메뉴 건너뛰기




Volumn 62, Issue 3, 2016, Pages 397-408

Structural Basis for Noncanonical Substrate Recognition of Cofilin/ADF Proteins by LIM Kinases

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ACTIN DEPOLYMERIZING FACTOR; COFILIN 1; LIM KINASE; CFL1 PROTEIN, HUMAN; COF1 PROTEIN, S CEREVISIAE; LIMK1 PROTEIN, HUMAN; PROTEIN BINDING; SACCHAROMYCES CEREVISIAE PROTEIN; SERINE;

EID: 84966659416     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2016.04.001     Document Type: Article
Times cited : (44)

References (69)
  • 2
    • 0035413606 scopus 로고    scopus 로고
    • Kinetic and catalytic mechanisms of protein kinases
    • Adams J.A. Kinetic and catalytic mechanisms of protein kinases. Chem. Rev. 2001, 101:2271-2290.
    • (2001) Chem. Rev. , vol.101 , pp. 2271-2290
    • Adams, J.A.1
  • 4
    • 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. J. Biol. Chem. 1995, 270:17582-17587.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17582-17587
    • Agnew, B.J.1    Minamide, L.S.2    Bamburg, J.R.3
  • 5
    • 0035865682 scopus 로고    scopus 로고
    • LIM-kinase 2 induces formation of stress fibres, focal adhesions and membrane blebs, dependent on its activation by Rho-associated kinase-catalysed phosphorylation at threonine-505
    • Amano T., Tanabe K., Eto T., Narumiya S., Mizuno K. LIM-kinase 2 induces formation of stress fibres, focal adhesions and membrane blebs, dependent on its activation by Rho-associated kinase-catalysed phosphorylation at threonine-505. Biochem. J. 2001, 354:149-159.
    • (2001) Biochem. J. , vol.354 , pp. 149-159
    • Amano, T.1    Tanabe, K.2    Eto, T.3    Narumiya, S.4    Mizuno, K.5
  • 6
    • 33749046492 scopus 로고    scopus 로고
    • Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilin
    • Andrianantoandro E., Pollard T.D. Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilin. Mol. Cell 2006, 24:13-23.
    • (2006) Mol. Cell , vol.24 , pp. 13-23
    • Andrianantoandro, E.1    Pollard, T.D.2
  • 8
    • 0033198879 scopus 로고    scopus 로고
    • Putting a new twist on actin: ADF/cofilins modulate actin dynamics
    • Bamburg J.R., McGough A., Ono S. Putting a new twist on actin: ADF/cofilins modulate actin dynamics. Trends Cell Biol. 1999, 9:364-370.
    • (1999) Trends Cell Biol. , vol.9 , pp. 364-370
    • Bamburg, J.R.1    McGough, A.2    Ono, S.3
  • 10
    • 84921326187 scopus 로고    scopus 로고
    • Molecular features of product release for the PKA catalytic cycle
    • Bastidas A.C., Wu J., Taylor S.S. Molecular features of product release for the PKA catalytic cycle. Biochemistry 2015, 54:2-10.
    • (2015) Biochemistry , vol.54 , pp. 2-10
    • Bastidas, A.C.1    Wu, J.2    Taylor, S.S.3
  • 12
    • 33746363486 scopus 로고    scopus 로고
    • Domains, motifs, and scaffolds: the role of modular interactions in the evolution and wiring of cell signaling circuits
    • Bhattacharyya R.P., Reményi A., Yeh B.J., Lim W.A. Domains, motifs, and scaffolds: the role of modular interactions in the evolution and wiring of cell signaling circuits. Annu. Rev. Biochem. 2006, 75:655-680.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 655-680
    • Bhattacharyya, R.P.1    Reményi, A.2    Yeh, B.J.3    Lim, W.A.4
  • 13
    • 0032566659 scopus 로고    scopus 로고
    • Interaction of actin monomers with Acanthamoeba actophorin (ADF/cofilin) and profilin
    • Blanchoin L., Pollard T.D. Interaction of actin monomers with Acanthamoeba actophorin (ADF/cofilin) and profilin. J. Biol. Chem. 1998, 273:25106-25111.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25106-25111
    • Blanchoin, L.1    Pollard, T.D.2
  • 14
    • 0033060250 scopus 로고    scopus 로고
    • Mechanism of interaction of Acanthamoeba actophorin (ADF/Cofilin) with actin filaments
    • Blanchoin L., Pollard T.D. Mechanism of interaction of Acanthamoeba actophorin (ADF/Cofilin) with actin filaments. J. Biol. Chem. 1999, 274:15538-15546.
    • (1999) J. Biol. Chem. , vol.274 , pp. 15538-15546
    • Blanchoin, L.1    Pollard, T.D.2
  • 15
    • 0034687235 scopus 로고    scopus 로고
    • Interactions of ADF/cofilin, Arp2/3 complex, capping protein and profilin in remodeling of branched actin filament networks
    • Blanchoin L., Pollard T.D., Mullins R.D. Interactions of ADF/cofilin, Arp2/3 complex, capping protein and profilin in remodeling of branched actin filament networks. Curr. Biol. 2000, 10:1273-1282.
    • (2000) Curr. Biol. , vol.10 , pp. 1273-1282
    • Blanchoin, L.1    Pollard, T.D.2    Mullins, R.D.3
  • 16
    • 0034645797 scopus 로고    scopus 로고
    • Phosphorylation of Acanthamoeba actophorin (ADF/cofilin) blocks interaction with actin without a change in atomic structure
    • 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. J. Mol. Biol. 2000, 295:203-211.
    • (2000) J. Mol. Biol. , vol.295 , pp. 203-211
    • Blanchoin, L.1    Robinson, R.C.2    Choe, S.3    Pollard, T.D.4
  • 19
    • 25144502820 scopus 로고    scopus 로고
    • Higher-order substrate recognition of eIF2alpha by the RNA-dependent protein kinase PKR
    • Dar A.C., Dever T.E., Sicheri F. Higher-order substrate recognition of eIF2alpha by the RNA-dependent protein kinase PKR. Cell 2005, 122:887-900.
    • (2005) Cell , vol.122 , pp. 887-900
    • Dar, A.C.1    Dever, T.E.2    Sicheri, F.3
  • 20
    • 77950022821 scopus 로고    scopus 로고
    • How cofilin severs an actin filament
    • De La Cruz E.M. How cofilin severs an actin filament. Biophys. Rev. 2009, 1:51-59.
    • (2009) Biophys. Rev. , vol.1 , pp. 51-59
    • De La Cruz, E.M.1
  • 21
    • 0033194037 scopus 로고    scopus 로고
    • Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics
    • Edwards D.C., Sanders L.C., Bokoch G.M., Gill G.N. Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics. Nat. Cell Biol. 1999, 1:253-259.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 253-259
    • Edwards, D.C.1    Sanders, L.C.2    Bokoch, G.M.3    Gill, G.N.4
  • 22
    • 84876041581 scopus 로고    scopus 로고
    • Biophysics of actin filament severing by cofilin
    • Elam W.A., Kang H., De la Cruz E.M. Biophysics of actin filament severing by cofilin. FEBS Lett. 2013, 587:1215-1219.
    • (2013) FEBS Lett. , vol.587 , pp. 1215-1219
    • Elam, W.A.1    Kang, H.2    De la Cruz, E.M.3
  • 25
    • 0025739664 scopus 로고
    • Rational scanning mutagenesis of a protein kinase identifies functional regions involved in catalysis and substrate interactions
    • Gibbs C.S., Zoller M.J. Rational scanning mutagenesis of a protein kinase identifies functional regions involved in catalysis and substrate interactions. J. Biol. Chem. 1991, 266:8923-8931.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8923-8931
    • Gibbs, C.S.1    Zoller, M.J.2
  • 26
    • 36849043083 scopus 로고    scopus 로고
    • Substrate and docking interactions in serine/threonine protein kinases
    • Goldsmith E.J., Akella R., Min X., Zhou T., Humphreys J.M. Substrate and docking interactions in serine/threonine protein kinases. Chem. Rev. 2007, 107:5065-5081.
    • (2007) Chem. Rev. , vol.107 , pp. 5065-5081
    • Goldsmith, E.J.1    Akella, R.2    Min, X.3    Zhou, T.4    Humphreys, J.M.5
  • 28
    • 0027475652 scopus 로고
    • Isolation of a yeast essential gene, COF1, that encodes a homologue of mammalian cofilin, a low-M(r) actin-binding and depolymerizing protein
    • Iida K., Moriyama K., Matsumoto S., Kawasaki H., Nishida E., Yahara I. Isolation of a yeast essential gene, COF1, that encodes a homologue of mammalian cofilin, a low-M(r) actin-binding and depolymerizing protein. Gene 1993, 124:115-120.
    • (1993) Gene , vol.124 , pp. 115-120
    • Iida, K.1    Moriyama, K.2    Matsumoto, S.3    Kawasaki, H.4    Nishida, E.5    Yahara, I.6
  • 29
    • 0032403116 scopus 로고    scopus 로고
    • Complete amino acid sequences and phosphorylation sites, determined by Edman degradation and mass spectrometry, of rat parotid destrin- and cofilin-like proteins
    • Kanamori T., Suzuki M., Titani K. Complete amino acid sequences and phosphorylation sites, determined by Edman degradation and mass spectrometry, of rat parotid destrin- and cofilin-like proteins. Arch. Oral Biol. 1998, 43:955-967.
    • (1998) Arch. Oral Biol. , vol.43 , pp. 955-967
    • Kanamori, T.1    Suzuki, M.2    Titani, K.3
  • 31
    • 0024326947 scopus 로고
    • Isolation and characterization of ERBB3, a third member of the ERBB/epidermal growth factor receptor family: evidence for overexpression in a subset of human mammary tumors
    • Kraus M.H., Issing W., Miki T., Popescu N.C., Aaronson S.A. Isolation and characterization of ERBB3, a third member of the ERBB/epidermal growth factor receptor family: evidence for overexpression in a subset of human mammary tumors. Proc. Natl. Acad. Sci. USA 1989, 86:9193-9197.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9193-9197
    • Kraus, M.H.1    Issing, W.2    Miki, T.3    Popescu, N.C.4    Aaronson, S.A.5
  • 32
    • 0030880186 scopus 로고    scopus 로고
    • Essential functions and actin-binding surfaces of yeast cofilin revealed by systematic mutagenesis
    • Lappalainen P., Fedorov E.V., Fedorov A.A., Almo S.C., Drubin D.G. Essential functions and actin-binding surfaces of yeast cofilin revealed by systematic mutagenesis. EMBO J. 1997, 16:5520-5530.
    • (1997) EMBO J. , vol.16 , pp. 5520-5530
    • Lappalainen, P.1    Fedorov, E.V.2    Fedorov, A.A.3    Almo, S.C.4    Drubin, D.G.5
  • 33
  • 34
    • 46349099824 scopus 로고    scopus 로고
    • Structural basis for the recognition of c-Src by its inactivator Csk
    • Levinson N.M., Seeliger M.A., Cole P.A., Kuriyan J. Structural basis for the recognition of c-Src by its inactivator Csk. Cell 2008, 134:124-134.
    • (2008) Cell , vol.134 , pp. 124-134
    • Levinson, N.M.1    Seeliger, M.A.2    Cole, P.A.3    Kuriyan, J.4
  • 38
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes by molecular replacement with Phaser
    • McCoy A.J. Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallogr. D Biol. Crystallogr. 2007, 63:32-41.
    • (2007) Acta Crystallogr. D Biol. Crystallogr. , vol.63 , pp. 32-41
    • McCoy, A.J.1
  • 40
    • 84858953576 scopus 로고    scopus 로고
    • Development of a high-throughput screening method for LIM kinase 1 using a luciferase-based assay of ATP consumption
    • Mezna M., Wong A.C., Ainger M., Scott R.W., Hammonds T., Olson M.F. Development of a high-throughput screening method for LIM kinase 1 using a luciferase-based assay of ATP consumption. J. Biomol. Screen. 2012, 17:460-468.
    • (2012) J. Biomol. Screen. , vol.17 , pp. 460-468
    • Mezna, M.1    Wong, A.C.2    Ainger, M.3    Scott, R.W.4    Hammonds, T.5    Olson, M.F.6
  • 41
    • 84870557707 scopus 로고    scopus 로고
    • Signaling mechanisms and functional roles of cofilin phosphorylation and dephosphorylation
    • Mizuno K. Signaling mechanisms and functional roles of cofilin phosphorylation and dephosphorylation. Cell. Signal. 2013, 25:457-469.
    • (2013) Cell. Signal. , vol.25 , pp. 457-469
    • Mizuno, K.1
  • 42
    • 0028335706 scopus 로고
    • Identification of a human cDNA encoding a novel protein kinase with two repeats of the LIM/double zinc finger motif
    • Mizuno K., Okano I., Ohashi K., Nunoue K., Kuma K., Miyata T., Nakamura T. Identification of a human cDNA encoding a novel protein kinase with two repeats of the LIM/double zinc finger motif. Oncogene 1994, 9:1605-1612.
    • (1994) Oncogene , vol.9 , pp. 1605-1612
    • Mizuno, K.1    Okano, I.2    Ohashi, K.3    Nunoue, K.4    Kuma, K.5    Miyata, T.6    Nakamura, T.7
  • 43
    • 0027446345 scopus 로고
    • Cofilin is an essential component of the yeast cortical cytoskeleton
    • Moon A.L., Janmey P.A., Louie K.A., Drubin D.G. Cofilin is an essential component of the yeast cortical cytoskeleton. J. Cell Biol. 1993, 120:421-435.
    • (1993) J. Cell Biol. , vol.120 , pp. 421-435
    • Moon, A.L.1    Janmey, P.A.2    Louie, K.A.3    Drubin, D.G.4
  • 45
    • 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 Cells 1996, 1:73-86.
    • (1996) Genes Cells , vol.1 , pp. 73-86
    • Moriyama, K.1    Iida, K.2    Yahara, I.3
  • 47
    • 0037169335 scopus 로고    scopus 로고
    • Control of actin reorganization by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin
    • 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, 108:233-246.
    • (2002) Cell , vol.108 , pp. 233-246
    • Niwa, R.1    Nagata-Ohashi, K.2    Takeichi, M.3    Mizuno, K.4    Uemura, T.5
  • 48
    • 0036854364 scopus 로고    scopus 로고
    • The two ADF-H domains of twinfilin play functionally distinct roles in interactions with actin monomers
    • Ojala P.J., Paavilainen V.O., Vartiainen M.K., Tuma R., Weeds A.G., Lappalainen P. The two ADF-H domains of twinfilin play functionally distinct roles in interactions with actin monomers. Mol. Biol. Cell 2002, 13:3811-3821.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3811-3821
    • Ojala, P.J.1    Paavilainen, V.O.2    Vartiainen, M.K.3    Tuma, R.4    Weeds, A.G.5    Lappalainen, P.6
  • 49
    • 0029594144 scopus 로고
    • Identification and characterization of a novel family of serine/threonine kinases containing two N-terminal LIM motifs
    • Okano I., Hiraoka J., Otera H., Nunoue K., Ohashi K., Iwashita S., Hirai M., Mizuno K. Identification and characterization of a novel family of serine/threonine kinases containing two N-terminal LIM motifs. J. Biol. Chem. 1995, 270:31321-31330.
    • (1995) J. Biol. Chem. , vol.270 , pp. 31321-31330
    • Okano, I.1    Hiraoka, J.2    Otera, H.3    Nunoue, K.4    Ohashi, K.5    Iwashita, S.6    Hirai, M.7    Mizuno, K.8
  • 51
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Academic Press (New York), C.W. Carter, R.M. Sweet (Eds.)
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods in Enzymology 1997, 307-326. Academic Press (New York). C.W. Carter, R.M. Sweet (Eds.).
    • (1997) Methods in Enzymology , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 52
    • 47549090623 scopus 로고    scopus 로고
    • Structure of the actin-depolymerizing factor homology domain in complex with actin
    • Paavilainen V.O., Oksanen E., Goldman A., Lappalainen P. Structure of the actin-depolymerizing factor homology domain in complex with actin. J. Cell Biol. 2008, 182:51-59.
    • (2008) J. Cell Biol. , vol.182 , pp. 51-59
    • Paavilainen, V.O.1    Oksanen, E.2    Goldman, A.3    Lappalainen, P.4
  • 53
    • 80052990415 scopus 로고    scopus 로고
    • Actin-depolymerizing factor homology domain: a conserved fold performing diverse roles in cytoskeletal dynamics
    • Poukkula M., Kremneva E., Serlachius M., Lappalainen P. Actin-depolymerizing factor homology domain: a conserved fold performing diverse roles in cytoskeletal dynamics. Cytoskeleton (Hoboken) 2011, 68:471-490.
    • (2011) Cytoskeleton (Hoboken) , vol.68 , pp. 471-490
    • Poukkula, M.1    Kremneva, E.2    Serlachius, M.3    Lappalainen, P.4
  • 54
    • 33947256308 scopus 로고    scopus 로고
    • Docking interactions in protein kinase and phosphatase networks
    • Reményi A., Good M.C., Lim W.A. Docking interactions in protein kinase and phosphatase networks. Curr. Opin. Struct. Biol. 2006, 16:676-685.
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 676-685
    • Reményi, A.1    Good, M.C.2    Lim, W.A.3
  • 55
    • 0032516848 scopus 로고    scopus 로고
    • Kinetic analysis of the interaction of actin-depolymerizing factor (ADF)/cofilin with G- and F-actins. Comparison of plant and human ADFs and effect of phosphorylation
    • Ressad F., Didry D., Xia G.X., Hong Y., Chua N.H., Pantaloni D., Carlier M.F. Kinetic analysis of the interaction of actin-depolymerizing factor (ADF)/cofilin with G- and F-actins. Comparison of plant and human ADFs and effect of phosphorylation. J. Biol. Chem. 1998, 273:20894-20902.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20894-20902
    • Ressad, F.1    Didry, D.2    Xia, G.X.3    Hong, Y.4    Chua, N.H.5    Pantaloni, D.6    Carlier, M.F.7
  • 56
    • 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
    • Røsok O., Pedeutour F., Ree A.H., Aasheim H.C. Identification and characterization of TESK2, a novel member of the LIMK/TESK family of protein kinases, predominantly expressed in testis. Genomics 1999, 61:44-54.
    • (1999) Genomics , vol.61 , pp. 44-54
    • Røsok, O.1    Pedeutour, F.2    Ree, A.H.3    Aasheim, H.C.4
  • 57
    • 34249887660 scopus 로고    scopus 로고
    • LIM kinases: function, regulation and association with human disease
    • Scott R.W., Olson M.F. LIM kinases: function, regulation and association with human disease. J. Mol. Med. 2007, 85:555-568.
    • (2007) J. Mol. Med. , vol.85 , pp. 555-568
    • Scott, R.W.1    Olson, M.F.2
  • 58
    • 77952338791 scopus 로고    scopus 로고
    • ErbB3/HER3 intracellular domain is competent to bind ATP and catalyze autophosphorylation
    • Shi F., Telesco S.E., Liu Y., Radhakrishnan R., Lemmon M.A. ErbB3/HER3 intracellular domain is competent to bind ATP and catalyze autophosphorylation. Proc. Natl. Acad. Sci. USA 2010, 107:7692-7697.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 7692-7697
    • Shi, F.1    Telesco, S.E.2    Liu, Y.3    Radhakrishnan, R.4    Lemmon, M.A.5
  • 61
    • 34250878954 scopus 로고    scopus 로고
    • Mechanisms of specificity in protein phosphorylation
    • Ubersax J.A., Ferrell J.E. Mechanisms of specificity in protein phosphorylation. Nat. Rev. Mol. Cell Biol. 2007, 8:530-541.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 530-541
    • Ubersax, J.A.1    Ferrell, J.E.2
  • 63
    • 0037140764 scopus 로고    scopus 로고
    • Proton demand inversion in a mutant protein tyrosine kinase reaction
    • Williams D.M., Cole P.A. Proton demand inversion in a mutant protein tyrosine kinase reaction. J. Am. Chem. Soc. 2002, 124:5956-5957.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 5956-5957
    • Williams, D.M.1    Cole, P.A.2
  • 64
    • 84885868361 scopus 로고    scopus 로고
    • Structural insights into RIP3-mediated necroptotic signaling
    • Xie T., Peng W., Yan C., Wu J., Gong X., Shi Y. Structural insights into RIP3-mediated necroptotic signaling. Cell Rep. 2013, 5:70-78.
    • (2013) Cell Rep. , vol.5 , pp. 70-78
    • Xie, T.1    Peng, W.2    Yan, C.3    Wu, J.4    Gong, X.5    Shi, Y.6
  • 65
    • 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., Mizuno K. Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization. Nature 1998, 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
  • 66
    • 1542335568 scopus 로고    scopus 로고
    • LIM kinase 1 activates cAMP-responsive element-binding protein during the neuronal differentiation of immortalized hippocampal progenitor cells
    • Yang E.J., Yoon J.H., Min D.S., Chung K.C. LIM kinase 1 activates cAMP-responsive element-binding protein during the neuronal differentiation of immortalized hippocampal progenitor cells. J. Biol. Chem. 2004, 279:8903-8910.
    • (2004) J. Biol. Chem. , vol.279 , pp. 8903-8910
    • Yang, E.J.1    Yoon, J.H.2    Min, D.S.3    Chung, K.C.4
  • 67
    • 0025277362 scopus 로고
    • Inhibition of the interactions of cofilin, destrin, and deoxyribonuclease I with actin by phosphoinositides
    • Yonezawa N., Nishida E., Iida K., Yahara I., Sakai H. Inhibition of the interactions of cofilin, destrin, and deoxyribonuclease I with actin by phosphoinositides. J. Biol. Chem. 1990, 265:8382-8386.
    • (1990) J. Biol. Chem. , vol.265 , pp. 8382-8386
    • Yonezawa, N.1    Nishida, E.2    Iida, K.3    Yahara, I.4    Sakai, H.5
  • 68
    • 0015236388 scopus 로고
    • Adenylyl imidodiphosphate, an adenosine triphosphate analog containing a P-N-P linkage
    • Yount R.G., Babcock D., Ballantyne W., Ojala D. Adenylyl imidodiphosphate, an adenosine triphosphate analog containing a P-N-P linkage. Biochemistry 1971, 10:2484-2489.
    • (1971) Biochemistry , vol.10 , pp. 2484-2489
    • Yount, R.G.1    Babcock, D.2    Ballantyne, W.3    Ojala, D.4
  • 69
    • 77956646000 scopus 로고    scopus 로고
    • ADF/cofilin binds phosphoinositides in a multivalent manner to act as a PIP(2)-density sensor
    • Zhao H., Hakala M., Lappalainen P. ADF/cofilin binds phosphoinositides in a multivalent manner to act as a PIP(2)-density sensor. Biophys. J. 2010, 98:2327-2336.
    • (2010) Biophys. J. , vol.98 , pp. 2327-2336
    • Zhao, H.1    Hakala, M.2    Lappalainen, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.