메뉴 건너뛰기




Volumn , Issue , 2012, Pages 61-96

Actin: Structure, function and disease

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84892269950     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (3)

References (169)
  • 1
    • 52449089651 scopus 로고    scopus 로고
    • Comparative dynamics of retrograde actin flow and focal adhesions: formation of nascent adhesions triggers transition from fast to slow flow
    • Alexandrova, A. Y.,Arnold, K., Schaub, S., Vasiliev, J.M., Meister, J.J., Bershadsky, A.D. and Verkhovsky, A.B. (2008). Comparative dynamics of retrograde actin flow and focal adhesions: formation of nascent adhesions triggers transition from fast to slow flow. PLoS ONE, 3, e3234.
    • (2008) PLoS ONE , vol.3
    • Alexandrova, A.Y.1    Arnold, K.2    Schaub, S.3    Vasiliev, J.M.4    Meister, J.J.5    Bershadsky, A.D.6    Verkhovsky, A.B.7
  • 2
    • 0000293742 scopus 로고
    • Uber eine eigenartige Erkankung der Hirnrinde
    • Alzheimer, A. (1907). Uber eine eigenartige Erkankung der Hirnrinde. Allgem Z. Psych. Med., 64, 146-148.
    • (1907) Allgem Z. Psych. Med. , vol.64 , pp. 146-148
    • Alzheimer, A.1
  • 3
    • 0031048791 scopus 로고    scopus 로고
    • Formation of actin stress fibers and focal adhesions enhanced by Rho-kinase
    • Amano, M., Chihara, K., Fukata, Y., Nakamura, N. and Kaibuchi, K. (1997). Formation of actin stress fibers and focal adhesions enhanced by Rho-kinase.Science, 275, 1308-1311.
    • (1997) Science , vol.275 , pp. 1308-1311
    • Amano, M.1    Chihara, K.2    Fukata, Y.3    Nakamura, N.4    Kaibuchi, K.5
  • 4
    • 0001360883 scopus 로고
    • Dephosphorylation of adenosine triphosphate in actin solutions at low concentrations of magnesium
    • Asakura, S. and Oosawa, F. (1960). Dephosphorylation of adenosine triphosphate in actin solutions at low concentrations of magnesium.Arch. Biochem.Biophys, 87, 273-280.
    • (1960) Arch. Biochem.Biophys , vol.87 , pp. 273-280
    • Asakura, S.1    Oosawa, F.2
  • 5
    • 0036900955 scopus 로고    scopus 로고
    • ADF/cofilin and actin dynamics in disease
    • Bamburg, J.R. and Wiggan, O.P. (2002). ADF/cofilin and actin dynamics in disease.Trends Cell Biol., 12, 598-605.
    • (2002) Trends Cell Biol. , vol.12 , pp. 598-605
    • Bamburg, J.R.1    Wiggan, O.P.2
  • 6
    • 67749133983 scopus 로고    scopus 로고
    • Cytoskeletal pathologies of Alzheimer disease
    • Bamburg, J.R. and Bloom, G.S. (2009). Cytoskeletal pathologies of Alzheimer disease.Cell Motil.Cytoskeleton, 66, 635-649.
    • (2009) Cell Motil.Cytoskeleton , vol.66 , pp. 635-649
    • Bamburg, J.R.1    Bloom, G.S.2
  • 7
    • 33645730485 scopus 로고    scopus 로고
    • Sparks, signals and shock absorbers: how dystrophin loss causes muscular dystrophy
    • Batchelor, C.L. and Winder, S.J. (2006). Sparks, signals and shock absorbers: how dystrophin loss causes muscular dystrophy. Trends Cell Biol., 16, 198-205.
    • (2006) Trends Cell Biol. , vol.16 , pp. 198-205
    • Batchelor, C.L.1    Winder, S.J.2
  • 10
    • 0035928737 scopus 로고    scopus 로고
    • Inhibition of the Arp2/3 complex-nucleated actin polymerization and branch formation by tropomyosin
    • Blanchoin, L., Pollard, T.D. and Hitchock-Degregori, S.E. (2001). Inhibition of the Arp2/3 complex-nucleated actin polymerization and branch formation by tropomyosin.Curr.Biol., 11, 1300-1304.
    • (2001) Curr.Biol. , vol.11 , pp. 1300-1304
    • Blanchoin, L.1    Pollard, T.D.2    Hitchock-Degregori, S.E.3
  • 11
    • 78650637719 scopus 로고    scopus 로고
    • The Wiskott-Aldrich syndrome: The actin cytoskeleton and immune cell function
    • Blundell, M.P., Worth, A., Bouma, G. and Thrasher, A.J. (2010). The Wiskott-Aldrich syndrome: The actin cytoskeleton and immune cell function. Disease Markers, 29, 157-175.
    • (2010) Disease Markers , vol.29 , pp. 157-175
    • Blundell, M.P.1    Worth, A.2    Bouma, G.3    Thrasher, A.J.4
  • 12
    • 33644891379 scopus 로고    scopus 로고
    • Signal transduction and actin in the regulation of the G1-phase progression
    • Boonstra, J. and Moes, J.A. (2005). Signal transduction and actin in the regulation of the G1-phase progression.Crit. Rev. Euk Gene Expr., 15, 255-275.
    • (2005) Crit. Rev. Euk Gene Expr. , vol.15 , pp. 255-275
    • Boonstra, J.1    Moes, J.A.2
  • 13
    • 43449117577 scopus 로고    scopus 로고
    • Balancing structure and function at hippocampal dendritic spines
    • Bourne, J.N. and Harris, K.M. (2008). Balancing structure and function at hippocampal dendritic spines. Ann. Rev.Neurosci., 31, 47-67.
    • (2008) Ann. Rev.Neurosci. , vol.31 , pp. 47-67
    • Bourne, J.N.1    Harris, K.M.2
  • 14
    • 34548225942 scopus 로고    scopus 로고
    • Control of synaptic consolidation in the dendate gyrus: mechanisms, functions, and therapeutic implications
    • Bramham, C.R. (2007). Control of synaptic consolidation in the dendate gyrus: mechanisms, functions, and therapeutic implications. Prog. Brain Res. Rev., 163, 453-471.
    • (2007) Prog. Brain Res. Rev. , vol.163 , pp. 453-471
    • Bramham, C.R.1
  • 16
    • 0035898659 scopus 로고    scopus 로고
    • Myosin VI isoform localized to clathrin-coated vesicles with a role in clathrin-mediated endocytosis
    • Buss, F., Arden, S.D., Lindsay, M., Luzio, J.P. and Kendrick-Jones, J. (2001). Myosin VI isoform localized to clathrin-coated vesicles with a role in clathrin-mediated endocytosis.EMBO J., 20, 3676-3684.
    • (2001) EMBO J. , vol.20 , pp. 3676-3684
    • Buss, F.1    Arden, S.D.2    Lindsay, M.3    Luzio, J.P.4    Kendrick-Jones, J.5
  • 17
    • 77952929975 scopus 로고    scopus 로고
    • Molecular bases of cell-cell junctions stability and dynamics
    • Cavey, M. and Lecuit, T. (2009). Molecular bases of cell-cell junctions stability and dynamics. Cold Spring Harbor Perspect.Biol., 1, a002998.
    • (2009) Cold Spring Harbor Perspect.Biol. , vol.1
    • Cavey, M.1    Lecuit, T.2
  • 18
    • 0018607228 scopus 로고
    • Rapid induction of morphological changes in human carcinoma A431 cells by epidermal growth factor
    • Chinkers, M., McKanna, J.A. and Cohen, S. (1979). Rapid induction of morphological changes in human carcinoma A431 cells by epidermal growth factor. J. Cell Biol., 83,260-265.
    • (1979) J. Cell Biol. , vol.83 , pp. 260-265
    • Chinkers, M.1    McKanna, J.A.2    Cohen, S.3
  • 19
    • 51049104617 scopus 로고    scopus 로고
    • Actin and a-actinin orchestrate the assembly and maturation of nascent adhesions in a myosin II motor-independent manner
    • Choi, C.K., Manzanares, M.V., Zareno, J., Whitmore, L.A., Mogilner, A. and Horwitz, A.R. (2008). Actin and a-actinin orchestrate the assembly and maturation of nascent adhesions in a myosin II motor-independent manner. Nature Cell Biol., 10, 1039-1050.
    • (2008) Nature Cell Biol. , vol.10 , pp. 1039-1050
    • Choi, C.K.1    Manzanares, M.V.2    Zareno, J.3    Whitmore, L.A.4    Mogilner, A.5    Horwitz, A.R.6
  • 20
    • 42349091996 scopus 로고    scopus 로고
    • Actin in action: the interplay between the actin cytoskeleton and synaptic efficacy
    • Cingolani, L.A. and Goda, Y. (2008). Actin in action: the interplay between the actin cytoskeleton and synaptic efficacy. Nat. Rev.Neurosci., 9, 344-356.
    • (2008) Nat. Rev.Neurosci. , vol.9 , pp. 344-356
    • Cingolani, L.A.1    Goda, Y.2
  • 21
    • 7944229031 scopus 로고    scopus 로고
    • Congenital myopathies: diseases of the actin cytoskeleton
    • Clarkson, E., Costa, C.F. and Machesky, L.M. (2004). Congenital myopathies: diseases of the actin cytoskeleton. J.Pathol., 204, 407-417.
    • (2004) J.Pathol. , vol.204 , pp. 407-417
    • Clarkson, E.1    Costa, C.F.2    Machesky, L.M.3
  • 23
    • 0032786906 scopus 로고    scopus 로고
    • Membrane tether formation from blebbing cells
    • Dai, J. and Sheetz, M.P. (1999). Membrane tether formation from blebbing cells.Biophys. J., 77, 3363-3370.
    • (1999) Biophys. J. , vol.77 , pp. 3363-3370
    • Dai, J.1    Sheetz, M.P.2
  • 24
    • 15644366485 scopus 로고    scopus 로고
    • The secretion-coupled endocytosis correlates with membrane tension changes in RBL 2H3 cells
    • Dai, J., Ting-Beall, H.P. and Sheetz, M.P. (1997). The secretion-coupled endocytosis correlates with membrane tension changes in RBL 2H3 cells. J. Gen.Physiol., 110, 1-10.
    • (1997) J. Gen.Physiol. , vol.110 , pp. 1-10
    • Dai, J.1    Ting-Beall, H.P.2    Sheetz, M.P.3
  • 26
    • 26444449581 scopus 로고    scopus 로고
    • Distinct pathways control recruitment and maintenance of myosin II at the cleavage furrow during cytokinesis
    • Dean, S.O., Rogers, S.L., Stuurman, N., Vale, R.D. and Spudich, J.A. (2005). Distinct pathways control recruitment and maintenance of myosin II at the cleavage furrow during cytokinesis. Proc. Natl. Acad. Sci.USA, 102, 13473-13478.
    • (2005) Proc. Natl. Acad. Sci.USA , vol.102 , pp. 13473-13478
    • Dean, S.O.1    Rogers, S.L.2    Stuurman, N.3    Vale, R.D.4    Spudich, J.A.5
  • 27
    • 59649092177 scopus 로고    scopus 로고
    • The control of vascular integrity cell junctions: molecular basis and pathological implications
    • Dejana, E., Tournier-Lasserve, E. and Weinstein, B.M. (2009). The control of vascular integrity cell junctions: molecular basis and pathological implications. Dev.Cell, 16, 209-221.
    • (2009) Dev.Cell , vol.16 , pp. 209-221
    • Dejana, E.1    Tournier-Lasserve, E.2    Weinstein, B.M.3
  • 31
    • 0033569627 scopus 로고    scopus 로고
    • Vesicle transport: the role of actin filaments and myosin motors
    • DePina, A.S. and Langford, G.M. (1999). Vesicle transport: the role of actin filaments and myosin motors. Microsc. Res. Techniq, 47, 93-106.
    • (1999) Microsc. Res. Techniq , vol.47 , pp. 93-106
    • DePina, A.S.1    Langford, G.M.2
  • 32
    • 0029017989 scopus 로고
    • Epidermal growth factor induces rapid and transient association of phos- pholipase C-γ1 with EGF-receptor and filamentous actin at membrane ruffles of A431 cells
    • Diakonova, M., Payrastre, B., van Velzen, A.G., Hage, W.J., van Bergen en Henegouwen, P.M.P., Boonstra, J., Cremers, A.F.M. and Humbel, B.M. (1995). Epidermal growth factor induces rapid and transient association of phos- pholipase C-γ1 with EGF-receptor and filamentous actin at membrane ruffles of A431 cells. J. Cell Sci., 108, 2499-2509.
    • (1995) J. Cell Sci. , vol.108 , pp. 2499-2509
    • Diakonova, M.1    Payrastre, B.2    van Velzen, A.G.3    Hage, W.J.4    van Bergen en Henegouwen, P.M.P.5    Boonstra, J.6    Cremers, A.F.M.7    Humbel, B.M.8
  • 33
    • 77954766868 scopus 로고    scopus 로고
    • Actin-related proteins in the nucleus: Life beyond chromatin remodelers
    • Dion, V., Shimada, K. and Gasser, S.M. (2010). Actin-related proteins in the nucleus: Life beyond chromatin remodelers. Curr. Op. Cell Biol., 22, 383-391.
    • (2010) Curr. Op. Cell Biol. , vol.22 , pp. 383-391
    • Dion, V.1    Shimada, K.2    Gasser, S.M.3
  • 34
    • 48249134102 scopus 로고    scopus 로고
    • Mediation,modulation and consequences of membrane-cytoskeleton interactions
    • Doherty, G.J. and McMahon, H.T. (2008). Mediation,modulation and consequences of membrane-cytoskeleton interactions.Ann. Rev.Biophys.,37, 65-95.
    • (2008) Ann. Rev.Biophys. , vol.37 , pp. 65-95
    • Doherty, G.J.1    McMahon, H.T.2
  • 35
    • 79955859521 scopus 로고    scopus 로고
    • Actin structure and function
    • Dominguez, R. and Holmes, K.C. (2011). Actin structure and function.Ann. Rev.Biophys., 40, 169-186.
    • (2011) Ann. Rev.Biophys. , vol.40 , pp. 169-186
    • Dominguez, R.1    Holmes, K.C.2
  • 37
    • 84892212758 scopus 로고    scopus 로고
    • Signal transduction pathways: from receptor to the actin cytoskeleton
    • Dubreuil, C.I. and Van Vactor, D.L. (2011). Signal transduction pathways: from receptor to the actin cytoskeleton. Adv.Neurobiol., 5, 235-263.
    • (2011) Adv.Neurobiol. , vol.5 , pp. 235-263
    • Dubreuil, C.I.1    Van Vactor, D.L.2
  • 38
    • 77950271947 scopus 로고    scopus 로고
    • Control of cell shape and plasticity during development and disease by the actin-binding protein drebrin
    • Dun, X. and Chilton, J.K. (2010).Control of cell shape and plasticity during development and disease by the actin-binding protein drebrin.Histol.Histopathol., 25, 533-540.
    • (2010) Histol.Histopathol. , vol.25 , pp. 533-540
    • Dun, X.1    Chilton, J.K.2
  • 39
    • 64049108784 scopus 로고    scopus 로고
    • The cellular context of T cell signaling
    • Dustin, M.L. (2009). The cellular context of T cell signaling.Immunity, 30, 482-492.
    • (2009) Immunity , vol.30 , pp. 482-492
    • Dustin, M.L.1
  • 40
    • 33846271135 scopus 로고    scopus 로고
    • Dystrophin, its interactions with other proteins, and implications for muscular dystrophy
    • Ervasti, J.M. (2007). Dystrophin, its interactions with other proteins, and implications for muscular dystrophy.Biochim Biophys Acta, 1772, 108-117.
    • (2007) Biochim Biophys Acta , vol.1772 , pp. 108-117
    • Ervasti, J.M.1
  • 41
    • 0032771080 scopus 로고    scopus 로고
    • The Emery-Dreifuss muscular dystrophy phenotype arises from aberrant targeting and binding of emerin at the inner nuclear membrane
    • Fairley, E. A., Kendrick-Jones, J. and Ellis, J. A. (1999). The Emery-Dreifuss muscular dystrophy phenotype arises from aberrant targeting and binding of emerin at the inner nuclear membrane. J. Cell Sci., 112, 2571-2582.
    • (1999) J. Cell Sci. , vol.112 , pp. 2571-2582
    • Fairley, E.A.1    Kendrick-Jones, J.2    Ellis, J.A.3
  • 42
    • 28244472125 scopus 로고    scopus 로고
    • Cytoplasmic YY1 is associated with increased smooth muscle-specific gene expression: implications for neonatal pulmonary hypertension
    • Favot, L., Hall, S.M., Haworth, S.G.and Kemp, P.R. (2005). Cytoplasmic YY1 is associated with increased smooth muscle-specific gene expression: implications for neonatal pulmonary hypertension. Am. J.Pathol., 167, 1497-1509.
    • (2005) Am. J.Pathol. , vol.167 , pp. 1497-1509
    • Favot, L.1    Hall, S.M.2    Haworth S.G.and Kemp, P.R.3
  • 43
    • 0028988989 scopus 로고
    • V-Src-induced degradation of focal adhesion kinase during morphological transformation of chicken embryo fibroblasts
    • Fincham, V.J., Wycke, J.A. and Frame, M.C. (1995). v-Src-induced degradation of focal adhesion kinase during morphological transformation of chicken embryo fibroblasts. Oncogene, 10, 2247-2252.
    • (1995) Oncogene , vol.10 , pp. 2247-2252
    • Fincham, V.J.1    Wycke, J.A.2    Frame, M.C.3
  • 44
    • 0036467581 scopus 로고    scopus 로고
    • Advances in Rho-dependent actin regulation and oncogenic transformation
    • Frame, M.C. and Brunton, V.G. (2002).Advances in Rho-dependent actin regulation and oncogenic transformation.Curr. Opin. Gen Develop, 12, 36-43.
    • (2002) Curr. Opin. Gen Develop , vol.12 , pp. 36-43
    • Frame, M.C.1    Brunton, V.G.2
  • 45
    • 0030802568 scopus 로고    scopus 로고
    • The structure, function, and assembly of actin filament bundles
    • Furukawa, R. and Fechheimer, M. (1997). The structure, function, and assembly of actin filament bundles.Int. Rev. Cytol, 175, 29-90.
    • (1997) Int. Rev. Cytol , vol.175 , pp. 29-90
    • Furukawa, R.1    Fechheimer, M.2
  • 46
    • 32544447916 scopus 로고    scopus 로고
    • Actin cytoskeletal dynamics in smooth muscle contraction
    • Gerthoffer, W.T. (2005). Actin cytoskeletal dynamics in smooth muscle contraction.Can. J. Physiol.Pharmacol., 83, 851-856.
    • (2005) Can. J. Physiol.Pharmacol. , vol.83 , pp. 851-856
    • Gerthoffer, W.T.1
  • 47
    • 0031026750 scopus 로고    scopus 로고
    • Cell-cell contact changes the dynamics of lamellar activity in nontransformed epitheliocytes but not in their ras-transformed descendants
    • Gloushankova, N.A., Alieva, N.A., Krendel, M.F., Bonder, E.M., Feder, H.H., Vasiliev, J.M. and Gelfand, I.M. (1997). Cell-cell contact changes the dynamics of lamellar activity in nontransformed epitheliocytes but not in their ras-transformed descendants. Proc. Natl. Acad. Sci.USA, 94, 879-883.
    • (1997) Proc. Natl. Acad. Sci.USA , vol.94 , pp. 879-883
    • Gloushankova, N.A.1    Alieva, N.A.2    Krendel, M.F.3    Bonder, E.M.4    Feder, H.H.5    Vasiliev, J.M.6    Gelfand, I.M.7
  • 48
    • 44049096985 scopus 로고    scopus 로고
    • T cell activation and the cytoskeleton: you can't have one without the other
    • Gomez,T.S. and Billadeau, D.D. (2008). T cell activation and the cytoskeleton: you can't have one without the other. Adv. Immunol., 97, 1-64.
    • (2008) Adv. Immunol. , vol.97 , pp. 1-64
    • Gomez, T.S.1    Billadeau, D.D.2
  • 50
    • 11844304062 scopus 로고    scopus 로고
    • The role of the Rho GTPases in neuronal development
    • Govek, E.E., Newey, S.E. and Van Aelst, L. (2005). The role of the Rho GTPases in neuronal development.Genes Dev.,19, 1-49.
    • (2005) Genes Dev. , vol.19 , pp. 1-49
    • Govek, E.E.1    Newey, S.E.2    Van Aelst, L.3
  • 51
    • 23144442645 scopus 로고    scopus 로고
    • Regulation of cadherin-mediated adhesion in morphogenesis
    • Gumbiner, B.M. (2005). Regulation of cadherin-mediated adhesion in morphogenesis.Nat. Rev. Mol. Cell Biol., 6, 622-634.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 622-634
    • Gumbiner, B.M.1
  • 52
    • 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. (1994). ATPase kinetics of recombinant bovine 70 kDa heat shock cognate protein and its amino-terminal ATPase domain.Biochem., 33, 14625-14635.
    • (1994) Biochem. , vol.33 , pp. 14625-14635
    • Ha, J.H.1    McKay, D.B.2
  • 53
    • 10344225666 scopus 로고    scopus 로고
    • Subcellular localization of multiple PREP2 isoforms is regulated by actin, tubulin, and nuclear export
    • Haller, K., Rambaldi, I., Daniels, E. and Featherstone, M. (2004). Subcellular localization of multiple PREP2 isoforms is regulated by actin, tubulin, and nuclear export. J. Biol.Chem., 279, 49384-49394.
    • (2004) J. Biol.Chem. , vol.279 , pp. 49384-49394
    • Haller, K.1    Rambaldi, I.2    Daniels, E.3    Featherstone, M.4
  • 54
    • 0030025216 scopus 로고    scopus 로고
    • Disappearance of actin-binding protein, drebrin, from hippocampal synapses in Alzheimer's disease
    • Harigaya, Y., Shoji, M., Shirao, T. and Hirai, S. (1996). Disappearance of actin-binding protein, drebrin, from hippocampal synapses in Alzheimer's disease. J. Neurosci Res., 43, 87-92.
    • (1996) J. Neurosci Res. , vol.43 , pp. 87-92
    • Harigaya, Y.1    Shoji, M.2    Shirao, T.3    Hirai, S.4
  • 55
    • 39849100440 scopus 로고    scopus 로고
    • Adherens and tight junctions: structure, function and connections to actin cytoskeleton
    • Hartsock, A. and Nelson, W.J. (2008). Adherens and tight junctions: structure, function and connections to actin cytoskeleton. Biochim. Biophys.Acta, 1778, 660-669.
    • (2008) Biochim. Biophys.Acta , vol.1778 , pp. 660-669
    • Hartsock, A.1    Nelson, W.J.2
  • 56
    • 0029825623 scopus 로고    scopus 로고
    • Modulatory role of drebrin on the cytoskeleton within dendritic spines in the rat cerebral cortex
    • Hayashi, K., Ishikawa, R., Ye, L. H., He, X. L., Takata, K., Kohama, K. and Shirao, T. (1996).Modulatory role of drebrin on the cytoskeleton within dendritic spines in the rat cerebral cortex.J. Neurosci.,16, 7161-7170.
    • (1996) J. Neurosci. , vol.16 , pp. 7161-7170
    • Hayashi, K.1    Ishikawa, R.2    Ye, L.H.3    He, X.L.4    Takata, K.5    Kohama, K.6    Shirao, T.7
  • 60
    • 78650348130 scopus 로고    scopus 로고
    • Conformational dynamics of actin: effectors and implications for biological function
    • Hild, G., Bugyi, B. and Nyitrai, M. (2010). Conformational dynamics of actin: effectors and implications for biological function. Cytoskel, 67, 609-629.
    • (2010) Cytoskel , vol.67 , pp. 609-629
    • Hild, G.1    Bugyi, B.2    Nyitrai, M.3
  • 62
    • 34547642520 scopus 로고    scopus 로고
    • An emerin "proteome": purification of distinct emerin-containing complexes from HeLa cells suggests molecular basis for diverse roles including gene regulation, mRNA splicing, signaling, mechanosensing, and nuclear architecture
    • Holaska, J. M. and Wilson, K. L. (2007). An emerin "proteome": purification of distinct emerin-containing complexes from HeLa cells suggests molecular basis for diverse roles including gene regulation, mRNA splicing, signaling, mechanosensing, and nuclear architecture. Biochem., 46, 8897-8908.
    • (2007) Biochem. , vol.46 , pp. 8897-8908
    • Holaska, J.M.1    Wilson, K.L.2
  • 63
    • 40249097516 scopus 로고    scopus 로고
    • The subspine organization of actin fibers regulates the structure and plasticity of dendritic spines
    • Honkura, N., Matsuzaki, M., Noguchi, J., Ellis-Davies, G.C. and Kasai, H. (2008). The subspine organization of actin fibers regulates the structure and plasticity of dendritic spines. Neuron, 57, 719-729.
    • (2008) Neuron , vol.57 , pp. 719-729
    • Honkura, N.1    Matsuzaki, M.2    Noguchi, J.3    Ellis-Davies, G.C.4    Kasai, H.5
  • 64
    • 77952334420 scopus 로고    scopus 로고
    • Actin in dendritic spines: connecting dynamics to function
    • Hotulainen, P. and Hoogenraad, C.C. (2010). Actin in dendritic spines: connecting dynamics to function. J. Cell Biol., 189, 619-629.
    • (2010) J. Cell Biol. , vol.189 , pp. 619-629
    • Hotulainen, P.1    Hoogenraad, C.C.2
  • 65
    • 55549091059 scopus 로고    scopus 로고
    • Chronophin mediates an ATP-sensing mechanism of cofilin dephosphorylation and neuronal cofolin-actin rod formation
    • Huang, T.Y., Minamide, L.S., Bamburg, J.R. and Bokoch, G.M. (2008). Chronophin mediates an ATP-sensing mechanism of cofilin dephosphorylation and neuronal cofolin-actin rod formation. Develop.Cell, 15, 691-703.
    • (2008) Develop.Cell , vol.15 , pp. 691-703
    • Huang, T.Y.1    Minamide, L.S.2    Bamburg, J.R.3    Bokoch, G.M.4
  • 67
    • 33846371992 scopus 로고    scopus 로고
    • Molecular scale imaging of F-actin assemblies immobilized on a photopolymer surface
    • Ikawa, T., Hoshino, F., Watanabe, O., Li, Y., Pincus, P. and Safinya, R.C. (2007).Molecular scale imaging of F-actin assemblies immobilized on a photopolymer surface.Phys.Rev. Letters, 98, 018101-1-018101-4.
    • (2007) Phys.Rev. Letters , vol.98 , pp. 0181011-0181014
    • Ikawa, T.1    Hoshino, F.2    Watanabe, O.3    Li, Y.4    Pincus, P.5    Safinya, R.C.6
  • 68
    • 28444452974 scopus 로고    scopus 로고
    • Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins
    • Itoh, T., Erdmann, K.S., Roux, A., Habermann, B., Werner, H. and De Camilli, P. (2005) Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins. Development Cell, 9, 791-804
    • (2005) Development Cell , vol.9 , pp. 791-804
    • Itoh, T.1    Erdmann, K.S.2    Roux, A.3    Habermann, B.4    Werner, H.5    De Camilli, P.6
  • 69
    • 64849109211 scopus 로고    scopus 로고
    • Drebrin A regulates dendritic spine plasticity and synaptic function in mature cultured hippocampal neurons
    • Ivanov, A., Esclapez, M., Pellegrino, C., Shirao, T. and Ferhat, T. (2009) Drebrin A regulates dendritic spine plasticity and synaptic function in mature cultured hippocampal neurons. J. Cell Sci., 122, 524-534.
    • (2009) J. Cell Sci. , vol.122 , pp. 524-534
    • Ivanov, A.1    Esclapez, M.2    Pellegrino, C.3    Shirao, T.4    Ferhat, T.5
  • 70
    • 27944479854 scopus 로고    scopus 로고
    • Rho GTPases: biochemistry and biology
    • Jaffe A.B. and Hall A. (2005). Rho GTPases: biochemistry and biology. Ann. Rev. Cell Devel.Biol., 21, 247-269.
    • (2005) Ann. Rev. Cell Devel.Biol. , vol.21 , pp. 247-269
    • Jaffe, A.B.1    Hall, A.2
  • 71
    • 0031850240 scopus 로고    scopus 로고
    • The cytoskeleton and cell signaling: component localization and mechanical coupling
    • Janmey, P.A. (1998). The cytoskeleton and cell signaling: component localization and mechanical coupling. Physiol Rev, 78, 763-781.
    • (1998) Physiol Rev , vol.78 , pp. 763-781
    • Janmey, P.A.1
  • 72
    • 77149151225 scopus 로고    scopus 로고
    • Upregulation of cytoplasmic gelsolin, an amyloid-β-binding protein, under oxidative stress conditions: involvement of protein kinase C
    • Ji, L., Chauhan, A. and Chauhan, V. (2010). Upregulation of cytoplasmic gelsolin, an amyloid-β-binding protein, under oxidative stress conditions: involvement of protein kinase C. J. Alzh.Dis, 19, 829-838.
    • (2010) J. Alzh.Dis , vol.19 , pp. 829-838
    • Ji, L.1    Chauhan, A.2    Chauhan, V.3
  • 73
    • 33845888826 scopus 로고    scopus 로고
    • Basal-to-apical cadherin flow at cell junctions
    • Kametani, Y. and Takeichi, M. (2007). Basal-to-apical cadherin flow at cell junctions.Nat. Cell Biol.,9, 92-98.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 92-98
    • Kametani, Y.1    Takeichi, M.2
  • 75
    • 72549088299 scopus 로고    scopus 로고
    • PINK1 gene knockdown leads to increased binding of parkin with actin filament
    • Kim, K-H. and Son, J.H. (2010). PINK1 gene knockdown leads to increased binding of parkin with actin filament. Neurosci.Lett., 468, 272-276.
    • (2010) Neurosci.Lett. , vol.468 , pp. 272-276
    • Kim, K.-H.1    Son, J.H.2
  • 76
    • 3042777656 scopus 로고    scopus 로고
    • Actin- and protein-4.1-containing filaments link nuclear pore complexes to subnuclear organelles in Xenopus oocyte nuclei
    • Kiseleva, E., Drummond, S. P., Goldberg, M. W., Rutherford, S. A., Allen, T. D. and Wilson, K. L. (2004). Actin- and protein-4.1-containing filaments link nuclear pore complexes to subnuclear organelles in Xenopus oocyte nuclei. J. Cell Sci., 117, 2481-2490.
    • (2004) J. Cell Sci. , vol.117 , pp. 2481-2490
    • Kiseleva, E.1    Drummond, S.P.2    Goldberg, M.W.3    Rutherford, S.A.4    Allen, T.D.5    Wilson, K.L.6
  • 77
    • 80051547256 scopus 로고    scopus 로고
    • Role of cellular mechanics in the function and life span of vascular endothelium
    • doi: 10.1007/s00424-011-0929-2
    • Kliche, K., Jeggle, P., Pavenstädt, H. and Oberleithner, H. (2011). Role of cellular mechanics in the function and life span of vascular endothelium.Pflugers Arch. Eur. J.Physiol.,doi: 10.1007/s00424-011-0929-2.
    • (2011) Pflugers Arch. Eur. J.Physiol.
    • Kliche, K.1    Jeggle, P.2    Pavenstädt, H.3    Oberleithner, H.4
  • 78
    • 34247632141 scopus 로고    scopus 로고
    • Synaptic dysfunction and disruption of postsynaptic drebrin-actin complex: a study of neurological disorders accompanied by cognitive deficits
    • Kojima, A. and Shirao, T. (2007). Synaptic dysfunction and disruption of postsynaptic drebrin-actin complex: a study of neurological disorders accompanied by cognitive deficits. NeurosciRes, 58, 1-5
    • (2007) NeurosciRes , vol.58 , pp. 1-5
    • Kojima, A.1    Shirao, T.2
  • 79
    • 84870595597 scopus 로고    scopus 로고
    • The sliding filament theory of muscle contraction
    • Krans,J. L. (2010).The sliding filament theory of muscle contraction.Nature Education,3, 66.
    • (2010) Nature Education , vol.3 , pp. 66
    • Krans, J.L.1
  • 80
    • 16244382549 scopus 로고    scopus 로고
    • Muscle-specific signaling mechanism that links actin dynamics to serum-response factor
    • Kuwahara, K., Barrientos, T., Pipes, G.C., Li, S. and Olson, E.N. (2005). Muscle-specific signaling mechanism that links actin dynamics to serum-response factor.Mol. Cell Biol., 25, 3173-3181.
    • (2005) Mol. Cell Biol. , vol.25 , pp. 3173-3181
    • Kuwahara, K.1    Barrientos, T.2    Pipes, G.C.3    Li, S.4    Olson, E.N.5
  • 81
    • 0022487183 scopus 로고
    • Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicate actin-binding domain
    • Kwiatkowski, D.J., Stossel, T.P., Orkin, S.H., Mole, J.E., Colten, H. and Yin H.L. (1986). Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicate actin-binding domain. Nature, 323, 455- 458.
    • (1986) Nature , vol.323 , pp. 455-458
    • Kwiatkowski, D.J.1    Stossel, T.P.2    Orkin, S.H.3    Mole, J.E.4    Colten, H.5    Yin, H.L.6
  • 82
    • 0036080574 scopus 로고    scopus 로고
    • Ischemia induces alterations in actin filaments in renal vascular smooth muscle cells
    • Kwon, O. and Phillips, C.L. Ischemia induces alterations in actin filaments in renal vascular smooth muscle cells. Am. J.Physiol., 282, F1012-F1019.
    • Am. J.Physiol. , vol.282
    • Kwon, O.1    Phillips, C.L.2
  • 84
    • 33749240943 scopus 로고    scopus 로고
    • Mechanisms of Parkinson's disease linked to pathological a-synuclein: new targets for drug discovery
    • Lee, H.-J. and Trojanowski, J.Q. (2006). Mechanisms of Parkinson's disease linked to pathological a-synuclein: new targets for drug discovery. Neuron, 52, 33-38.
    • (2006) Neuron , vol.52 , pp. 33-38
    • Lee, H.-J.1    Trojanowski, J.Q.2
  • 85
    • 79959923467 scopus 로고    scopus 로고
    • Protein aggregate spreading in neurodegenerative diseases: problems and perspectives
    • Doi: 10.1016/j.neures.2011.05.008
    • Lee, S-J., Lim, H-S., Masliah, E. and Lee, H.-J. (2011). Protein aggregate spreading in neurodegenerative diseases: problems and perspectives. Neurosci. Res., Doi: 10.1016/j.neures.2011.05.008.
    • (2011) Neurosci. Res.
    • Lee, S.-J.1    Lim, H.-S.2    Masliah, E.3    Lee, H.-J.4
  • 86
    • 77953491510 scopus 로고    scopus 로고
    • Proteomic profiling of the dystrophin-deficient MDX heart reveals drastically altered levels of key metabolic and contractile proteins
    • Doi: 10.1155/2010/648501
    • Lewis, C., Jockusch, H. and Ohlendieck, K. (2010). Proteomic profiling of the dystrophin-deficient MDX heart reveals drastically altered levels of key metabolic and contractile proteins. J. Biomed Biotechnol.,Doi: 10.1155/2010/648501.
    • (2010) J. Biomed Biotechnol.
    • Lewis, C.1    Jockusch, H.2    Ohlendieck, K.3
  • 87
    • 0028953495 scopus 로고
    • Growth cone advance is inversely proportional to retrograde F-actin flow
    • Lin, C.H. and Forscher, P. (1995). Growth cone advance is inversely proportional to retrograde F-actin flow. Neuron, 14, 763-771.
    • (1995) Neuron , vol.14 , pp. 763-771
    • Lin, C.H.1    Forscher, P.2
  • 88
    • 34347347236 scopus 로고    scopus 로고
    • Cofilin-mediated neurodegeneration in Alzheimer's disease and other amyloidopathies
    • Maloney, M.T. and Bamburg, J.R. (2007). Cofilin-mediated neurodegeneration in Alzheimer's disease and other amyloidopathies.Mol.Neurobiol., 35, 21-44.
    • (2007) Mol.Neurobiol. , vol.35 , pp. 21-44
    • Maloney, M.T.1    Bamburg, J.R.2
  • 89
    • 30544447666 scopus 로고    scopus 로고
    • Beta-secretase-cleaved amyloid precursor protein accumulates at actin inclusions induced in neurons by stress or amyloid-beta: a feedforward mechanism for Alzheimers disease
    • Maloney, M.T., Minamide, L.S., Kinley, A.W., Boyle, J.A. and Bamburg, J.R. (2005). Beta-secretase-cleaved amyloid precursor protein accumulates at actin inclusions induced in neurons by stress or amyloid-beta: a feedforward mechanism for Alzheimers disease. J.Neurosci., 25, 11313-11321.
    • (2005) J.Neurosci. , vol.25 , pp. 11313-11321
    • Maloney, M.T.1    Minamide, L.S.2    Kinley, A.W.3    Boyle, J.A.4    Bamburg, J.R.5
  • 90
    • 79960361814 scopus 로고    scopus 로고
    • Recent advances in the genetics of Parkinson's disease
    • doi: 10.1146/annurev-genom-082410-101440
    • Martin, I., Dawson, V.L. and Dawson, T.M. (2011). Recent advances in the genetics of Parkinson's disease. Annu Rev Genom Hum Genet 12, doi: 10.1146/annurev-genom-082410-101440.
    • (2011) Annu Rev Genom Hum Genet , vol.12
    • Martin, I.1    Dawson, V.L.2    Dawson, T.M.3
  • 91
    • 33845888826 scopus 로고    scopus 로고
    • Basal-to-apical cadherin flow at cell junctions
    • Kametani, Y. and Takeichi, M. (2007). Basal-to-apical cadherin flow at cell junctions.Nat. Cell Biol.,9, 92-98.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 92-98
    • Kametani, Y.1    Takeichi, M.2
  • 93
    • 72549088299 scopus 로고    scopus 로고
    • PINK1 gene knockdown leads to increased binding of parkin with actin filament
    • Kim, K-H. and Son, J.H. (2010). PINK1 gene knockdown leads to increased binding of parkin with actin filament. Neurosci.Lett., 468, 272-276.
    • (2010) Neurosci.Lett. , vol.468 , pp. 272-276
    • Kim, K.-H.1    Son, J.H.2
  • 94
    • 3042777656 scopus 로고    scopus 로고
    • Actin- and protein-4.1-containing filaments link nuclear pore complexes to subnuclear organelles in Xenopus oocyte nuclei
    • Kiseleva, E., Drummond, S. P., Goldberg, M. W., Rutherford, S. A., Allen, T. D. and Wilson, K. L. (2004). Actin- and protein-4.1-containing filaments link nuclear pore complexes to subnuclear organelles in Xenopus oocyte nuclei. J. Cell Sci., 117, 2481-2490.
    • (2004) J. Cell Sci. , vol.117 , pp. 2481-2490
    • Kiseleva, E.1    Drummond, S.P.2    Goldberg, M.W.3    Rutherford, S.A.4    Allen, T.D.5    Wilson, K.L.6
  • 95
    • 80051547256 scopus 로고    scopus 로고
    • Role of cellular mechanics in the function and life span of vascular endothelium
    • doi: 10.1007/s00424-011-0929-2
    • Kliche, K., Jeggle, P., Pavenstädt, H. and Oberleithner, H. (2011). Role of cellular mechanics in the function and life span of vascular endothelium.Pflugers Arch. Eur. J.Physiol.,doi: 10.1007/s00424-011-0929-2.
    • (2011) Pflugers Arch. Eur. J.Physiol.
    • Kliche, K.1    Jeggle, P.2    Pavenstädt, H.3    Oberleithner, H.4
  • 96
    • 34247632141 scopus 로고    scopus 로고
    • Synaptic dysfunction and disruption of postsynaptic drebrin-actin complex: a study of neurological disorders accompanied by cognitive deficits
    • Kojima, A. and Shirao, T. (2007). Synaptic dysfunction and disruption of postsynaptic drebrin-actin complex: a study of neurological disorders accompanied by cognitive deficits. NeurosciRes, 58, 1-5
    • (2007) NeurosciRes , vol.58 , pp. 1-5
    • Kojima, A.1    Shirao, T.2
  • 97
    • 84870595597 scopus 로고    scopus 로고
    • The sliding filament theory of muscle contraction
    • Krans,J. L. (2010).The sliding filament theory of muscle contraction.Nature Education,3, 66.
    • (2010) Nature Education , vol.3 , pp. 66
    • Krans, J.L.1
  • 98
    • 16244382549 scopus 로고    scopus 로고
    • Muscle-specific signaling mechanism that links actin dynamics to serum-response factor
    • Kuwahara, K., Barrientos, T., Pipes, G.C., Li, S. and Olson, E.N. (2005). Muscle-specific signaling mechanism that links actin dynamics to serum-response factor.Mol. Cell Biol., 25, 3173-3181.
    • (2005) Mol. Cell Biol. , vol.25 , pp. 3173-3181
    • Kuwahara, K.1    Barrientos, T.2    Pipes, G.C.3    Li, S.4    Olson, E.N.5
  • 99
    • 0022487183 scopus 로고
    • Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicate actin-binding domain
    • Kwiatkowski, D.J., Stossel, T.P., Orkin, S.H., Mole, J.E., Colten, H. and Yin H.L. (1986). Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicate actin-binding domain. Nature, 323, 455- 458.
    • (1986) Nature , vol.323 , pp. 455-458
    • Kwiatkowski, D.J.1    Stossel, T.P.2    Orkin, S.H.3    Mole, J.E.4    Colten, H.5    Yin, H.L.6
  • 100
    • 0036080574 scopus 로고    scopus 로고
    • Ischemia induces alterations in actin filaments in renal vascular smooth muscle cells
    • Kwon, O. and Phillips, C.L. Ischemia induces alterations in actin filaments in renal vascular smooth muscle cells. Am. J.Physiol., 282, F1012-F1019.
    • Am. J.Physiol. , vol.282
    • Kwon, O.1    Phillips, C.L.2
  • 102
    • 33749240943 scopus 로고    scopus 로고
    • Mechanisms of Parkinson's disease linked to pathological a-synuclein: new targets for drug discovery
    • Lee, H.-J. and Trojanowski, J.Q. (2006). Mechanisms of Parkinson's disease linked to pathological a-synuclein: new targets for drug discovery. Neuron, 52, 33-38.
    • (2006) Neuron , vol.52 , pp. 33-38
    • Lee, H.-J.1    Trojanowski, J.Q.2
  • 103
    • 79959923467 scopus 로고    scopus 로고
    • Protein aggregate spreading in neurodegenerative diseases: problems and perspectives
    • Doi: 10.1016/j.neures.2011.05.008
    • Lee, S-J., Lim, H-S., Masliah, E. and Lee, H.-J. (2011). Protein aggregate spreading in neurodegenerative diseases: problems and perspectives. Neurosci. Res., Doi: 10.1016/j.neures.2011.05.008.
    • (2011) Neurosci. Res.
    • Lee, S.-J.1    Lim, H.-S.2    Masliah, E.3    Lee, H.-J.4
  • 104
    • 77953491510 scopus 로고    scopus 로고
    • Proteomic profiling of the dystrophin-deficient MDX heart reveals drastically altered levels of key metabolic and contractile proteins
    • Doi: 10.1155/2010/648501
    • Lewis, C., Jockusch, H. and Ohlendieck, K. (2010). Proteomic profiling of the dystrophin-deficient MDX heart reveals drastically altered levels of key metabolic and contractile proteins. J. Biomed Biotechnol.,Doi: 10.1155/2010/648501.
    • (2010) J. Biomed Biotechnol.
    • Lewis, C.1    Jockusch, H.2    Ohlendieck, K.3
  • 105
    • 0028953495 scopus 로고
    • Growth cone advance is inversely proportional to retrograde F-actin flow
    • Lin, C.H. and Forscher, P. (1995). Growth cone advance is inversely proportional to retrograde F-actin flow. Neuron, 14, 763-771.
    • (1995) Neuron , vol.14 , pp. 763-771
    • Lin, C.H.1    Forscher, P.2
  • 106
    • 34347347236 scopus 로고    scopus 로고
    • Cofilin-mediated neurodegeneration in Alzheimer's disease and other amyloidopathies
    • Maloney, M.T. and Bamburg, J.R. (2007). Cofilin-mediated neurodegeneration in Alzheimer's disease and other amyloidopathies.Mol.Neurobiol., 35, 21-44.
    • (2007) Mol.Neurobiol. , vol.35 , pp. 21-44
    • Maloney, M.T.1    Bamburg, J.R.2
  • 107
    • 30544447666 scopus 로고    scopus 로고
    • Beta-secretase-cleaved amyloid precursor protein accumulates at actin inclusions induced in neurons by stress or amyloid-beta: a feedforward mechanism for Alzheimers disease
    • Maloney, M.T., Minamide, L.S., Kinley, A.W., Boyle, J.A. and Bamburg, J.R. (2005). Beta-secretase-cleaved amyloid precursor protein accumulates at actin inclusions induced in neurons by stress or amyloid-beta: a feedforward mechanism for Alzheimers disease. J.Neurosci., 25, 11313-11321.
    • (2005) J.Neurosci. , vol.25 , pp. 11313-11321
    • Maloney, M.T.1    Minamide, L.S.2    Kinley, A.W.3    Boyle, J.A.4    Bamburg, J.R.5
  • 108
    • 79960361814 scopus 로고    scopus 로고
    • Recent advances in the genetics of Parkinson's disease
    • doi: 10.1146/annurev-genom-082410-101440
    • Martin, I., Dawson, V.L. and Dawson, T.M. (2011). Recent advances in the genetics of Parkinson's disease. Annu Rev Genom Hum Genet 12, doi: 10.1146/annurev-genom-082410-101440.
    • (2011) Annu Rev Genom Hum Genet , vol.12
    • Martin, I.1    Dawson, V.L.2    Dawson, T.M.3
  • 110
    • 0038737042 scopus 로고    scopus 로고
    • Actin dynamics control SRF activity by regulation of its coactivator MAL
    • Miralles, F., Posern, G., Zaramytidou, A.I. and Treisman, R. (2003). Actin dynamics control SRF activity by regulation of its coactivator MAL. Cell, 113, 329-342.
    • (2003) Cell , vol.113 , pp. 329-342
    • Miralles, F.1    Posern, G.2    Zaramytidou, A.I.3    Treisman, R.4
  • 111
    • 33646495978 scopus 로고    scopus 로고
    • Actin in transcription and transcription regulation
    • Miralles, F. and Visa, N. (2006). Actin in transcription and transcription regulation.Curr. Opin. Cell Biol., 18, 261-266.
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 261-266
    • Miralles, F.1    Visa, N.2
  • 112
    • 0022416568 scopus 로고
    • Ultrastructural localization of actin in nuclear matrices from mouse leukemia L5178Y cells
    • Nakayasu, H. and Ueda, K. (1985). Ultrastructural localization of actin in nuclear matrices from mouse leukemia L5178Y cells. Cell Struct Func, 10, 305-309.
    • (1985) Cell Struct Func , vol.10 , pp. 305-309
    • Nakayasu, H.1    Ueda, K.2
  • 113
    • 78149469722 scopus 로고    scopus 로고
    • RhoA/Rho-kinase and vascular diseases: what is the link? Cell Mol
    • Nunes, K.P., Rigsby, C.S. and Webb, R.C. (2010). RhoA/Rho-kinase and vascular diseases: what is the link? Cell Mol. Life Sci., 67, 3823-3826.
    • (2010) Life Sci. , vol.67 , pp. 3823-3826
    • Nunes, K.P.1    Rigsby, C.S.2    Webb, R.C.3
  • 115
    • 84892343184 scopus 로고    scopus 로고
    • Diseases with abnormal actin in actin-binding proteins in leukocyte and nonmuscle cells
    • Nunoi, H. (2008). Diseases with abnormal actin in actin-binding proteins in leukocyte and nonmuscle cells.Protein Rev., 8, 278-289.
    • (2008) Protein Rev. , vol.8 , pp. 278-289
    • Nunoi, H.1
  • 116
    • 7044267351 scopus 로고    scopus 로고
    • Rapid and persistent modulation of actin dynamics regulates postsynaptic reorganization underlying bidirectional plasticity
    • Okamoto, K., Nagai, T., Miyawaki, A. and Hayashi, Y. (2004). Rapid and persistent modulation of actin dynamics regulates postsynaptic reorganization underlying bidirectional plasticity. Nature Neurosci., 7, 1104-1112.
    • (2004) Nature Neurosci. , vol.7 , pp. 1104-1112
    • Okamoto, K.1    Nagai, T.2    Miyawaki, A.3    Hayashi, Y.4
  • 117
    • 0032936755 scopus 로고    scopus 로고
    • Etiology and pathogenesis of Parkinson's disease
    • Olanow, C.W. and Tatton, W.G. (1999). Etiology and pathogenesis of Parkinson's disease.Annu. Rev.Neurosci., 22, 123-144.
    • (1999) Annu. Rev.Neurosci. , vol.22 , pp. 123-144
    • Olanow, C.W.1    Tatton, W.G.2
  • 118
    • 0035997387 scopus 로고    scopus 로고
    • Nuclear actin and actin-related proteins in chromatin remodeling
    • Olave, I.A., Reck-Peterson, S.L. and Crabtree, G.R. (2002). Nuclear actin and actin-related proteins in chromatin remodeling.Ann. Rev.Biochem., 71, 755-781.
    • (2002) Ann. Rev.Biochem. , vol.71 , pp. 755-781
    • Olave, I.A.1    Reck-Peterson, S.L.2    Crabtree, G.R.3
  • 119
    • 77958557373 scopus 로고    scopus 로고
    • Our trials and trials in the subsarcolemmal cytoskeleton network and muscular dystrophy researches in the dystrophin era
    • Ozawa, E. (2010).Our trials and trials in the subsarcolemmal cytoskeleton network and muscular dystrophy researches in the dystrophin era.Proc. Jpn Acad.Sci., 86, 798-820.
    • (2010) Proc. Jpn Acad.Sci. , vol.86 , pp. 798-820
    • Ozawa, E.1
  • 121
    • 77956064817 scopus 로고    scopus 로고
    • Cell adhesion: integrating cytoskeletal dynamics and cellular tension
    • Parsons, J.T., Horwitz, A.R. and Schartz, M.A. (2010). Cell adhesion: integrating cytoskeletal dynamics and cellular tension. Nature Rev. Mol.Cell Biol., 11, 633-643.
    • (2010) Nature Rev. Mol.Cell Biol. , vol.11 , pp. 633-643
    • Parsons, J.T.1    Horwitz, A.R.2    Schartz, M.A.3
  • 122
    • 0025990831 scopus 로고
    • Phosphoinositide kinase, diacylglycerol kinase, and phospholipase C activities associated to the cytoskeleton: effect of epidermal growth factor
    • Payrastre, B., van Bergen en Henegouwen, P.M.P., Breton, M., den Hartigh, J.C., Plantavid, M., Verkleij, A.J. and Boonstra, J. (1991). Phosphoinositide kinase, diacylglycerol kinase, and phospholipase C activities associated to the cytoskeleton: effect of epidermal growth factor. J.Cell Biol., 115, 121-128.
    • (1991) J.Cell Biol. , vol.115 , pp. 121-128
    • Payrastre, B.1    van Bergen en Henegouwen, P.M.P.2    Breton, M.3    den Hartigh, J.C.4    Plantavid, M.5    Verkleij, A.J.6    Boonstra, J.7
  • 123
    • 84892284078 scopus 로고    scopus 로고
    • Impaired regulation of synaptic actin cytoskeleton in Alzheimer's disease
    • Penzes, P. and van Leeuwen, J.E. (2011). Impaired regulation of synaptic actin cytoskeleton in Alzheimer's disease.Br.Res.Rev , 20, 1-9.
    • (2011) Br.Res.Rev , vol.20 , pp. 1-9
    • Penzes, P.1    van Leeuwen, J.E.2
  • 124
    • 33645285000 scopus 로고    scopus 로고
    • Molecular functions of nuclear actin in transcription
    • Percipalle, P. and Visa, N. (2006). Molecular functions of nuclear actin in transcription.J. Cell Biol., 172, 967-971.
    • (2006) J. Cell Biol. , vol.172 , pp. 967-971
    • Percipalle, P.1    Visa, N.2
  • 125
    • 33746706949 scopus 로고    scopus 로고
    • Spatial control of actin organization at adherens junctions by a synaptotagmin like protein Btsz
    • Pilot, F., Philippe, J., Lemmers, C. and Lecuit, T. (2006).Spatial control of actin organization at adherens junctions by a synaptotagmin like protein Btsz.Nature, 442, 580-584.
    • (2006) Nature , vol.442 , pp. 580-584
    • Pilot, F.1    Philippe, J.2    Lemmers, C.3    Lecuit, T.4
  • 126
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard, T. D. and Borisy, G. G. (2003).Cellular motility driven by assembly and disassembly of actin filaments.Cell, 112, 453-465.
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 129
    • 77950858612 scopus 로고    scopus 로고
    • NuMA after 30 years: the matrix revisited
    • Radulescu, A.E. and Cleveland, D.W. (2010). NuMA after 30 years: the matrix revisited. Trends Cell Biol., 20, 214-222.
    • (2010) Trends Cell Biol. , vol.20 , pp. 214-222
    • Radulescu, A.E.1    Cleveland, D.W.2
  • 130
    • 0030039226 scopus 로고    scopus 로고
    • Catenins and zonula occludens-1 form a complex during early stages in the assembly of tight junctions
    • Rajasekaran, A.K., Hojo, M., Huima, T. and Rodriguez-Boulan, E. (1996). Catenins and zonula occludens-1 form a complex during early stages in the assembly of tight junctions. J. Cell Biol., 132, 451-463.
    • (1996) J. Cell Biol. , vol.132 , pp. 451-463
    • Rajasekaran, A.K.1    Hojo, M.2    Huima, T.3    Rodriguez-Boulan, E.4
  • 131
    • 0034627878 scopus 로고    scopus 로고
    • Cell spreading and lamellipodial extension rate is regulated by membrane tension
    • Raucher, D. and Sheetz, M.P. (2000). Cell spreading and lamellipodial extension rate is regulated by membrane tension. J. Cell Biol., 148, 127-136.
    • (2000) J. Cell Biol. , vol.148 , pp. 127-136
    • Raucher, D.1    Sheetz, M.P.2
  • 133
    • 63849095895 scopus 로고    scopus 로고
    • Control of the postsynaptic membrane viscosity
    • Renner, M., Choquet, D. and Triller, A. (2009).Control of the postsynaptic membrane viscosity.J.Neurosci., 29, 2926-2937.
    • (2009) J.Neurosci. , vol.29 , pp. 2926-2937
    • Renner, M.1    Choquet, D.2    Triller, A.3
  • 134
    • 0022922682 scopus 로고
    • Cytoplasmic concentrations of inorganic phosphate affect the critical concentrations for actin assembly in the presence of cytochalasin D or ADP
    • Rickard, J.E. and Sheterline, P. (1986). Cytoplasmic concentrations of inorganic phosphate affect the critical concentrations for actin assembly in the presence of cytochalasin D or ADP. J. Mol.Biol., 191, 273-280.
    • (1986) J. Mol.Biol. , vol.191 , pp. 273-280
    • Rickard, J.E.1    Sheterline, P.2
  • 136
    • 0028303798 scopus 로고
    • Searchin for the 1 in 2,400,000: a review of dystrophin gene point mutations
    • Roberts, R.G., Gardner, R.J. and Bobrow, M. (1994). Searchin for the 1 in 2,400,000: a review of dystrophin gene point mutations. Hum Mutat, 4, 1-11.
    • (1994) Hum Mutat , vol.4 , pp. 1-11
    • Roberts, R.G.1    Gardner, R.J.2    Bobrow, M.3
  • 137
    • 0034605070 scopus 로고    scopus 로고
    • The dystrophin complex forms a mechanically strong link between the sarcolemma and costameric actin
    • Rybakova, I.N., Patel, J.R. and Ervasti, J.M. (2000) The dystrophin complex forms a mechanically strong link between the sarcolemma and costameric actin. J. Cell Biol., 150, 1209-1214.
    • (2000) J. Cell Biol. , vol.150 , pp. 1209-1214
    • Rybakova, I.N.1    Patel, J.R.2    Ervasti, J.M.3
  • 138
    • 4444326252 scopus 로고    scopus 로고
    • Actin myopathy with nemaline bodies, intranuclear rods, and a heterozygous mutation in ACTA1 (Asp154Asn)
    • Schöder, J.M., Durling, H. and Laing, N. (2004). Actin myopathy with nemaline bodies, intranuclear rods, and a heterozygous mutation in ACTA1 (Asp154Asn).Act. Neuropath, 108, 250-256.
    • (2004) Act. Neuropath , vol.108 , pp. 250-256
    • Schöder, J.M.1    Durling, H.2    Laing, N.3
  • 139
    • 28944449940 scopus 로고    scopus 로고
    • Conformation-specific antibodies reveal distinct actin structures in the nucleus and the cytoplasm
    • Schoenenberger, C.A., Buchmeier, S., Boerries, M., Sutterlin, R., Aebi, U. and Jockusch, B.M. (2005). Conformation-specific antibodies reveal distinct actin structures in the nucleus and the cytoplasm. J. Struct Biol., 152, 157-168.
    • (2005) J. Struct Biol. , vol.152 , pp. 157-168
    • Schoenenberger, C.A.1    Buchmeier, S.2    Boerries, M.3    Sutterlin, R.4    Aebi, U.5    Jockusch, B.M.6
  • 140
    • 33947314641 scopus 로고    scopus 로고
    • Natural oligomers of the Alzheimer amyloid-beta protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway
    • Shankar, G.M., Bloodgood, B.L., Townsend, M., Walsh, D.M., Selkoe, D.J. and Sabatini, B.L. (2007). Natural oligomers of the Alzheimer amyloid-beta protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway. J.Neurosci., 27, 2866-2875.
    • (2007) J.Neurosci. , vol.27 , pp. 2866-2875
    • Shankar, G.M.1    Bloodgood, B.L.2    Townsend, M.3    Walsh, D.M.4    Selkoe, D.J.5    Sabatini, B.L.6
  • 141
    • 77954326094 scopus 로고    scopus 로고
    • Myosin light chain kinase in microvascular endothelial barrier function
    • Shen, Q., Rigor, R.R., Pivetti, C.D., Wu, M.H. and Yuan, S.Y. (2010). Myosin light chain kinase in microvascular endothelial barrier function.Cardiovasc Res, 87, 272-280.
    • (2010) Cardiovasc Res , vol.87 , pp. 272-280
    • Shen, Q.1    Rigor, R.R.2    Pivetti, C.D.3    Wu, M.H.4    Yuan, S.Y.5
  • 142
    • 33845699085 scopus 로고    scopus 로고
    • Actin regulation in endocytosis
    • Smythe, E. and Ayscough, K.R. (2006). Actin regulation in endocytosis.J. Cell Sci., 119, 4589-4598
    • (2006) J. Cell Sci. , vol.119 , pp. 4589-4598
    • Smythe, E.1    Ayscough, K.R.2
  • 145
  • 146
    • 43949104415 scopus 로고    scopus 로고
    • Physiologic properties and regulation of the actin cytoskeleton in vascular smooth muscle
    • Tang, D.D. and Anfinogenova, Y. (2008). Physiologic properties and regulation of the actin cytoskeleton in vascular smooth muscle.J. Cardiovasc. Pharmacol.therapeut, 13, 130-140.
    • (2008) J. Cardiovasc. Pharmacol.therapeut , vol.13 , pp. 130-140
    • Tang, D.D.1    Anfinogenova, Y.2
  • 147
    • 0025740949 scopus 로고
    • Actin microfilament dynamics in locomoting cells
    • Theriot, J.A. and Mitchison, T.J. (1991). Actin microfilament dynamics in locomoting cells.Nature, 352, 126-131.
    • (1991) Nature , vol.352 , pp. 126-131
    • Theriot, J.A.1    Mitchison, T.J.2
  • 149
    • 56649088324 scopus 로고    scopus 로고
    • A review of actin binding proteins: new perspectives
    • Uribe, R. and Jay, D. (2009). A review of actin binding proteins: new perspectives. Mol. Biol. Rep., 36, 121-125.
    • (2009) Mol. Biol. Rep. , vol.36 , pp. 121-125
    • Uribe, R.1    Jay, D.2
  • 150
    • 0042845698 scopus 로고    scopus 로고
    • Targets for pharmacological intervention of endothelial hyperpermeability and barrier function
    • van Nieuw Amerongen, G.P., and van Hinsbergh, V.W. (2002). Targets for pharmacological intervention of endothelial hyperpermeability and barrier function.Vascul. Pharmacol.39, 257-272.
    • (2002) Vascul. Pharmacol. , vol.39 , pp. 257-272
    • van Nieuw Amerongen, G.P.1    van Hinsbergh, V.W.2
  • 153
    • 77950887914 scopus 로고    scopus 로고
    • Myopathy-causing actin mutations promote defects in serum response factor signaling
    • Visegrady, B. and Machesky, L.M. (2009). Myopathy-causing actin mutations promote defects in serum response factor signaling. Biochem. J., 427, 41-48.
    • (2009) Biochem. J. , vol.427 , pp. 41-48
    • Visegrady, B.1    Machesky, L.M.2
  • 154
    • 0033625535 scopus 로고    scopus 로고
    • The EAST protein of Drosophila controls an expandable nuclear endoskeleton
    • Wasser, M. and Chia, W. (2000). The EAST protein of Drosophila controls an expandable nuclear endoskeleton. Nature Cell Biol.,2, 268-275.
    • (2000) Nature Cell Biol. , vol.2 , pp. 268-275
    • Wasser, M.1    Chia, W.2
  • 155
    • 70350435136 scopus 로고    scopus 로고
    • Activated ADF/cofilin sequesters phosphorylated microtubule-associated-protein during the assembly of Alzheimer-like neuritic cytoskeletal striations
    • doi: 10.1523/JNEUROSCI.3531-09.2009
    • Whiteman, I.T., Gervasio, O.L., Cullen, K.M., Guillemin, G.J., Jeong, E.V., Witting, P.K., Antao, S.T., Minamide, L.S., Bamburg, J.R. and Goldsbury, C. (2009). Activated ADF/cofilin sequesters phosphorylated microtubule-associated-protein during the assembly of Alzheimer-like neuritic cytoskeletal striations. J.Neurosci., 29, doi: 10.1523/JNEUROSCI.3531-09.2009
    • (2009) J.Neurosci. , vol.29
    • Whiteman, I.T.1    Gervasio, O.L.2    Cullen, K.M.3    Guillemin, G.J.4    Jeong, E.V.5    Witting, P.K.6    Antao, S.T.7    Minamide, L.S.8    Bamburg, J.R.9    Goldsbury, C.10
  • 156
    • 75749111318 scopus 로고    scopus 로고
    • Immune pathology associated with altered actin cytoskeleton regulation
    • Wickramarachchi, D.C., Theofilopoulos, A.N. and Kono, D.H. (2010). Immune pathology associated with altered actin cytoskeleton regulation. Autoimmun, 43, 64-75.
    • (2010) Autoimmun , vol.43 , pp. 64-75
    • Wickramarachchi, D.C.1    Theofilopoulos, A.N.2    Kono, D.H.3
  • 157
    • 0022512060 scopus 로고
    • Epidermal growth factor receptors associated to cytoskeletal elements of epidermoid carcinoma (A431) cells
    • Wiegant, F.A.C., Blok, F. J., Defize, L.H.K., Linnemans, W.A.M., Verkleij, A.J. and Boonstra, J. (1986). Epidermal growth factor receptors associated to cytoskeletal elements of epidermoid carcinoma (A431) cells. J. Cell Biol., 103, 87-94.
    • (1986) J. Cell Biol. , vol.103 , pp. 87-94
    • Wiegant, F.A.C.1    Blok, F.J.2    Defize, L.H.K.3    Linnemans, W.A.M.4    Verkleij, A.J.5    Boonstra, J.6
  • 158
    • 79953653114 scopus 로고    scopus 로고
    • The Parkinson disease protein a-synuclein inhibits autophagy
    • Winslow, A. and Rubinsztein, D.C. (2011). The Parkinson disease protein a-synuclein inhibits autophagy. Autophagy, 7, 429-431.
    • (2011) Autophagy , vol.7 , pp. 429-431
    • Winslow, A.1    Rubinsztein, D.C.2
  • 159
    • 34247468876 scopus 로고    scopus 로고
    • Regulation of the actin cytoskeleton in cancer cell migration and invasion
    • Yamaguchi, H. and Condeelis, J. (2006). Regulation of the actin cytoskeleton in cancer cell migration and invasion.Biochim. Biophys.Acta, 1773, 642-652.
    • (2006) Biochim. Biophys.Acta , vol.1773 , pp. 642-652
    • Yamaguchi, H.1    Condeelis, J.2
  • 160
    • 20444451210 scopus 로고    scopus 로고
    • Parkin stabilizes microtubules through strong binding mediated by three independent domains
    • Yang, F., Jiang, Q., Zhao, J., Ren, Y., Sutton, M.D. and Feng, J. (2005). Parkin stabilizes microtubules through strong binding mediated by three independent domains. J. Biol.Chem., 280, 17154-17162
    • (2005) J. Biol.Chem. , vol.280 , pp. 17154-17162
    • Yang, F.1    Jiang, Q.2    Zhao, J.3    Ren, Y.4    Sutton, M.D.5    Feng, J.6
  • 161
    • 0038311944 scopus 로고    scopus 로고
    • Phosphoinositide regulation of the actin cytoskeleton
    • Yin, H.L. and Janmey, P.A. (2003).Phosphoinositide regulation of the actin cytoskeleton.Ann. Rev.Physiol., 65, 761-789.
    • (2003) Ann. Rev.Physiol. , vol.65 , pp. 761-789
    • Yin, H.L.1    Janmey, P.A.2
  • 162
  • 163
    • 0035833255 scopus 로고    scopus 로고
    • Myosin II dynamics and cortical flow Turing contractile ring formation in Dictyostelium cells
    • Yumura, S. (2001). Myosin II dynamics and cortical flow Turing contractile ring formation in Dictyostelium cells. J. Cell Biol., 154, 137-146.
    • (2001) J. Cell Biol. , vol.154 , pp. 137-146
    • Yumura, S.1
  • 164
    • 0029814578 scopus 로고    scopus 로고
    • Nuclear lamina and nuclear matrix organization in sperm pronuclei assembled in Xenopus egg extract
    • Zhang, C., Jenkins, H., Goldberg, M. W., Allen, T. D. and Hutchison, C. J. (1996). Nuclear lamina and nuclear matrix organization in sperm pronuclei assembled in Xenopus egg extract. J. Cell Sci., 109, 2275-2286.
    • (1996) J. Cell Sci. , vol.109 , pp. 2275-2286
    • Zhang, C.1    Jenkins, H.2    Goldberg, M.W.3    Allen, T.D.4    Hutchison, C.J.5
  • 165
    • 70350431889 scopus 로고    scopus 로고
    • Contributions of Wiskott-Aldrich syndrome family cytoskeletal regulatory adapters to immune regulation
    • Zhang, J., Dong, B. and Siminovitch, K.A. (2009). Contributions of Wiskott-Aldrich syndrome family cytoskeletal regulatory adapters to immune regulation.Immunolog.Rev., 232, 175-194.
    • (2009) Immunolog.Rev. , vol.232 , pp. 175-194
    • Zhang, J.1    Dong, B.2    Siminovitch, K.A.3
  • 166
    • 14844293207 scopus 로고    scopus 로고
    • PAK and other Rho-associated kinases--effectors with surprisingly diverse mechanisms of regulation
    • Zhao, Z.S. and Manser, E. (2005). PAK and other Rho-associated kinases--effectors with surprisingly diverse mechanisms of regulation.Biochem. J., 386, 201-214.
    • (2005) Biochem. J. , vol.386 , pp. 201-214
    • Zhao, Z.S.1    Manser, E.2
  • 168
    • 79952455313 scopus 로고    scopus 로고
    • Rho-associated coiled-coil-forming kinases (ROCKs): potential targets for the treatment of atherosclerosis and vascular disease
    • Zhou, Q., Gensch, C. and Liao, J.K. (2011). Rho-associated coiled-coil-forming kinases (ROCKs): potential targets for the treatment of atherosclerosis and vascular disease. Trends Pharmacol.Sci., 32, 1-7.
    • (2011) Trends Pharmacol.Sci. , vol.32 , pp. 1-7
    • Zhou, Q.1    Gensch, C.2    Liao, J.K.3
  • 169
    • 0030021649 scopus 로고    scopus 로고
    • Signal transduction and actin filament organization
    • Zigmond, S.H. (1996). Signal transduction and actin filament organization.Curr. Opin. Cell Biol, 8, 66-73.
    • (1996) Curr. Opin. Cell Biol , vol.8 , pp. 66-73
    • Zigmond, S.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.