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Volumn 453, Issue 2, 2013, Pages 249-259

ATP-dependent regulation of actin monomer-filament equilibrium by cyclase-associated protein and ADF/cofilin

Author keywords

Actin depolymerizing factor (ADF) cofilin; Actin dynamics; Cyclase associated protein (CAP); Depolymerization; Nucleotide exchange; Polymerization

Indexed keywords

ACTIN; ACTIN DEPOLYMERIZING FACTOR; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; CAENORHABDITIS ELEGANS PROTEIN; COFILIN; CYCLASE ASSOCIATED PROTEIN; MONOMER; NUCLEOTIDE; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 84879576268     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20130491     Document Type: Article
Times cited : (20)

References (50)
  • 1
    • 33847295719 scopus 로고    scopus 로고
    • Mechanism of depolymerization and severing of actin filaments and its significance in cytoskeletal dynamics
    • Ono, S. (2007) Mechanism of depolymerization and severing of actin filaments and its significance in cytoskeletal dynamics. Int. Rev. Cytol. 258, 1-82
    • (2007) Int. Rev. Cytol. , vol.258 , pp. 1-82
    • Ono, S.1
  • 2
    • 0021964668 scopus 로고
    • Opposite effects of cofilin and profilin from porcine brain on rate of exchange of actin-bound adenosine 5′ -triphosphate
    • Nishida, E. (1985) Opposite effects of cofilin and profilin from porcine brain on rate of exchange of actin-bound adenosine 5′ -triphosphate. Biochemistry 24, 1160-1164
    • (1985) Biochemistry , vol.24 , pp. 1160-1164
    • Nishida, E.1
  • 3
    • 0028357931 scopus 로고
    • Actophorin preferentially binds monomeric ADP-actin over ATP-bound actin: Consequences for cell locomotion
    • DOI 10.1016/0014-5793(94)00552-4
    • Maciver, S. K. and Weeds, A. G. (1994) Actophorin preferentially binds monomeric ADP-actin over ATP-bound actin: consequences for cell locomotion. FEBS Lett. 347, 251-256 (Pubitemid 24215406)
    • (1994) FEBS Letters , vol.347 , Issue.2-3 , pp. 251-256
    • Maciver, S.K.1
  • 4
    • 2642580847 scopus 로고    scopus 로고
    • In vitro activity differences between proteins of the ADF/cofilin family define two distinct subgroups
    • DOI 10.1021/bi049797n
    • Chen, H., Bernstein, B. W., Sneider, J. M., Boyle, J. A., Minamide, L. S. and Bamburg, J. R. (2004) In vitro activity differences between proteins of the ADF/cofilin family define two distinct subgroups. Biochemistry 43, 7127-7142 (Pubitemid 38720530)
    • (2004) Biochemistry , vol.43 , Issue.22 , pp. 7127-7142
    • Chen, H.1    Bernstein, B.W.2    Sneider, J.M.3    Boyle, J.A.4    Minamide, L.S.5    Bamburg, J.R.6
  • 5
    • 27444441098 scopus 로고    scopus 로고
    • The two Caenorhabditis elegans actin-depolymerizing factor/cofilin proteins differently enhance actin filament severing and depolymerization
    • DOI 10.1021/bi050933d
    • Yamashiro, S., Mohri, K. and Ono, S. (2005) The two Caenorhabditis elegans actin depolymerizing factor/cofilin proteins differently enhance actin filament severing and depolymerization. Biochemistry 44, 14238-14247 (Pubitemid 41533048)
    • (2005) Biochemistry , vol.44 , Issue.43 , pp. 14238-14247
    • Yamashiro, S.1    Mohri, K.2    Ono, S.3
  • 6
    • 0032475981 scopus 로고    scopus 로고
    • Synergy between actin depolymerizing factor/cofilin and profilin in increasing actin filament turnover
    • DOI 10.1074/jbc.273.40.25602
    • Didry, D., Carlier, M. F. and Pantaloni, D. (1998) Synergy between actin depolymerizing factor/cofilin and profilin in increasing actin filament turnover. J. Biol. Chem. 273, 25602-25611 (Pubitemid 28475780)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.40 , pp. 25602-25611
    • Didry, D.1    Carlier, M.-F.2    Pantaloni, D.3
  • 7
    • 0032566659 scopus 로고    scopus 로고
    • Interaction of actin monomers with Acanthamoeba actophorin (ADF/cofilin) and profilin
    • DOI 10.1074/jbc.273.39.25106
    • Blanchoin, L. and Pollard, T. D. (1998) Interaction of actin monomers with Acanthamoeba actophorin (ADF/cofilin) and profilin. J. Biol. Chem. 273, 25106-25111 (Pubitemid 28443268)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.39 , pp. 25106-25111
    • Blanchoin, L.1    Pollard, T.D.2
  • 8
    • 0027772556 scopus 로고
    • How profilin promotes actin filament assembly in the presence of thymosin β4
    • DOI 10.1016/0092-8674(93)90544-Z
    • Pantaloni, D. and Carlier, M. F. (1993) How profilin promotes actin filament assembly in the presence of thymosin β4. Cell 75, 1007-1014 (Pubitemid 24014557)
    • (1993) Cell , vol.75 , Issue.5 , pp. 1007-1014
    • Pantaloni, D.1    Carlier, M.-F.2
  • 9
    • 77951917756 scopus 로고    scopus 로고
    • A central role for the WH2 domain of Srv2/CAP in recharging actin monomers to drive actin turnover in vitro and in vivo
    • Chaudhry, F., Little, K., Talarico, L., Quintero-Monzon, O. and Goode, B. L. (2010) A central role for the WH2 domain of Srv2/CAP in recharging actin monomers to drive actin turnover in vitro and in vivo. Cytoskeleton 67, 120-133
    • (2010) Cytoskeleton , vol.67 , pp. 120-133
    • Chaudhry, F.1    Little, K.2    Talarico, L.3    Quintero-Monzon, O.4    Goode, B.L.5
  • 10
    • 15844401321 scopus 로고    scopus 로고
    • Role of nucleotide exchange and hydrolysis in the function of profilin in actin assembly
    • DOI 10.1074/jbc.271.21.12302
    • Perelroizen, I., Didry, D., Christensen, H., Chua, N. H. and Carlier, M. F. (1996) Role of nucleotide exchange and hydrolysis in the function of profilin in action assembly. J. Biol. Chem. 271, 12302-12309 (Pubitemid 26160894)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.21 , pp. 12302-12309
    • Perelroizen, I.1    Didry, D.2    Christensen, H.3    Chua, N.-H.4    Carlier, M.-F.5
  • 11
    • 0034067715 scopus 로고    scopus 로고
    • Maize profilin isoforms are functionally distinct
    • DOI 10.1105/tpc.12.4.583
    • Kovar, D. R., Drobak, B. K. and Staiger, C. J. (2000) Maize profilin isoforms are functionally distinct. Plant Cell 12, 583-598 (Pubitemid 30254874)
    • (2000) Plant Cell , vol.12 , Issue.4 , pp. 583-598
    • Kovar, D.R.1    Drobak, B.K.2    Staiger, C.J.3
  • 12
    • 0037093266 scopus 로고    scopus 로고
    • Human CAP1 is a key factor in the recycling of cofilin and actin for rapid actin turnover
    • Moriyama, K. and Yahara, I. (2002) Human CAP1 is a key factor in the recycling of cofilin and actin for rapid actin turnover. J. Cell Sci. 115, 1591-1601 (Pubitemid 34520589)
    • (2002) Journal of Cell Science , vol.115 , Issue.8 , pp. 1591-1601
    • Moriyama, K.1    Yahara, I.2
  • 13
    • 34547803604 scopus 로고    scopus 로고
    • Identification of Arabidopsis cyclase-associated protein 1 as the first nucleotide exchange factor for plant actin
    • DOI 10.1091/mbc.E06-11-1041
    • Chaudhry, F., Guerin, C., von Witsch, M., Blanchoin, L. and Staiger, C. J. (2007) Identification of Arabidopsis cyclase-associated protein 1 as the first nucleotide exchange factor for plant actin. Mol. Biol. Cell 18, 3002-3014 (Pubitemid 47240913)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.8 , pp. 3002-3014
    • Chaudhry, F.1    Guerin, C.2    Von Witsch, M.3    Blanchoin, L.4    Staiger, C.J.5
  • 14
    • 67449107876 scopus 로고    scopus 로고
    • Reconstitution and dissection of the 600-kDa Srv2/CAP complex: Roles for oligomerization and cofilin-actin binding in driving actin turnover
    • Quintero-Monzon, O., Jonasson, E. M., Bertling, E., Talarico, L., Chaudhry, F., Sihvo, M., Lappalainen, P. and Goode, B. L. (2009) Reconstitution and dissection of the 600-kDa Srv2/CAP complex: roles for oligomerization and cofilin-actin binding in driving actin turnover. J. Biol. Chem. 284, 10923-10934
    • (2009) J. Biol. Chem. , vol.284 , pp. 10923-10934
    • Quintero-Monzon, O.1    Jonasson, E.M.2    Bertling, E.3    Talarico, L.4    Chaudhry, F.5    Sihvo, M.6    Lappalainen, P.7    Goode, B.L.8
  • 15
    • 84872278687 scopus 로고    scopus 로고
    • Mammalian and malaria parasite cyclase-associated proteins catalyze nucleotide exchange on G-actin through a conserved mechanism
    • Makkonen, M., Bertling, E., Chebotareva, N. A., Baum, J. and Lappalainen, P. (2013) Mammalian and malaria parasite cyclase-associated proteins catalyze nucleotide exchange on G-actin through a conserved mechanism. J. Biol. Chem. 288, 984-994
    • (2013) J. Biol. Chem. , vol.288 , pp. 984-994
    • Makkonen, M.1    Bertling, E.2    Chebotareva, N.A.3    Baum, J.4    Lappalainen, P.5
  • 17
    • 6344225310 scopus 로고    scopus 로고
    • A high-affinity interaction with ADP-actin monomers underlies the mechanism and in vivo function of Srv2/cyclase-associated protein
    • DOI 10.1091/mbc.E04-06-0444
    • Mattila, P. K., Quintero-Monzon, O., Kugler, J., Moseley, J. B., Almo, S. C., Lappalainen, P. and Goode, B. L. (2004) A high-affinity interaction with ADP-actin monomers underlies the mechanism and in vivo function of Srv2/cyclase-associated protein. Mol. Biol. Cell 15, 5158-5171 (Pubitemid 39392227)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.11 , pp. 5158-5171
    • Mattila, P.K.1    Quintero-Monzon, O.2    Kugler, J.3    Moseley, J.B.4    Almo, S.C.5    Lappalainen, P.6    Goode, B.L.7
  • 18
    • 84869116801 scopus 로고    scopus 로고
    • CAS-1, a C. elegans cyclase-associated protein, is required for sarcomeric actin assembly in striated muscle
    • Nomura, K., Ono, K. and Ono, S. (2012) CAS-1, a C. elegans cyclase-associated protein, is required for sarcomeric actin assembly in striated muscle. J. Cell Sci. 125, 4077-4089
    • (2012) J. Cell Sci. , vol.125 , pp. 4077-4089
    • Nomura, K.1    Ono, K.2    Ono, S.3
  • 19
    • 84867436458 scopus 로고    scopus 로고
    • Cyclase-associated protein (CAP) acts directly on F-actin to accelerate cofilin-mediated actin severing across the range of physiological pH
    • Normoyle, K. P. and Brieher, W. M. (2012) Cyclase-associated protein (CAP) acts directly on F-actin to accelerate cofilin-mediated actin severing across the range of physiological pH. J. Biol. Chem. 287, 35722-35732
    • (2012) J. Biol. Chem. , vol.287 , pp. 35722-35732
    • Normoyle, K.P.1    Brieher, W.M.2
  • 21
    • 84871882289 scopus 로고    scopus 로고
    • Srv2/cyclase-associated protein forms hexameric shurikens that directly catalyze actin filament severing by cofilin
    • Chaudhry, F., Breitsprecher, D., Little, K., Sharov, G., Sokolova, O. and Goode, B. L. (2013) Srv2/cyclase-associated protein forms hexameric shurikens that directly catalyze actin filament severing by cofilin. Mol. Biol. Cell 24, 31-41
    • (2013) Mol. Biol. Cell , vol.24 , pp. 31-41
    • Chaudhry, F.1    Breitsprecher, D.2    Little, K.3    Sharov, G.4    Sokolova, O.5    Goode, B.L.6
  • 22
    • 0025361043 scopus 로고
    • SRV2, a gene required for RAS activation of adenylate cyclase in yeast
    • Fedor-Chaiken, M., Deschenes, R. J. and Broach, J. R. (1990) SRV2, a gene required for RAS activation of adenylate cyclase in yeast. Cell 61, 329-340
    • (1990) Cell , vol.61 , pp. 329-340
    • Fedor-Chaiken, M.1    Deschenes, R.J.2    Broach, J.R.3
  • 24
    • 0028321973 scopus 로고
    • Comparison of human CAP and CAP2, homologs of the yeast adenylyl cyclase-associated proteins
    • Yu, G., Swiston, J. and Young, D. (1994) Comparison of human CAP and CAP2, homologs of the yeast adenylyl cyclase-associated proteins. J. Cell Sci. 107, 1671-1678 (Pubitemid 24198485)
    • (1994) Journal of Cell Science , vol.107 , Issue.6 , pp. 1671-1678
    • Yu, G.1    Swiston, J.2    Young, D.3
  • 25
    • 2342514815 scopus 로고    scopus 로고
    • Cyclase-associated Protein 1 (CAP1) Promotes Cofilin-induced Actin Dynamics in Mammalian Nonmuscle Cells
    • DOI 10.1091/mbc.E04-01-0048
    • Bertling, E., Hotulainen, P., Mattila, P. K., Matilainen, T., Salminen, M. and Lappalainen, P. (2004) Cyclase-associated protein 1 (CAP1) promotes cofilin-induced actin dynamics in mammalian nonmuscle cells. Mol. Biol. Cell 15, 2324-2334 (Pubitemid 38580649)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.5 , pp. 2324-2334
    • Bertling, E.1    Hotulainen, P.2    Mattila, P.K.3    Matilainen, T.4    Salminen, M.5    Lappalainen, P.6
  • 26
    • 0035755471 scopus 로고    scopus 로고
    • Systematic analysis of gene expression of the C. elegans genome
    • Kohara, Y. (2001) Systematic analysis of gene expression of the C. elegans genome. Tanpakushitsu Kakusan Koso 46, 2425-2431
    • (2001) Tanpakushitsu Kakusan Koso , vol.46 , pp. 2425-2431
    • Kohara, Y.1
  • 27
    • 0020021878 scopus 로고
    • Purification of muscle actin
    • Pardee, J. D. and Spudich, J. A. (1982) Purification of muscle actin. Methods Enzymol. 85, 164-181
    • (1982) Methods Enzymol. , vol.85 , pp. 164-181
    • Pardee, J.D.1    Spudich, J.A.2
  • 28
    • 0019427215 scopus 로고
    • Fluorimetry study of N-(1-pyrenyl)iodoacetamide-labelled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin
    • Kouyama, T. and Mihashi, K. (1981) Fluorimetry study of N-(1-pyrenyl)iodoacetamide-labelled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin. Eur. J. Biochem. 114, 33-38 (Pubitemid 11101489)
    • (1981) European Journal of Biochemistry , vol.114 , Issue.1 , pp. 33-38
    • Kouyama, T.1    Mihashi, K.2
  • 29
    • 0032488999 scopus 로고    scopus 로고
    • Two Caenorhabditis elegans actin depolymerizing factor/cofilin proteins, encoded by the unc-60 gene, differentially regulate actin filament dynamics
    • DOI 10.1074/jbc.273.6.3778
    • Ono, S. and Benian, G. M. (1998) Two Caenorhabditis elegans actin depolymerizing factor/cofilin proteins, encoded by the unc-60 gene, differentially regulate actin filament dynamics. J. Biol. Chem. 273, 3778-3783 (Pubitemid 28109808)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.6 , pp. 3778-3783
    • Ono, S.1    Benian, G.M.2
  • 31
    • 28844475180 scopus 로고    scopus 로고
    • 6-MBP fusion proteins in the cytoplasm and periplasm of Escherichia coli
    • DOI 10.1110/ps.051718605
    • Nallamsetty, S., Austin, B. P., Penrose, K. J. and Waugh, D. S. (2005) Gateway vectors for the production of combinatorially-tagged His6-MBP fusion proteins in the cytoplasm and periplasm of Escherichia coli. Protein Sci. 14, 2964-2971 (Pubitemid 41770137)
    • (2005) Protein Science , vol.14 , Issue.12 , pp. 2964-2971
    • Nallamsetty, S.1    Austin, B.P.2    Penrose, K.J.3    Waugh, D.S.4
  • 33
    • 0028920045 scopus 로고
    • An actin monomer binding activity localizes to the carboxyl-terminal half of the Saccharomyces cerevisiae cyclase-associated protein
    • Freeman, N. L., Chen, Z., Horenstein, J., Weber, A. and Field, J. (1995) An actin monomer binding activity localizes to the carboxyl-terminal half of the Saccharomyces cerevisiae cyclase-associated protein. J. Biol. Chem. 270, 5680-5685
    • (1995) J. Biol. Chem. , vol.270 , pp. 5680-5685
    • Freeman, N.L.1    Chen, Z.2    Horenstein, J.3    Weber, A.4    Field, J.5
  • 34
    • 84872690927 scopus 로고    scopus 로고
    • Rapid nucleotide exchange renders asp-11 mutant actins resistant to depolymerizing activity of cofilin, leading to dominant toxicity in vivo
    • Umeki, N., Nakajima, J., Noguchi, T. Q., Tokuraku, K., Nagasaki, A., Ito, K., Hirose, K. and Uyeda, T. Q. (2013) Rapid nucleotide exchange renders asp-11 mutant actins resistant to depolymerizing activity of cofilin, leading to dominant toxicity in vivo. J. Biol. Chem. 288, 1739-1749
    • (2013) J. Biol. Chem. , vol.288 , pp. 1739-1749
    • Umeki, N.1    Nakajima, J.2    Noguchi, T.Q.3    Tokuraku, K.4    Nagasaki, A.5    Ito, K.6    Hirose, K.7    Uyeda, T.Q.8
  • 35
    • 0037900004 scopus 로고    scopus 로고
    • Specific requirement for two ADF/cofilin isoforms in distinct actin-dependent processes in Caenorhabditis elegans
    • DOI 10.1242/jcs.00421
    • Ono, K., Parast, M., Alberico, C., Benian, G. M. and Ono, S. (2003) Specific requirement for two ADF/cofilin isoforms in distinct actin-dependent processes in Caenorhabditis elegans. J. Cell Sci. 116, 2073-2085 (Pubitemid 36622304)
    • (2003) Journal of Cell Science , vol.116 , Issue.10 , pp. 2073-2085
    • Ono, K.1    Parast, M.2    Alberico, C.3    Benian, G.M.4    Ono, S.5
  • 36
    • 52649164001 scopus 로고    scopus 로고
    • Essential role of ADF/cofilin for assembly of contractile actin networks in the C. elegans somatic gonad
    • Ono, K., Yamashiro, S. and Ono, S. (2008) Essential role of ADF/cofilin for assembly of contractile actin networks in the C. elegans somatic gonad. J. Cell Sci. 121, 2662-2670
    • (2008) J. Cell Sci. , vol.121 , pp. 2662-2670
    • Ono, K.1    Yamashiro, S.2    Ono, S.3
  • 37
    • 0037015303 scopus 로고    scopus 로고
    • PPW-1, a PAZ/PIWI protein required for efficient germline RNAi, is defective in a natural isolate of C. elegans
    • DOI 10.1016/S0960-9822(02)01110-7, PII S0960982202011107
    • Tijsterman, M., Okihara, K. L., Thijssen, K. and Plasterk, R. H. (2002) PPW-1, a PAZ/PIWI protein required for efficient germline RNAi, is defective in a natural isolate of C. elegans. Curr. Biol. 12, 1535-1540 (Pubitemid 35036654)
    • (2002) Current Biology , vol.12 , Issue.17 , pp. 1535-1540
    • Tijsterman, M.1    Okihara, K.L.2    Thijssen, K.3    Plasterk, R.H.A.4
  • 38
    • 44049084957 scopus 로고    scopus 로고
    • Control of the ability of profilin to bind and facilitate nucleotide exchange from G-actin
    • Wen, K. K., McKane, M., Houtman, J. C. and Rubenstein, P. A. (2008) Control of the ability of profilin to bind and facilitate nucleotide exchange from G-actin. J. Biol. Chem. 283, 9444-9453
    • (2008) J. Biol. Chem. , vol.283 , pp. 9444-9453
    • Wen, K.K.1    McKane, M.2    Houtman, J.C.3    Rubenstein, P.A.4
  • 41
    • 59349088624 scopus 로고    scopus 로고
    • Sarcomeric actin organization is synergistically promoted by tropomodulin, ADF/cofilin, AIP1 and profilin in C. elegans
    • Yamashiro, S., Cox, E. A., Baillie, D. L., Hardin, J. D. and Ono, S. (2008) Sarcomeric actin organization is synergistically promoted by tropomodulin, ADF/cofilin, AIP1 and profilin in C. elegans. J. Cell Sci. 121, 3867-3877
    • (2008) J. Cell Sci. , vol.121 , pp. 3867-3877
    • Yamashiro, S.1    Cox, E.A.2    Baillie, D.L.3    Hardin, J.D.4    Ono, S.5
  • 42
    • 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. and Weeds, A. (2002) Determining the differences in actin binding by human ADF and cofilin. J. Mol. Biol. 315, 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
  • 43
    • 34248227301 scopus 로고    scopus 로고
    • Cofilin promotes stimulus-induced lamellipodium formation by generating an abundant supply of actin monomers
    • DOI 10.1083/jcb.200610005
    • Kiuchi, T., Ohashi, K., Kurita, S. and Mizuno, K. (2007) Cofilin promotes stimulus-induced lamellipodium formation by generating an abundant supply of actin monomers. J. Cell Biol. 177, 465-476 (Pubitemid 46718275)
    • (2007) Journal of Cell Biology , vol.177 , Issue.3 , pp. 465-476
    • Kiuchi, T.1    Ohashi, K.2    Kurita, S.3    Mizuno, K.4
  • 45
    • 77949903357 scopus 로고    scopus 로고
    • Toxoplasma gondii actin depolymerizing factor acts primarily to sequester G-actin
    • Mehta, S. and Sibley, L. D. (2010) Toxoplasma gondii actin depolymerizing factor acts primarily to sequester G-actin. J. Biol. Chem. 285, 6835-6847
    • (2010) J. Biol. Chem. , vol.285 , pp. 6835-6847
    • Mehta, S.1    Sibley, L.D.2
  • 46
    • 54249123694 scopus 로고    scopus 로고
    • Actin-depolymerizing factor, ADF/cofilin, is essentially required in assembly of Leishmania flagellum
    • Tammana, T. V., Sahasrabuddhe, A. A., Mitra, K., Bajpai, V. K. and Gupta, C. M. (2008) Actin-depolymerizing factor, ADF/cofilin, is essentially required in assembly of Leishmania flagellum. Mol. Microbiol. 70, 837-852
    • (2008) Mol. Microbiol. , vol.70 , pp. 837-852
    • Tammana, T.V.1    Sahasrabuddhe, A.A.2    Mitra, K.3    Bajpai, V.K.4    Gupta, C.M.5
  • 47
    • 24344440631 scopus 로고    scopus 로고
    • A Plasmodium actin-depolymerizing factor that binds exclusively to actin monomers
    • DOI 10.1091/mbc.E05-02-0086
    • Schuler, H., Mueller, A. K. and Matuschewski, K. (2005) A Plasmodium actin-depolymerizing factor that binds exclusively to actin monomers. Mol. Biol. Cell 16, 4013-4023 (Pubitemid 41262874)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.9 , pp. 4013-4023
    • Schuler, H.1    Mueller, A.-K.2    Matuschewski, K.3
  • 48
    • 79954584860 scopus 로고    scopus 로고
    • Actin depolymerizing factor controls actin turnover and gliding motility in Toxoplasma gondii
    • Mehta, S. and Sibley, L. D. (2011) Actin depolymerizing factor controls actin turnover and gliding motility in Toxoplasma gondii. Mol. Biol. Cell 22, 1290-1299
    • (2011) Mol. Biol. Cell , vol.22 , pp. 1290-1299
    • Mehta, S.1    Sibley, L.D.2
  • 49
    • 77953164097 scopus 로고    scopus 로고
    • ADF/cofilin-driven actin dynamics in early events of Leishmania cell division
    • Tammana, T. V., Sahasrabuddhe, A. A., Bajpai, V. K. and Gupta, C. M. (2010) ADF/cofilin-driven actin dynamics in early events of Leishmania cell division. J. Cell Sci. 123, 1894-1901
    • (2010) J. Cell Sci. , vol.123 , pp. 1894-1901
    • Tammana, T.V.1    Sahasrabuddhe, A.A.2    Bajpai, V.K.3    Gupta, C.M.4
  • 50
    • 77951247304 scopus 로고    scopus 로고
    • Structure and function of a G-actin sequestering protein with a vital role in malaria oocyst development inside the mosquito vector
    • Hliscs, M., Sattler, J. M., Tempel, W., Artz, J. D., Dong, A., Hui, R., Matuschewski, K. and Schuler, H. (2010) Structure and function of a G-actin sequestering protein with a vital role in malaria oocyst development inside the mosquito vector. J. Biol. Chem. 285, 11572-11583
    • (2010) J. Biol. Chem. , vol.285 , pp. 11572-11583
    • Hliscs, M.1    Sattler, J.M.2    Tempel, W.3    Artz, J.D.4    Dong, A.5    Hui, R.6    Matuschewski, K.7    Schuler, H.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.