메뉴 건너뛰기




Volumn 20, Issue 11, 2009, Pages 2650-2660

Reactive oxygen species regulate a slingshot-cofilin activation pathway

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ANGIOTENSIN II; COFILIN; GREEN FLUORESCENT PROTEIN; HYDROGEN PEROXIDE; PHOSPHATASE; PROTEIN SSH 1L; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; UNCLASSIFIED DRUG;

EID: 66349108700     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E09-02-0131     Document Type: Article
Times cited : (161)

References (57)
  • 1
    • 0034536444 scopus 로고    scopus 로고
    • The serine phosphatases PP1 and PP2A associate with and activate the actin-binding protein cofilin in human T lymphocytes
    • Ambach, A., Saunus, J., Konstandin, M., Wesselborg, S., Meuer, S. C., and Samstag, Y. (2000). The serine phosphatases PP1 and PP2A associate with and activate the actin-binding protein cofilin in human T lymphocytes. Eur. J. Immunol. 30, 3422-3431.
    • (2000) Eur. J. Immunol. , vol.30 , pp. 3422-3431
    • Ambach, A.1    Saunus, J.2    Konstandin, M.3    Wesselborg, S.4    Meuer, S.C.5    Samstag, Y.6
  • 2
    • 0032565962 scopus 로고    scopus 로고
    • Regulation of actin dynamics through phosphorylation of cofilin by LIM- Kinase
    • DOI 10.1038/31729
    • Arber, S., Barbayannis, F. A., Hanser, H., Schneider, C., Stanyon, C. A., Bernard, O., and Caroni, P. (1998). Regulation of actin dynamics through phosphorylation of cofilin by LIM-kinase. Nature 393, 805-809. (Pubitemid 28299494)
    • (1998) Nature , vol.393 , Issue.6687 , pp. 805-809
    • Arber, S.1    Barbayannis, F.A.2    Hanser, H.3    Schnelder, C.4    Stanyon, C.A.5    Bernards, O.6    Caroni, P.7
  • 3
    • 0033280237 scopus 로고    scopus 로고
    • Proteins of the ADF/cofilin family: Essential regulators of actin dynamics
    • Bamburg, J. R. (1999). Proteins of the ADF/cofilin family: essential regulators of actin dynamics. Annu. Rev. Cell Dev. Biol. 15, 185-230.
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 185-230
    • Bamburg, J.R.1
  • 4
    • 33846794822 scopus 로고    scopus 로고
    • The NOX family of ROS-generating NADPH oxidases: Physiology and pathophysiology
    • Bedard, K., and Krause, K. H. (2007). The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology. Physiol. Rev. 87, 245-313.
    • (2007) Physiol. Rev. , vol.87 , pp. 245-313
    • Bedard, K.1    Krause, K.H.2
  • 5
    • 0347711117 scopus 로고    scopus 로고
    • NADPH oxidases: Not just for leukocytes anymore!
    • DOI 10.1016/S0968-0004(03)00194-4, PII S0968000403001944
    • Bokoch, G.M., and Knaus, U.G. (2003). NADPH oxidases: not just for leukocytes anymore! Trends Biochem. Sci. 28, 502-508. (Pubitemid 38340415)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.9 , pp. 502-508
    • Bokoch, G.M.1    Knaus, U.G.2
  • 6
    • 38049173243 scopus 로고    scopus 로고
    • Mechanism of angiotensin II-induced superoxide production in cells reconstituted with angiotensin type 1 receptor and the components of NADPH oxidase
    • Choi, H., Leto, T. L., Hunyady, L., Catt, K. J., Bae, Y. S., and Rhee, S. G. (2008). Mechanism of angiotensin II-induced superoxide production in cells reconstituted with angiotensin type 1 receptor and the components of NADPH oxidase. J. Biol. Chem. 283, 255-267.
    • (2008) J. Biol. Chem. , vol.283 , pp. 255-267
    • Choi, H.1    Leto, T.L.2    Hunyady, L.3    Catt, K.J.4    Bae, Y.S.5    Rhee, S.G.6
  • 7
    • 0024985037 scopus 로고
    • The structure and regulation of protein phosphatases
    • Cohen, P. (1990). The structure and regulation of protein phosphatases. Adv. Second Messenger Phosphoprot. Res. 24, 230-235.
    • (1990) Adv. Second Messenger Phosphoprot. Res. , vol.24 , pp. 230-235
    • Cohen, P.1
  • 8
    • 0027333420 scopus 로고
    • Life at the leading edge: The formation of cell protrusions
    • Condeelis, J. (1993). Life at the leading edge: the formation of cell protrusions. Annu. Rev. Cell Biol. 9, 411-444.
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 411-444
    • Condeelis, J.1
  • 9
    • 33750915802 scopus 로고    scopus 로고
    • Regulation of signal transduction through protein cysteine oxidation
    • Cross, J. V., and Templeton, D. J. (2006). Regulation of signal transduction through protein cysteine oxidation. Antioxid. Redox Signal. 8, 1819-1827.
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 1819-1827
    • Cross, J.V.1    Templeton, D.J.2
  • 10
    • 23944434473 scopus 로고    scopus 로고
    • Angiotensin receptors: A new role in cancer?
    • Deshayes, F., and Nahmias, C. (2005). Angiotensin receptors: a new role in cancer? Trends Endocrinol. Metab. 16, 293-299.
    • (2005) Trends Endocrinol. Metab. , vol.16 , pp. 293-299
    • Deshayes, F.1    Nahmias, C.2
  • 12
    • 62949101948 scopus 로고    scopus 로고
    • NADPH oxidases and angiotensin II receptor signaling
    • Garrido, A. M., and Griendling, K. K. (2008). NADPH oxidases and angiotensin II receptor signaling. Mol. Cell. Endocrinol. 302, 148-158.
    • (2008) Mol. Cell. Endocrinol. , vol.302 , pp. 148-158
    • Garrido, A.M.1    Griendling, K.K.2
  • 13
    • 12344250639 scopus 로고    scopus 로고
    • Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics
    • Gohla, A., Birkenfeld, J., and Bokoch, G. M. (2005). Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics. Nat. Cell Biol. 7, 21-29.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 21-29
    • Gohla, A.1    Birkenfeld, J.2    Bokoch, G.M.3
  • 14
    • 0030756377 scopus 로고    scopus 로고
    • Cofilin undergoes rapid dephosphorylation in stimulated neutrophils and translocates to ruffled membranes enriched in products of the NADPH oxidase complex. Evidence for a novel cycle of phosphorylation and dephosphorylation
    • Heyworth, P. G., Robinson, J. M., Ding, J., Ellis, B. A., and Badwey, J. A. (1997). Cofilin undergoes rapid dephosphorylation in stimulated neutrophils and translocates to ruffled membranes enriched in products of the NADPH oxidase complex. Evidence for a novel cycle of phosphorylation and dephosphorylation. Histochem. Cell Biol. 108, 221-233.
    • (1997) Histochem. Cell Biol. , vol.108 , pp. 221-233
    • Heyworth, P.G.1    Robinson, J.M.2    Ding, J.3    Ellis, B.A.4    Badwey, J.A.5
  • 15
    • 0034911925 scopus 로고    scopus 로고
    • Regulation of actin filament network formation through ARP2/3 complex: Activation by a diverse array of proteins
    • Higgs, H. N., and Pollard, T. D. (2001). Regulation of actin filament network formation through ARP2/3 complex: activation by a diverse array of proteins. Annu. Rev. Biochem. 70, 649-676.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 649-676
    • Higgs, H.N.1    Pollard, T.D.2
  • 17
    • 55549091059 scopus 로고    scopus 로고
    • Chronophin mediates an ATP-sensing mechanism for cofilin dephosphorylation and neuronal cofilin-actin rod formation
    • Huang, T. Y., Minamide, L. S., Bamburg, J. R., and Bokoch, G. M. (2008). Chronophin mediates an ATP-sensing mechanism for cofilin dephosphorylation and neuronal cofilin-actin rod formation. Dev. Cell 15, 691-703.
    • (2008) Dev. Cell , vol.15 , pp. 691-703
    • Huang, T.Y.1    Minamide, L.S.2    Bamburg, J.R.3    Bokoch, G.M.4
  • 20
    • 36849030223 scopus 로고    scopus 로고
    • Regulation of Nox1 activity via protein kinase A-mediated phosphorylation of NoxA1 and 14-3-3 binding
    • Kim, J. S., Diebold, B. A., Babior, B. M., Knaus, U. G., and Bokoch, G. M. (2007). Regulation of Nox1 activity via protein kinase A-mediated phosphorylation of NoxA1 and 14-3-3 binding. J. Biol. Chem. 282, 34787-34800.
    • (2007) J. Biol. Chem. , vol.282 , pp. 34787-34800
    • Kim, J.S.1    Diebold, B.A.2    Babior, B.M.3    Knaus, U.G.4    Bokoch, G.M.5
  • 21
    • 33748697413 scopus 로고    scopus 로고
    • Transforming growth factor-beta1 regulates macrophage migration via RhoA
    • Kim, J. S., et al. (2006). Transforming growth factor-beta1 regulates macrophage migration via RhoA. Blood 108, 1821-1829.
    • (2006) Blood , vol.108 , pp. 1821-1829
    • Kim, J.S.1
  • 22
    • 36148996844 scopus 로고    scopus 로고
    • The slingshot family of phosphatases mediates Rac1 regulation of cofilin phosphorylation, laminin-332 organization, and motility behavior of keratinocytes
    • Kligys, K., et al. (2007). The slingshot family of phosphatases mediates Rac1 regulation of cofilin phosphorylation, laminin-332 organization, and motility behavior of keratinocytes. J. Biol. Chem. 282, 32520-32528.
    • (2007) J. Biol. Chem. , vol.282 , pp. 32520-32528
    • Kligys, K.1
  • 23
    • 34250888056 scopus 로고    scopus 로고
    • Regulation of Nox and Duox enzymatic activity and expression
    • Lambeth, J. D., Kawahara, T., and Diebold, B. (2007). Regulation of Nox and Duox enzymatic activity and expression. Free Radic. Biol. Med. 43, 319-331.
    • (2007) Free Radic. Biol. Med. , vol.43 , pp. 319-331
    • Lambeth, J.D.1    Kawahara, T.2    Diebold, B.3
  • 25
    • 0035844030 scopus 로고    scopus 로고
    • Novel gp91(phox) homologues in vascular smooth muscle cells: Nox1 mediates angiotensin II-induced superoxide formation and redox-sensitive signaling pathways
    • Lassegue, B., Sorescu, D., Szocs, K., Yin, Q., Akers, M., Zhang, Y., Grant, S. L., Lambeth, J. D., and Griendling, K. K. (2001). Novel gp91(phox) homologues in vascular smooth muscle cells: nox1 mediates angiotensin II-induced superoxide formation and redox-sensitive signaling pathways. Circ. Res. 88, 888-894.
    • (2001) Circ. Res. , vol.88 , pp. 888-894
    • Lassegue, B.1    Sorescu, D.2    Szocs, K.3    Yin, Q.4    Akers, M.5    Zhang, Y.6    Grant, S.L.7    Lambeth, J.D.8    Griendling, K.K.9
  • 27
    • 33845999557 scopus 로고    scopus 로고
    • Proteomic profiling and identification of cofilin responding to oxidative stress in vascular smooth muscle
    • Lee, C. K., et al. (2006). Proteomic profiling and identification of cofilin responding to oxidative stress in vascular smooth muscle. Proteomics 6, 6455-6475.
    • (2006) Proteomics , vol.6 , pp. 6455-6475
    • Lee, C.K.1
  • 28
    • 63449105018 scopus 로고    scopus 로고
    • Mechanisms of vascular smooth muscle NADPH oxidase 1 (Nox1) contribution to injury-induced neointimal formation
    • Lee, M. Y., et al. (2009). Mechanisms of vascular smooth muscle NADPH oxidase 1 (Nox1) contribution to injury-induced neointimal formation. Arterioscler. Thromb Vasc. Biol. 29, 480-487.
    • (2009) Arterioscler. Thromb Vasc. Biol. , vol.29 , pp. 480-487
    • Lee, M.Y.1
  • 29
    • 33846362954 scopus 로고    scopus 로고
    • Angiotensin II cell signaling: Physiological and pathological effects in the cardiovascular system
    • Mehta, P. K., and Griendling, K. K. (2007). Angiotensin II cell signaling: physiological and pathological effects in the cardiovascular system. Am. J. Physiol. Cell Physiol. 292, C82-C97.
    • (2007) Am. J. Physiol. Cell Physiol. , vol.292
    • Mehta, P.K.1    Griendling, K.K.2
  • 30
    • 0034282106 scopus 로고    scopus 로고
    • Neurodegenerative stimuli induce persistent ADF/cofilin-actin rods that disrupt distal neurite function
    • Minamide, L. S., Striegl, A. M., Boyle, J. A., Meberg, P. J., and Bamburg, J. R. (2000). Neurodegenerative stimuli induce persistent ADF/cofilin-actin rods that disrupt distal neurite function. Nat. Cell Biol. 2, 628-636.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 628-636
    • Minamide, L.S.1    Striegl, A.M.2    Boyle, J.A.3    Meberg, P.J.4    Bamburg, J.R.5
  • 32
    • 58149336903 scopus 로고    scopus 로고
    • Reactive oxygen species regulate F-actin dynamics in neuronal growth cones and neurite outgrowth
    • Munnamalai, V., and Suter, D. M. (2009). Reactive oxygen species regulate F-actin dynamics in neuronal growth cones and neurite outgrowth. J. Neurochem. 108, 644-661.
    • (2009) J. Neurochem. , vol.108 , pp. 644-661
    • Munnamalai, V.1    Suter, D.M.2
  • 33
    • 2542430292 scopus 로고    scopus 로고
    • A pathway of neuregulin-induced activation of cofilin-phosphatase Slingshot and cofilin in lamellipodia
    • Nagata-Ohashi, K., et al. (2004). A pathway of neuregulin-induced activation of cofilin-phosphatase Slingshot and cofilin in lamellipodia. J. Cell Biol. 165, 465-471.
    • (2004) J. Cell Biol. , vol.165 , pp. 465-471
    • Nagata-Ohashi, K.1
  • 34
    • 27544502276 scopus 로고    scopus 로고
    • Spatial and temporal regulation of cofilin activity by LIM kinase and Slingshot is critical for directional cell migration
    • DOI 10.1083/jcb.200504029
    • Nishita, M., Tomizawa, C., Yamamoto, M., Horita, Y., Ohashi, K., and Mizuno, K. (2005). Spatial and temporal regulation of cofilin activity by LIM kinase and Slingshot is critical for directional cell migration. J. Cell Biol. 171, 349-359. (Pubitemid 41540026)
    • (2005) Journal of Cell Biology , vol.171 , Issue.2 , pp. 349-359
    • Nishita, M.1    Tomizawa, C.2    Yamamoto, M.3    Horita, Y.4    Ohashi, K.5    Mizuno, K.6
  • 35
    • 0037169335 scopus 로고    scopus 로고
    • Control of actin reorganization by slingshot, a family of phosphatases that dephosphorylate ADF/cofilin
    • DOI 10.1016/S0092-8674(01)00638-9
    • Niwa, R., Nagata-Ohashi, K., Takeichi, M., Mizuno, K., and Uemura, T. (2002). Control of actin reorganization by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin. Cell 108, 233-246. (Pubitemid 34161143)
    • (2002) Cell , vol.108 , Issue.2 , pp. 233-246
    • Niwa, R.1    Nagata-Ohashi, K.2    Takeichi, M.3    Mizuno, K.4    Uemura, T.5
  • 36
    • 0027321433 scopus 로고
    • Effect of reactive oxygen intermediates on the in vitro invasive capacity of tumor cells and liver metastasis in mice
    • Nonaka, Y., Iwagaki, H., Kimura, T., Fuchimoto, S., and Orita, K. (1993). Effect of reactive oxygen intermediates on the in vitro invasive capacity of tumor cells and liver metastasis in mice. Int. J. Cancer 54, 983-986. (Pubitemid 23267473)
    • (1993) International Journal of Cancer , vol.54 , Issue.6 , pp. 983-986
    • Nonaka, Y.1    Iwagaki, H.2    Kimura, T.3    Fuchimoto, S.4    Orita, K.5
  • 37
    • 0037178706 scopus 로고    scopus 로고
    • Role of formins in actin assembly: Nucleation and barbed-end association
    • DOI 10.1126/science.1072309
    • Pruyne, D., Evangelista, M., Yang, C., Bi, E., Zigmond, S., Bretscher, A., and Boone, C. (2002). Role of formins in actin assembly: nucleation and barbed- end association. Science 297, 612-615. (Pubitemid 34815347)
    • (2002) Science , vol.297 , Issue.5581 , pp. 612-615
    • Pruyne, D.1    Evangelista, M.2    Yang, C.3    Bi, E.4    Zigmond, S.5    Bretscher, A.6    Boone, C.7
  • 40
    • 41949112355 scopus 로고    scopus 로고
    • Dual regulation of cofilin activity by LIM kinase and Slingshot-1L phosphatase controls platelet-derived growth factor-induced migration of human aortic smooth muscle cells
    • San Martin, A., Lee, M. Y., Williams, H. C., Mizuno, K., Lassegue, B., and Griendling, K. K. (2008). Dual regulation of cofilin activity by LIM kinase and Slingshot-1L phosphatase controls platelet-derived growth factor-induced migration of human aortic smooth muscle cells. Circ. Res. 102, 432-438.
    • (2008) Circ. Res. , vol.102 , pp. 432-438
    • San Martin, A.1    Lee, M.Y.2    Williams, H.C.3    Mizuno, K.4    Lassegue, B.5    Griendling, K.K.6
  • 41
    • 34249314785 scopus 로고    scopus 로고
    • Oxidative damage of 14-3-3 zeta and gamma isoforms in Alzheimer's disease and cerebral amyloid angiopathy
    • Santpere, G., Puig, B., and Ferrer, I. (2007). Oxidative damage of 14-3-3 zeta and gamma isoforms in Alzheimer's disease and cerebral amyloid angiopathy. Neuroscience 146, 1640-1651.
    • (2007) Neuroscience , vol.146 , pp. 1640-1651
    • Santpere, G.1    Puig, B.2    Ferrer, I.3
  • 43
    • 0028037021 scopus 로고
    • Quantification and morphologic demonstration of reactive oxygen species produced by Walker 256 tumor cells in vitro and during metastasis in vivo
    • Soares, F. A., Shaughnessy, S. G., MacLarkey, W. R., and Orr, F. W. (1994). Quantification and morphologic demonstration of reactive oxygen species produced by Walker 256 tumor cells in vitro and during metastasis in vivo. Lab. Invest. 71, 480-489.
    • (1994) Lab. Invest. , vol.71 , pp. 480-489
    • Soares, F.A.1    Shaughnessy, S.G.2    MacLarkey, W.R.3    Orr, F.W.4
  • 45
    • 0033620689 scopus 로고    scopus 로고
    • Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia
    • Svitkina, T. M., and Borisy, G. G. (1999). Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia. J. Cell Biol. 145, 1009-1026.
    • (1999) J. Cell Biol. , vol.145 , pp. 1009-1026
    • Svitkina, T.M.1    Borisy, G.G.2
  • 46
    • 0026021362 scopus 로고
    • Production of large amounts of hydrogen peroxide by human tumor cells
    • Szatrowski, T. P., and Nathan, C. F. (1991). Production of large amounts of hydrogen peroxide by human tumor cells. Cancer Res. 51, 794-798.
    • (1991) Cancer Res. , vol.51 , pp. 794-798
    • Szatrowski, T.P.1    Nathan, C.F.2
  • 47
    • 20444400257 scopus 로고    scopus 로고
    • Redox redux: Revisiting PTPs and the control of cell signaling
    • Tonks, N. K. (2005). Redox redux: revisiting PTPs and the control of cell signaling. Cell 121, 667-670.
    • (2005) Cell , vol.121 , pp. 667-670
    • Tonks, N.K.1
  • 48
    • 65349157681 scopus 로고    scopus 로고
    • Compartmentalization of redox signaling through NADPH oxidase-derived ROS
    • in press
    • Ushio-Fukai, M. (2009). Compartmentalization of redox signaling through NADPH oxidase-derived ROS. Antioxid. Redox Signal. (in press).
    • (2009) Antioxid. Redox Signal.
    • Ushio-Fukai, M.1
  • 49
    • 0035049226 scopus 로고    scopus 로고
    • Epidermal growth factor receptor transactivation by angiotensin II requires reactive oxygen species in vascular smooth muscle cells
    • Ushio-Fukai, M., Griendling, K. K., Becker, P. L., Hilenski, L., Halleran, S., and Alexander, R. W. (2001). Epidermal growth factor receptor transactivation by angiotensin II requires reactive oxygen species in vascular smooth muscle cells. Arterioscler. Thromb. Vasc. Biol. 21, 489-495.
    • (2001) Arterioscler. Thromb. Vasc. Biol. , vol.21 , pp. 489-495
    • Ushio-Fukai, M.1    Griendling, K.K.2    Becker, P.L.3    Hilenski, L.4    Halleran, S.5    Alexander, R.W.6
  • 50
    • 34249281332 scopus 로고    scopus 로고
    • The cofilin pathway in breast cancer invasion and metastasis
    • Wang, W., Eddy, R., and Condeelis, J. (2007). The cofilin pathway in breast cancer invasion and metastasis. Nat. Rev. Cancer 7, 429-440.
    • (2007) Nat. Rev. Cancer , vol.7 , pp. 429-440
    • Wang, W.1    Eddy, R.2    Condeelis, J.3
  • 51
    • 16844372470 scopus 로고    scopus 로고
    • Calcium signal-induced cofilin dephosphorylation is mediated by Slingshot via calcineurin
    • Wang, Y., Shibasaki, F., and Mizuno, K. (2005). Calcium signal-induced cofilin dephosphorylation is mediated by Slingshot via calcineurin. J. Biol. Chem. 280, 12683-12689.
    • (2005) J. Biol. Chem. , vol.280 , pp. 12683-12689
    • Wang, Y.1    Shibasaki, F.2    Mizuno, K.3
  • 52
    • 2442666453 scopus 로고    scopus 로고
    • Phosphoinositide-dependent kinase 1 and p21-activated protein kinase mediate reactive oxygen species-dependent regulation of platelet-derived growth factor-induced smooth muscle cell migration
    • Weber, D. S., Taniyama, Y., Rocic, P., Seshiah, P. N., Dechert, M. A., Gerthoffer, W. T., and Griendling, K. K. (2004). Phosphoinositide-dependent kinase 1 and p21-activated protein kinase mediate reactive oxygen species-dependent regulation of platelet-derived growth factor-induced smooth muscle cell migration. Circ. Res. 94, 1219-1226.
    • (2004) Circ. Res. , vol.94 , pp. 1219-1226
    • Weber, D.S.1    Taniyama, Y.2    Rocic, P.3    Seshiah, P.N.4    Dechert, M.A.5    Gerthoffer, W.T.6    Griendling, K.K.7
  • 53
    • 0141703529 scopus 로고    scopus 로고
    • Vascular endothelial growth factor causes translocation of p47phox to membrane ruf-fles through WAVE1
    • Wu, R. F., Gu, Y., Xu, Y. C., Nwariaku, F. E., and Terada, L. S. (2003). Vascular endothelial growth factor causes translocation of p47phox to membrane ruf-fles through WAVE1. J. Biol. Chem. 278, 36830-36840.
    • (2003) J. Biol. Chem. , vol.278 , pp. 36830-36840
    • Wu, R.F.1    Gu, Y.2    Xu, Y.C.3    Nwariaku, F.E.4    Terada, L.S.5
  • 54
    • 33846117134 scopus 로고    scopus 로고
    • The signaling mechanism of ROS in tumor progression
    • Wu, W. S. (2006). The signaling mechanism of ROS in tumor progression. Cancer Metastasis Rev. 25, 695-705.
    • (2006) Cancer Metastasis Rev. , vol.25 , pp. 695-705
    • Wu, W.S.1
  • 55
    • 0032573507 scopus 로고    scopus 로고
    • Probing cellular protein targets of H2O2 with fluorescein-conjugated iodoacetamide and antibodies to fluorescein
    • Wu, Y., Kwon, K. S., and Rhee, S. G. (1998). Probing cellular protein targets of H2O2 with fluorescein-conjugated iodoacetamide and antibodies to fluorescein. FEBS Lett. 440, 111-115.
    • (1998) FEBS Lett. , vol.440 , pp. 111-115
    • Wu, Y.1    Kwon, K.S.2    Rhee, S.G.3
  • 56
    • 34247468876 scopus 로고    scopus 로고
    • Regulation of the actin cytoskeleton in cancer cell migration and invasion
    • Yamaguchi, H., and Condeelis, J. (2007). Regulation of the actin cytoskeleton in cancer cell migration and invasion. Biochim. Biophys. Acta 1773, 642-652.
    • (2007) Biochim. Biophys. Acta , vol.1773 , pp. 642-652
    • Yamaguchi, H.1    Condeelis, J.2
  • 57
    • 0032565769 scopus 로고    scopus 로고
    • Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization
    • Yang, N., Higuchi, O., Ohashi, K., Nagata, K., Wada, A., Kangawa, K., Nishida, E., and Mizuno, K. (1998). Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization. Nature 393, 809-812.
    • (1998) Nature , vol.393 , pp. 809-812
    • Yang, N.1    Higuchi, O.2    Ohashi, K.3    Nagata, K.4    Wada, A.5    Kangawa, K.6    Nishida, E.7    Mizuno, K.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.