메뉴 건너뛰기




Volumn , Issue , 2012, Pages

The ADF/cofilin-pathway and actin dynamics in podocyte injury

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; COFILIN; COFILIN 1;

EID: 84855577474     PISSN: 16878876     EISSN: 16878884     Source Type: Journal    
DOI: 10.1155/2012/320531     Document Type: Review
Times cited : (24)

References (78)
  • 1
    • 0037207471 scopus 로고    scopus 로고
    • Cell biology of the glomerular podocyte
    • Pavenstdt H., Kriz W., Kretzler M., Cell biology of the glomerular podocyte Physiological Reviews 2003 83 1 253 307 (Pubitemid 36459882)
    • (2003) Physiological Reviews , vol.83 , Issue.1 , pp. 253-307
    • Pavenstadt, H.1    Kriz, W.2    Kretzler, M.3
  • 3
    • 0033452520 scopus 로고    scopus 로고
    • The role of the podocyte in glomerulosclerosis
    • DOI 10.1097/00041552-199907000-00014
    • Kriz W., Lemley K. V., The role of the podocyte in glomerulosclerosis Current Opinion in Nephrology and Hypertension 1999 8 4 489 497 (Pubitemid 30004174)
    • (1999) Current Opinion in Nephrology and Hypertension , vol.8 , Issue.4 , pp. 489-497
    • Kriz, W.1    Lemley, K.V.2
  • 4
    • 0036900955 scopus 로고    scopus 로고
    • ADF/cofilin and actin dynamics in disease
    • DOI 10.1016/S0962-8924(02)02404-2, PII S0962892402024042
    • Bamburg J. R., Wiggan O. P., ADF/cofilin and actin dynamics in disease Trends in Cell Biology 2002 12 12 598 605 (Pubitemid 35461859)
    • (2002) Trends in Cell Biology , vol.12 , Issue.12 , pp. 598-605
    • Bamburg, J.R.1    Wiggan, O.P.2
  • 5
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • DOI 10.1016/S0092-8674(03)00120-X
    • Pollard T. D., Borisy G. G., Cellular motility driven by assembly and disassembly of actin filaments Cell 2003 112 4 453 465 (Pubitemid 36263079)
    • (2003) Cell , vol.112 , Issue.4 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 6
    • 0033280237 scopus 로고    scopus 로고
    • Proteins of the ADF/cofilin family: Essential regulators of actin dynamics
    • DOI 10.1146/annurev.cellbio.15.1.185
    • Bamburg J. R., Proteins of the ADF/cofilin family: essential regulators of actin dynamics Annual Review of Cell and Developmental Biology 1999 15 185 230 (Pubitemid 32250375)
    • (1999) Annual Review of Cell and Developmental Biology , vol.15 , pp. 185-230
    • Bamburg, J.R.1
  • 7
    • 0033620689 scopus 로고    scopus 로고
    • Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia
    • DOI 10.1083/jcb.145.5.1009
    • Svitkina T. M., Borisy G. G., Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia Journal of Cell Biology 1999 145 5 1009 1026 (Pubitemid 29270059)
    • (1999) Journal of Cell Biology , vol.145 , Issue.5 , pp. 1009-1026
    • Svitkina, T.M.1    Borisy, G.G.2
  • 8
    • 0036153765 scopus 로고    scopus 로고
    • The three mouse actin-depolymerizing factor/cofilins evolved to fulfill cell-type-specific requirements for actin dynamics
    • DOI 10.1091/mbc.01-07-0331
    • Vartiainen M. K., Mustonen T., Mattila P. K., Ojala P. J., Thesleff I., Partanen J., Lappalainen P., The three mouse actin-depolymerizing factor/cofilins evolved to fulfill cell-type-specific requirements for actin dynamics Molecular Biology of the Cell 2002 13 1 183 194 (Pubitemid 34106068)
    • (2002) Molecular Biology of the Cell , vol.13 , Issue.1 , pp. 183-194
    • Vartiainen, M.K.1    Mustonen, T.2    Mattila, P.K.3    Ojala, P.J.4    Thesleff, I.5    Partanen, J.6    Lappalainen, P.7
  • 12
    • 0017802361 scopus 로고
    • Polarity of actin at the leading edge of cultured cells
    • DOI 10.1038/272638a0
    • Small J. V., Isenberg G., Celis J. E., Polarity of actin at the leading edge of cultured cells Nature 1978 272 5654 638 639 (Pubitemid 8305197)
    • (1978) Nature , vol.272 , Issue.5654 , pp. 638-639
    • Small, J.V.1    Isenberg, G.2    Celis, J.E.3
  • 13
    • 0030843484 scopus 로고    scopus 로고
    • Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: Implication in actin-based motility
    • DOI 10.1083/jcb.136.6.1307
    • Carlier M. F., Laurent V., Santolini J., Melki R., Didry D., Xia G. X., Hong Y., Chua N. H., Pantaloni D., Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: implication in actin-based motility Journal of Cell Biology 1997 136 6 1307 1322 (Pubitemid 27421917)
    • (1997) Journal of Cell Biology , vol.136 , Issue.6 , pp. 1307-1322
    • Carlier, M.-F.1    Laurent, V.2    Santolini, J.3    Melki, R.4    Didry, D.5    Xia, G.-X.6    Hong, Y.7    Chua, N.-H.8    Pantaloni, D.9
  • 14
    • 0030820734 scopus 로고    scopus 로고
    • Cofilin changes the twist of F-actin: Implications for actin filament dynamics and cellular function
    • DOI 10.1083/jcb.138.4.771
    • McGough A., Pope B., Chiu W., Weeds A., Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function Journal of Cell Biology 1997 138 4 771 781 (Pubitemid 27365041)
    • (1997) Journal of Cell Biology , vol.138 , Issue.4 , pp. 771-781
    • McGough, A.1    Pope, B.2    Chiu, W.3    Weeds, A.4
  • 15
    • 0035795407 scopus 로고    scopus 로고
    • Actin depolymerizing factor stabilizes an existing state of F-actin and can change the tilt of F-actin subunits
    • DOI 10.1083/jcb.153.1.75
    • Galkin V. E., Orlova A., Lukoyanova N., Wriggersd W., Egelman E. H., Actin depolymerizing factor stabilizes an existing state of F-actin and can change the tilt of F-actin subunits Journal of Cell Biology 2001 153 1 75 86 (Pubitemid 34280195)
    • (2001) Journal of Cell Biology , vol.153 , Issue.1 , pp. 75-86
    • Galkin, V.E.1    Orlova, A.2    Lukoyanova, N.3    Wriggersd, W.4    Egelman, E.H.5
  • 16
    • 0034113924 scopus 로고    scopus 로고
    • Actin filaments are severed by both native and recombinant Dictyostelium cofilin but to different extents
    • DOI 10.1002/(SICI)1097-0169(200004)45:4<293::AID-CM5>3.0.CO;2-1
    • Ichetovkin I., Han J., Pang K. M., Knecht D. A., Condeelis J. S., Actin filaments are severed by both native and recombinant Dictyostelium cofilin but to different extents Cell Motility and the Cytoskeleton 2000 45 4 293 306 (Pubitemid 30196645)
    • (2000) Cell Motility and the Cytoskeleton , vol.45 , Issue.4 , pp. 293-306
    • Ichetovkin, I.1    Han, J.2    Pang, K.M.3    Knecht, D.A.4    Condeelis, J.S.5
  • 17
    • 0021964668 scopus 로고
    • Opposite effects of cofilin and profilin from porcine brain on rate of exchange of actin-bound adenosine 5'-triphosphate
    • DOI 10.1021/bi00326a015
    • Nishida E., Opposite effects of cofilin and profilin from porcine brain on rate of exchange of actin-bound adenosine 5′-triphosphate Biochemistry 1985 24 5 1160 1164 (Pubitemid 15096766)
    • (1985) Biochemistry , vol.24 , Issue.5 , pp. 1160-1164
    • Nishida, E.1
  • 18
  • 19
    • 33749046492 scopus 로고    scopus 로고
    • Mechanism of Actin Filament Turnover by Severing and Nucleation at Different Concentrations of ADF/Cofilin
    • DOI 10.1016/j.molcel.2006.08.006, PII S109727650600565X
    • Andrianantoandro E., Pollard T. D., Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilin Molecular Cell 2006 24 1 13 23 (Pubitemid 44466682)
    • (2006) Molecular Cell , vol.24 , Issue.1 , pp. 13-23
    • Andrianantoandro, E.1    Pollard, T.D.2
  • 21
    • 0032536820 scopus 로고    scopus 로고
    • Nuclear export of actin: A novel mechanism regulating the subcellular localization of a major cytoskeletal protein
    • DOI 10.1093/emboj/17.6.1635
    • Wada A., Fukuda M., Mishima M., Nishida E., Nuclear export of actin: a novel mechanism regulating the subcellular localization of a major cytoskeletal protein EMBO Journal 1998 17 6 1635 1641 (Pubitemid 28119117)
    • (1998) EMBO Journal , vol.17 , Issue.6 , pp. 1635-1641
    • Wada, A.1    Fukuda, M.2    Mishima, M.3    Nishida, E.4
  • 22
    • 0029149885 scopus 로고
    • Reactivation of phosphorylated actin depolymerizing factor and identification of the regulatory site
    • Agnew B. J., Minamide L. S., Bamburg J. R., Reactivation of phosphorylated actin depolymerizing factor and identification of the regulatory site Journal of Biological Chemistry 1995 270 29 17582 17587
    • (1995) Journal of Biological Chemistry , vol.270 , Issue.29 , pp. 17582-17587
    • Agnew, B.J.1    Minamide, L.S.2    Bamburg, J.R.3
  • 23
    • 0029678546 scopus 로고    scopus 로고
    • Phosphorylation of Ser-3 of cofilin regulates its essential function on actin
    • Moriyama K., Iida K., Yahara I., Phosphorylation of Ser-3 of cofilin regulates its essential function on actin Genes to Cells 1996 1 1 73 86 (Pubitemid 126673108)
    • (1996) Genes to Cells , vol.1 , Issue.1 , pp. 73-86
    • Moriyama, K.1    Iida, K.2    Yahara, I.3
  • 24
    • 0034645797 scopus 로고    scopus 로고
    • Phosphorylation of Acanthamoeba actophorin (ADF/cofilin) blocks interaction with actin without a change in atomic structure
    • DOI 10.1006/jmbi.1999.3336
    • Blanchoin L., Robinson R. C., Choe S., Pollard T. D., Phosphorylation of Acanthamoeba actophorin (ADF/cofilin) blocks interaction with actin without a change in atomic structure Journal of Molecular Biology 2000 295 2 203 211 (Pubitemid 30045354)
    • (2000) Journal of Molecular Biology , vol.295 , Issue.2 , pp. 203-211
    • Blanchoin, L.1    Robinson, R.C.2    Choe, S.3    Pollard, T.D.4
  • 25
    • 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., Schnelder C., Stanyon C. A., Bernards O., Caroni P., Regulation of actin dynamics through phosphorylation of cofilin by LIM- kinase Nature 1998 393 6687 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
  • 26
    • 0032565769 scopus 로고    scopus 로고
    • Cofflin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization
    • DOI 10.1038/31735
    • Yang N., Higuchi O., Ohashi K., Nagata K., Wada A., Kangawa K., Nishida E., Mizuno K., Cofflin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization Nature 1998 393 6687 809 812 (Pubitemid 28299495)
    • (1998) Nature , vol.393 , Issue.6687 , 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
  • 27
    • 0035171699 scopus 로고    scopus 로고
    • Cofilin phosphorylation by protein kinase testicular protein kinase 1 and its role in integrin-mediated actin reorganization and focal adhesion formation
    • Toshima J., Toshima J. Y., Amano T., Yang N., Narumiya S., Mizuno K., Cofilin phosphorylation by protein kinase testicular protein kinase 1 and its role in integrin-mediated actin reorganization and focal adhesion formation Molecular Biology of the Cell 2001 12 4 1131 1145 (Pubitemid 33052004)
    • (2001) Molecular Biology of the Cell , vol.12 , Issue.4 , pp. 1131-1145
    • Toshima, J.1    Toshima, J.Y.2    Amano, T.3    Yang, N.4    Narumiya, S.5    Mizuno, K.6
  • 28
    • 0035903099 scopus 로고    scopus 로고
    • Cofilin Phosphorylation and Actin Reorganization Activities of Testicular Protein Kinase 2 and Its Predominant Expression in Testicular Sertoli Cells
    • DOI 10.1074/jbc.M102988200
    • Toshima J., Toshima J. Y., Takeuchi K., Mori R., Mizuno K., Cofilin phosphorylation and actin reorganization activities of testicular protein kinase 2 and its predominant expression in testicular Sertoli cells Journal of Biological Chemistry 2001 276 33 31449 31458 (Pubitemid 37385018)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.33 , pp. 31449-31458
    • Toshima, J.1    Toshima, J.Y.2    Takeuchi, K.3    Mori, R.4    Mizuno, K.5
  • 30
    • 20444400572 scopus 로고    scopus 로고
    • Actopaxin interacts with TESK1 to regulate cell spreading on fibronectin
    • DOI 10.1074/jbc.M500752200
    • LaLonde D. P., Brown M. C., Bouverat B. P., Turner C. E., Actopaxin interacts with TESK1 to regulate cell spreading on fibronectin Journal of Biological Chemistry 2005 280 22 21680 21688 (Pubitemid 40805739)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.22 , pp. 21680-21688
    • LaLonde, D.P.1    Brown, M.C.2    Bouverat, B.P.3    Turner, C.E.4
  • 32
    • 0033611107 scopus 로고    scopus 로고
    • Cofilin phosphorylation and actin cytoskeletal dynamics regulated by Rho- and Cdc42-activated LIM-kinase 2
    • DOI 10.1083/jcb.147.7.1519
    • Sumi T., Matsumoto K., Takai Y., Nakamura T., Cofilin phosphorylation and actin cytoskeletal dynamics regulated by Rho- and Cdc42-activated LIM-kinase 2 Journal of Cell Biology 1999 147 7 1519 1532 (Pubitemid 30027406)
    • (1999) Journal of Cell Biology , vol.147 , Issue.7 , pp. 1519-1532
    • Sumi, T.1    Matsumoto, K.2    Takai, Y.3    Nakamura, T.4
  • 33
    • 0035943704 scopus 로고    scopus 로고
    • Cytoskeletal changes regulated by the PAK4 serine/threonine kinase are mediated by LIM kinase 1 and cofilin
    • Dan C., Kelly A., Bernard O., Minden A., Cytoskeletal changes regulated by the PAK4 serine/threonine kinase are mediated by LIM kinase 1 and cofilin Journal of Biological Chemistry 2001 276 34 32115 32121
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.34 , pp. 32115-32121
    • Dan, C.1    Kelly, A.2    Bernard, O.3    Minden, A.4
  • 34
    • 22544456920 scopus 로고    scopus 로고
    • 2-macroglobulin to its cell surface receptor GRP78 in 1-LN prostate cancer cells regulates PAK-2-dependent activation of LIMK
    • DOI 10.1074/jbc.M414467200
    • Misra U. K., Deedwania R., Pizzo S. V., Binding of activated 2-macroglobulin to its cell surface receptor GRP78 in 1-LN prostate cancer cells regulates PAK-2-dependent activation of LIMK Journal of Biological Chemistry 2005 280 28 26278 26286 (Pubitemid 41022225)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.28 , pp. 26278-26286
    • Misra, U.K.1    Deedwania, R.2    Pizzo, S.V.3
  • 35
    • 23744432051 scopus 로고    scopus 로고
    • Essential role of CIB1 in regulating PAK1 activation and cell migration
    • DOI 10.1083/jcb.200502090
    • Leisner T. M., Liu M., Jaffer Z. M., Chernoff J., Parise L. V., Essential role of CIB1 in regulating PAK1 activation and cell migration Journal of Cell Biology 2005 170 3 465 476 (Pubitemid 41126945)
    • (2005) Journal of Cell Biology , vol.170 , Issue.3 , pp. 465-476
    • Leisner, T.M.1    Liu, M.2    Jaffer, Z.M.3    Chernoff, J.4    Parise, L.V.5
  • 36
    • 33644508365 scopus 로고    scopus 로고
    • MAPKAPK-2-mediated LIM-kinase activation is critical for VEGF-induced actin remodeling and cell migration
    • DOI 10.1038/sj.emboj.7600973, PII 7600973
    • Kobayashi M., Nishita M., Mishima T., Ohashi K., Mizuno K., MAPKAPK-2-mediated LIM-kinase activation is critical for VEGF-induced actin remodeling and cell migration EMBO Journal 2006 25 4 713 726 (Pubitemid 43292434)
    • (2006) EMBO Journal , vol.25 , Issue.4 , pp. 713-726
    • Kobayashi, M.1    Nishita, M.2    Mishima, T.3    Ohashi, K.4    Mizuno, K.5
  • 37
    • 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., Uemura T., Control of actin reorganization by slingshot, a family of phosphatases that dephosphorylate ADF/cofilin Cell 2002 108 2 233 246 (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
  • 38
    • 12344250639 scopus 로고    scopus 로고
    • Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics
    • DOI 10.1038/ncb1201
    • Gohla A., Birkenfeld J., Bokoch G. M., Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics Nature Cell Biology 2005 7 1 21 29 (Pubitemid 40123379)
    • (2005) Nature Cell Biology , vol.7 , Issue.1 , pp. 21-29
    • Gohla, A.1    Birkenfeld, J.2    Bokoch, G.M.3
  • 39
    • 30844443048 scopus 로고    scopus 로고
    • Cofilin phosphatases and regulation of actin dynamics
    • DOI 10.1016/j.ceb.2005.11.005, PII S095506740500181X, Cell Structure and Dynamics
    • Huang T. Y., Dermardirossian C., Bokoch G. M., Cofilin phosphatases and regulation of actin dynamics Current Opinion in Cell Biology 2006 18 1 26 31 (Pubitemid 43107604)
    • (2006) Current Opinion in Cell Biology , vol.18 , Issue.1 , pp. 26-31
    • Huang, T.Y.1    Dermardirossian, C.2    Bokoch, G.M.3
  • 41
    • 36148996844 scopus 로고    scopus 로고
    • The slingshot family of phosphatases mediates Rac1 regulation of cofilin phosphorylation, laminin-332 organization, and motility behavior of keratinocytes
    • DOI 10.1074/jbc.M707041200
    • Kligys K., Claiborne J. N., DeBiase P. J., Hopkinson S. B., Wu Y., Mizuno K., Jones J. C. R., The slingshot family of phosphatases mediates Rac1 regulation of cofilin phosphorylation, laminin-332 organization, and motility behavior of keratinocytes Journal of Biological Chemistry 2007 282 44 32520 32528 (Pubitemid 350106481)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.44 , pp. 32520-32528
    • Kligys, K.1    Claiborne, J.N.2    DeBiase, P.J.3    Hopkinson, S.B.4    Wu, Y.5    Mizuno, K.6    Jones, J.C.R.7
  • 45
    • 0027439319 scopus 로고
    • Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments
    • DOI 10.1021/bi00089a014
    • Hawkins M., Pope B., Maciver S. K., Weeds A. G., Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments Biochemistry 1993 32 38 9985 9993 (Pubitemid 23312424)
    • (1993) Biochemistry , vol.32 , Issue.38 , pp. 9985-9993
    • Hawkins, M.1    Pope, B.2    Maciver, S.K.3    Weeds, A.G.4
  • 47
    • 0031281984 scopus 로고    scopus 로고
    • Signaling pathways involved in dephosphorylation and localization of the actin-binding protein cofilin in stimulated human neutrophils
    • DOI 10.1006/excr.1997.3731
    • Djafarzadeh S., Niggli V., Signaling pathways involved in dephosphorylation and localization of the actin-binding protein cofilin in stimulated human neutrophils Experimental Cell Research 1997 236 2 427 435 (Pubitemid 27505595)
    • (1997) Experimental Cell Research , vol.236 , Issue.2 , pp. 427-435
    • Djafarzadeh, S.1    Niggli, V.2
  • 49
    • 65249132407 scopus 로고    scopus 로고
    • Hyperosmotic stress induces Rho/Rho kinase/LIM kinase-mediated cofilin phosphorylation in tubular cells: Key role in the osmotically triggered F-actin response
    • Thirone A. C. P., Speight P., Zulys M., Rotstein O. D., Szszi K., Pedersen S. F., Kapus A., Hyperosmotic stress induces Rho/Rho kinase/LIM kinase-mediated cofilin phosphorylation in tubular cells: key role in the osmotically triggered F-actin response American Journal of Physiology 2009 296 3 C463 C475
    • (2009) American Journal of Physiology , vol.296 , Issue.3
    • Thirone, A.C.P.1    Speight, P.2    Zulys, M.3    Rotstein, O.D.4    Szszi, K.5    Pedersen, S.F.6    Kapus, A.7
  • 50
    • 40849137975 scopus 로고    scopus 로고
    • High glucose increases phosphocofilin via phosphorylation of LIM kinase due to Rho/Rho kinase activation in cultured pig proximal tubular epithelial cells
    • Ishibashi F., High glucose increases phosphocofilin via phosphorylation of LIM kinase due to Rho/Rho kinase activation in cultured pig proximal tubular epithelial cells Diabetes Research and Clinical Practice 2008 80 1 24 33
    • (2008) Diabetes Research and Clinical Practice , vol.80 , Issue.1 , pp. 24-33
    • Ishibashi, F.1
  • 51
    • 0029940563 scopus 로고    scopus 로고
    • Cytoskeletal changes in podocytes associated with foot process effacement in Masugi nephritis
    • Shirato I., Sakai T., Kimura K., Tomino Y., Kriz W., Cytoskeletal changes in podocytes associated with foot process effacement in Masugi nephritis American Journal of Pathology 1996 148 4 1283 1296 (Pubitemid 26111083)
    • (1996) American Journal of Pathology , vol.148 , Issue.4 , pp. 1283-1296
    • Shirato, I.1    Sakai, T.2    Kimura, K.3    Tomino, Y.4    Kriz, W.5
  • 52
    • 0034954343 scopus 로고    scopus 로고
    • Loss of glomerular foot processes is associated with uncoupling of podocalyxin from the actin cytoskeleton
    • DOI 10.1172/JCI200112539
    • Takeda T., McQuistan T., Orlando R. A., Farquhar M. G., Loss of glomerular foot processes is associated with uncoupling of podocalyxin from the actin cytoskeleton Journal of Clinical Investigation 2001 108 2 289 301 (Pubitemid 32656253)
    • (2001) Journal of Clinical Investigation , vol.108 , Issue.2 , pp. 289-301
    • Takeda, T.1    McQuistan, T.2    Orlando, R.A.3    Farquhar, M.G.4
  • 53
    • 0031910264 scopus 로고    scopus 로고
    • Regulation of podocyte structure during the development of nephrotic syndrome
    • DOI 10.1007/s001090050206
    • Smoyer W. E., Mundel P., Regulation of podocyte structure during the development of nephrotic syndrome Journal of Molecular Medicine 1998 76 3-4 172 183 (Pubitemid 28098703)
    • (1998) Journal of Molecular Medicine , vol.76 , Issue.3-4 , pp. 172-183
    • Smoyer, W.E.1    Mundel, P.2
  • 54
    • 0842280714 scopus 로고    scopus 로고
    • Dynamic (re)organization of the podocyte actin cytoskeleton in the nephrotic syndrome
    • DOI 10.1007/s00467-003-1367-y
    • Oh J., Reiser J., Mundel P., Dynamic (re)organization of the podocyte actin cytoskeleton in the nephrotic syndrome Pediatric Nephrology 2004 19 2 130 137 (Pubitemid 38181002)
    • (2004) Pediatric Nephrology , vol.19 , Issue.2 , pp. 130-137
    • Oh, J.1    Reiser, J.2    Mundel, P.3
  • 55
    • 0035210580 scopus 로고    scopus 로고
    • Caught flat-footed: Podocyte damage and the molecular bases of focal glomerulosclerosis
    • DOI 10.1172/JCI200114629
    • Kerjaschki D., Caught flat-footed: podocyte damage and the molecular bases of focal glomerulosclerosis Journal of Clinical Investigation 2001 108 11 1583 1587 (Pubitemid 33144868)
    • (2001) Journal of Clinical Investigation , vol.108 , Issue.11 , pp. 1583-1587
    • Kerjaschki, D.1
  • 56
    • 0034126357 scopus 로고    scopus 로고
    • Getting a foothold in nephrotic syndrome
    • DOI 10.1038/74139
    • Somlo S., Mundel P., Getting a foothold in nephrotic syndrome Nature Genetics 2000 24 4 333 335 (Pubitemid 30187426)
    • (2000) Nature Genetics , vol.24 , Issue.4 , pp. 333-335
    • Somlo, S.1    Mundel, P.2
  • 59
  • 61
    • 0038136885 scopus 로고    scopus 로고
    • CD2-associated protein haploinsufficiency is linked to glomerular disease susceptibility
    • DOI 10.1126/science.1081068
    • Kim J. H., Wu H., Green G., Winkler C. A., Kopp J. B., Miner J. H., Unanue E. R., Shawl A. S., CD2-associated protein haploinsufficiency is linked to glomerular disease susceptibility Science 2003 300 5623 1298 1300 (Pubitemid 36618242)
    • (2003) Science , vol.300 , Issue.5623 , pp. 1298-1300
    • Kim, J.H.1    Wu, H.2    Green, G.3    Winkler, C.A.4    Kopp, J.B.5    Miner, J.H.6    Unanue, E.R.7    Shawl, A.S.8
  • 62
    • 28244484957 scopus 로고    scopus 로고
    • Two mouse cofilin isoforms, muscle-type (MCF) and non-muscle type (NMCF), interact with F-actin with different efficiencies
    • DOI 10.1093/jb/mvi152
    • Nakashima K., Sato N., Nakagaki T., Abe H., Ono S., Obinata T., Two mouse cofilin isoforms, muscle-type (MCF) and non-muscle type (NMCF), interact with F-actin with different efficiencies Journal of Biochemistry 2005 138 4 519 526 (Pubitemid 41703706)
    • (2005) Journal of Biochemistry , vol.138 , Issue.4 , pp. 519-526
    • Nakashima, K.1    Sato, N.2    Nakagaki, T.3    Abe, H.4    Ono, S.5    Obinata, T.6
  • 63
    • 0036304481 scopus 로고    scopus 로고
    • Determining the differences in actin binding by human ADF and cofilin
    • DOI 10.1006/jmbi.2001.5280
    • Yeoh S., Pope B., Mannherz H. G., Weeds A., Determining the differences in actin binding by human ADF and cofilin Journal of Molecular Biology 2002 315 4 911 925 (Pubitemid 34729336)
    • (2002) Journal of Molecular Biology , vol.315 , Issue.4 , pp. 911-925
    • Yeoh, S.1    Pope, B.2    Mannherz, H.G.3    Weeds, A.4
  • 64
    • 79952637148 scopus 로고    scopus 로고
    • The F-actin severing protein cofilin-1 is required for RNA polymerase II transcription elongation
    • Obrdlik A., Percipalle P., The F-actin severing protein cofilin-1 is required for RNA polymerase II transcription elongation Nucleus 2011 2 1 72 79
    • (2011) Nucleus , vol.2 , Issue.1 , pp. 72-79
    • Obrdlik, A.1    Percipalle, P.2
  • 66
    • 5344270514 scopus 로고    scopus 로고
    • Regulation of ADF/cofilin phosphorylation and synaptic function by LIM-kinase
    • DOI 10.1016/j.neuropharm.2004.06.030, PII S0028390804001868, The Cytoskeleton and Synaptic Function
    • Meng Y., Takahashi H., Meng J., Zhang Y., Lu G., Asrar S., Nakamura T., Jia Z., Regulation of ADF/cofilin phosphorylation and synaptic function by LIM-kinase Neuropharmacology 2004 47 5 746 754 (Pubitemid 39348956)
    • (2004) Neuropharmacology , vol.47 , Issue.5 , pp. 746-754
    • Meng, Y.1    Takahashi, H.2    Meng, J.3    Zhang, Y.4    Lu, G.5    Asrar, S.6    Nakamura, T.7    Jia, Z.8
  • 67
    • 45549088754 scopus 로고    scopus 로고
    • Slingshot-3 dephosphorylates ADF/cofilin but is dispensable for mouse development
    • DOI 10.1002/dvg.20389
    • Kousaka K., Kiyonari H., Oshima N., Nagafuchi A., Shima Y., Chisaka O., Uemura T., Slingshot-3 dephosphorylates ADF/cofilin but is dispensable for mouse development Genesis 2008 46 5 246 255 (Pubitemid 351961760)
    • (2008) Genesis , vol.46 , Issue.5 , pp. 246-255
    • Kousaka, K.1    Kiyonari, H.2    Oshima, N.3    Nagafuchi, A.4    Shima, Y.5    Chisaka, O.6    Uemura, T.7
  • 70
    • 33644877366 scopus 로고    scopus 로고
    • TGF-β concentration specifies differential signaling profiles of growth arrest/differentiation and apoptosis in podocytes
    • DOI 10.1681/ASN.2004121055
    • Wu D. T., Bitzer M., Ju W., Mundel P., Bttinger E. P., TGF- concentration specifies differential signaling profiles of growth arrest/differentiation and apoptosis in podocytes Journal of the American Society of Nephrology 2005 16 11 3211 3221 (Pubitemid 46179327)
    • (2005) Journal of the American Society of Nephrology , vol.16 , Issue.11 , pp. 3211-3221
    • Wu, D.T.1    Bitzer, M.2    Ju, W.3    Mundel, P.4    Bottinger, E.P.5
  • 71
    • 34447634510 scopus 로고    scopus 로고
    • Phorbol 12-myristate 13-acetate (PMA)-induced migration of glioblastoma cells is mediated via p38MAPK/Hsp27 pathway
    • DOI 10.1016/j.bcp.2007.06.018, PII S0006295207003644
    • Nomura N., Nomura M., Sugiyama K., Hamada J. I., Phorbol 12-myristate 13-acetate (PMA)-induced migration of glioblastoma cells is mediated via p38MAPK/Hsp27 pathway Biochemical Pharmacology 2007 74 5 690 701 (Pubitemid 47087761)
    • (2007) Biochemical Pharmacology , vol.74 , Issue.5 , pp. 690-701
    • Nomura, N.1    Nomura, M.2    Sugiyama, K.3    Hamada, J.-I.4
  • 72
    • 79551485331 scopus 로고    scopus 로고
    • PMA-induced up-regulation of TBX3 is mediated by AP-1 and contributes to breast cancer cell migration
    • Mowla S., Pinnock R., Leaner V. D., Goding C. R., Prince S., PMA-induced up-regulation of TBX3 is mediated by AP-1 and contributes to breast cancer cell migration Biochemical Journal 2011 433 1 145 153
    • (2011) Biochemical Journal , vol.433 , Issue.1 , pp. 145-153
    • Mowla, S.1    Pinnock, R.2    Leaner, V.D.3    Goding, C.R.4    Prince, S.5
  • 73
    • 1042302750 scopus 로고    scopus 로고
    • High Glucose-Induced Upregulation of Osteopontin Is Mediated via Rho/Rho Kinase Pathway in Cultured Rat Aortic Smooth Muscle Cells
    • DOI 10.1161/01.ATV.0000112012.33770.2a
    • Kawamura H., Yokote K., Asaumi S., Kobayashi K., Fujimoto M., Maezawa Y., Saito Y., Mori S., High glucose-induced upregulation of osteopontin is mediated via Rho/Rho kinase pathway in cultured rat aortic smooth muscle cells Arteriosclerosis, Thrombosis, and Vascular Biology 2004 24 2 276 281 (Pubitemid 38197578)
    • (2004) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.24 , Issue.2 , pp. 276-281
    • Kawamura, H.1    Yokote, K.2    Asaumi, S.3    Kobayashi, K.4    Fujimoto, M.5    Maezawa, Y.6    Saito, Y.7    Mori, S.8
  • 74
    • 0037062481 scopus 로고    scopus 로고
    • 3-Hydroxy-3-methylglutaryl CoA reductase inhibitors prevent high glucose-induced proliferation of mesangial cells via modulation of Rho GTPase/p21 signaling pathway: Implications for diabetic nephropathy
    • DOI 10.1073/pnas.122228799
    • Danesh F. R., Sadeghit M. M., Amro N., Philips C., Zeng L., Lin S., Sahai A., Kanwar Y. S., 3-Hydroxy-3-methylglutaryl CoA reductase inhibitors prevent high glucose-induced proliferation of mesangial cells via modulation of Rho GTPase/p21 signaling pathway: implications for diabetic nephropathy Proceedings of the National Academy of Sciences of the United States of America 2002 99 12 8301 8305 (Pubitemid 34651047)
    • (2002) Proceedings of the National Academy of Sciences of the United States of America , vol.99 , Issue.12 , pp. 8301-8305
    • Danesh, F.R.1    Sadeghit, M.M.2    Amro, N.3    Philips, C.4    Zeng, L.5    Lin, S.6    Sahai, A.7    Kanwar, Y.S.8
  • 75
    • 40949137434 scopus 로고    scopus 로고
    • Targeting of RhoA/ROCK signaling ameliorates progression of diabetic nephropathy independent of glucose control
    • Kolavennu V., Zeng L., Peng H., Wang Y., Danesh F. R., Targeting of RhoA/ROCK signaling ameliorates progression of diabetic nephropathy independent of glucose control Diabetes 2008 57 3 714 723
    • (2008) Diabetes , vol.57 , Issue.3 , pp. 714-723
    • Kolavennu, V.1    Zeng, L.2    Peng, H.3    Wang, Y.4    Danesh, F.R.5
  • 77
    • 78650162527 scopus 로고    scopus 로고
    • Effects of systemic inhibition of Rho kinase on blood pressure and renal haemodynamics in diabetic rats
    • Komers R., Oyama T. T., Beard D. R., Anderson S., Effects of systemic inhibition of Rho kinase on blood pressure and renal haemodynamics in diabetic rats British Journal of Pharmacology 2011 162 1 163 174
    • (2011) British Journal of Pharmacology , vol.162 , Issue.1 , pp. 163-174
    • Komers, R.1    Oyama, T.T.2    Beard, D.R.3    Anderson, S.4
  • 78
    • 24144479246 scopus 로고    scopus 로고
    • Cofilin, actin and their complex observed in vivo using fluorescence resonance energy transfer
    • DOI 10.1529/biophysj.105.062083
    • Chhabra D., Dos Remedios C. G., Cofilin, actin and their complex observed in vivo using fluorescence resonance energy transfer Biophysical Journal 2005 89 3 1902 1908 (Pubitemid 41233545)
    • (2005) Biophysical Journal , vol.89 , Issue.3 , pp. 1902-1908
    • Chhabra, D.1    Dos Remedios, C.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.