메뉴 건너뛰기




Volumn 9, Issue 8, 1999, Pages 405-415

Rho-family GTPases require the Arp2/3 complex to stimulate actin polymerization in Acanthamoeba extracts

Author keywords

[No Author keywords available]

Indexed keywords

ACANTHAMOEBA; ANIMALIA;

EID: 0033594548     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(99)80187-0     Document Type: Article
Times cited : (64)

References (60)
  • 1
    • 0019503649 scopus 로고
    • Actin filaments elongate from their membrane-associated ends
    • 1. Tilney LG, Bonder EM, DeRosier DJ: Actin filaments elongate from their membrane-associated ends. J Cell Biol 1981, 90:485-494.
    • (1981) J Cell Biol , vol.90 , pp. 485-494
    • Tilney, L.G.1    Bonder, E.M.2    DeRosier, D.J.3
  • 2
    • 0021020399 scopus 로고
    • Stimulation by chemoattractant factor of actin associated with the cytoskeleton in rabbit neutrophils. Effects of calcium and cytochalaisin B
    • 2. White JR, Naccache PH, Sha'afi RI: Stimulation by chemoattractant factor of actin associated with the cytoskeleton in rabbit neutrophils. Effects of calcium and cytochalaisin B. J Biol Chem 1983, 258:14041-14047.
    • (1983) J Biol Chem , vol.258 , pp. 14041-14047
    • White, J.R.1    Naccache, P.H.2    Sha'Afi, R.I.3
  • 3
    • 0022390903 scopus 로고
    • Exchange of actin subunits at the leading edge of living fibroblasts: Possible role of treadmilling
    • 3. Wang Y: Exchange of actin subunits at the leading edge of living fibroblasts: possible role of treadmilling. J Cell Biol 1985,101:597-602.
    • (1985) J Cell Biol , vol.101 , pp. 597-602
    • Wang, Y.1
  • 4
    • 0029775654 scopus 로고    scopus 로고
    • Cell motility driven by actin polymerization
    • 4. Mogilner A, Oster G: Cell motility driven by actin polymerization. Biophys J 1996, 71:3030-3045.
    • (1996) Biophys J , vol.71 , pp. 3030-3045
    • Mogilner, A.1    Oster, G.2
  • 5
    • 0016751044 scopus 로고
    • Control of cell-contact sites by cyclic AMP pulses in differentiating Dictyostelium cells
    • 5. Gerisch G, Fromm H, Huesgen A, Wick U: Control of cell-contact sites by cyclic AMP pulses in differentiating Dictyostelium cells. Nature 1975, 255:547-549.
    • (1975) Nature , vol.255 , pp. 547-549
    • Gerisch, G.1    Fromm, H.2    Huesgen, A.3    Wick, U.4
  • 6
    • 0030474160 scopus 로고    scopus 로고
    • D3 phosphoinositides and outside-in integrin signaling by glycoprotein IIb-IIIa mediate platelet actin assembly and filopodial extension induced by phorbol 12-myristate 13-acetate
    • 6. Hartwig JH, Kung S, Kovacsovics T, Janmey PA, Cantley LC, Stossel TP, Toker A: D3 phosphoinositides and outside-in integrin signaling by glycoprotein IIb-IIIa mediate platelet actin assembly and filopodial extension induced by phorbol 12-myristate 13-acetate. J Biol Chem 1996, 271:32986-32993.
    • (1996) J Biol Chem , vol.271 , pp. 32986-32993
    • Hartwig, J.H.1    Kung, S.2    Kovacsovics, T.3    Janmey, P.A.4    Cantley, L.C.5    Stossel, T.P.6    Toker, A.7
  • 7
    • 0032006817 scopus 로고    scopus 로고
    • Control of actin dynamics
    • 7. Carlier MF: Control of actin dynamics. Curr Opin Cell Biol 1998, 10:45-51.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 45-51
    • Carlier, M.F.1
  • 8
    • 0017065560 scopus 로고
    • Unpolymerized actin in fibroblasts and brain
    • 8. Bray D, Thomas C: Unpolymerized actin in fibroblasts and brain. J Mol Biol 1976, 105:527-544.
    • (1976) J Mol Biol , vol.105 , pp. 527-544
    • Bray, D.1    Thomas, C.2
  • 9
    • 0025740949 scopus 로고
    • Actin microfilament dynamics in locomoting cells
    • 9. Theriot JA, Mitchison TJ: Actin microfilament dynamics in locomoting cells. Nature 1991, 352:126-131.
    • (1991) Nature , vol.352 , pp. 126-131
    • Theriot, J.A.1    Mitchison, T.J.2
  • 10
    • 0027489905 scopus 로고
    • Focusing on unpolymerized actin
    • 10. FechheiMer M, Zigmond SH: Focusing on unpolymerized actin. J Cell Biol 1993, 123:1-5.
    • (1993) J Cell Biol , vol.123 , pp. 1-5
    • Fechheimer, M.1    Zigmond, S.H.2
  • 11
    • 0032563603 scopus 로고    scopus 로고
    • Mechanism of Cdc42-induced actin polymerization in neutrophil extracts
    • 11. Zigmond SH, Joyce M, Yang C, Brown K, Huang M, Pring M: Mechanism of Cdc42-induced actin polymerization in neutrophil extracts. J Cell Biol 1998, 142:1001-1012.
    • (1998) J Cell Biol , vol.142 , pp. 1001-1012
    • Zigmond, S.H.1    Joyce, M.2    Yang, C.3    Brown, K.4    Huang, M.5    Pring, M.6
  • 12
    • 0029795850 scopus 로고    scopus 로고
    • Dynamics of capping protein and actin assembly in vitro: Uncapping barbed ends by polyphosphoinositides
    • 12. Schafer DA, Jennings PB, Cooper JA: Dynamics of capping protein and actin assembly in vitro: uncapping barbed ends by polyphosphoinositides. J Cell Biol 1996, 135:169-179.
    • (1996) J Cell Biol , vol.135 , pp. 169-179
    • Schafer, D.A.1    Jennings, P.B.2    Cooper, J.A.3
  • 13
    • 0023157142 scopus 로고
    • Modulation of gelsolin function by phosphatidylinositol 4,5-biphosphate
    • 13. Janmey PA, Stossel TP: Modulation of gelsolin function by phosphatidylinositol 4,5-biphosphate. Nature 1987, 325:362-364.
    • (1987) Nature , vol.325 , pp. 362-364
    • Janmey, P.A.1    Stossel, T.P.2
  • 14
    • 0030728491 scopus 로고    scopus 로고
    • Capping protein terminates but does not initiate chemoattractant-induced actin assembly in Dictyostelium
    • 14. Eddy RJ, Han J, Condeelis JS: Capping protein terminates but does not initiate chemoattractant-induced actin assembly in Dictyostelium. J Cell Biol 1997, 139:1243-1253.
    • (1997) J Cell Biol , vol.139 , pp. 1243-1253
    • Eddy, R.J.1    Han, J.2    Condeelis, J.S.3
  • 15
    • 0026340941 scopus 로고
    • Characterization of actin filament severing by actophorin from Acanthamoeba castellanii
    • 15. Maciver SK, Zot HG, Pollard TD: Characterization of actin filament severing by actophorin from Acanthamoeba castellanii. J Cell Biol 1991, 115:1611-1620.
    • (1991) J Cell Biol , vol.115 , pp. 1611-1620
    • Maciver, S.K.1    Zot, H.G.2    Pollard, T.D.3
  • 16
    • 0030821155 scopus 로고    scopus 로고
    • Xenopus actin depolymerizing factor/cofilin (XAC) is responsible for the turnover of actin filaments in Listeria monocytogenes tails
    • 16. Rosenblatt J, Agnew BJ, Abe H, Bamburg JR, Mitchison TJ: Xenopus actin depolymerizing factor/cofilin (XAC) is responsible for the turnover of actin filaments in Listeria monocytogenes tails. J Cell Biol 1997, 136:1323-1332.
    • (1997) J Cell Biol , vol.136 , pp. 1323-1332
    • Rosenblatt, J.1    Agnew, B.J.2    Abe, H.3    Bamburg, J.R.4    Mitchison, T.J.5
  • 17
    • 0026784141 scopus 로고
    • Mechanisms of actin rearrangements mediating platelet activation
    • 17. Hartwig JH: Mechanisms of actin rearrangements mediating platelet activation. J Cell Biol 1992, 118:1421-1442.
    • (1992) J Cell Biol , vol.118 , pp. 1421-1442
    • Hartwig, J.H.1
  • 18
    • 0032568874 scopus 로고    scopus 로고
    • G proteins and small GTpases: Distant relatives keep in touch
    • 18. Hall A: G proteins and small GTpases: distant relatives keep in touch. Science 1998, 280:2074-2075.
    • (1998) Science , vol.280 , pp. 2074-2075
    • Hall, A.1
  • 19
    • 0026654125 scopus 로고
    • The small GTP-binding protein rac regulates growth factor-induced membrane ruffling
    • 19. Ridley AJ, Paterson HF, Johnston CL, Diekmann D, Hall A: The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell 1992, 70:401-410.
    • (1992) Cell , vol.70 , pp. 401-410
    • Ridley, A.J.1    Paterson, H.F.2    Johnston, C.L.3    Diekmann, D.4    Hall, A.5
  • 21
    • 0030849454 scopus 로고    scopus 로고
    • Regulation of actin polymerization in cell-free systems by GTPγS and Cdc42
    • 21. Zigmond SH, Joyce M, Borleis J, Bokoch GM, Devreotes PN: Regulation of actin polymerization in cell-free systems by GTPγS and Cdc42. J Cell Biol 1997, 138:363-374.
    • (1997) J Cell Biol , vol.138 , pp. 363-374
    • Zigmond, S.H.1    Joyce, M.2    Borleis, J.3    Bokoch, G.M.4    Devreotes, P.N.5
  • 22
    • 0031863308 scopus 로고    scopus 로고
    • GTPgammaS-induced actin polymerisation in vitro: ATP- and phosphoinositide-independent signalling via Rho-family proteins and a plasma membrane-associated guanine nucleotide exchange factor
    • 22. Katanaev VL, Wymann MP: GTPgammaS-induced actin polymerisation in vitro: ATP- and phosphoinositide-independent signalling via Rho-family proteins and a plasma membrane-associated guanine nucleotide exchange factor. J Cell Sci 1998, 111:1583-1594.
    • (1998) J Cell Sci , vol.111 , pp. 1583-1594
    • Katanaev, V.L.1    Wymann, M.P.2
  • 23
    • 0032498854 scopus 로고    scopus 로고
    • Corequirement of specific phosphoinositides and small GTP-binding protein Cdc42 in inducing actin assembly in Xenopus egg extracts
    • 23. Ma L, Cantley LC, Janmey PA, Kirschner MW: Corequirement of specific phosphoinositides and small GTP-binding protein Cdc42 in inducing actin assembly in Xenopus egg extracts. J Cell Biol 1998, 140:1125-1136.
    • (1998) J Cell Biol , vol.140 , pp. 1125-1136
    • Ma, L.1    Cantley, L.C.2    Janmey, P.A.3    Kirschner, M.W.4
  • 24
    • 0032568650 scopus 로고    scopus 로고
    • The interaction of Arp2/3 complex with actin: Nucleation, high-affinity pointed end capping, and formation of branching networks of filaments
    • 24. Mullins RD, Heuser JA, Pollard TD: The interaction of Arp2/3 complex with actin: nucleation, high-affinity pointed end capping, and formation of branching networks of filaments. Proc Natl Acad Sci USA 1998, 95:6181-6186.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6181-6186
    • Mullins, R.D.1    Heuser, J.A.2    Pollard, T.D.3
  • 25
    • 0032479578 scopus 로고    scopus 로고
    • Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation
    • 25. Welch MD, Rosenblatt J, Skoble J, Portnoy DA, Mitchison TJ: Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation. Science 1998, 281:105-108.
    • (1998) Science , vol.281 , pp. 105-108
    • Welch, M.D.1    Rosenblatt, J.2    Skoble, J.3    Portnoy, D.A.4    Mitchison, T.J.5
  • 26
    • 0026571486 scopus 로고
    • New yeast actin-like gene required late in the cell cycle
    • 26. Schwob E, Martin RP: New yeast actin-like gene required late in the cell cycle. Nature 1992, 355:179-182.
    • (1992) Nature , vol.355 , pp. 179-182
    • Schwob, E.1    Martin, R.P.2
  • 27
    • 0031193920 scopus 로고    scopus 로고
    • The complex containing actin-related proteins Arp2 and Arp3 is required for the motility and integrity of yeast actin patches
    • 27. Winter D, Podtelejnikov AV, Mann M, Li R: The complex containing actin-related proteins Arp2 and Arp3 is required for the motility and integrity of yeast actin patches. Curr Biol 1997, 7:519-529.
    • (1997) Curr Biol , vol.7 , pp. 519-529
    • Winter, D.1    Podtelejnikov, A.V.2    Mann, M.3    Li, R.4
  • 28
    • 0031021153 scopus 로고    scopus 로고
    • Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes
    • 28. Welch MD, Iwamatsu A, Mitchison TJ: Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes. Nature 1997, 385:265-269.
    • (1997) Nature , vol.385 , pp. 265-269
    • Welch, M.D.1    Iwamatsu, A.2    Mitchison, T.J.3
  • 29
    • 0017303511 scopus 로고
    • Characterization of a cytoplasmic actin isolated from Acanthamoeba castellanii by a new method
    • 29. Gordon DJ, Eisenberg E, Korn ED: Characterization of a cytoplasmic actin isolated from Acanthamoeba castellanii by a new method. J Biol Chem 1976, 251:4778-4786.
    • (1976) J Biol Chem , vol.251 , pp. 4778-4786
    • Gordon, D.J.1    Eisenberg, E.2    Korn, E.D.3
  • 30
    • 0017227487 scopus 로고
    • The role of actin in the temperature dependent gelation and contraction of extracts of Acanthamoeba
    • 30. Pollard TD: The role of actin in the temperature dependent gelation and contraction of extracts of Acanthamoeba. J Cell Biol 1976, 68:579-601.
    • (1976) J Cell Biol , vol.68 , pp. 579-601
    • Pollard, T.D.1
  • 31
    • 0018934798 scopus 로고
    • Viscometric analysis of the gelation of Acanthamoeba extracts and purification of two gelation factors
    • 31. MacLean-Fletcher S, Pollard TD: Viscometric analysis of the gelation of Acanthamoeba extracts and purification of two gelation factors. J Cell Biol 1980, 85:414-428.
    • (1980) J Cell Biol , vol.85 , pp. 414-428
    • Maclean-Fletcher, S.1    Pollard, T.D.2
  • 32
    • 0027497240 scopus 로고
    • Rabbit skeletal muscle actin behaves differently than Acanthamoeba actin when added to soluble extracts of Acanthamoeba castellanii
    • 32. Holliday LS, Bubb MR, Korn ED: Rabbit skeletal muscle actin behaves differently than Acanthamoeba actin when added to soluble extracts of Acanthamoeba castellanii. Biochem Biophys Res Commun 1993, 196:569-575.
    • (1993) Biochem Biophys Res Commun , vol.196 , pp. 569-575
    • Holliday, L.S.1    Bubb, M.R.2    Korn, E.D.3
  • 33
    • 0032483044 scopus 로고    scopus 로고
    • Interactions of Acanthamoeba profilin with actin and nucleotides bound to actin
    • 33. Vinson VK, De La Cruz EM, Higgs HN, Pollard TD: Interactions of Acanthamoeba profilin with actin and nucleotides bound to actin. Biochemistry 1998, 37:10871-10880.
    • (1998) Biochemistry , vol.37 , pp. 10871-10880
    • Vinson, V.K.1    De La Cruz, E.M.2    Higgs, H.N.3    Pollard, T.D.4
  • 34
    • 0028882496 scopus 로고
    • Actin filament barbed-end capping activity in neutrophil lysates: The role of capping protein-β2
    • 34. DiNubile MJ, Cassimeris L, Joyce M, Zigmond SH: Actin filament barbed-end capping activity in neutrophil lysates: the role of capping protein-β2. Mol Biol Cell 1995, 6:1659-1671.
    • (1995) Mol Biol Cell , vol.6 , pp. 1659-1671
    • DiNubile, M.J.1    Cassimeris, L.2    Joyce, M.3    Zigmond, S.H.4
  • 35
    • 0019256032 scopus 로고
    • An actin binding protein from Acanthamoeba regulates actin filament polymerization and interactions
    • 35. Isenberg GH, Aebi U, Pollard TD: An actin binding protein from Acanthamoeba regulates actin filament polymerization and interactions. Nature 1980, 288:455-459.
    • (1980) Nature , vol.288 , pp. 455-459
    • Isenberg, G.H.1    Aebi, U.2    Pollard, T.D.3
  • 36
    • 0021259403 scopus 로고
    • Acanthamoeba castellanii capping protein: Properties, mechanism of action, immunologic cross-reactivity, and localization
    • 36. Cooper JA, Blum JD, Pollard TD: Acanthamoeba castellanii capping protein: properties, mechanism of action, immunologic cross-reactivity, and localization. J Cell Biol 1984, 99:217-225.
    • (1984) J Cell Biol , vol.99 , pp. 217-225
    • Cooper, J.A.1    Blum, J.D.2    Pollard, T.D.3
  • 37
    • 0024404311 scopus 로고
    • Rabbit intestine contains a protein that inhibits the dissociation of GDP from and the subsequent binding of GTP to rhoB p20, a ras p21-like GTP-binding protein
    • 37. Ohga N, Kikuchi A, Ueda T, Yamamoto J, Takai Y: Rabbit intestine contains a protein that inhibits the dissociation of GDP from and the subsequent binding of GTP to rhoB p20, a ras p21-like GTP-binding protein. Biochem Biophys Res Commun 1989, 163:1523-1533.
    • (1989) Biochem Biophys Res Commun , vol.163 , pp. 1523-1533
    • Ohga, N.1    Kikuchi, A.2    Ueda, T.3    Yamamoto, J.4    Takai, Y.5
  • 38
    • 0030298138 scopus 로고    scopus 로고
    • Rac and Cdc42 induce actin polymerization and G1 cell cycle progression independently of p65PAK and the JNK/SAPK MAP kinase cascade
    • 38. Lamarche N, Tapon N, Stowers L, Burbelo PD, Aspenstrom P, Bridges T, et al.: Rac and Cdc42 induce actin polymerization and G1 cell cycle progression independently of p65PAK and the JNK/SAPK MAP kinase cascade. Cell 1996, 87:519-529.
    • (1996) Cell , vol.87 , pp. 519-529
    • Lamarche, N.1    Tapon, N.2    Stowers, L.3    Burbelo, P.D.4    Aspenstrom, P.5    Bridges, T.6
  • 39
    • 0017873769 scopus 로고
    • Biochemistry of actomyosin-dependent cell motility
    • 39. Korn ED: Biochemistry of actomyosin-dependent cell motility. Proc Natl Acad Sci USA 1978, 75:588-599.
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 588-599
    • Korn, E.D.1
  • 40
    • 0030843484 scopus 로고    scopus 로고
    • Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: Implication in actin-based motility
    • 40. Carlier MF, Laurent V, Santolini J, Melki R, Didry D, Xia GX, et al.: Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: implication in actin-based motility. J Cell Biol 1997, 136:1307-1322.
    • (1997) J Cell Biol , vol.136 , pp. 1307-1322
    • Carlier, M.F.1    Laurent, V.2    Santolini, J.3    Melki, R.4    Didry, D.5    Xia, G.X.6
  • 41
    • 84886632310 scopus 로고
    • Actin polymerizability is influenced by profilin, a low molecular weight protein in non-muscle cells
    • 41. Carlsson L, Nyström L-E, Sundkvist I, Markey F, Lindberg U: Actin polymerizability is influenced by profilin, a low molecular weight protein in non-muscle cells. J Mol Biol 1977, 115:465-483.
    • (1977) J Mol Biol , vol.115 , pp. 465-483
    • Carlsson, L.1    Nyström, L.-E.2    Sundkvist, I.3    Markey, F.4    Lindberg, U.5
  • 42
    • 0021766640 scopus 로고
    • Quantitative analysis of the effect of Acanthamoeba profilin on actin filament nucleation and elongation
    • 42. Pollard TD, Cooper JA: Quantitative analysis of the effect of Acanthamoeba profilin on actin filament nucleation and elongation. Biochemistry 1984, 23:6631-6641.
    • (1984) Biochemistry , vol.23 , pp. 6631-6641
    • Pollard, T.D.1    Cooper, J.A.2
  • 43
    • 0020790453 scopus 로고
    • Actin from Thyone briareus sperm assembles on only one end of an actin filament: A behavior regulated by profilin
    • 43. Tilney LG, Bonder EM, Coluccio LM, Mooseker MS: Actin from Thyone briareus sperm assembles on only one end of an actin filament: a behavior regulated by profilin. J Cell Biol 1983, 97:112-142.
    • (1983) J Cell Biol , vol.97 , pp. 112-142
    • Tilney, L.G.1    Bonder, E.M.2    Coluccio, L.M.3    Mooseker, M.S.4
  • 45
    • 0027104517 scopus 로고
    • The control of actin nucleotide exchange by thymosinβ4 and profilin. A potential regulatory mechanism for actin polymerization in cells
    • 45. Goldschmidt-Clermont PJ, Furman MI, Wachsstock D, Safer D, Nachmias VT, Pollard TD: The control of actin nucleotide exchange by thymosinβ4 and profilin. A potential regulatory mechanism for actin polymerization in cells. Mol Biol Cell 1992, 3:1015-1024.
    • (1992) Mol Biol Cell , vol.3 , pp. 1015-1024
    • Goldschmidt-Clermont, P.J.1    Furman, M.I.2    Wachsstock, D.3    Safer, D.4    Nachmias, V.T.5    Pollard, T.D.6
  • 46
    • 0025856003 scopus 로고
    • Thymosin beta 4 and Fx, an actin-sequestering peptide, are indistinguishable
    • 46. Safer D, Elzinga M, Nachmias VT: Thymosin beta 4 and Fx, an actin-sequestering peptide, are indistinguishable. J Biol Chem 1991, 266:4029-4032.
    • (1991) J Biol Chem , vol.266 , pp. 4029-4032
    • Safer, D.1    Elzinga, M.2    Nachmias, V.T.3
  • 47
    • 0027772556 scopus 로고
    • How profilin promotes actin filament assembly in the presence of thymosin β4
    • 47. Pantaloni D, Carlier MF: How profilin promotes actin filament assembly in the presence of thymosin β4. Cell 1993, 75:1007-1014.
    • (1993) Cell , vol.75 , pp. 1007-1014
    • Pantaloni, D.1    Carlier, M.F.2
  • 48
    • 0032430263 scopus 로고    scopus 로고
    • The Arp2/3 complex mediates actin polymerization induced by the small GTP-binding protein Cdc42
    • 48. Ma L, Rohatgi R, Kirschner MW: The Arp2/3 complex mediates actin polymerization induced by the small GTP-binding protein Cdc42. Proc Natl Acad Sci USA 1998, 95:15362-15367.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 15362-15367
    • Ma, L.1    Rohatgi, R.2    Kirschner, M.W.3
  • 49
    • 0032585538 scopus 로고    scopus 로고
    • Scar1 and the related Wiskott-Aldrich Syndrome Protein, WASP, regulate the actin cytoskeleton through Arp2/3 complex
    • 49. Machesky LM, Insall RH: Scar1 and the related Wiskott-Aldrich Syndrome Protein, WASP, regulate the actin cytoskeleton through Arp2/3 complex. Curr Biol 1998, 8:1347-1356.
    • (1998) Curr Biol , vol.8 , pp. 1347-1356
    • Machesky, L.M.1    Insall, R.H.2
  • 51
    • 0021200245 scopus 로고
    • Polymerization of ADP-actin
    • 51. Pollard TD: Polymerization of ADP-actin. J Cell Biol 1984, 99:769-777.
    • (1984) J Cell Biol , vol.99 , pp. 769-777
    • Pollard, T.D.1
  • 52
    • 0028136434 scopus 로고
    • Purification of a cortical complex containing two unconventional actins from Acanthamoeba by affinity chromatography on profilin agarose
    • 52. Machesky LM, Atkinson SJ, Ampe C, Vandekerckhove J, Pollard TD: Purification of a cortical complex containing two unconventional actins from Acanthamoeba by affinity chromatography on profilin agarose. J Cell Biol 1994, 127:107-115.
    • (1994) J Cell Biol , vol.127 , pp. 107-115
    • Machesky, L.M.1    Atkinson, S.J.2    Ampe, C.3    Vandekerckhove, J.4    Pollard, T.D.5
  • 53
    • 0027467339 scopus 로고
    • Requirement for posttranslational processing of Rac GTP-binding proteins for activation of human neutrophil NADPH oxidase
    • 53. Heyworth PG, Knaus UG, Xu DJ, Uhlinger DJ, Conroy L, Bokoch GM, Curnutte JT: Requirement for posttranslational processing of Rac GTP-binding proteins for activation of human neutrophil NADPH oxidase. Mol Biol Cell 1993, 4:261-269.
    • (1993) Mol Biol Cell , vol.4 , pp. 261-269
    • Heyworth, P.G.1    Knaus, U.G.2    Xu, D.J.3    Uhlinger, D.J.4    Conroy, L.5    Bokoch, G.M.6    Curnutte, J.T.7
  • 54
    • 0028786352 scopus 로고
    • Sequences, structural models, and cellular localization of the actin-related proteins Arp2 and Arp3 from Acanthamoeba
    • 54. Kelleher JF, Atkinson SJ, Pollard TD: Sequences, structural models, and cellular localization of the actin-related proteins Arp2 and Arp3 from Acanthamoeba. J Cell Biol 1995, 131:385-397.
    • (1995) J Cell Biol , vol.131 , pp. 385-397
    • Kelleher, J.F.1    Atkinson, S.J.2    Pollard, T.D.3
  • 55
    • 0031051993 scopus 로고    scopus 로고
    • Structure, subunit topology, and actin-binding activity of the Arp2/3 complex from Acanthamoeba
    • 55. Mullins RD, Stafford WF, Pollard TD: Structure, subunit topology, and actin-binding activity of the Arp2/3 complex from Acanthamoeba. J Cell Biol 1997, 136:331-343.
    • (1997) J Cell Biol , vol.136 , pp. 331-343
    • Mullins, R.D.1    Stafford, W.F.2    Pollard, T.D.3
  • 56
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 56. Laemmli UK: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 57
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedures and some applications
    • 57. Towbin H, Stahelin T, Gordon J: Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedures and some applications. Proc Natl Acad Sci USA 1979, 76:4350-4354.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Stahelin, T.2    Gordon, J.3
  • 59
    • 0014601237 scopus 로고
    • Species variations in phospholipid class distribution of organs. I. Kidney, liver and spleen
    • 59. Rouser G, Simon G, Kritchevsky G: Species variations in phospholipid class distribution of organs. I. Kidney, liver and spleen. Lipids 1969, 4:599-606.
    • (1969) Lipids , vol.4 , pp. 599-606
    • Rouser, G.1    Simon, G.2    Kritchevsky, G.3
  • 60
    • 0014289435 scopus 로고
    • Modified spray for the detection of phospholipids on thin-layer chromatograms
    • 60. Vaskovsky VE, Kostetsky EY: Modified spray for the detection of phospholipids on thin-layer chromatograms. J Lipid Res 1968, 9:396.
    • (1968) J Lipid Res , vol.9 , pp. 396
    • Vaskovsky, V.E.1    Kostetsky, E.Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.