rac GTPases promotes drug-induced apoptosis in human lymphoma cells
    • Zhang B, Zhang Y, Shacter E. Caspase 3-mediated inactivation of rac GTPases promotes drug-induced apoptosis in human lymphoma cells. Mol Cell Biol 2003;23:5716-25.
    • (2003) Mol Cell Biol , vol.23 , pp. 5716-5725
    • Zhang, B.1    Zhang, Y.2    Shacter, E.3
  • 30
    • 0035375053 scopus 로고    scopus 로고
    • Cdc42 is a substrate for caspases and influences Fas-induced apoptosis
    • Tu S, Cerione RA. Cdc42 is a substrate for caspases and influences Fas-induced apoptosis. J Biol Chem 2001;276:19656-63.
    • (2001) J Biol Chem , vol.276 , pp. 19656-19663
    • Tu, S.1    Cerione, R.A.2
  • 31
    • 0035075597 scopus 로고    scopus 로고
    • Caspase-3-mediated cleavage of ROCK I induces MLC phosphorylation and apoptotic membrane blebbing
    • Sebbagh M, Renvoize C, Hamelin J, Riche N, Bertoglio J, Breard J. Caspase-3-mediated cleavage of ROCK I induces MLC phosphorylation and apoptotic membrane blebbing. Nat Cell Biol 2001;3:346-52.
    • (2001) Nat Cell Biol , vol.3 , pp. 346-352
    • Sebbagh, M.1    Renvoize, C.2    Hamelin, J.3    Riche, N.4    Bertoglio, J.5    Breard, J.6
  • 32
    • 0035834730 scopus 로고    scopus 로고
    • Gα11 induces caspase-mediated proteolytic activation of Rho-associated kinase, ROCK-I, in HeLa cells
    • Ueda H, Morishita R, Itoh H, et al. Gα11 induces caspase-mediated proteolytic activation of Rho-associated kinase, ROCK-I, in HeLa cells. J Biol Chem 2001;276:42527-33.
    • (2001) J Biol Chem , vol.276 , pp. 42527-42533
    • Ueda, H.1    Morishita, R.2    Itoh, H.3
  • 33
    • 26244434596 scopus 로고    scopus 로고
    • Regulating cell migration: Calpains make the cut
    • Franco SJ, Huttenlocher A. Regulating cell migration: calpains make the cut. J Cell Sci 2005;118:3829-38.
    • (2005) J Cell Sci , vol.118 , pp. 3829-3838
    • Franco, S.J.1    Huttenlocher, A.2
  • 34
    • 0034116930 scopus 로고    scopus 로고
    • Disruption of the murine calpain small subunit gene, Capn4: Calpain is essential for embryonic development but not for cell growth and division
    • Arthur JS, Elce JS, Hegadorn C, Williams K, Greer PA. Disruption of the murine calpain small subunit gene, Capn4: calpain is essential for embryonic development but not for cell growth and division. Mol Cell Biol 2000;20:4474-81.
    • (2000) Mol Cell Biol , vol.20 , pp. 4474-4481
    • Arthur, J.S.1    Elce, J.S.2    Hegadorn, C.3    Williams, K.4    Greer, P.A.5
  • 35
    • 0036229049 scopus 로고    scopus 로고
    • Motility is rate-limiting for invasion of bladder carcinoma cell lines
    • Kassis J, Radinsky R, Wells A. Motility is rate-limiting for invasion of bladder carcinoma cell lines. Int J Biochem Cell Biol 2002;34:762-75.
    • (2002) Int J Biochem Cell Biol , vol.34 , pp. 762-775
    • Kassis, J.1    Radinsky, R.2    Wells, A.3
  • 36
    • 1642349839 scopus 로고    scopus 로고
    • Calpain activity is generally elevated during transformation but has oncogene-specific biological functions
    • Carragher NO, Fonseca BD, Frame MC. Calpain activity is generally elevated during transformation but has oncogene-specific biological functions. Neoplasia 2004;6:53-73.
    • (2004) Neoplasia , vol.6 , pp. 53-73
    • Carragher, N.O.1    Fonseca, B.D.2    Frame, M.C.3
  • 37
    • 0041633860 scopus 로고    scopus 로고
    • Calpain-2 as a target for limiting prostate cancer invasion
    • Mamoune A, Luo JH, Lauffenburger DA, Wells A. Calpain-2 as a target for limiting prostate cancer invasion. Cancer Res 2003;63:4632-40.
    • (2003) Cancer Res , vol.63 , pp. 4632-4640
    • Mamoune, A.1    Luo, J.H.2    Lauffenburger, D.A.3    Wells, A.4
  • 38
    • 0032913644 scopus 로고    scopus 로고
    • Expression of calpain I messenger RNA in human renal cell carcinoma: Correlation with lymph node metastasis and histological type
    • Braun C, Engel M, Seifert M, et al. Expression of calpain I messenger RNA in human renal cell carcinoma: correlation with lymph node metastasis and histological type. Int J Cancer 1999;84:6-9.
    • (1999) Int J Cancer , vol.84 , pp. 6-9
    • Braun, C.1    Engel, M.2    Seifert, M.3
  • 39
    • 5644271513 scopus 로고    scopus 로고
    • Cleavage of β-catenin by calpain in prostate and mammary tumor cells
    • Rios-Doria J, Kuefer R, Ethier SP, Day ML. Cleavage of β-catenin by calpain in prostate and mammary tumor cells. Cancer Res 2004;64:7237-40.
    • (2004) Cancer Res , vol.64 , pp. 7237-7240
    • Rios-Doria, J.1    Kuefer, R.2    Ethier, S.P.3    Day, M.L.4
  • 40
    • 0037428430 scopus 로고    scopus 로고
    • The role of calpain in the proteolytic cleavage of E-cadherin in prostate and mammary epithelial cells
    • Rios-Doria J, Day KC, Kuefer R, et al. The role of calpain in the proteolytic cleavage of E-cadherin in prostate and mammary epithelial cells. J Biol Chem 2003;278:1372-9.
    • (2003) J Biol Chem , vol.278 , pp. 1372-1379
    • Rios-Doria, J.1    Day, K.C.2    Kuefer, R.3
  • 41
    • 13844310310 scopus 로고    scopus 로고
    • Gene-expression profiles to predict distant metastasis of lymph-node-negative primary breast cancer
    • Wang Y, Klijn JG, Zhang Y, et al. Gene-expression profiles to predict distant metastasis of lymph-node-negative primary breast cancer. Lancet 2005;365:671-9.
    • (2005) Lancet , vol.365 , pp. 671-679
    • Wang, Y.1    Klijn, J.G.2    Zhang, Y.3
  • 42
    • 0033709907 scopus 로고    scopus 로고
    • Deficiency in caspase-9 or caspase-3 induces compensatory caspase activation
    • Zheng TS, Hunot S, Kuida K, et al. Deficiency in caspase-9 or caspase-3 induces compensatory caspase activation. Nat Med 2000;6:1241-7.
    • (2000) Nat Med , vol.6 , pp. 1241-1247
    • Zheng, T.S.1    Hunot, S.2    Kuida, K.3
  • 43
    • 0034723310 scopus 로고    scopus 로고
    • Epidermal growth factor receptor activation of calpain is required for fibroblast motility and occurs via an ERK/MAP kinase signaling pathway
    • Glading A, Chang P, Lauffenburger DA, Wells A. Epidermal growth factor receptor activation of calpain is required for fibroblast motility and occurs via an ERK/MAP kinase signaling pathway. J Biol Chem 2000;275:2390-8.
    • (2000) J Biol Chem , vol.275 , pp. 2390-2398
    • Glading, A.1    Chang, P.2    Lauffenburger, D.A.3    Wells, A.4
  • 44
    • 0030977847 scopus 로고    scopus 로고
    • Target protease specificity of the viral serpin CrmA. Analysis of five caspases
    • Zhou Q, Snipas S, Orth K, Muzio M, Dixit VM, Salvesen GS. Target protease specificity of the viral serpin CrmA. Analysis of five caspases. J Biol Chem 1997;272:7797-800.
    • (1997) J Biol Chem , vol.272 , pp. 7797-7800
    • Zhou, Q.1    Snipas, S.2    Orth, K.3    Muzio, M.4    Dixit, V.M.5    Salvesen, G.S.6
  • 45
    • 0034066405 scopus 로고    scopus 로고
    • Caspase 8 is deleted or silenced preferentially in childhood neuroblastomas with amplification of MYCN
    • Teitz T, Wei T, Valentine MB, et al. Caspase 8 is deleted or silenced preferentially in childhood neuroblastomas with amplification of MYCN. Nat Med 2000;6:529-35.
    • (2000) Nat Med , vol.6 , pp. 529-535
    • Teitz, T.1    Wei, T.2    Valentine, M.B.3
  • 46
    • 3242798339 scopus 로고    scopus 로고
    • Interaction of calpastatin with calpain: A review
    • Wendt A, Thompson VF, Goll DE. Interaction of calpastatin with calpain: a review. Biol Chem 2004;385:465-72.
    • (2004) Biol Chem , vol.385 , pp. 465-472
    • Wendt, A.1    Thompson, V.F.2    Goll, D.E.3
  • 47
    • 0037926319 scopus 로고    scopus 로고
    • MEKK1 regulates calpain-dependent proteolysis of focal adhesion proteins for rear-end detachment of migrating fibroblasts
    • Cuevas BD, Abell AN, Witowsky JA, et al. MEKK1 regulates calpain-dependent proteolysis of focal adhesion proteins for rear-end detachment of migrating fibroblasts. EMBO J 2003;22:3346-55.
    • (2003) EMBO J , vol.22 , pp. 3346-3355
    • Cuevas, B.D.1    Abell, A.N.2    Witowsky, J.A.3
  • 48
    • 1542344328 scopus 로고    scopus 로고
    • Epidermal growth factor activates m-calpain (calpain II), at least in part, by extracellular signal-regulated kinase-mediated phosphorylation
    • Glading A, Bodnar RJ, Reynolds IJ, et al. Epidermal growth factor activates m-calpain (calpain II), at least in part, by extracellular signal-regulated kinase-mediated phosphorylation. Mol Cell Biol 2004;24:2499-512.
    • (2004) Mol Cell Biol , vol.24 , pp. 2499-2512
    • Glading, A.1    Bodnar, R.J.2    Reynolds, I.J.3
  • 50
    • 30144434107 scopus 로고    scopus 로고
    • Potentiation of neuroblastoma metastasis by loss of caspase-8
    • Stupack DG, Teitz T, Potter MD, et al. Potentiation of neuroblastoma metastasis by loss of caspase-8. Nature 2006;439:95-9.
    • (2006) Nature , vol.439 , pp. 95-99
    • Stupack, D.G.1    Teitz, T.2    Potter, M.D.3
  • 51
    • 0035930548 scopus 로고    scopus 로고
    • Reduced cell migration and disruption of the actin cytoskeleton in calpain-deficient embryonic fibroblasts
    • Dourdin N, Bhatt AK, Dutt P, et al. Reduced cell migration and disruption of the actin cytoskeleton in calpain-deficient embryonic fibroblasts. J Biol Chem 2001;276:48382-8.
    • (2001) J Biol Chem , vol.276 , pp. 48382-48388
    • Dourdin, N.1    Bhatt, A.K.2    Dutt, P.3
  • 52
    • 14044267645 scopus 로고    scopus 로고
    • SH3 domain of spectrin participates in the activation of Rac in specialized calpain-induced integrin signaling complexes
    • Bialkowska K, Saido TC, Fox JE. SH3 domain of spectrin participates in the activation of Rac in specialized calpain-induced integrin signaling complexes. J Cell Sci 2005;118:381-95.
    • (2005) J Cell Sci , vol.118 , pp. 381-395
    • Bialkowska, K.1    Saido, T.C.2    Fox, J.E.3
  • 53
    • 4043077024 scopus 로고    scopus 로고
    • Isoform specific function of calpain 2 in regulating membrane protrusion
    • Franco S, Perrin B, Huttenlocher A. Isoform specific function of calpain 2 in regulating membrane protrusion. Exp Cell Res 2004;299:179-87.
    • (2004) Exp Cell Res , vol.299 , pp. 179-187
    • Franco, S.1    Perrin, B.2    Huttenlocher, A.3
  • 54
    • 0041924982 scopus 로고    scopus 로고
    • A novel role for FAK as a protease-targeting adaptor protein: Regulation by p42 ERK and Src
    • Carragher NO, Westhoff MA, Fincham VJ, Schaller MD, Frame MC. A novel role for FAK as a protease-targeting adaptor protein: regulation by p42 ERK and Src. Curr Biol 2003;13:1442-50.
    • (2003) Curr Biol , vol.13 , pp. 1442-1450
    • Carragher, N.O.1    Westhoff, M.A.2    Fincham, V.J.3    Schaller, M.D.4    Frame, M.C.5
  • 55
    • 1642358909 scopus 로고    scopus 로고
    • Activation of m-calpain is required for chromosome alignment on the metaphase plate during mitosis
    • Honda S, Marumoto T, Hirota T, et al. Activation of m-calpain is required for chromosome alignment on the metaphase plate during mitosis. J Biol Chem 2004;279:10615-23.
    • (2004) J Biol Chem , vol.279 , pp. 10615-10623
    • Honda, S.1    Marumoto, T.2    Hirota, T.3
  • 56
    • 27144507868 scopus 로고    scopus 로고
    • Cytokinesis failure generating tetraploids promotes tumorigenesis in p53-null cells
    • Fujiwara T, Bandi M, Nitta M, Ivanova EV, Bronson RT, Pellman D. Cytokinesis failure generating tetraploids promotes tumorigenesis in p53-null cells. Nature 2005;437:1043-7.
    • (2005) Nature , vol.437 , pp. 1043-1047
    • Fujiwara, T.1    Bandi, M.2    Nitta, M.3    Ivanova, E.V.4    Bronson, R.T.5    Pellman, D.6
  • 57


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.