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Volumn 37, Issue , 2006, Pages 49-66

The Connection Between Actin ATPase and Polymerization

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EID: 37849189130     PISSN: 15692558     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1569-2558(06)37003-8     Document Type: Review
Times cited : (6)

References (96)
  • 1
    • 0001360883 scopus 로고
    • Dephosphorylation of adenosine triphosphate in actin solutions at low concentrations of magnesium
    • Asakura S., and Oosawa F. Dephosphorylation of adenosine triphosphate in actin solutions at low concentrations of magnesium. Arch. Biochem. Biophys. 87 (1960) 273-280
    • (1960) Arch. Biochem. Biophys. , vol.87 , pp. 273-280
    • Asakura, S.1    Oosawa, F.2
  • 2
    • 0027248807 scopus 로고
    • Mutations in beta-actin: Influence on polymer formation and on interactions with myosin and profilin
    • Aspenström P., Schutt C.E., Lindberg U., and Karlsson R. Mutations in beta-actin: Influence on polymer formation and on interactions with myosin and profilin. FEBS Lett. 329 (1993) 163-170
    • (1993) FEBS Lett. , vol.329 , pp. 163-170
    • Aspenström, P.1    Schutt, C.E.2    Lindberg, U.3    Karlsson, R.4
  • 4
    • 0034837025 scopus 로고    scopus 로고
    • ATPase-defective derivatives of Escherichia coli DnaK that behave differently with respect to ATP-induced conformational change and peptide release
    • Barthel T.K., Zhang J., and Walker G.C. ATPase-defective derivatives of Escherichia coli DnaK that behave differently with respect to ATP-induced conformational change and peptide release. J. Bacteriol. 183 (2001) 5482-5490
    • (2001) J. Bacteriol. , vol.183 , pp. 5482-5490
    • Barthel, T.K.1    Zhang, J.2    Walker, G.C.3
  • 5
    • 0033524402 scopus 로고    scopus 로고
    • A change in actin conformation associated with filament instability after Pi release
    • Belmont L.D., Orlova A., Drubin D.G., and Egelman E.H. A change in actin conformation associated with filament instability after Pi release. Proc. Natl. Acad. Sci. USA 96 (1999) 29-34
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 29-34
    • Belmont, L.D.1    Orlova, A.2    Drubin, D.G.3    Egelman, E.H.4
  • 6
    • 0032566659 scopus 로고    scopus 로고
    • Interaction of actin monomers with Acanthamoeba actophorin (ADF/cofilin) and profilin
    • Blanchoin L., and Pollard T.D. Interaction of actin monomers with Acanthamoeba actophorin (ADF/cofilin) and profilin. J. Biol. Chem. 273 (1998) 25106-25111
    • (1998) J. Biol. Chem. , vol.273 , pp. 25106-25111
    • Blanchoin, L.1    Pollard, T.D.2
  • 7
    • 0033060250 scopus 로고    scopus 로고
    • Mechanism of interaction of Acanthamoeba actophorin (ADF/cofilin) with actin filaments
    • Blanchoin L., and Pollard T.D. Mechanism of interaction of Acanthamoeba actophorin (ADF/cofilin) with actin filaments. J. Biol. Chem. 274 (1999) 15538-15546
    • (1999) J. Biol. Chem. , vol.274 , pp. 15538-15546
    • Blanchoin, L.1    Pollard, T.D.2
  • 8
    • 0020598145 scopus 로고
    • Direct electron microscopic visualization of barbed end capping and filament cutting by intestinal microvillar 95-k dalton protein (villin): A new actin assembly assay using the Limulus acrosomal process
    • Bonder E.M., and Mooseker M.S. Direct electron microscopic visualization of barbed end capping and filament cutting by intestinal microvillar 95-k dalton protein (villin): A new actin assembly assay using the Limulus acrosomal process. J. Cell Biol. 96 (1983) 1097-1107
    • (1983) J. Cell Biol. , vol.96 , pp. 1097-1107
    • Bonder, E.M.1    Mooseker, M.S.2
  • 9
    • 0018890176 scopus 로고
    • The effects of cytochalasins on actin polymerization and actin ATPase provide insights into the mechanism of polymerization
    • Brenner S.L., and Korn E.D. The effects of cytochalasins on actin polymerization and actin ATPase provide insights into the mechanism of polymerization. J. Biol. Chem. 255 (1980) 841-844
    • (1980) J. Biol. Chem. , vol.255 , pp. 841-844
    • Brenner, S.L.1    Korn, E.D.2
  • 10
    • 0022876860 scopus 로고
    • Direct evidence for ADP-Pi-F-actin as the major intermediate in ATP-actin polymerization
    • Carlier M.F., and Pantaloni D. Direct evidence for ADP-Pi-F-actin as the major intermediate in ATP-actin polymerization. Biochemistry 25 (1986) 7789-7792
    • (1986) Biochemistry , vol.25 , pp. 7789-7792
    • Carlier, M.F.1    Pantaloni, D.2
  • 11
    • 0022971380 scopus 로고
    • Fluorescence measurements of the binding of cations to high-affinity and low-affinity sites on ATP-G-actin
    • Carlier M.F., Pantaloni D., and Korn E.D. Fluorescence measurements of the binding of cations to high-affinity and low-affinity sites on ATP-G-actin. J. Biol. Chem. 261 (1986) 10778-10784
    • (1986) J. Biol. Chem. , vol.261 , pp. 10778-10784
    • Carlier, M.F.1    Pantaloni, D.2    Korn, E.D.3
  • 12
    • 0027163104 scopus 로고
    • Modulation of the interaction between G-actin and thymosin beta 4 by the ATP/ADP ratio: Possible implication in the regulation of actin dynamics
    • Carlier M.F., Jean C., Rieger K.J., Lenfant M., and Pantaloni D. Modulation of the interaction between G-actin and thymosin beta 4 by the ATP/ADP ratio: Possible implication in the regulation of actin dynamics. Proc. Natl. Acad. Sci. USA 90 (1993) 5034-5038
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5034-5038
    • Carlier, M.F.1    Jean, C.2    Rieger, K.J.3    Lenfant, M.4    Pantaloni, D.5
  • 14
    • 0028999056 scopus 로고
    • A mutation in an ATP-binding loop of Saccharomyces cerevisiae actin (S14A) causes a temperature-sensitive phenotype in vivo and in vitro
    • Chen X., and Rubenstein P.A. A mutation in an ATP-binding loop of Saccharomyces cerevisiae actin (S14A) causes a temperature-sensitive phenotype in vivo and in vitro. J. Biol. Chem. 270 (1995) 11406-11414
    • (1995) J. Biol. Chem. , vol.270 , pp. 11406-11414
    • Chen, X.1    Rubenstein, P.A.2
  • 15
    • 28044470753 scopus 로고    scopus 로고
    • Actin-bound structures of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 and the implications for filament assembly
    • Chereau D., Kerff F., Graceffa P., Grabarek Z., Langsetmo K., and Dominguez R. Actin-bound structures of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 and the implications for filament assembly. Proc. Natl. Acad. Sci. USA 102 (2005) 16644-16649
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 16644-16649
    • Chereau, D.1    Kerff, F.2    Graceffa, P.3    Grabarek, Z.4    Langsetmo, K.5    Dominguez, R.6
  • 16
    • 0030575783 scopus 로고    scopus 로고
    • The structure of an open state of beta-actin at 2. 65 A resolution
    • Chik J.K., Lindberg U., and Schutt C.E. The structure of an open state of beta-actin at 2. 65 A resolution. J. Mol. Biol. 263 (1996) 607-623
    • (1996) J. Mol. Biol. , vol.263 , pp. 607-623
    • Chik, J.K.1    Lindberg, U.2    Schutt, C.E.3
  • 17
    • 0026794025 scopus 로고
    • Removal of the amino-terminal acidic residues of yeast actin. Studies in vitro and in vivo
    • Cook R.K., Blake W.T., and Rubenstein P.A. Removal of the amino-terminal acidic residues of yeast actin. Studies in vitro and in vivo. J. Biol. Chem. 267 (1992) 9430-9496
    • (1992) J. Biol. Chem. , vol.267 , pp. 9430-9496
    • Cook, R.K.1    Blake, W.T.2    Rubenstein, P.A.3
  • 18
    • 0027449986 scopus 로고
    • Enhanced stimulation of myosin subfragment 1 ATPase activity by addition of negatively charged residues to the yeast actin NH2 terminus
    • Cook R.K., Root D., Miller C., Reisler E., and Rubenstein P.A. Enhanced stimulation of myosin subfragment 1 ATPase activity by addition of negatively charged residues to the yeast actin NH2 terminus. J. Biol. Chem. 268 (1993) 2410-2415
    • (1993) J. Biol. Chem. , vol.268 , pp. 2410-2415
    • Cook, R.K.1    Root, D.2    Miller, C.3    Reisler, E.4    Rubenstein, P.A.5
  • 19
    • 0015814765 scopus 로고
    • Interaction of actin with analogs of adenosine triphosphate
    • Cooke R., and Murdoch L. Interaction of actin with analogs of adenosine triphosphate. Biochemistry 12 (1973) 3927-3932
    • (1973) Biochemistry , vol.12 , pp. 3927-3932
    • Cooke, R.1    Murdoch, L.2
  • 20
    • 0025931818 scopus 로고
    • Product release is not the rate-limiting step during cytochalasin B-induced ATPase activity of monomeric actin
    • Dancker P., Hess L., and Ritter K. Product release is not the rate-limiting step during cytochalasin B-induced ATPase activity of monomeric actin. Z. Naturforsch. [C] 46 (1991) 139-144
    • (1991) Z. Naturforsch. [C] , vol.46 , pp. 139-144
    • Dancker, P.1    Hess, L.2    Ritter, K.3
  • 21
    • 0036402424 scopus 로고    scopus 로고
    • A direct-transfer polymerization model explains how the multiple profilin-binding sites in the actoclampin motor promote rapid actin-based motility
    • Dickinson R.B., Southwick F.S., and Purich D.L. A direct-transfer polymerization model explains how the multiple profilin-binding sites in the actoclampin motor promote rapid actin-based motility. Arch. Biochem. Biophys. 406 (2002) 296-301
    • (2002) Arch. Biochem. Biophys. , vol.406 , pp. 296-301
    • Dickinson, R.B.1    Southwick, F.S.2    Purich, D.L.3
  • 22
    • 0027528476 scopus 로고
    • Mutations within the nucleotide binding site of immunoglobulin-binding protein inhibit ATPase activity and interfere with release of immunoglobulin heavy chain
    • Gaut J.R., and Hendershot L.M. Mutations within the nucleotide binding site of immunoglobulin-binding protein inhibit ATPase activity and interfere with release of immunoglobulin heavy chain. J. Biol. Chem. 268 (1993) 7248-7255
    • (1993) J. Biol. Chem. , vol.268 , pp. 7248-7255
    • Gaut, J.R.1    Hendershot, L.M.2
  • 23
    • 0025317410 scopus 로고
    • Inhibition of cytochalasin D-stimulated G-actin ATPase by ADP-ribosylation with Clostridium perfringens iota toxin
    • Geipel U., Just I., and Aktories K. Inhibition of cytochalasin D-stimulated G-actin ATPase by ADP-ribosylation with Clostridium perfringens iota toxin. Biochem. J. 266 (1990) 335-339
    • (1990) Biochem. J. , vol.266 , pp. 335-339
    • Geipel, U.1    Just, I.2    Aktories, K.3
  • 24
    • 0037482886 scopus 로고    scopus 로고
    • A crucial role for profilin-actin in the intracellular motility of Listeria monocytogenes
    • Grenklo S., Geese M., Lindberg U., Wehland J., Karlsson R., and Sechi A.S. A crucial role for profilin-actin in the intracellular motility of Listeria monocytogenes. EMBO Rep. 4 (2003) 526-529
    • (2003) EMBO Rep. , vol.4 , pp. 526-529
    • Grenklo, S.1    Geese, M.2    Lindberg, U.3    Wehland, J.4    Karlsson, R.5    Sechi, A.S.6
  • 25
    • 0028584378 scopus 로고
    • ATPase kinetics of recombinant bovine 70 kDa heat shock cognate protein and its amino-terminal ATPase domain
    • Ha J.H., and McKay D.B. ATPase kinetics of recombinant bovine 70 kDa heat shock cognate protein and its amino-terminal ATPase domain. Biochemistry 33 (1994) 14625-14635
    • (1994) Biochemistry , vol.33 , pp. 14625-14635
    • Ha, J.H.1    McKay, D.B.2
  • 26
    • 0342368848 scopus 로고    scopus 로고
    • Effects of cross-linked profilin: β/γ-Actin on the dynamics of the microfilament system in cultured cells
    • Hajkova L., Nyman T., Lindberg U., and Karlsson R. Effects of cross-linked profilin: β/γ-Actin on the dynamics of the microfilament system in cultured cells. Exp. Cell Res. 256 (2000) 112-121
    • (2000) Exp. Cell Res. , vol.256 , pp. 112-121
    • Hajkova, L.1    Nyman, T.2    Lindberg, U.3    Karlsson, R.4
  • 27
    • 0027494863 scopus 로고
    • Analysis of the interactions of actin depolymerizing factor with G- and F-actin
    • Hayden S.M., Miller P.S., Brauweiler A., and Bamburg J.R. 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    Miller, P.S.2    Brauweiler, A.3    Bamburg, J.R.4
  • 28
    • 0013791376 scopus 로고
    • Conformational changes associated with polymerization and nucleotide binding in actin molecules
    • Higashi S., and Oosawa F. Conformational changes associated with polymerization and nucleotide binding in actin molecules. J. Mol. Biol. 12 (1965) 843-865
    • (1965) J. Mol. Biol. , vol.12 , pp. 843-865
    • Higashi, S.1    Oosawa, F.2
  • 30
    • 0037039167 scopus 로고    scopus 로고
    • Cofilin produces newly polymerized actin filaments that are preferred for dendritic nucleation by the Arp2/3 complex
    • Ichetovkin I., Grant W., and Condeelis J. 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    Grant, W.2    Condeelis, J.3
  • 32
    • 13344281021 scopus 로고
    • Analysis of three DnaK mutant proteins suggests that progression through the ATPase cycle requires conformational changes
    • Kamath-Loeb A.S., Lu C.Z., Suh W.C., Lonetto M.A., and Gross C.A. Analysis of three DnaK mutant proteins suggests that progression through the ATPase cycle requires conformational changes. J. Biol. Chem. 270 (1995) 30051-30059
    • (1995) J. Biol. Chem. , vol.270 , pp. 30051-30059
    • Kamath-Loeb, A.S.1    Lu, C.Z.2    Suh, W.C.3    Lonetto, M.A.4    Gross, C.A.5
  • 33
    • 0002172352 scopus 로고
    • The cooperative nature of G-F transformation of actin
    • Kasai M., Asakura S., and Oosawa F. The cooperative nature of G-F transformation of actin. Biophys. Biochem. Acta 57 (1962) 22-31
    • (1962) Biophys. Biochem. Acta , vol.57 , pp. 22-31
    • Kasai, M.1    Asakura, S.2    Oosawa, F.3
  • 35
    • 0027418763 scopus 로고
    • Nucleotide binding to actin. Cation dependence of nucleotide dissociation and exchange rates
    • Kinosian H.J., Selden L.A., Estes J.E., and Gershman L.C. Nucleotide binding to actin. Cation dependence of nucleotide dissociation and exchange rates. J. Biol. Chem. 268 (1993) 8683-8691
    • (1993) J. Biol. Chem. , vol.268 , pp. 8683-8691
    • Kinosian, H.J.1    Selden, L.A.2    Estes, J.E.3    Gershman, L.C.4
  • 37
    • 0023637721 scopus 로고
    • Actin polymerization and ATP hydrolysis
    • Korn E.D., Carlier M.F., and Pantaloni D. Actin polymerization and ATP hydrolysis. Science 238 (1987) 638-644
    • (1987) Science , vol.238 , pp. 638-644
    • Korn, E.D.1    Carlier, M.F.2    Pantaloni, D.3
  • 38
    • 0141707869 scopus 로고    scopus 로고
    • Solution properties of tetramethylrhodamine-modified G-actin
    • Kudryashov D.S., and Reisler E. Solution properties of tetramethylrhodamine-modified G-actin. Biophys. J. 85 (2003) 2466-2475
    • (2003) Biophys. J. , vol.85 , pp. 2466-2475
    • Kudryashov, D.S.1    Reisler, E.2
  • 39
    • 0027286199 scopus 로고
    • Selective binding of gelsolin to actin monomers containing ADP
    • Laham L.E., Lamb J.A., Allen P.G., and Janmey P.A. Selective binding of gelsolin to actin monomers containing ADP. J. Biol. Chem. 268 (1993) 14202-14207
    • (1993) J. Biol. Chem. , vol.268 , pp. 14202-14207
    • Laham, L.E.1    Lamb, J.A.2    Allen, P.G.3    Janmey, P.A.4
  • 40
    • 0021750640 scopus 로고
    • Preparation and polymerization of skeletal muscle ADP-actin
    • Lal A.A., Brenner S.L., and Korn E.D. Preparation and polymerization of skeletal muscle ADP-actin. J. Biol. Chem. 259 (1984) 13061-13065
    • (1984) J. Biol. Chem. , vol.259 , pp. 13061-13065
    • Lal, A.A.1    Brenner, S.L.2    Korn, E.D.3
  • 41
    • 0028024049 scopus 로고
    • Small angle X-ray scattering and electron cryomicroscopy study of actin filaments: Role of the bound nucleotide in the structure of F-actin
    • Lepault J., Ranck J.L., Erk I., and Carlier M.F. Small angle X-ray scattering and electron cryomicroscopy study of actin filaments: Role of the bound nucleotide in the structure of F-actin. J. Struct. Biol. 112 (1994) 79-91
    • (1994) J. Struct. Biol. , vol.112 , pp. 79-91
    • Lepault, J.1    Ranck, J.L.2    Erk, I.3    Carlier, M.F.4
  • 42
    • 0024292833 scopus 로고
    • Aromatic rings act as hydrogen bond acceptors
    • Levitt M., and Perutz M.F. Aromatic rings act as hydrogen bond acceptors. J. Mol. Biol. 204 (1988) 751-754
    • (1988) J. Mol. Biol. , vol.204 , pp. 751-754
    • Levitt, M.1    Perutz, M.F.2
  • 43
    • 0024289542 scopus 로고
    • The use of poly(L-proline)-Sepharose in the isolation of profilin and profilactin complexes
    • Lindberg U., Schutt C.E., Hellsten E., Tjader A.C., and Hult T. The use of poly(L-proline)-Sepharose in the isolation of profilin and profilactin complexes. Biochem. Biophys. Acta 967 (1988) 391-400
    • (1988) Biochem. Biophys. Acta , vol.967 , pp. 391-400
    • Lindberg, U.1    Schutt, C.E.2    Hellsten, E.3    Tjader, A.C.4    Hult, T.5
  • 44
    • 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
    • Mattila P.K., Quintero-Monzon O., Kugler J., Moseley J.B., Almo S.C., Lappalainen P., and Goode B.L. A high-affinity interaction with ADP-actin monomers underlies the mechanism and in vivo function of Srv2/cyclase-associated protein. Mol. Biol. Cell 15 (2004) 5158-5171
    • (2004) Mol. Biol. Cell , vol.15 , 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
  • 45
    • 0026076490 scopus 로고
    • DnaK as a thermometer: Threonine-199 is site of autophosphorylation and is critical for ATPase activity
    • McCarty J.S., and Walker G.C. DnaK as a thermometer: Threonine-199 is site of autophosphorylation and is critical for ATPase activity. Proc. Natl. Acad. Sci. USA 88 (1991) 9513-9517
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9513-9517
    • McCarty, J.S.1    Walker, G.C.2
  • 46
    • 0027954650 scopus 로고
    • DnaK mutants defective in ATPase activity are defective in negative regulation of the heat shock response: Expression of mutant DnaK proteins results in filamentation
    • McCarty J.S., and Walker G.C. DnaK mutants defective in ATPase activity are defective in negative regulation of the heat shock response: Expression of mutant DnaK proteins results in filamentation. J. Bacteriol. 176 (1994) 764-780
    • (1994) J. Bacteriol. , vol.176 , pp. 764-780
    • McCarty, J.S.1    Walker, G.C.2
  • 47
    • 0029661920 scopus 로고    scopus 로고
    • Continuous monitoring of Pi release following nucleotide hydrolysis in actin or tubulin assembly using 2-amino-6-mercapto-7-methylpurine ribonucleoside and purine-nucleoside phosphorylase as an enzyme-linked assay
    • Melki R., Fievez S., and Carlier M.F. Continuous monitoring of Pi release following nucleotide hydrolysis in actin or tubulin assembly using 2-amino-6-mercapto-7-methylpurine ribonucleoside and purine-nucleoside phosphorylase as an enzyme-linked assay. Biochemistry 35 (1996) 12038-12045
    • (1996) Biochemistry , vol.35 , pp. 12038-12045
    • Melki, R.1    Fievez, S.2    Carlier, M.F.3
  • 48
    • 0023266420 scopus 로고
    • Changes in OD at 235 nm do not correspond to the polymerization step of actin
    • Merkler I., Stournaras C., and Faulstich H. Changes in OD at 235 nm do not correspond to the polymerization step of actin. Biochem. Biophys. Res. Commun. 145 (1987) 46-51
    • (1987) Biochem. Biophys. Res. Commun. , vol.145 , pp. 46-51
    • Merkler, I.1    Stournaras, C.2    Faulstich, H.3
  • 49
    • 0033046726 scopus 로고    scopus 로고
    • Divalent cation-, nucleotide-, and polymerization-dependent changes in the conformation of subdomain 2 of actin
    • Moraczewska J., Wawro B., Seguro K., and Strzelecka-Golaszewska H. Divalent cation-, nucleotide-, and polymerization-dependent changes in the conformation of subdomain 2 of actin. Biophys. J. 77 (1999) 373-385
    • (1999) Biophys. J. , vol.77 , pp. 373-385
    • Moraczewska, J.1    Wawro, B.2    Seguro, K.3    Strzelecka-Golaszewska, H.4
  • 50
    • 0021986804 scopus 로고
    • Actin oligomers below the critical concentration detected by fluorescence photobleaching recovery
    • Mozo-Villarias A., and Ware B.R. Actin oligomers below the critical concentration detected by fluorescence photobleaching recovery. Biochemistry 24 (1985) 1544-1548
    • (1985) Biochemistry , vol.24 , pp. 1544-1548
    • Mozo-Villarias, A.1    Ware, B.R.2
  • 52
    • 0021985484 scopus 로고
    • The presence of oligomers at subcritical actin concentrations
    • Newman J., Estes J.E., Selden L.A., and Gershman L.C. The presence of oligomers at subcritical actin concentrations. Biochemistry 24 (1985) 1538-1544
    • (1985) Biochemistry , vol.24 , pp. 1538-1544
    • Newman, J.1    Estes, J.E.2    Selden, L.A.3    Gershman, L.C.4
  • 54
    • 0027484169 scopus 로고
    • Threonine 204 of the chaperone protein Hsc70 influences the structure of the active site, but is not essential for ATP hydrolysis
    • O'Brien M.C., and McKay D.B. Threonine 204 of the chaperone protein Hsc70 influences the structure of the active site, but is not essential for ATP hydrolysis. J. Biol. Chem. 268 (1993) 24323-24329
    • (1993) J. Biol. Chem. , vol.268 , pp. 24323-24329
    • O'Brien, M.C.1    McKay, D.B.2
  • 55
    • 0030018744 scopus 로고    scopus 로고
    • Lysine 71 of the chaperone protein Hsc70 is essential for ATP hydrolysis
    • O'Brien M.C., Flaherty K.M., and McKay D.B. Lysine 71 of the chaperone protein Hsc70 is essential for ATP hydrolysis. J. Biol. Chem. 271 (1996) 15874-15878
    • (1996) J. Biol. Chem. , vol.271 , pp. 15874-15878
    • O'Brien, M.C.1    Flaherty, K.M.2    McKay, D.B.3
  • 56
    • 0028033464 scopus 로고
    • Mechanism of ATP hydrolysis by polymeric actin
    • Ohm T., and Wegner A. Mechanism of ATP hydrolysis by polymeric actin. Biochim. Biophys. Acta 1208 (1994) 8-14
    • (1994) Biochim. Biophys. Acta , vol.1208 , pp. 8-14
    • Ohm, T.1    Wegner, A.2
  • 57
    • 0035958757 scopus 로고    scopus 로고
    • The crystal structure of uncomplexed actin in the ADP state
    • Otterbein L.R., Graceffa P., and Dominguez R. The crystal structure of uncomplexed actin in the ADP state. Science 293 (2001) 708-711
    • (2001) Science , vol.293 , pp. 708-711
    • Otterbein, L.R.1    Graceffa, P.2    Dominguez, R.3
  • 59
    • 0035886026 scopus 로고    scopus 로고
    • Interactions with PIP2, ADP-actin monomers, and capping protein regulate the activity and localization of yeast twinfilin
    • Palmgren S., Ojala P.J., Wear M.A., Cooper J.A., and Lappalainen P. Interactions with PIP2, ADP-actin monomers, and capping protein regulate the activity and localization of yeast twinfilin. J. Cell Biol. 155 (2001) 251-260
    • (2001) J. Cell Biol. , vol.155 , pp. 251-260
    • Palmgren, S.1    Ojala, P.J.2    Wear, M.A.3    Cooper, J.A.4    Lappalainen, P.5
  • 61
    • 0029885751 scopus 로고    scopus 로고
    • The end of a polymerizing actin filament contains numerous ATP-subunit segments that are disconnected by ADP-subunits resulting from ATP hydrolysis
    • Pieper U., and Wegner A. The end of a polymerizing actin filament contains numerous ATP-subunit segments that are disconnected by ADP-subunits resulting from ATP hydrolysis. Biochemistry 35 (1996) 4396-4402
    • (1996) Biochemistry , vol.35 , pp. 4396-4402
    • Pieper, U.1    Wegner, A.2
  • 62
    • 0029083041 scopus 로고
    • The effect on actin ATPase of phalloidin and tetramethylrhodamine phalloidin
    • Pinaev G., Schutt C.E., and Lindberg U. The effect on actin ATPase of phalloidin and tetramethylrhodamine phalloidin. FEBS Lett. 369 (1995) 144-148
    • (1995) FEBS Lett. , vol.369 , pp. 144-148
    • Pinaev, G.1    Schutt, C.E.2    Lindberg, U.3
  • 63
    • 0021200245 scopus 로고
    • Polymerization of ADP-actin
    • Pollard T.D. Polymerization of ADP-actin. J. Cell Biol. 99 (1984) 769-777
    • (1984) J. Cell Biol. , vol.99 , pp. 769-777
    • Pollard, T.D.1
  • 64
    • 0022881322 scopus 로고
    • Rate constants for the reactions of ATP- and ADP-actin with the ends of actin filaments
    • Pollard T.D. Rate constants for the reactions of ATP- and ADP-actin with the ends of actin filaments. J. Cell Biol. 103 (1986) 2747-2754
    • (1986) J. Cell Biol. , vol.103 , pp. 2747-2754
    • Pollard, T.D.1
  • 65
    • 0021259215 scopus 로고
    • The rate constant for ATP hydrolysis by polymerized actin
    • Pollard T.D., and Weeds A.G. The rate constant for ATP hydrolysis by polymerized actin. FEBS Lett. 170 (1984) 94-98
    • (1984) FEBS Lett. , vol.170 , pp. 94-98
    • Pollard, T.D.1    Weeds, A.G.2
  • 66
    • 0024307635 scopus 로고
    • The complex of actin and deoxyribonuclease I as a model system to study the interactions of nucleotides, cations and cytochalasin D with monomeric actin
    • Polzar B., Nowak E., Goody R.S., and Mannherz H.G. The complex of actin and deoxyribonuclease I as a model system to study the interactions of nucleotides, cations and cytochalasin D with monomeric actin. Eur. J. Biochem. 182 (1989) 267-275
    • (1989) Eur. J. Biochem. , vol.182 , pp. 267-275
    • Polzar, B.1    Nowak, E.2    Goody, R.S.3    Mannherz, H.G.4
  • 67
    • 0032546548 scopus 로고    scopus 로고
    • Characterization of D10S and K71E mutants of human cytosolic hsp70
    • Rajapandi T., Wu C., Eisenberg E., and Greene L. Characterization of D10S and K71E mutants of human cytosolic hsp70. Biochemistry 37 (1998) 7244-7250
    • (1998) Biochemistry , vol.37 , pp. 7244-7250
    • Rajapandi, T.1    Wu, C.2    Eisenberg, E.3    Greene, L.4
  • 68
    • 0017160659 scopus 로고
    • Detection of conformational changes in actin by proteolytic digestion: Evidence for a new monomeric species
    • Rich S.A., and Estes J.E. Detection of conformational changes in actin by proteolytic digestion: Evidence for a new monomeric species. J. Mol. Biol. 104 (1976) 777-792
    • (1976) J. Mol. Biol. , vol.104 , pp. 777-792
    • Rich, S.A.1    Estes, J.E.2
  • 69
    • 0022922682 scopus 로고
    • Cytoplasmic concentrations of inorganic phosphate affect the critical concentration for assembly of actin in the presence of cytochalasin D or ADP
    • Rickard J.E., and Sheterline P. Cytoplasmic concentrations of inorganic phosphate affect the critical concentration for assembly of actin in the presence of cytochalasin D or ADP. J. Mol. Biol. 191 (1986) 273-280
    • (1986) J. Mol. Biol. , vol.191 , pp. 273-280
    • Rickard, J.E.1    Sheterline, P.2
  • 70
    • 0023903044 scopus 로고
    • Effect of ATP removal and inorganic phosphate on length redistribution of sheared actin filament populations. Evidence for a mechanism of end-to-end annealing
    • Rickard J.E., and Sheterline P. Effect of ATP removal and inorganic phosphate on length redistribution of sheared actin filament populations. Evidence for a mechanism of end-to-end annealing. J. Mol. Biol. 201 (1988) 675-681
    • (1988) J. Mol. Biol. , vol.201 , pp. 675-681
    • Rickard, J.E.1    Sheterline, P.2
  • 71
    • 7044224754 scopus 로고    scopus 로고
    • Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis
    • Romero S., LeClainche C., Didry D., Egile C., Pantaloni D., and Carlier M.F. Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis. Cell 119 (2004) 419-429
    • (2004) Cell , vol.119 , pp. 419-429
    • Romero, S.1    LeClainche, C.2    Didry, D.3    Egile, C.4    Pantaloni, D.5    Carlier, M.F.6
  • 72
    • 0019358370 scopus 로고
    • The first step in the polymerisation of actin
    • Rouayrenc J.F., and Travers F. The first step in the polymerisation of actin. Eur. J. Biochem. 116 (1981) 73-77
    • (1981) Eur. J. Biochem. , vol.116 , pp. 73-77
    • Rouayrenc, J.F.1    Travers, F.2
  • 74
    • 0024351527 scopus 로고
    • Molecular packing in profilin: Actin crystals and its implications
    • Schutt C.E., Lindberg U., Myslik J., and Strauss N. Molecular packing in profilin: Actin crystals and its implications. J. Mol. Biol. 209 (1989) 735-746
    • (1989) J. Mol. Biol. , vol.209 , pp. 735-746
    • Schutt, C.E.1    Lindberg, U.2    Myslik, J.3    Strauss, N.4
  • 76
  • 77
    • 0035909233 scopus 로고    scopus 로고
    • ATPase activity and conformational changes in the regulation of actin
    • Schüler H. ATPase activity and conformational changes in the regulation of actin. Biochim. Biophys. Acta 1549 (2001) 137-147
    • (2001) Biochim. Biophys. Acta , vol.1549 , pp. 137-147
    • Schüler, H.1
  • 78
    • 0342504193 scopus 로고    scopus 로고
    • Mutational analysis of Ser14 and Asp157 in the nucleotide-binding site of beta-actin
    • Schüler H., Korenbaum E., Schutt C.E., Lindberg U., and Karlsson R. Mutational analysis of Ser14 and Asp157 in the nucleotide-binding site of beta-actin. Eur. J. Biochem. 265 (1999) 210-220
    • (1999) Eur. J. Biochem. , vol.265 , pp. 210-220
    • Schüler, H.1    Korenbaum, E.2    Schutt, C.E.3    Lindberg, U.4    Karlsson, R.5
  • 79
    • 0000186456 scopus 로고    scopus 로고
    • Thermal unfolding of G-actin monitored with the DNase I-inhibition assay stabilities of actin isoforms
    • Schüler H., Lindberg U., Schutt C.E., and Karlsson R. Thermal unfolding of G-actin monitored with the DNase I-inhibition assay stabilities of actin isoforms. Eur. J. Biochem. 267 (2000) 476-486
    • (2000) Eur. J. Biochem. , vol.267 , pp. 476-486
    • Schüler, H.1    Lindberg, U.2    Schutt, C.E.3    Karlsson, R.4
  • 80
    • 0002588647 scopus 로고    scopus 로고
    • Mutational analysis of arginine 177 in the nucleotide binding site of beta-actin
    • Schüler H., Nyåkern M., Schutt C.E., Lindberg U., and Karlsson R. Mutational analysis of arginine 177 in the nucleotide binding site of beta-actin. Eur. J. Biochem. 267 (2000) 4054-4062
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4054-4062
    • Schüler, H.1    Nyåkern, M.2    Schutt, C.E.3    Lindberg, U.4    Karlsson, R.5
  • 81
    • 0034616882 scopus 로고    scopus 로고
    • Covalent binding of ATPgammaS to the nucleotide-binding site in S14C-actin
    • Schüler H., Schutt C.E., Lindberg U., and Karlsson R. Covalent binding of ATPgammaS to the nucleotide-binding site in S14C-actin. FEBS Lett. 476 (2000) 155-159
    • (2000) FEBS Lett. , vol.476 , pp. 155-159
    • Schüler, H.1    Schutt, C.E.2    Lindberg, U.3    Karlsson, R.4
  • 83
    • 0030804033 scopus 로고    scopus 로고
    • A correlative analysis of actin filament assembly, structure, and dynamics
    • Steinmetz M.O., Goldie K.N., and Aebi U. A correlative analysis of actin filament assembly, structure, and dynamics. J. Cell Biol. 138 (1997) 559-574
    • (1997) J. Cell Biol. , vol.138 , pp. 559-574
    • Steinmetz, M.O.1    Goldie, K.N.2    Aebi, U.3
  • 85
    • 0027523454 scopus 로고
    • Localization of the tightly bound divalent-cation-dependent and nucleotide-dependent conformation changes in G-actin using limited proteolytic digestion
    • Strzelecka-Golaszewska H., Moraczewska J., Khaitlina S.Y., and Mossakowska M. Localization of the tightly bound divalent-cation-dependent and nucleotide-dependent conformation changes in G-actin using limited proteolytic digestion. Eur. J. Biochem. 211 (1993) 731-742
    • (1993) Eur. J. Biochem. , vol.211 , pp. 731-742
    • Strzelecka-Golaszewska, H.1    Moraczewska, J.2    Khaitlina, S.Y.3    Mossakowska, M.4
  • 86
    • 0029847601 scopus 로고    scopus 로고
    • 2+, bound at the high-affinity site and of the ionic composition of the solution on the structure of F-actin
    • 2+, bound at the high-affinity site and of the ionic composition of the solution on the structure of F-actin. Biochem. J. 316 (1996) 713-721
    • (1996) Biochem. J. , vol.316 , pp. 713-721
    • Strzelecka-Golaszewska, H.1    Wozniak, A.2    Hult, T.3    Lindberg, U.4
  • 87
    • 0022980864 scopus 로고
    • Gelsolin inhibits nucleotide exchange from actin
    • Tellam R.L. Gelsolin inhibits nucleotide exchange from actin. Biochemistry 25 (1986) 5799-5804
    • (1986) Biochemistry , vol.25 , pp. 5799-5804
    • Tellam, R.L.1
  • 88
    • 0019948311 scopus 로고
    • The regulation of actin polymerization and the inhibition of monomeric actin ATPase activity by Acanthamoeba profilin
    • Tobacman L.S., and Korn E.D. The regulation of actin polymerization and the inhibition of monomeric actin ATPase activity by Acanthamoeba profilin. J. Biol. Chem. 257 (1982) 4166-4170
    • (1982) J. Biol. Chem. , vol.257 , pp. 4166-4170
    • Tobacman, L.S.1    Korn, E.D.2
  • 89
    • 0032483044 scopus 로고    scopus 로고
    • Interactions of Acanthamoeba profilin with actin and nucleotides bound to actin
    • Vinson V.K., De La Cruz E.M., Higgs H.N., and Pollard T.D. Interactions of Acanthamoeba profilin with actin and nucleotides bound to actin. Biochemistry 37 (1998) 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
  • 91
    • 0017176529 scopus 로고
    • Head to tail polymerization of actin
    • Wegner A. Head to tail polymerization of actin. J. Mol. Biol. 108 (1976) 139-150
    • (1976) J. Mol. Biol. , vol.108 , pp. 139-150
    • Wegner, A.1
  • 92
    • 0026737363 scopus 로고
    • Systematic mutational analysis of the yeast ACT1 gene
    • Wertman K.F., Drubin D.G., and Botstein D. Systematic mutational analysis of the yeast ACT1 gene. Genetics 132 (1992) 337-350
    • (1992) Genetics , vol.132 , pp. 337-350
    • Wertman, K.F.1    Drubin, D.G.2    Botstein, D.3
  • 93
    • 0028938819 scopus 로고
    • How potassium affects the activity of the molecular chaperone Hsc70. II. Potassium binds specifically in the ATPase active site
    • Wilbanks S.M., and McKay D.B. How potassium affects the activity of the molecular chaperone Hsc70. II. Potassium binds specifically in the ATPase active site. J. Biol. Chem. 270 (1995) 2251-2257
    • (1995) J. Biol. Chem. , vol.270 , pp. 2251-2257
    • Wilbanks, S.M.1    McKay, D.B.2
  • 94
    • 0028287525 scopus 로고
    • Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. I. Kinetic analyses of active site mutants
    • Wilbanks S.M., DeLuca-Flaherty C., and McKay D.B. Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. I. Kinetic analyses of active site mutants. J. Biol. Chem. 269 (1994) 12893-12898
    • (1994) J. Biol. Chem. , vol.269 , pp. 12893-12898
    • Wilbanks, S.M.1    DeLuca-Flaherty, C.2    McKay, D.B.3
  • 95
    • 0030787462 scopus 로고    scopus 로고
    • Stability and dynamics of G-actin: Back-door water diffusion and behavior of a subdomain 3/4 loop
    • Wriggers W., and Schulten K. Stability and dynamics of G-actin: Back-door water diffusion and behavior of a subdomain 3/4 loop. Biophys. J. 73 (1997) 624-639
    • (1997) Biophys. J. , vol.73 , pp. 624-639
    • Wriggers, W.1    Schulten, K.2
  • 96
    • 0033601126 scopus 로고    scopus 로고
    • His(73), often methylated, is an important structural determinant for actin
    • Yao X., Grade S., Wriggers W., and Rubenstein P.A. His(73), often methylated, is an important structural determinant for actin. J. Biol. Chem. 274 (1999) 37443-37449
    • (1999) J. Biol. Chem. , vol.274 , pp. 37443-37449
    • Yao, X.1    Grade, S.2    Wriggers, W.3    Rubenstein, P.A.4


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