메뉴 건너뛰기




Volumn 370, Issue 2, 2007, Pages 331-348

Molecular and Structural Basis for Redox Regulation of β-Actin

Author keywords

ADP actin; antiparallel dimer; cysteine sulfinic acid; H2O2; thioredoxin

Indexed keywords

5,5' DITHIOBIS(2 NITROBENZOIC ACID); ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ALPHA ACTIN; BETA ACTIN; CALCIUM ION; CYSTEINE; CYSTEINE SULFINIC ACID; DEOXYRIBONUCLEASE I; DIAMIDE; HYDROGEN PEROXIDE; PROFILIN; THIOL GROUP; THIOREDOXIN;

EID: 34249723277     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.04.056     Document Type: Article
Times cited : (128)

References (104)
  • 1
    • 0028973482 scopus 로고
    • Requirement for generation of H2O2 for platelet-derived growth factor signal transduction
    • Sundaresan M., Yu Z.X., Ferrans V.J., Irani K., and Finkel T. Requirement for generation of H2O2 for platelet-derived growth factor signal transduction. Science 270 (1995) 296-299
    • (1995) Science , vol.270 , pp. 296-299
    • Sundaresan, M.1    Yu, Z.X.2    Ferrans, V.J.3    Irani, K.4    Finkel, T.5
  • 2
    • 33745223933 scopus 로고    scopus 로고
    • Reactive oxygen species in vascular endothelial cell motility. Roles of NAD(P)H oxidase and Rac1
    • Moldovan L., Mythreye K., Goldschmidt-Clermont P.J., and Satterwhite L.L. Reactive oxygen species in vascular endothelial cell motility. Roles of NAD(P)H oxidase and Rac1. Cardiovasc. Res. 71 (2006) 236-246
    • (2006) Cardiovasc. Res. , vol.71 , pp. 236-246
    • Moldovan, L.1    Mythreye, K.2    Goldschmidt-Clermont, P.J.3    Satterwhite, L.L.4
  • 3
    • 33847063469 scopus 로고    scopus 로고
    • Redox signalling in anchorage-dependent cell growth
    • Chiarugi P., and Fiaschi T. Redox signalling in anchorage-dependent cell growth. Cell Signal 19 (2007) 672-682
    • (2007) Cell Signal , vol.19 , pp. 672-682
    • Chiarugi, P.1    Fiaschi, T.2
  • 4
    • 33744948517 scopus 로고    scopus 로고
    • Critical role of phospholipase Cgamma1 in the generation of H2O2-evoked [Ca2+]i oscillations in cultured rat cortical astrocytes
    • Hong J.H., Moon S.J., Byun H.M., Kim M.S., Jo H., Bae Y.S., et al. Critical role of phospholipase Cgamma1 in the generation of H2O2-evoked [Ca2+]i oscillations in cultured rat cortical astrocytes. J. Biol. Chem. 281 (2006) 13057-13067
    • (2006) J. Biol. Chem. , vol.281 , pp. 13057-13067
    • Hong, J.H.1    Moon, S.J.2    Byun, H.M.3    Kim, M.S.4    Jo, H.5    Bae, Y.S.6
  • 5
    • 0037039770 scopus 로고    scopus 로고
    • Single-molecule speckle analysis of actin filament turnover in lamellipodia
    • Watanabe N., and Mitchison T.J. Single-molecule speckle analysis of actin filament turnover in lamellipodia. Science 295 (2002) 1083-1086
    • (2002) Science , vol.295 , pp. 1083-1086
    • Watanabe, N.1    Mitchison, T.J.2
  • 7
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard T.D., and Borisy G.G. Cellular motility driven by assembly and disassembly of actin filaments. Cell 112 (2003) 453-465
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 9
    • 18344390036 scopus 로고    scopus 로고
    • Identification by redox proteomics of glutathionylated proteins in oxidatively stressed human T lymphocytes
    • Fratelli M., Demol H., Puype M., Casagrande S., Eberini I., Salmona M., et al. Identification by redox proteomics of glutathionylated proteins in oxidatively stressed human T lymphocytes. Proc. Natl Acad. Sci. USA 99 (2002) 3505-3510
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 3505-3510
    • Fratelli, M.1    Demol, H.2    Puype, M.3    Casagrande, S.4    Eberini, I.5    Salmona, M.6
  • 10
    • 0036401454 scopus 로고    scopus 로고
    • Identification of S-glutathionylated cellular proteins during oxidative stress and constitutive metabolism by affinity purification and proteomic analysis
    • Lind C., Gerdes R., Hamnell Y., Schuppe-Koistinen I., von Lowenhielm H.B., Holmgren A., and Cotgreave I.A. Identification of S-glutathionylated cellular proteins during oxidative stress and constitutive metabolism by affinity purification and proteomic analysis. Arch. Biochem. Biophys. 406 (2002) 229-240
    • (2002) Arch. Biochem. Biophys. , vol.406 , pp. 229-240
    • Lind, C.1    Gerdes, R.2    Hamnell, Y.3    Schuppe-Koistinen, I.4    von Lowenhielm, H.B.5    Holmgren, A.6    Cotgreave, I.A.7
  • 11
    • 0142211205 scopus 로고    scopus 로고
    • Actin glutathionylation increases in fibroblasts of patients with Friedreich's ataxia: a potential role in the pathogenesis of the disease
    • Pastore A., Tozzi G., Gaeta L.M., Bertini E., Serafini V., Di Cesare S., et al. Actin glutathionylation increases in fibroblasts of patients with Friedreich's ataxia: a potential role in the pathogenesis of the disease. J. Biol. Chem. 278 (2003) 42588-42595
    • (2003) J. Biol. Chem. , vol.278 , pp. 42588-42595
    • Pastore, A.1    Tozzi, G.2    Gaeta, L.M.3    Bertini, E.4    Serafini, V.5    Di Cesare, S.6
  • 13
    • 0035893961 scopus 로고    scopus 로고
    • The actin cytoskeleton response to oxidants: from small heat shock protein phosphorylation to changes in the redox state of actin itself
    • Dalle-Donne I., Rossi R., Milzani A., Di Simplicio P., and Colombo R. The actin cytoskeleton response to oxidants: from small heat shock protein phosphorylation to changes in the redox state of actin itself. Free Radic. Biol. Med. 31 (2001) 1624-3162
    • (2001) Free Radic. Biol. Med. , vol.31 , pp. 1624-3162
    • Dalle-Donne, I.1    Rossi, R.2    Milzani, A.3    Di Simplicio, P.4    Colombo, R.5
  • 14
    • 0025947354 scopus 로고
    • A reversible conformational transition in muscle actin is caused by nucleotide exchange and uncovers cysteine in position 10
    • Drewes G., and Faulstich H. A reversible conformational transition in muscle actin is caused by nucleotide exchange and uncovers cysteine in position 10. J. Biol. Chem. 266 (1991) 5508-5513
    • (1991) J. Biol. Chem. , vol.266 , pp. 5508-5513
    • Drewes, G.1    Faulstich, H.2
  • 15
    • 0018038933 scopus 로고
    • Selective assay of monomeric and filamentous actin in cell extracts, using inhibition of deoxyribonuclease I
    • Blikstad I., Markey F., Carlsson L., Persson T., and Lindberg U. Selective assay of monomeric and filamentous actin in cell extracts, using inhibition of deoxyribonuclease I. Cell 15 (1978) 935-943
    • (1978) Cell , vol.15 , pp. 935-943
    • Blikstad, I.1    Markey, F.2    Carlsson, L.3    Persson, T.4    Lindberg, U.5
  • 16
    • 0020081847 scopus 로고
    • On the dynamics of the microfilament system in HeLa cells
    • Blikstad I., and Carlsson L. On the dynamics of the microfilament system in HeLa cells. J. Cell Biol. 93 (1982) 122-128
    • (1982) J. Cell Biol. , vol.93 , pp. 122-128
    • Blikstad, I.1    Carlsson, L.2
  • 18
    • 0030575783 scopus 로고    scopus 로고
    • The structure of an open state of beta-actin at 2.65 Å resolution
    • Chik J.K., Lindberg U., and Schutt C.E. The structure of an open state of beta-actin at 2.65 Å 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
  • 20
    • 0032788590 scopus 로고    scopus 로고
    • Amino acid neighbours and detailed conformational analysis of cysteines in proteins
    • Petersen M.T., Jonson P.H., and Petersen S.B. Amino acid neighbours and detailed conformational analysis of cysteines in proteins. Protein Eng. 12 (1999) 535-548
    • (1999) Protein Eng. , vol.12 , pp. 535-548
    • Petersen, M.T.1    Jonson, P.H.2    Petersen, S.B.3
  • 21
    • 0015207874 scopus 로고
    • The conformational energy map for the disulphide bridge in proteins
    • Perahia D., and Pullman B. The conformational energy map for the disulphide bridge in proteins. Biochem. Biophys. Res. Commun. 43 (1971) 65-68
    • (1971) Biochem. Biophys. Res. Commun. , vol.43 , pp. 65-68
    • Perahia, D.1    Pullman, B.2
  • 22
    • 33745161382 scopus 로고    scopus 로고
    • Allosteric disulfide bonds
    • Schmidt B., Ho L., and Hogg P.J. Allosteric disulfide bonds. Biochemistry 45 (2006) 7429-7433
    • (2006) Biochemistry , vol.45 , pp. 7429-7433
    • Schmidt, B.1    Ho, L.2    Hogg, P.J.3
  • 23
    • 3242712276 scopus 로고    scopus 로고
    • Redox signaling: thiol chemistry defines which reactive oxygen and nitrogen species can act as second messengers
    • Forman H.J., Fukuto J.M., and Torres M. Redox signaling: thiol chemistry defines which reactive oxygen and nitrogen species can act as second messengers. Am. J. Physiol. Cell Physiol. 287 (2004) C246-C256
    • (2004) Am. J. Physiol. Cell Physiol. , vol.287
    • Forman, H.J.1    Fukuto, J.M.2    Torres, M.3
  • 24
    • 9344259718 scopus 로고    scopus 로고
    • Reversible oxidation and inactivation of the tumor suppressor PTEN in cells stimulated with peptide growth factors
    • Kwon J., Lee S.R., Yang K.S., Ahn Y., Kim Y.J., Stadtman E.R., and Rhee S.G. Reversible oxidation and inactivation of the tumor suppressor PTEN in cells stimulated with peptide growth factors. Proc. Natl Acad. Sci. USA 101 (2004) 16419-16424
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 16419-16424
    • Kwon, J.1    Lee, S.R.2    Yang, K.S.3    Ahn, Y.4    Kim, Y.J.5    Stadtman, E.R.6    Rhee, S.G.7
  • 25
    • 0027248807 scopus 로고
    • Mutations in beta-actin: influence on polymer formation and on interactions with myosin and profilin
    • Aspenstrom 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 Letters 329 (1993) 163-170
    • (1993) FEBS Letters , vol.329 , pp. 163-170
    • Aspenstrom, P.1    Schutt, C.E.2    Lindberg, U.3    Karlsson, R.4
  • 26
    • 0031442195 scopus 로고    scopus 로고
    • General acid/base catalysis in the active site of Escherichia coli thioredoxin
    • Chivers P.T., and Raines R.T. General acid/base catalysis in the active site of Escherichia coli thioredoxin. Biochemistry 36 (1997) 15810-15816
    • (1997) Biochemistry , vol.36 , pp. 15810-15816
    • Chivers, P.T.1    Raines, R.T.2
  • 27
    • 0030729017 scopus 로고    scopus 로고
    • The role of the buried aspartate of Escherichia coli thioredoxin in the activation of the mixed disulfide intermediate
    • LeMaster D.M., Springer P.A., and Unkefer C.J. The role of the buried aspartate of Escherichia coli thioredoxin in the activation of the mixed disulfide intermediate. J. Biol. Chem. 272 (1997) 29998-30001
    • (1997) J. Biol. Chem. , vol.272 , pp. 29998-30001
    • LeMaster, D.M.1    Springer, P.A.2    Unkefer, C.J.3
  • 29
    • 33747691035 scopus 로고    scopus 로고
    • Analysis of tetramethylrhodamine-labeled actin polymerization and interaction with actin regulatory proteins
    • Pelikan Conchaudron A., Didry D., Le K.H., Larquet E., Boisset N., Pantaloni D., and Carlier M.F. Analysis of tetramethylrhodamine-labeled actin polymerization and interaction with actin regulatory proteins. J. Biol. Chem. 281 (2006) 24036-24047
    • (2006) J. Biol. Chem. , vol.281 , pp. 24036-24047
    • Pelikan Conchaudron, A.1    Didry, D.2    Le, K.H.3    Larquet, E.4    Boisset, N.5    Pantaloni, D.6    Carlier, M.F.7
  • 30
    • 0027452835 scopus 로고
    • Proteolytic removal of three C-terminal residues of actin alters the monomer-monomer interactions
    • Mossakowska M., Moraczewska J., Khaitlina S., and Strzelecka-Golaszewska H. Proteolytic removal of three C-terminal residues of actin alters the monomer-monomer interactions. Biochem. J. 289 (1993) 897-902
    • (1993) Biochem. J. , vol.289 , pp. 897-902
    • Mossakowska, M.1    Moraczewska, J.2    Khaitlina, S.3    Strzelecka-Golaszewska, H.4
  • 31
    • 0027967683 scopus 로고
    • Structural connectivity in actin: effect of C-terminal modifications on the properties of actin
    • Crosbie R.H., Miller C., Cheung P., Goodnight T., Muhlrad A., and Reisler E. Structural connectivity in actin: effect of C-terminal modifications on the properties of actin. Biophys. J. 67 (1994) 1957-1964
    • (1994) Biophys. J. , vol.67 , pp. 1957-1964
    • Crosbie, R.H.1    Miller, C.2    Cheung, P.3    Goodnight, T.4    Muhlrad, A.5    Reisler, E.6
  • 33
    • 17444377916 scopus 로고    scopus 로고
    • The strength of receptor signaling is centrally controlled through a cooperative loop between Ca2+ and an oxidant signal
    • Singh D.K., Kumar D., Siddiqui Z., Basu S.K., Kumar V., and Rao K.V. The strength of receptor signaling is centrally controlled through a cooperative loop between Ca2+ and an oxidant signal. Cell 121 (2005) 281-293
    • (2005) Cell , vol.121 , pp. 281-293
    • Singh, D.K.1    Kumar, D.2    Siddiqui, Z.3    Basu, S.K.4    Kumar, V.5    Rao, K.V.6
  • 34
    • 0037082127 scopus 로고    scopus 로고
    • Oxidation of proteinaceous cysteine residues by dopamine-derived H2O2 in PC12 cells
    • Kim J.R., Kwon K.S., Yoon H.W., Lee S.R., and Rhee S.G. Oxidation of proteinaceous cysteine residues by dopamine-derived H2O2 in PC12 cells. Arch. Biochem. Biophys. 397 (2002) 414-423
    • (2002) Arch. Biochem. Biophys. , vol.397 , pp. 414-423
    • Kim, J.R.1    Kwon, K.S.2    Yoon, H.W.3    Lee, S.R.4    Rhee, S.G.5
  • 35
    • 0026558989 scopus 로고
    • Removing the two C-terminal residues of actin affects the filament structure
    • O'Donoghue S.I., Miki M., and dos Remedios C.G. Removing the two C-terminal residues of actin affects the filament structure. Arch. Biochem. Biophys. 293 (1992) 110-116
    • (1992) Arch. Biochem. Biophys. , vol.293 , pp. 110-116
    • O'Donoghue, S.I.1    Miki, M.2    dos Remedios, C.G.3
  • 38
    • 0028950817 scopus 로고
    • Characterizing the microenvironment surrounding protein sites
    • Bagley S.C., and Altman R.B. Characterizing the microenvironment surrounding protein sites. Protein Sci. 4 (1995) 622-635
    • (1995) Protein Sci. , vol.4 , pp. 622-635
    • Bagley, S.C.1    Altman, R.B.2
  • 39
    • 0028861589 scopus 로고
    • Normal modes as refinement parameters for the F-actin model
    • Tirion M.M., ben-Avraham D., Lorenz M., and Holmes K.C. Normal modes as refinement parameters for the F-actin model. Biophys. J. 68 (1995) 5-12
    • (1995) Biophys. J. , vol.68 , pp. 5-12
    • Tirion, M.M.1    ben-Avraham, D.2    Lorenz, M.3    Holmes, K.C.4
  • 40
    • 33846020951 scopus 로고    scopus 로고
    • Crystal structures of expressed non-polymerizable monomeric actin in the ADP and ATP states
    • Rould M.A., Wan Q., Joel P.B., Lowey S., and Trybus K.M. Crystal structures of expressed non-polymerizable monomeric actin in the ADP and ATP states. J. Biol. Chem. 281 (2006) 31909-31919
    • (2006) J. Biol. Chem. , vol.281 , pp. 31909-31919
    • Rould, M.A.1    Wan, Q.2    Joel, P.B.3    Lowey, S.4    Trybus, K.M.5
  • 42
    • 33747364924 scopus 로고    scopus 로고
    • Crystal structure of polymerization-competent actin
    • Klenchin V.A., Khaitlina S.Y., and Rayment I. Crystal structure of polymerization-competent actin. J. Mol. Biol. 362 (2006) 140-150
    • (2006) J. Mol. Biol. , vol.362 , pp. 140-150
    • Klenchin, V.A.1    Khaitlina, S.Y.2    Rayment, I.3
  • 43
    • 14644442348 scopus 로고    scopus 로고
    • Disulfide bonds, their stereospecific environment and conservation in protein structures
    • Bhattacharyya R., Pal D., and Chakrabarti P. Disulfide bonds, their stereospecific environment and conservation in protein structures. Protein Eng. Des. Sel. 17 (2004) 795-808
    • (2004) Protein Eng. Des. Sel. , vol.17 , pp. 795-808
    • Bhattacharyya, R.1    Pal, D.2    Chakrabarti, P.3
  • 44
    • 0027134875 scopus 로고
    • The actin monomers in the ternary gelsolin: 2 actin complex are in an antiparallel orientation
    • Hesterkamp T., Weeds A.G., and Mannherz H.G. The actin monomers in the ternary gelsolin: 2 actin complex are in an antiparallel orientation. Eur. J. Biochem. 218 (1993) 507-513
    • (1993) Eur. J. Biochem. , vol.218 , pp. 507-513
    • Hesterkamp, T.1    Weeds, A.G.2    Mannherz, H.G.3
  • 45
    • 0023840623 scopus 로고
    • Probing actin polymerization by intermolecular cross-linking
    • Millonig R., Salvo H., and Aebi U. Probing actin polymerization by intermolecular cross-linking. J. Cell Biol. 106 (1988) 785-796
    • (1988) J. Cell Biol. , vol.106 , pp. 785-796
    • Millonig, R.1    Salvo, H.2    Aebi, U.3
  • 46
    • 0019877189 scopus 로고
    • Isolation and characterization of covalently cross-linked actin dimer
    • Mockrin S.C., and Korn E.D. Isolation and characterization of covalently cross-linked actin dimer. J. Biol. Chem. 256 (1981) 8228-8233
    • (1981) J. Biol. Chem. , vol.256 , pp. 8228-8233
    • Mockrin, S.C.1    Korn, E.D.2
  • 48
    • 0033065593 scopus 로고    scopus 로고
    • Thiol oxidation of actin produces dimers that enhance the elasticity of the F-actin network
    • Tang J.X., Janmey P.A., Stossel T.P., and Ito T. Thiol oxidation of actin produces dimers that enhance the elasticity of the F-actin network. Biophys. J. 76 (1999) 2208-2215
    • (1999) Biophys. J. , vol.76 , pp. 2208-2215
    • Tang, J.X.1    Janmey, P.A.2    Stossel, T.P.3    Ito, T.4
  • 49
    • 0037036364 scopus 로고    scopus 로고
    • Polylysine induces an antiparallel actin dimer that nucleates filament assembly: crystal structure at 3.5-Å resolution
    • Bubb M.R., Govindasamy L., Yarmola E.G., Vorobiev S.M., Almo S.C., Somasundaram T., et al. Polylysine induces an antiparallel actin dimer that nucleates filament assembly: crystal structure at 3.5-Å resolution. J. Biol. Chem. 277 (2002) 20999-21006
    • (2002) J. Biol. Chem. , vol.277 , pp. 20999-21006
    • Bubb, M.R.1    Govindasamy, L.2    Yarmola, E.G.3    Vorobiev, S.M.4    Almo, S.C.5    Somasundaram, T.6
  • 50
    • 33746855102 scopus 로고    scopus 로고
    • A steric antagonism of actin polymerization by a Salmonella virulence protein
    • Margarit S.M., Davidson W., Frego L., and Stebbins C. A steric antagonism of actin polymerization by a Salmonella virulence protein. Structure 14 (2006) 1219-1229
    • (2006) Structure , vol.14 , pp. 1219-1229
    • Margarit, S.M.1    Davidson, W.2    Frego, L.3    Stebbins, C.4
  • 51
    • 1942425451 scopus 로고    scopus 로고
    • Actin crystal dynamics: structural implications for F-actin nucleation, polymerization, and branching mediated by the anti-parallel dimer
    • Reutzel R., Yoshioka C., Govindasamy L., Yarmola E.G., Agbandje-McKenna M., Bubb M.R., and McKenna R. Actin crystal dynamics: structural implications for F-actin nucleation, polymerization, and branching mediated by the anti-parallel dimer. J. Struct. Biol. 146 (2004) 291-301
    • (2004) J. Struct. Biol. , vol.146 , pp. 291-301
    • Reutzel, R.1    Yoshioka, C.2    Govindasamy, L.3    Yarmola, E.G.4    Agbandje-McKenna, M.5    Bubb, M.R.6    McKenna, R.7
  • 52
    • 33751076785 scopus 로고    scopus 로고
    • Cell biology: brief encounters bolster contacts
    • Blundell T.L., and Fernandez-Recio J. Cell biology: brief encounters bolster contacts. Nature 444 (2006) 279-280
    • (2006) Nature , vol.444 , pp. 279-280
    • Blundell, T.L.1    Fernandez-Recio, J.2
  • 53
    • 33749037156 scopus 로고    scopus 로고
    • The ARP2/3 complex: an actin nucleator comes of age
    • Goley E.D., and Welch M.D. The ARP2/3 complex: an actin nucleator comes of age. Nature Rev. Mol. Cell Biol. 7 (2006) 713-726
    • (2006) Nature Rev. Mol. Cell Biol. , vol.7 , pp. 713-726
    • Goley, E.D.1    Welch, M.D.2
  • 54
    • 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
  • 55
    • 0038313144 scopus 로고    scopus 로고
    • ATP hydrolysis on actin-related protein 2/3 complex causes debranching of dendritic actin arrays
    • Le Clainche C., Pantaloni D., and Carlier M.F. ATP hydrolysis on actin-related protein 2/3 complex causes debranching of dendritic actin arrays. Proc. Natl Acad. Sci. USA 100 (2003) 6337-6342
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 6337-6342
    • Le Clainche, C.1    Pantaloni, D.2    Carlier, M.F.3
  • 56
    • 19644394554 scopus 로고    scopus 로고
    • Regulation of PDGF signalling and vascular remodelling by peroxiredoxin II
    • Choi M.H., Lee I.K., Kim G.W., Kim B.U., Han Y.H., Yu D.Y., et al. Regulation of PDGF signalling and vascular remodelling by peroxiredoxin II. Nature 435 (2005) 347-353
    • (2005) Nature , vol.435 , pp. 347-353
    • Choi, M.H.1    Lee, I.K.2    Kim, G.W.3    Kim, B.U.4    Han, Y.H.5    Yu, D.Y.6
  • 57
    • 0034633602 scopus 로고    scopus 로고
    • Hydrogen peroxide: a key messenger that modulates protein phosphorylation through cysteine oxidation
    • Rhee S.G., Bae Y.S., Lee S.R., and Kwon J. Hydrogen peroxide: a key messenger that modulates protein phosphorylation through cysteine oxidation. Sci. STKE 2000 (2000) PE1
    • (2000) Sci. STKE , vol.2000
    • Rhee, S.G.1    Bae, Y.S.2    Lee, S.R.3    Kwon, J.4
  • 58
    • 24944557079 scopus 로고    scopus 로고
    • Reactive oxygen species production via NADPH oxidase mediates TGF-beta-induced cytoskeletal alterations in endothelial cells
    • Hu T., Ramachandrarao S.P., Siva S., Valancius C., Zhu Y., Mahadev K., et al. Reactive oxygen species production via NADPH oxidase mediates TGF-beta-induced cytoskeletal alterations in endothelial cells. Am. J. Physiol. Renal Physiol. 289 (2005) F816-F825
    • (2005) Am. J. Physiol. Renal Physiol. , vol.289
    • Hu, T.1    Ramachandrarao, S.P.2    Siva, S.3    Valancius, C.4    Zhu, Y.5    Mahadev, K.6
  • 60
    • 0037205457 scopus 로고    scopus 로고
    • Intracellular localization and preassembly of the NADPH oxidase complex in cultured endothelial cells
    • Li J.M., and Shah A.M. Intracellular localization and preassembly of the NADPH oxidase complex in cultured endothelial cells. J. Biol. Chem. 277 (2002) 19952-19960
    • (2002) J. Biol. Chem. , vol.277 , pp. 19952-19960
    • Li, J.M.1    Shah, A.M.2
  • 62
    • 0025944684 scopus 로고
    • Activation of the NADPH oxidase involves the small GTP-binding protein p21rac1
    • Abo A., Pick E., Hall A., Totty N., Teahan C.G., and Segal A.W. Activation of the NADPH oxidase involves the small GTP-binding protein p21rac1. Nature 353 (1991) 668-670
    • (1991) Nature , vol.353 , pp. 668-670
    • Abo, A.1    Pick, E.2    Hall, A.3    Totty, N.4    Teahan, C.G.5    Segal, A.W.6
  • 64
    • 0030980641 scopus 로고    scopus 로고
    • Mitogenic signaling mediated by oxidants in Ras-transformed fibroblasts
    • Irani K., Xia Y., Zweier J.L., Sollott S.J., Der C.J., Fearon E.R., et al. Mitogenic signaling mediated by oxidants in Ras-transformed fibroblasts. Science 275 (1997) 1649-1652
    • (1997) Science , vol.275 , pp. 1649-1652
    • Irani, K.1    Xia, Y.2    Zweier, J.L.3    Sollott, S.J.4    Der, C.J.5    Fearon, E.R.6
  • 65
    • 0042698618 scopus 로고    scopus 로고
    • Two poles and a compass
    • Meili R., and Firtel R.A. Two poles and a compass. Cell 114 (2003) 153-156
    • (2003) Cell , vol.114 , pp. 153-156
    • Meili, R.1    Firtel, R.A.2
  • 67
    • 15044362438 scopus 로고    scopus 로고
    • Intracellular messenger function of hydrogen peroxide and its regulation by peroxiredoxins
    • Rhee S.G., Kang S.W., Jeong W., Chang T.S., Yang K.S., and Woo H.A. Intracellular messenger function of hydrogen peroxide and its regulation by peroxiredoxins. Curr. Opin. Cell Biol. 17 (2005) 183-189
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 183-189
    • Rhee, S.G.1    Kang, S.W.2    Jeong, W.3    Chang, T.S.4    Yang, K.S.5    Woo, H.A.6
  • 68
    • 0001288948 scopus 로고    scopus 로고
    • Platelet-derived growth factor-induced H(2)O(2) production requires the activation of phosphatidylinositol 3-kinase
    • Bae Y.S., Sung J.Y., Kim O.S., Kim Y.J., Hur K.C., Kazlauskas A., and Rhee S.G. Platelet-derived growth factor-induced H(2)O(2) production requires the activation of phosphatidylinositol 3-kinase. J. Biol. Chem. 275 (2000) 10527-10531
    • (2000) J. Biol. Chem. , vol.275 , pp. 10527-10531
    • Bae, Y.S.1    Sung, J.Y.2    Kim, O.S.3    Kim, Y.J.4    Hur, K.C.5    Kazlauskas, A.6    Rhee, S.G.7
  • 69
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall A. Rho GTPases and the actin cytoskeleton. Science 279 (1998) 509-514
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 70
    • 0025214940 scopus 로고
    • Polyphosphoinositide synthesis in platelets stimulated with low concentrations of thrombin is enhanced before the activation of phospholipase C
    • Lassing I., and Lindberg U. Polyphosphoinositide synthesis in platelets stimulated with low concentrations of thrombin is enhanced before the activation of phospholipase C. FEBS Letters 262 (1990) 231-233
    • (1990) FEBS Letters , vol.262 , pp. 231-233
    • Lassing, I.1    Lindberg, U.2
  • 71
    • 0028036684 scopus 로고
    • The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells
    • Chong L.D., Traynor-Kaplan A., Bokoch G.M., and Schwartz M.A. The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells. Cell 79 (1994) 507-513
    • (1994) Cell , vol.79 , pp. 507-513
    • Chong, L.D.1    Traynor-Kaplan, A.2    Bokoch, G.M.3    Schwartz, M.A.4
  • 72
    • 0021179713 scopus 로고
    • The organization of microfilaments in spreading platelets: a comparison with fibroblasts and glial cells
    • Karlsson R., Lassing I., Hoglund A.S., and Lindberg U. The organization of microfilaments in spreading platelets: a comparison with fibroblasts and glial cells. J. Cell Physiol. 121 (1984) 96-113
    • (1984) J. Cell Physiol. , vol.121 , pp. 96-113
    • Karlsson, R.1    Lassing, I.2    Hoglund, A.S.3    Lindberg, U.4
  • 74
    • 17144439652 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate induces actin-based movement of raft-enriched vesicles through WASP-Arp2/3
    • Rozelle A.L., Machesky L.M., Yamamoto M., Driessens M.H., Insall R.H., Roth M.G., et al. Phosphatidylinositol 4,5-bisphosphate induces actin-based movement of raft-enriched vesicles through WASP-Arp2/3. Curr. Biol. 10 (2000) 311-320
    • (2000) Curr. Biol. , vol.10 , pp. 311-320
    • Rozelle, A.L.1    Machesky, L.M.2    Yamamoto, M.3    Driessens, M.H.4    Insall, R.H.5    Roth, M.G.6
  • 75
    • 0242384720 scopus 로고    scopus 로고
    • Activity-induced targeting of profilin and stabilization of dendritic spine morphology
    • Ackermann M., and Matus A. Activity-induced targeting of profilin and stabilization of dendritic spine morphology. Nature Neurosci. 6 (2003) 1194-2100
    • (2003) Nature Neurosci. , vol.6 , pp. 1194-2100
    • Ackermann, M.1    Matus, A.2
  • 76
    • 0037780966 scopus 로고    scopus 로고
    • Reactive oxygen species as essential mediators of cell adhesion: the oxidative inhibition of a FAK tyrosine phosphatase is required for cell adhesion
    • Chiarugi P., Pani G., Giannoni E., Taddei L., Colavitti R., Raugei G., et al. Reactive oxygen species as essential mediators of cell adhesion: the oxidative inhibition of a FAK tyrosine phosphatase is required for cell adhesion. J. Cell Biol. 161 (2003) 933-944
    • (2003) J. Cell Biol. , vol.161 , pp. 933-944
    • Chiarugi, P.1    Pani, G.2    Giannoni, E.3    Taddei, L.4    Colavitti, R.5    Raugei, G.6
  • 77
    • 0034626735 scopus 로고    scopus 로고
    • Oxidants, oxidative stress and the biology of ageing
    • Finkel T., and Holbrook N.J. Oxidants, oxidative stress and the biology of ageing. Nature 408 (2000) 239-247
    • (2000) Nature , vol.408 , pp. 239-247
    • Finkel, T.1    Holbrook, N.J.2
  • 79
    • 28844473846 scopus 로고    scopus 로고
    • Opinion: Radical medicine: treating ageing to cure disease
    • Finkel T. Opinion: Radical medicine: treating ageing to cure disease. Nature Rev. Mol. Cell Biol. 6 (2005) 971-976
    • (2005) Nature Rev. Mol. Cell Biol. , vol.6 , pp. 971-976
    • Finkel, T.1
  • 81
    • 33646142995 scopus 로고    scopus 로고
    • Pten regulates neuronal arborization and social interaction in mice
    • Kwon C.H., Luikart B.W., Powell C.M., Zhou J., Matheny S.A., Zhang W., et al. Pten regulates neuronal arborization and social interaction in mice. Neuron 50 (2006) 377-388
    • (2006) Neuron , vol.50 , pp. 377-388
    • Kwon, C.H.1    Luikart, B.W.2    Powell, C.M.3    Zhou, J.4    Matheny, S.A.5    Zhang, W.6
  • 82
    • 0029187491 scopus 로고
    • Thioredoxin and thioredoxin reductase
    • Holmgren A., and Bjornstedt M. Thioredoxin and thioredoxin reductase. Methods Enzymol. 252 (1995) 199-208
    • (1995) Methods Enzymol. , vol.252 , pp. 199-208
    • Holmgren, A.1    Bjornstedt, M.2
  • 83
    • 84884843176 scopus 로고    scopus 로고
    • Purification of nonmuscle actin
    • Celis J., et al. (Ed), Elsevier Science, New York
    • Schüler H., Karlsson R., and Lindberg U. Purification of nonmuscle actin. In: Celis J., et al. (Ed). Cell Biology: A Laboratory Handbook vol. 2 (2006), Elsevier Science, New York 165-171
    • (2006) Cell Biology: A Laboratory Handbook , vol.2 , pp. 165-171
    • Schüler, H.1    Karlsson, R.2    Lindberg, U.3
  • 84
  • 85
    • 0016294918 scopus 로고
    • The measurement of actin concentration in solution: a comparison of methods
    • Houk Jr. T.W., and Ue K. The measurement of actin concentration in solution: a comparison of methods. Anal. Biochem. 62 (1974) 66-74
    • (1974) Anal. Biochem. , vol.62 , pp. 66-74
    • Houk Jr., T.W.1    Ue, K.2
  • 86
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 88
    • 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. 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 (1981) 33-38
    • (1981) Eur. J. Biochem. , vol.114 , pp. 33-38
    • Kouyama, T.1    Mihashi, K.2
  • 89
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals and initially unknown symmetry and cell constants
    • Kabsch W. Automatic processing of rotation diffraction data from crystals and initially unknown symmetry and cell constants. J. Appl. Crystallog. 26 (1993) 795-800
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 90
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D 50 (1994) 760-763
    • (1994) Acta Crystallog. sect. D , vol.50 , pp. 760-763
  • 92
    • 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
  • 94
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallog. sect. D 53 (1997) 240-255
    • (1997) Acta Crystallog. sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 95
    • 0026597444 scopus 로고
    • Free R value: a novel statistical quantity for assessing the accuracy of crystal structures
    • Brunger A.T. Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355 (1992) 472-475
    • (1992) Nature , vol.355 , pp. 472-475
    • Brunger, A.T.1
  • 96
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallog. sect. D 60 (2004) 2126-2132
    • (2004) Acta Crystallog. sect. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 97
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn M.D., Isupov M.N., and Murshudov G.N. Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallog. sect. D 57 (2001) 122-133
    • (2001) Acta Crystallog. sect. D , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 98
    • 7544226311 scopus 로고    scopus 로고
    • PRODRG: a tool for high-throughput crystallography of protein-ligand complexes
    • Schuttelkopf A.W., and van Aalten D.M. PRODRG: a tool for high-throughput crystallography of protein-ligand complexes. Acta Crystallog. sect. D 60 (2004) 1355-1363
    • (2004) Acta Crystallog. sect. D , vol.60 , pp. 1355-1363
    • Schuttelkopf, A.W.1    van Aalten, D.M.2
  • 100
    • 0032922193 scopus 로고    scopus 로고
    • SFCHECK: a unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model
    • Vagin A.A., Richelle J., and Wodak S.J. SFCHECK: a unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model. Acta Crystallog. sect. D 55 (1999) 191-205
    • (1999) Acta Crystallog. sect. D , vol.55 , pp. 191-205
    • Vagin, A.A.1    Richelle, J.2    Wodak, S.J.3
  • 102
    • 0030028728 scopus 로고    scopus 로고
    • Principles of protein-protein interactions
    • Jones S., and Thornton J.M. Principles of protein-protein interactions. Proc. Natl Acad. Sci. USA 93 (1996) 13-20
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 13-20
    • Jones, S.1    Thornton, J.M.2
  • 103
    • 33748761481 scopus 로고    scopus 로고
    • Detection of Protein Assemblies in Crystals In Protein Interfaces, Surfaces and Assemblies Service PISA at European Bioinformatics Institute
    • Springer, Berlin-Heidelberg
    • Krissinel E., and Henrick K. Detection of Protein Assemblies in Crystals In Protein Interfaces, Surfaces and Assemblies Service PISA at European Bioinformatics Institute. CompLife 2005 (2005), Springer, Berlin-Heidelberg
    • (2005) CompLife 2005
    • Krissinel, E.1    Henrick, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.