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Volumn 12, Issue 12, 2002, Pages 598-605

ADF/cofilin and actin dynamics in disease

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; COFILIN; ACTIN; ACTIN BINDING PROTEIN; ACTIN DEPOLYMERIZING FACTOR; DSTN PROTEIN, HUMAN;

EID: 0036900955     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0962-8924(02)02404-2     Document Type: Review
Times cited : (238)

References (75)
  • 1
    • 0034992606 scopus 로고    scopus 로고
    • Nemaline myopathy caused by mutations in the muscle alpha-skeletal actin gene
    • Ilkovski B., et al. Nemaline myopathy caused by mutations in the muscle alpha-skeletal actin gene. Am. J. Hum. Genet. 68:2001;1333-1343.
    • (2001) Am. J. Hum. Genet. , vol.68 , pp. 1333-1343
    • Ilkovski, B.1
  • 2
    • 0021173559 scopus 로고
    • A mutation in actin associated with neoplastic transformation
    • Kakunaga T., et al. A mutation in actin associated with neoplastic transformation. Fed. Proc. 43:1984;2275-2279.
    • (1984) Fed. Proc. , vol.43 , pp. 2275-2279
    • Kakunaga, T.1
  • 3
    • 0031878090 scopus 로고    scopus 로고
    • The ADF homology (ADF-H) domain: A highly exploited actin-binding module
    • Lappalainen P., et al. The ADF homology (ADF-H) domain: a highly exploited actin-binding module. Mol. Biol. Cell. 9:1998;1951-1959.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1951-1959
    • Lappalainen, P.1
  • 4
    • 0033280237 scopus 로고    scopus 로고
    • Proteins of the ADF/cofilin family: Essential regulators of actin dynamics
    • Bamburg J.R. Proteins of the ADF/cofilin family: essential regulators of actin dynamics. Annu. Rev. Cell Dev. Biol. 15:1999;185-230.
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 185-230
    • Bamburg, J.R.1
  • 5
    • 0036153765 scopus 로고    scopus 로고
    • The three mouse ADF/cofilins evolved to fulfill cell-specific requirements for actin dynamics
    • Vartiainen M.K., et al. The three mouse ADF/cofilins evolved to fulfill cell-specific requirements for actin dynamics. Mol. Biol. Cell. 13:2002;183-194.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 183-194
    • Vartiainen, M.K.1
  • 6
    • 0027446345 scopus 로고
    • Cofilin is an essential component of the yeast cortical cytoskeleton
    • Moon A.L., et al. Cofilin is an essential component of the yeast cortical cytoskeleton. J. Cell Biol. 120:1993;421-435.
    • (1993) J. Cell Biol. , vol.120 , pp. 421-435
    • Moon, A.L.1
  • 7
    • 0027475652 scopus 로고
    • r actin-binding and depolymerizing protein
    • r actin-binding and depolymerizing protein. Gene. 124:1993;115-120.
    • (1993) Gene , vol.124 , pp. 115-120
    • Iida, K.1
  • 8
    • 0030797467 scopus 로고    scopus 로고
    • Cofilin promotes rapid actin filament turnover in vivo
    • Lappalainen P., Drubin D.G. Cofilin promotes rapid actin filament turnover in vivo. Nature. 388:1997;78-82.
    • (1997) Nature , vol.388 , pp. 78-82
    • Lappalainen, P.1    Drubin, D.G.2
  • 9
    • 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., Borisy G.G. Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia. J. Cell Biol. 145:1999;1009-1026.
    • (1999) J. Cell Biol. , vol.145 , pp. 1009-1026
    • Svitkina, T.M.1    Borisy, G.G.2
  • 10
    • 0027494863 scopus 로고
    • Analysis of the interactions of actin depolymerizing factor with G- and F-actin
    • Hayden S.M., et al. Analysis of the interactions of actin depolymerizing factor with G- and F-actin. Biochemistry. 32:1993;9994-10004.
    • (1993) Biochemistry , vol.32 , pp. 9994-10004
    • Hayden, S.M.1
  • 11
    • 0027439319 scopus 로고
    • Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments
    • Hawkins M., et al. Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments. Biochemistry. 32:1993;9985-9993.
    • (1993) Biochemistry , vol.32 , pp. 9985-9993
    • Hawkins, M.1
  • 12
    • 0028357931 scopus 로고
    • Actophorin preferentially binds monomeric ADP-actin over ATP-bound actin: Consequences for cell locomotion
    • Maciver S.K., Weeds A.G. Actophorin preferentially binds monomeric ADP-actin over ATP-bound actin: consequences for cell locomotion. FEBS Lett. 347:1994;251-256.
    • (1994) FEBS Lett. , vol.347 , pp. 251-256
    • Maciver, S.K.1    Weeds, A.G.2
  • 13
    • 0030843484 scopus 로고    scopus 로고
    • Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: Implication in actin-based motility
    • Carlier M.F., et al. Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: implication in actin-based motility. J. Cell Biol. 136:1997;1307-1322.
    • (1997) J. Cell Biol. , vol.136 , pp. 1307-1322
    • Carlier, M.F.1
  • 14
    • 0030820734 scopus 로고    scopus 로고
    • Cofilin changes the twist of F-actin: Implications for actin filament dynamics and cellular function
    • McGough A., et al. Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function. J. Cell Biol. 138:1997;771-781.
    • (1997) J. Cell Biol. , vol.138 , pp. 771-781
    • McGough, A.1
  • 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
    • Galkin V.E., et al. Actin depolymerizing factor stabilizes an existing state of F-actin and can change the tilt of F-actin subunits. J. Cell Biol. 153:2001;75-86.
    • (2001) J. Cell Biol. , vol.153 , pp. 75-86
    • Galkin, V.E.1
  • 16
    • 0021964668 scopus 로고
    • Opposite effects of cofilin and profilin from porcine brain on rate of exchange of actin-bound adenosine 5(-triphosphate
    • Nishida E. Opposite effects of cofilin and profilin from porcine brain on rate of exchange of actin-bound adenosine 5(-triphosphate. Biochemistry. 26:1985;1160-1164.
    • (1985) Biochemistry , vol.26 , pp. 1160-1164
    • Nishida, E.1
  • 17
    • 0035399959 scopus 로고    scopus 로고
    • How is actin polymerization nucleated in vivo?
    • Condeelis J. How is actin polymerization nucleated in vivo? Trends Cell Biol. 11:2001;288-293.
    • (2001) Trends Cell Biol. , vol.11 , pp. 288-293
    • Condeelis, J.1
  • 18
    • 0036304481 scopus 로고    scopus 로고
    • Determining the differences in actin binding by human ADF and cofilin
    • Yeoh S., et al. Determining the differences in actin binding by human ADF and cofilin. J. Mol. Biol. 315:2002;911-925.
    • (2002) J. Mol. Biol. , vol.315 , pp. 911-925
    • Yeoh, S.1
  • 19
    • 0023387681 scopus 로고
    • Cofilin is a component of intranuclear and cytoplasmic actin rods induced in cultured cells
    • Nishida E., et al. Cofilin is a component of intranuclear and cytoplasmic actin rods induced in cultured cells. Proc. Natl. Acad. Sci. U. S. A. 84:1987;5262-5266.
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , pp. 5262-5266
    • Nishida, E.1
  • 20
    • 0032536820 scopus 로고    scopus 로고
    • Nuclear export of actin: A novel mechanism regulating the subcellular localization of a major cytoskeletal protein
    • Wada A., et al. Nuclear export of actin: a novel mechanism regulating the subcellular localization of a major cytoskeletal protein. EMBO J. 17:1998;1635-1641.
    • (1998) EMBO J. , vol.17 , pp. 1635-1641
    • Wada, A.1
  • 21
    • 0032567080 scopus 로고    scopus 로고
    • Rapid and phosphoinositol-dependent binding of the SWI/SNF-like BAF complex to chromatin after T lymphocyte receptor signaling
    • Zhao K., et al. Rapid and phosphoinositol-dependent binding of the SWI/SNF-like BAF complex to chromatin after T lymphocyte receptor signaling. Cell. 95:1998;625-636.
    • (1998) Cell , vol.95 , pp. 625-636
    • Zhao, K.1
  • 22
    • 0037022632 scopus 로고    scopus 로고
    • Phosphatidylinositol-dependent actin filament binding by the SWI/SNF-like BAF chromatin remodeling complex
    • Rando O.J., et al. Phosphatidylinositol-dependent actin filament binding by the SWI/SNF-like BAF chromatin remodeling complex. Proc. Natl. Acad. Sci. U. S. A. 99:2002;2824-2829.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 2824-2829
    • Rando, O.J.1
  • 23
    • 0029149885 scopus 로고
    • Reactivation of phosphorylated actin depolymerizing factor and identification of the regulatory site
    • Agnew B.J., et al. Reactivation of phosphorylated actin depolymerizing factor and identification of the regulatory site. J. Biol. Chem. 270:1995;17582-17587.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17582-17587
    • Agnew, B.J.1
  • 24
    • 0029678546 scopus 로고    scopus 로고
    • Phosphorylation of Ser-3 of cofilin regulates its essential function on actin
    • Moriyama K., et al. Phosphorylation of Ser-3 of cofilin regulates its essential function on actin. Genes Cells. 1:1996;73-86.
    • (1996) Genes Cells , vol.1 , pp. 73-86
    • Moriyama, K.1
  • 25
    • 0034645797 scopus 로고    scopus 로고
    • Phosphorylation of Acanthamoeba actophorin (ADF/cofilin) blocks interaction with actin without a change in atomic structure
    • Blanchoin L., et al. Phosphorylation of Acanthamoeba actophorin (ADF/cofilin) blocks interaction with actin without a change in atomic structure. J. Mol. Biol. 295:2000;203-211.
    • (2000) J. Mol. Biol. , vol.295 , pp. 203-211
    • Blanchoin, L.1
  • 26
    • 0032565962 scopus 로고    scopus 로고
    • Regulation of actin dynamics through phosphorylation of cofilin by LIM-kinase
    • Arber S., et al. Regulation of actin dynamics through phosphorylation of cofilin by LIM-kinase. Nature. 393:1998;805-809.
    • (1998) Nature , vol.393 , pp. 805-809
    • Arber, S.1
  • 27
    • 0032565769 scopus 로고    scopus 로고
    • Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization
    • Yang N., et al. Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization. Nature. 393:1998;809-812.
    • (1998) Nature , vol.393 , pp. 809-812
    • Yang, N.1
  • 28
    • 0032853684 scopus 로고    scopus 로고
    • Identification and characterization of TESK2, a novel member of the LIMK/TESK family of protein kinases, predominantly expressed in testis
    • Rosok O., et al. Identification and characterization of TESK2, a novel member of the LIMK/TESK family of protein kinases, predominantly expressed in testis. Genomics. 61:1999;44-54.
    • (1999) Genomics , vol.61 , pp. 44-54
    • Rosok, O.1
  • 29
    • 0035943704 scopus 로고    scopus 로고
    • Cytoskeletal changes regulated by the PAK4 serine/threonine kinase are mediated by LIM kinase 1 and cofilin
    • Dan C., et al. Cytoskeletal changes regulated by the PAK4 serine/threonine kinase are mediated by LIM kinase 1 and cofilin. J. Biol. Chem. 276:2001;32115-32121.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32115-32121
    • Dan, C.1
  • 30
    • 0034806780 scopus 로고    scopus 로고
    • Cell-type-specific expression of a TESK1 promoter-linked lacZ gene in transgenic mice
    • Toshima J., et al. Cell-type-specific expression of a TESK1 promoter-linked lacZ gene in transgenic mice. Biochem. Biophys. Res. Commun. 286:2001;566-573.
    • (2001) Biochem. Biophys. Res. Commun. , vol.286 , pp. 566-573
    • Toshima, J.1
  • 31
    • 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., et al. Cofilin phosphorylation by protein kinase testicular protein kinase 1 and its role in integrin-mediated actin reorganization and focal adhesion formation. Mol. Biol. Cell. 12:2001;1131-1145.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1131-1145
    • Toshima, J.1
  • 32
    • 0036644975 scopus 로고    scopus 로고
    • Guanine nucleotide exchange factors for Rho GTPases: Turning on the switch
    • Schmidt A., Hall A. Guanine nucleotide exchange factors for Rho GTPases: turning on the switch. Genes Dev. 16:2002;1587-1609.
    • (2002) Genes Dev. , vol.16 , pp. 1587-1609
    • Schmidt, A.1    Hall, A.2
  • 33
    • 0036794093 scopus 로고    scopus 로고
    • 14-3-3 regulates actin dynamics by stabilizing phosphorylated cofilin
    • Gohla A., Bokoch G. 14-3-3 regulates actin dynamics by stabilizing phosphorylated cofilin. Curr. Biol. 12:2002;1704-1710.
    • (2002) Curr. Biol. , vol.12 , pp. 1704-1710
    • Gohla, A.1    Bokoch, G.2
  • 34
    • 0037169335 scopus 로고    scopus 로고
    • Control of actin reorganization by slingshot, a family of phosphatases that dephosphorylate ADF/cofilin
    • Niwa R., et al. Control of actin reorganization by slingshot, a family of phosphatases that dephosphorylate ADF/cofilin. Cell. 108:2002;233-246.
    • (2002) Cell , vol.108 , pp. 233-246
    • Niwa, R.1
  • 35
    • 0037343138 scopus 로고    scopus 로고
    • Specification of actin filament function and molecular composition by tropomyosin isoforms
    • in press)
    • Bryce, N.S. et al. Specification of actin filament function and molecular composition by tropomyosin isoforms, Mol. Biol. Cell (in press).
    • Mol. Biol. Cell
    • Bryce, N.S.1
  • 36
    • 0020025754 scopus 로고
    • Tropomyosin binding to F-actin protects the F-actin from disassembly by brain actin-depolymerizing factor (ADF)
    • Bernstein B.W., Bamburg J.R. Tropomyosin binding to F-actin protects the F-actin from disassembly by brain actin-depolymerizing factor (ADF). Cell Motil. 2:1982;1-8.
    • (1982) Cell Motil. , vol.2 , pp. 1-8
    • Bernstein, B.W.1    Bamburg, J.R.2
  • 37
    • 0037128928 scopus 로고    scopus 로고
    • Tropomyosin inhibits ADF/cofilin-dependent actin filament dynamics
    • Ono S., Ono K. Tropomyosin inhibits ADF/cofilin-dependent actin filament dynamics. J. Cell Biol. 156:2002;1065-1076.
    • (2002) J. Cell Biol. , vol.156 , pp. 1065-1076
    • Ono, S.1    Ono, K.2
  • 38
    • 0022453434 scopus 로고
    • Nucleotide exchange between cytosolic ATP and F-actin-bound ADP may be a major energy-utilizing process in unstimulated platelets
    • Daniel J.L., et al. Nucleotide exchange between cytosolic ATP and F-actin-bound ADP may be a major energy-utilizing process in unstimulated platelets. Eur. J. Biochem. 156:1986;677-684.
    • (1986) Eur. J. Biochem. , vol.156 , pp. 677-684
    • Daniel, J.L.1
  • 39
    • 0012009045 scopus 로고    scopus 로고
    • ATP-hydrolysis by actin is a major energy drain for neurons
    • in press
    • Bernstein, B.W. and Bamburg, J.R. ATP-hydrolysis by actin is a major energy drain for neurons. J. Neurosci. (in press).
    • J. Neurosci.
    • Bernstein, B.W.1    Bamburg, J.R.2
  • 40
    • 0032941377 scopus 로고    scopus 로고
    • Ischemia activates actin depolymerizing factor: Role in proximal tubule microvillar actin alterations
    • Schwartz N., et al. Ischemia activates actin depolymerizing factor: role in proximal tubule microvillar actin alterations. Am. J. Physiol. 276:1999;F544-F551.
    • (1999) Am. J. Physiol. , vol.276
    • Schwartz, N.1
  • 41
    • 0035026174 scopus 로고    scopus 로고
    • Ischemic injury induces ADF relocalization to the apical domain of rat proximal tubule cells
    • Ashworth S.L., et al. Ischemic injury induces ADF relocalization to the apical domain of rat proximal tubule cells. Am. J. Physiol. Renal Physiol. 280:2001;F886-F894.
    • (2001) Am. J. Physiol. Renal Physiol. , vol.280
    • Ashworth, S.L.1
  • 42
    • 0034282106 scopus 로고    scopus 로고
    • Neurodegenerative stimuli induce persistent ADF/cofilin-actin rods that disrupt distal neurite function
    • Minamide L.S., et al. Neurodegenerative stimuli induce persistent ADF/cofilin-actin rods that disrupt distal neurite function. Nat. Cell Biol. 2:2000;628-636.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 628-636
    • Minamide, L.S.1
  • 43
    • 0035965994 scopus 로고    scopus 로고
    • Human cofilin forms oligomers exhibiting actin bundling activity
    • Pfannstiel J., et al. Human cofilin forms oligomers exhibiting actin bundling activity. J. Biol. Chem. 276:2001;49476-49484.
    • (2001) J. Biol. Chem. , vol.276 , pp. 49476-49484
    • Pfannstiel, J.1
  • 44
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid β protein toxicity
    • Behl C., et al. Hydrogen peroxide mediates amyloid β protein toxicity. Cell. 77:1994;817-827.
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1
  • 45
    • 0036790789 scopus 로고    scopus 로고
    • Aggregation of actin and cofilin in identical twins with juvenile-onset dystonia
    • Gearing M., et al. Aggregation of actin and cofilin in identical twins with juvenile-onset dystonia. Ann. Neurol. 52:2002;465-476.
    • (2002) Ann. Neurol. , vol.52 , pp. 465-476
    • Gearing, M.1
  • 46
    • 0028286860 scopus 로고
    • Hirano bodies and related neuronal inclusions
    • Hirano A. Hirano bodies and related neuronal inclusions. Neuropathol. Appl. Neurobiol. 20:1994;3-11.
    • (1994) Neuropathol. Appl. Neurobiol. , vol.20 , pp. 3-11
    • Hirano, A.1
  • 47
    • 0036573221 scopus 로고    scopus 로고
    • Formation of Hirano bodies in Dictyostelium and mammalian cells induced by expression of a modified form of an actin-crosslinking protein
    • Maselli A.G., et al. Formation of Hirano bodies in Dictyostelium and mammalian cells induced by expression of a modified form of an actin-crosslinking protein. J. Cell Sci. 115:2002;1939-1952.
    • (2002) J. Cell Sci. , vol.115 , pp. 1939-1952
    • Maselli, A.G.1
  • 48
    • 0028803993 scopus 로고
    • Two actin binding proteins, actin depolymerizing factor and cofilin, are associated with Hirano bodies
    • Maciver S.K., Harrington C.R. Two actin binding proteins, actin depolymerizing factor and cofilin, are associated with Hirano bodies. Neuroreport. 6:1995;1985-1988.
    • (1995) Neuroreport , vol.6 , pp. 1985-1988
    • Maciver, S.K.1    Harrington, C.R.2
  • 49
    • 0023742179 scopus 로고
    • Colocalization of F-actin and 34-kilodalton actin bundling protein in Dictyostelium amoebae and cultured fibroblasts
    • Johns J.A., et al. Colocalization of F-actin and 34-kilodalton actin bundling protein in Dictyostelium amoebae and cultured fibroblasts. Cell Motil. Cytoskeleton. 9:1988;205-218.
    • (1988) Cell Motil. Cytoskeleton , vol.9 , pp. 205-218
    • Johns, J.A.1
  • 50
    • 0033813884 scopus 로고    scopus 로고
    • Comparative genomic sequence analysis of the Williams syndrome region (LIMK1-RFC2) of human chromosome 7q11.23
    • Martindale D.W., et al. Comparative genomic sequence analysis of the Williams syndrome region (LIMK1-RFC2) of human chromosome 7q11.23. Mamm. Genome. 11:2000;890-898.
    • (2000) Mamm. Genome , vol.11 , pp. 890-898
    • Martindale, D.W.1
  • 51
    • 0033134860 scopus 로고    scopus 로고
    • Bridging cognition, the brain and molecular genetics: Evidence from Williams syndrome
    • Bellugi U., et al. Bridging cognition, the brain and molecular genetics: evidence from Williams syndrome. Trends Neurosci. 22:1999;197-207.
    • (1999) Trends Neurosci. , vol.22 , pp. 197-207
    • Bellugi, U.1
  • 52
    • 18444372636 scopus 로고    scopus 로고
    • Abnormal spine morphology and enhanced LTP in LIMK-1 knockout mice
    • Meng Y., et al. Abnormal spine morphology and enhanced LTP in LIMK-1 knockout mice. Neuron. 35:2002;121-133.
    • (2002) Neuron , vol.35 , pp. 121-133
    • Meng, Y.1
  • 53
    • 0035096551 scopus 로고    scopus 로고
    • Phosphorylation of cofilin by LIM-kinase is necessary for semaphorin 3A-induced growth cone collapse
    • Aizawa H., et al. Phosphorylation of cofilin by LIM-kinase is necessary for semaphorin 3A-induced growth cone collapse. Nat. Neurosci. 4:2001;367-373.
    • (2001) Nat. Neurosci. , vol.4 , pp. 367-373
    • Aizawa, H.1
  • 54
    • 0024390193 scopus 로고
    • An actin-depolymerizing protein in embryonic chicken skeletal muscle: Purification and characterization
    • Abe H., Obinata T. An actin-depolymerizing protein in embryonic chicken skeletal muscle: purification and characterization. J. Biochem. (Tokyo). 106:1989;172-180.
    • (1989) J. Biochem. (Tokyo) , vol.106 , pp. 172-180
    • Abe, H.1    Obinata, T.2
  • 55
    • 0028283542 scopus 로고
    • Characterization of a novel cofilin isoform that is predominantly expressed in mammalian skeletal muscle
    • Ono S., et al. Characterization of a novel cofilin isoform that is predominantly expressed in mammalian skeletal muscle. J. Biol. Chem. 269:1994;15280-15286.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15280-15286
    • Ono, S.1
  • 56
    • 0033519332 scopus 로고    scopus 로고
    • UNC-60B, an ADF/cofilin family protein, is required for proper assembly of actin into myofibrils in Caenorhabditis elegans body wall muscle
    • Ono S., et al. UNC-60B, an ADF/cofilin family protein, is required for proper assembly of actin into myofibrils in Caenorhabditis elegans body wall muscle. J. Cell Biol. 145:1999;491-502.
    • (1999) J. Cell Biol. , vol.145 , pp. 491-502
    • Ono, S.1
  • 57
    • 0000456656 scopus 로고
    • Increased expression of cofilin in denervated chicken skeletal muscle
    • Shinagawa Y., et al. Increased expression of cofilin in denervated chicken skeletal muscle. Zool. Sci. 10:1993;611-618.
    • (1993) Zool. Sci , vol.10 , pp. 611-618
    • Shinagawa, Y.1
  • 58
    • 0027382214 scopus 로고
    • Increased expression of cofilin in dystrophic chicken and mouse skeletal muscles
    • Hayakawa K., et al. Increased expression of cofilin in dystrophic chicken and mouse skeletal muscles. J. Biochem. (Tokyo). 114:1993;582-587.
    • (1993) J. Biochem. (Tokyo) , vol.114 , pp. 582-587
    • Hayakawa, K.1
  • 59
    • 0034807581 scopus 로고    scopus 로고
    • Cytoskeletal regulation of pulmonary vascular permeability
    • Dudek S.M., Garcia J.G. Cytoskeletal regulation of pulmonary vascular permeability. J. Appl. Physiol. 91:2001;1487-1500.
    • (2001) J. Appl. Physiol. , vol.91 , pp. 1487-1500
    • Dudek, S.M.1    Garcia, J.G.2
  • 60
    • 0034799675 scopus 로고    scopus 로고
    • Sphingosine 1-phosphate promotes endothelial cell barrier integrity by Edg-dependent cytoskeletal rearrangement
    • Garcia J.G., et al. Sphingosine 1-phosphate promotes endothelial cell barrier integrity by Edg-dependent cytoskeletal rearrangement. J. Clin. Invest. 108:2001;689-701.
    • (2001) J. Clin. Invest. , vol.108 , pp. 689-701
    • Garcia, J.G.1
  • 61
    • 0037178873 scopus 로고    scopus 로고
    • MEK mediates v-Src-induced disruption of the actin cytoskeleton via inactivation of the Rho-ROCK-LIM kinase pathway
    • Pawlak G., Helfman D.M. MEK mediates v-Src-induced disruption of the actin cytoskeleton via inactivation of the Rho-ROCK-LIM kinase pathway. J. Biol. Chem. 277:2002;26927-26933.
    • (2002) J. Biol. Chem. , vol.277 , pp. 26927-26933
    • Pawlak, G.1    Helfman, D.M.2
  • 62
    • 0033977699 scopus 로고    scopus 로고
    • Regulating actin-filament dynamics in vivo
    • Chen H., et al. Regulating actin-filament dynamics in vivo. Trends Biochem. Sci. 25:2000;19-23.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 19-23
    • Chen, H.1
  • 63
    • 0037039167 scopus 로고    scopus 로고
    • Cofilin produces newly polymerized actin filaments that are preferred for dendritic nucleation by the Arp2/3 complex
    • Ichetovkin I., et al. Cofilin produces newly polymerized actin filaments that are preferred for dendritic nucleation by the Arp2/3 complex. Curr. Biol. 12:2002;79-84.
    • (2002) Curr. Biol. , vol.12 , pp. 79-84
    • Ichetovkin, I.1
  • 64
    • 0029867539 scopus 로고    scopus 로고
    • Xenopus laevis actin-depolymerizing factor/cofilin: A phosphorylation-regulated protein essential for development
    • Abe H., et al. Xenopus laevis actin-depolymerizing factor/cofilin: a phosphorylation-regulated protein essential for development. J. Cell Biol. 132:1996;871-885.
    • (1996) J. Cell Biol. , vol.132 , pp. 871-885
    • Abe, H.1
  • 65
    • 0037077214 scopus 로고    scopus 로고
    • Mitosis-specific activation of LIM motif-containing protein kinase and roles of cofilin phosphorylation and dephosphorylation in mitosis
    • Amano T., et al. Mitosis-specific activation of LIM motif-containing protein kinase and roles of cofilin phosphorylation and dephosphorylation in mitosis. J. Biol. Chem. 277:2002;22093-22102.
    • (2002) J. Biol. Chem. , vol.277 , pp. 22093-22102
    • Amano, T.1
  • 66
    • 0033653820 scopus 로고    scopus 로고
    • Intracellular pH modulation of ADF/cofilin proteins
    • Bernstein B.W., et al. Intracellular pH modulation of ADF/cofilin proteins. Cell Motil. Cytoskeleton. 47:2000;319-336.
    • (2000) Cell Motil. Cytoskeleton , vol.47 , pp. 319-336
    • Bernstein, B.W.1
  • 67
    • 0034279330 scopus 로고    scopus 로고
    • Changes in tumorigenesis- and angiogenesis-related gene transcript abundance profiles in ovarian cancer detected by tailored high density cDNA arrays
    • Martoglio A.M., et al. Changes in tumorigenesis- and angiogenesis-related gene transcript abundance profiles in ovarian cancer detected by tailored high density cDNA arrays. Mol. Med. 6:2000;750-765.
    • (2000) Mol. Med. , vol.6 , pp. 750-765
    • Martoglio, A.M.1
  • 68
    • 0035153556 scopus 로고    scopus 로고
    • Cofilin/ADF is required for cell motility during Drosophila ovary development and oogenesis
    • Chen J., et al. Cofilin/ADF is required for cell motility during Drosophila ovary development and oogenesis. Nat. Cell Biol. 3:2001;204-209.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 204-209
    • Chen, J.1
  • 69
    • 0035862811 scopus 로고    scopus 로고
    • Functional involvement of Xenopus LIM kinases in progression of oocyte maturation
    • Takahashi T., et al. Functional involvement of Xenopus LIM kinases in progression of oocyte maturation. Dev. Biol. 229:2001;554-567.
    • (2001) Dev. Biol. , vol.229 , pp. 554-567
    • Takahashi, T.1
  • 70
    • 0037081289 scopus 로고    scopus 로고
    • Impaired spermatogenic ability of testicular germ cells in mice deficient in the LIM-kinase 2 gene
    • Takahashi H., et al. Impaired spermatogenic ability of testicular germ cells in mice deficient in the LIM-kinase 2 gene. Dev. Biol. 241:2002;259-272.
    • (2002) Dev. Biol. , vol.241 , pp. 259-272
    • Takahashi, H.1
  • 71
    • 0034004460 scopus 로고    scopus 로고
    • Cofilin: A missing link between T cell co-stimulation and rearrangement of the actin cytoskeleton
    • Lee K.H., et al. Cofilin: a missing link between T cell co-stimulation and rearrangement of the actin cytoskeleton. Eur. J. Immunol. 30:2000;892-899.
    • (2000) Eur. J. Immunol. , vol.30 , pp. 892-899
    • Lee, K.H.1
  • 72
    • 0036142414 scopus 로고    scopus 로고
    • Stromal cell-derived factor 1alpha activates LIM kinase 1 and induces cofilin phosphorylation for T-cell chemotaxis
    • Nishita M., et al. Stromal cell-derived factor 1alpha activates LIM kinase 1 and induces cofilin phosphorylation for T-cell chemotaxis. Mol. Cell. Biol. 22:2002;774-783.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 774-783
    • Nishita, M.1
  • 73
    • 12244262321 scopus 로고    scopus 로고
    • Products of phosphoinositide specific phospholipase C can trigger dephosphorylation of cofilin in chemoattractant stimulated neutrophils
    • in press
    • Zhan, Q. et al. Products of phosphoinositide specific phospholipase C can trigger dephosphorylation of cofilin in chemoattractant stimulated neutrophils. Cell Motil. Cytoskeleton (in press).
    • Cell Motil. Cytoskeleton
    • Zhan, Q.1
  • 74
    • 0028799957 scopus 로고
    • Mutations in twinstar, a Drosophila gene encoding a cofilin/ADF homologue, result in defects in centrosome migration and cytokinesis
    • Gunsalus K.C., et al. Mutations in twinstar, a Drosophila gene encoding a cofilin/ADF homologue, result in defects in centrosome migration and cytokinesis. J. Cell Biol. 13:1995;1243-1259.
    • (1995) J. Cell Biol. , vol.13 , pp. 1243-1259
    • Gunsalus, K.C.1
  • 75
    • 0034640007 scopus 로고    scopus 로고
    • Mouse models for neural tube closure defects
    • Juriloff D.M., Harris M.J. Mouse models for neural tube closure defects. Hum. Mol. Genet. 9:2000;993-1000.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 993-1000
    • Juriloff, D.M.1    Harris, M.J.2


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