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Volumn 3, Issue 8, 2008, Pages

The actin-binding protein capulet genetically interacts with the microtubule motor kinesin to maintain neuronal dendrite homeostasis

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN BINDING PROTEIN; CAPULET; COFILIN; KINESIN; UNCLASSIFIED DRUG; ACTIN; ACTIN DEPOLYMERIZING FACTOR; CAPT PROTEIN, DROSOPHILA; DROSOPHILA PROTEIN;

EID: 52449113751     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0003054     Document Type: Article
Times cited : (16)

References (57)
  • 1
    • 0036264824 scopus 로고    scopus 로고
    • The ADF/cofilin family: Actin-remodeling proteins
    • reviews3007
    • Maciver SK, Hussey PJ (2002) The ADF/cofilin family: actin-remodeling proteins. Genome Biol 3: reviews3007.
    • (2002) Genome Biol , vol.3
    • Maciver, S.K.1    Hussey, P.J.2
  • 2
    • 33847295719 scopus 로고    scopus 로고
    • Mechanism of depolymerization and severing of actin filaments and its significance in cytoskeletal dynamics
    • Ono S (2007) Mechanism of depolymerization and severing of actin filaments and its significance in cytoskeletal dynamics. Int Rev Cytol 258: 1-82.
    • (2007) Int Rev Cytol , vol.258 , pp. 1-82
    • Ono, S.1
  • 4
    • 0348011602 scopus 로고    scopus 로고
    • Regulation of the neuronal actin cytoskeleton by ADF/cofilin
    • Sarmiere PD, Bamburg JR (2004) Regulation of the neuronal actin cytoskeleton by ADF/cofilin. J Neurobiol 58: 103-117.
    • (2004) J Neurobiol , vol.58 , pp. 103-117
    • Sarmiere, P.D.1    Bamburg, J.R.2
  • 5
    • 0037039167 scopus 로고    scopus 로고
    • Cofilin produces newly polymerized actin filaments that are preferred for dendritic, nucleation by the Arp2/3 complex
    • Ichetovkin I, Grant W, Condeelis J (2002) Cofilin produces newly polymerized actin filaments that are preferred for dendritic, nucleation by the Arp2/3 complex. Curr Biol 12: 79-84.
    • (2002) Curr Biol , vol.12 , pp. 79-84
    • Ichetovkin, I.1    Grant, W.2    Condeelis, J.3
  • 7
    • 0030820734 scopus 로고    scopus 로고
    • Cofilin changes the twist of F-actin: Implications for actin filament dynamics and cellular function
    • McGough A, Pope B, Chiu W, Weeds A (1997) Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function. J Cell Biol 138: 771-781.
    • (1997) J Cell Biol , vol.138 , pp. 771-781
    • McGough, A.1    Pope, B.2    Chiu, W.3    Weeds, A.4
  • 8
    • 2642580847 scopus 로고    scopus 로고
    • In vitro activity differences between proteins ofthe ADF/cofilin family define two distinct subgroups
    • Chen H, Bernstein BW, Sneider JM, Boyle JA, Minamide LS, et al. (2004) In vitro activity differences between proteins ofthe ADF/cofilin family define two distinct subgroups. Biochemistry 43: 7127-7142.
    • (2004) Biochemistry , vol.43 , pp. 7127-7142
    • Chen, H.1    Bernstein, B.W.2    Sneider, J.M.3    Boyle, J.A.4    Minamide, L.S.5
  • 9
    • 0032475981 scopus 로고    scopus 로고
    • Synergy between actin depolymerizing factor/cofilin and profilin in increasing actin filament turnover
    • Didry D, Carlier MF, Pantaloni D (1998) Synergy between actin depolymerizing factor/cofilin and profilin in increasing actin filament turnover. J Biol Chem 273: 25602-25611.
    • (1998) J Biol Chem , vol.273 , pp. 25602-25611
    • Didry, D.1    Carlier, M.F.2    Pantaloni, D.3
  • 10
    • 0036856301 scopus 로고    scopus 로고
    • Cofilin, but not profilin, is required for myosin-I-induced actin polymerization and the endocytic uptake in yeast
    • Idrissi FZ, Wolf BL, Geli MI (2002) Cofilin, but not profilin, is required for myosin-I-induced actin polymerization and the endocytic uptake in yeast. Mol Biel Cell 13: 4074-4087.
    • (2002) Mol Biel Cell , vol.13 , pp. 4074-4087
    • Idrissi, F.Z.1    Wolf, B.L.2    Geli, M.I.3
  • 11
    • 0036304481 scopus 로고    scopus 로고
    • Determining the differences in actin binding by human ADF and coffin
    • Yeoh S, Pope B, Mannherz HG, Weeds A (2002) Determining the differences in actin binding by human ADF and coffin. J Mol Biol 315: 911-925.
    • (2002) J Mol Biol , vol.315 , pp. 911-925
    • Yeoh, S.1    Pope, B.2    Mannherz, H.G.3    Weeds, A.4
  • 12
    • 0036205611 scopus 로고    scopus 로고
    • Cyclase-associated proteins: CAPacity for linking signal transduction and actin polymerization
    • Hubberstey AV, Mottillo EP (2002) Cyclase-associated proteins: CAPacity for linking signal transduction and actin polymerization. Faseb J 16: 487-499.
    • (2002) Faseb J , vol.16 , pp. 487-499
    • Hubberstey, A.V.1    Mottillo, E.P.2
  • 13
    • 0037093266 scopus 로고    scopus 로고
    • Human CAPI is a key factor in the recycling of cofilin and actin for rapid actin turnover
    • Moriyama K, Yahara I (2002) Human CAPI is a key factor in the recycling of cofilin and actin for rapid actin turnover. J Cell Sci 115: 1591-1601.
    • (2002) J Cell Sci , vol.115 , pp. 1591-1601
    • Moriyama, K.1    Yahara, I.2
  • 14
    • 0347664159 scopus 로고    scopus 로고
    • Coordinated regulation of actin filament turnover by a high-molecular-weight Srv2/CAP complex, cofilin, profilin, and Aipl
    • Balcer HI, Goodman AL, Rodal AA, Smith E, Kugler J, et al. (2003) Coordinated regulation of actin filament turnover by a high-molecular-weight Srv2/CAP complex, cofilin, profilin, and Aipl. Curr Biol 13: 2159-2169.
    • (2003) Curr Biol , vol.13 , pp. 2159-2169
    • Balcer, H.I.1    Goodman, A.L.2    Rodal, A.A.3    Smith, E.4    Kugler, J.5
  • 15
    • 0027772556 scopus 로고
    • How profilin promotes actin filament assembly in the presence of thymosin beta 4
    • Pantaloni D, Carlier MF (1993) How profilin promotes actin filament assembly in the presence of thymosin beta 4. Cell 75: 1007-1014.
    • (1993) Cell , vol.75 , pp. 1007-1014
    • Pantaloni, D.1    Carlier, M.F.2
  • 16
    • 15844401321 scopus 로고    scopus 로고
    • Role of nucleotide exchange and hydrolysis in the function of profilin in action assembly
    • Perelroizen I, Didry D, Christensen H, Chua NH, Carlier MF (1996) Role of nucleotide exchange and hydrolysis in the function of profilin in action assembly. J Biol Chem 271: 12302-12309.
    • (1996) J Biol Chem , vol.271 , pp. 12302-12309
    • Perelroizen, I.1    Didry, D.2    Christensen, H.3    Chua, N.H.4    Carlier, M.F.5
  • 17
    • 0032538888 scopus 로고    scopus 로고
    • The essential role of profilin in the assembly of actin for microspike formation
    • Suetsugu S, Miki H, Takenawa, T (1998) The essential role of profilin in the assembly of actin for microspike formation. Embo J 17: 651-6526.
    • (1998) Embo J , vol.17 , pp. 651-6526
    • Suetsugu, S.1    Miki, H.2    Takenawa, T.3
  • 18
    • 0034710563 scopus 로고    scopus 로고
    • A cyclase-associated protein regulates actin and cell polarity during Drosophila oogenesis and in yeast
    • Baum B, Li W, Perrimon N (2000) A cyclase-associated protein regulates actin and cell polarity during Drosophila oogenesis and in yeast. Corr Biol 10: 964-973.
    • (2000) Corr Biol , vol.10 , pp. 964-973
    • Baum, B.1    Li, W.2    Perrimon, N.3
  • 19
    • 26244451431 scopus 로고    scopus 로고
    • Influence of Notch on dorsoventral compartmentalization and actin organization in the Drosophila wing
    • Major RJ, Irvine KD (2005) Influence of Notch on dorsoventral compartmentalization and actin organization in the Drosophila wing. Development 132: 3823-3833.
    • (2005) Development , vol.132 , pp. 3823-3833
    • Major, R.J.1    Irvine, K.D.2
  • 20
    • 0034724535 scopus 로고    scopus 로고
    • act up controls actin polymerization to alter cell shape and restrict Hedgehog signaling in the Drosophila eye disc
    • Benlali A, Draskovic I, Hazelett DJ, Treisman JE (2000) act up controls actin polymerization to alter cell shape and restrict Hedgehog signaling in the Drosophila eye disc. Cell 101: 271-281.
    • (2000) Cell , vol.101 , pp. 271-281
    • Benlali, A.1    Draskovic, I.2    Hazelett, D.J.3    Treisman, J.E.4
  • 21
    • 0037079061 scopus 로고    scopus 로고
    • A Drosophila homolog of cyclase-associated proteins collaborates with the Ab1 tyrosine kinase to control midline axon pathfinding
    • Wills Z, Emerson M, Rusch J, Bikoff J, Baum B, et al. (2002) A Drosophila homolog of cyclase-associated proteins collaborates with the Ab1 tyrosine kinase to control midline axon pathfinding. Neuron 36: 611-622.
    • (2002) Neuron , vol.36 , pp. 611-622
    • Wills, Z.1    Emerson, M.2    Rusch, J.3    Bikoff, J.4    Baum, B.5
  • 22
    • 24344465919 scopus 로고    scopus 로고
    • Analysis of the kinesin superfamily: Insights into structure and function
    • Miki H, Okada Y, Hirokawa N (2005) Analysis of the kinesin superfamily: insights into structure and function. Trends Cell Biol 15: 467-476.
    • (2005) Trends Cell Biol , vol.15 , pp. 467-476
    • Miki, H.1    Okada, Y.2    Hirokawa, N.3
  • 23
    • 33646189851 scopus 로고    scopus 로고
    • A novel forward genetic screen for identifying mutations affecting larval neuronal dendrite development in Drosophila melanogaster
    • Medina PM, Swick LL, Andersen R, Blalock Z, Brenman JE (2006) A novel forward genetic screen for identifying mutations affecting larval neuronal dendrite development in Drosophila melanogaster. Genetics 172: 2325-2335.
    • (2006) Genetics , vol.172 , pp. 2325-2335
    • Medina, P.M.1    Swick, L.L.2    Andersen, R.3    Blalock, Z.4    Brenman, J.E.5
  • 24
    • 0035215432 scopus 로고    scopus 로고
    • Novel protein domains and repeats in Drosophila melanogaster: Insights into structure, function, and evolution
    • Ponting CP, Mott R, Bork P, Copley RR (2001) Novel protein domains and repeats in Drosophila melanogaster: insights into structure, function, and evolution. Genome Res 11: 1996-2008.
    • (2001) Genome Res , vol.11 , pp. 1996-2008
    • Ponting, C.P.1    Mott, R.2    Bork, P.3    Copley, R.R.4
  • 25
    • 0026081344 scopus 로고
    • CAP is a bifunctional component of the Saccharomyces cerevisiae adenylyl cyclase complex
    • Gerst JE, Ferguson K, Vojtek A, Wigler M, Field J (1991) CAP is a bifunctional component of the Saccharomyces cerevisiae adenylyl cyclase complex. Mol Cell Biol 11: 1248-1257.
    • (1991) Mol Cell Biol , vol.11 , pp. 1248-1257
    • Gerst, J.E.1    Ferguson, K.2    Vojtek, A.3    Wigler, M.4    Field, J.5
  • 26
    • 0028920045 scopus 로고
    • An actin monomer binding activity localizes to the carboxyl-terminal half of the Saccharomyces cerevisiae cyclase-associated protein
    • Freeman NL, Chen Z, Horenstein J, Weber A, Field J (1995) An actin monomer binding activity localizes to the carboxyl-terminal half of the Saccharomyces cerevisiae cyclase-associated protein. J Biol Chem 270: 5680-5685.
    • (1995) J Biol Chem , vol.270 , pp. 5680-5685
    • Freeman, N.L.1    Chen, Z.2    Horenstein, J.3    Weber, A.4    Field, J.5
  • 27
    • 33644835262 scopus 로고    scopus 로고
    • The structural basis of actin interaction with multiple WH2/beta-thymosin motif-containing proteins
    • Aguda AH, Xue B, Irobi E, Preat T, Robinson RC (2006) The structural basis of actin interaction with multiple WH2/beta-thymosin motif-containing proteins. Structure 14: 469-476.
    • (2006) Structure , vol.14 , pp. 469-476
    • Aguda, A.H.1    Xue, B.2    Irobi, E.3    Preat, T.4    Robinson, R.C.5
  • 28
    • 33847420373 scopus 로고    scopus 로고
    • Mechanism of actin network attachment to moving membranes: Barbed end capture by N-WASP WH2 domains
    • Co C, Wong DT, Gierke S, Chang V, Taunton J (2007) Mechanism of actin network attachment to moving membranes: barbed end capture by N-WASP WH2 domains. Cell 128: 901 913.
    • (2007) Cell , vol.128 , pp. 901-913
    • Co, C.1    Wong, D.T.2    Gierke, S.3    Chang, V.4    Taunton, J.5
  • 29
    • 0030048768 scopus 로고    scopus 로고
    • A conserved proline-rich region of the Saccharomyces cerevisiae cyclase-associated protein binds SH3 domains and modulates cytoskeletal localization
    • Freeman NL, Lila T, Mintzer KA, Chen Z, Pahk AJ, et al. (1996) A conserved proline-rich region of the Saccharomyces cerevisiae cyclase-associated protein binds SH3 domains and modulates cytoskeletal localization. Mol Cell Biol 16: 548-556.
    • (1996) Mol Cell Biol , vol.16 , pp. 548-556
    • Freeman, N.L.1    Lila, T.2    Mintzer, K.A.3    Chen, Z.4    Pahk, A.J.5
  • 30
    • 0034785272 scopus 로고    scopus 로고
    • Spatial control of the actin cytoskeleton in Drosophila epithelial cells
    • Baum B, Perrimon N (2001) Spatial control of the actin cytoskeleton in Drosophila epithelial cells. Nat Cell Biol 3: 883-890.
    • (2001) Nat Cell Biol , vol.3 , pp. 883-890
    • Baum, B.1    Perrimon, N.2
  • 31
    • 25644437117 scopus 로고    scopus 로고
    • Calcium/ calmodulin-dependent protein kinase II alters structural plasticity and cytoskeletal dynamics in Drosophila
    • Andersen R, Li Y, Resseguie M, Brenman JE (2005) Calcium/ calmodulin-dependent protein kinase II alters structural plasticity and cytoskeletal dynamics in Drosophila. J Neurosci 25: 887-8888.
    • (2005) J Neurosci , vol.25 , pp. 887-8888
    • Andersen, R.1    Li, Y.2    Resseguie, M.3    Brenman, J.E.4
  • 32
    • 0020394540 scopus 로고
    • Cytoplasmic actin in neuronal processes as a possible mediator of synaptic plasticity
    • Fifkova E, Delay RJ (1982) Cytoplasmic actin in neuronal processes as a possible mediator of synaptic plasticity. J Cell Biol 95: 345-350.
    • (1982) J Cell Biol , vol.95 , pp. 345-350
    • Fifkova, E.1    Delay, R.J.2
  • 33
    • 0007292851 scopus 로고    scopus 로고
    • Matus A, Ackermann M, Pehling G, Byers HR, Fujiwara K (1982) High actin concentrations in brain dendritic spines and postsynaptic densities. Proc Natl Arad Sci U S A 79: 7590-7594.
    • Matus A, Ackermann M, Pehling G, Byers HR, Fujiwara K (1982) High actin concentrations in brain dendritic spines and postsynaptic densities. Proc Natl Arad Sci U S A 79: 7590-7594.
  • 34
    • 2342514815 scopus 로고    scopus 로고
    • Cyclase-associated protein 1 (CAP1) promotes cofilin-induced actin dynamics in mammalian nonmuscle cells
    • Bertling E, Hotulainen P, Mattila PK, Matilainen T, Salminen M, et al. (2004) Cyclase-associated protein 1 (CAP1) promotes cofilin-induced actin dynamics in mammalian nonmuscle cells. Mol Biol Cell 15: 2324-2334.
    • (2004) Mol Biol Cell , vol.15 , pp. 2324-2334
    • Bertling, E.1    Hotulainen, P.2    Mattila, P.K.3    Matilainen, T.4    Salminen, M.5
  • 35
    • 33751082967 scopus 로고    scopus 로고
    • Formation of actin-ADF/ cofilin rods transiently retards decline of mitochondrial potential and ATP in stressed neurons
    • Bernstein BW, Chen H, Boyle JA, Bamburg JR (2006) Formation of actin-ADF/ cofilin rods transiently retards decline of mitochondrial potential and ATP in stressed neurons. Am J Physiol Cell Physiol 291: C828-839.
    • (2006) Am J Physiol Cell Physiol , vol.291
    • Bernstein, B.W.1    Chen, H.2    Boyle, J.A.3    Bamburg, J.R.4
  • 36
    • 0034282106 scopus 로고    scopus 로고
    • Neurodegenerative stimuli induce persistent ADF/cofilin-actin rods that disrupt distal neurite function
    • Minamide LS, Striegl AM, Boyle JA, Meberg PJ, Bamburg JR (2000) Neurodegenerative stimuli induce persistent ADF/cofilin-actin rods that disrupt distal neurite function. Nat Cell Biol 2: 628-636.
    • (2000) Nat Cell Biol , vol.2 , pp. 628-636
    • Minamide, L.S.1    Striegl, A.M.2    Boyle, J.A.3    Meberg, P.J.4    Bamburg, J.R.5
  • 37
    • 34347347236 scopus 로고    scopus 로고
    • Cofilin-mediated neurodegeneration in Alzheimer's disease and other amyloidopathies
    • Maloney MT, Bamburg JR (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
  • 38
    • 0034703428 scopus 로고    scopus 로고
    • A function for kinesin I in the posterior transport of oskar mRNA and Staufen protein
    • Brendza RP, Serbus LR, Duffy JB, Saxton WM (2000) A function for kinesin I in the posterior transport of oskar mRNA and Staufen protein. Science 289: 2120-2122.
    • (2000) Science , vol.289 , pp. 2120-2122
    • Brendza, R.P.1    Serbus, L.R.2    Duffy, J.B.3    Saxton, W.M.4
  • 39
    • 30544452263 scopus 로고    scopus 로고
    • The axonal transport of mitochondria
    • Hollenbeck PJ, Saxton WM (2005) The axonal transport of mitochondria. J Cell Sci 118: 5411-5419.
    • (2005) J Cell Sci , vol.118 , pp. 5411-5419
    • Hollenbeck, P.J.1    Saxton, W.M.2
  • 40
    • 0029911064 scopus 로고    scopus 로고
    • Kinesin mutations cause motor neuron disease phenotypes by disrupting fast axonal transport in Drosophila
    • Hurd DD, Saxton WM (1996) Kinesin mutations cause motor neuron disease phenotypes by disrupting fast axonal transport in Drosophila. Genetics 144: 1075-1085.
    • (1996) Genetics , vol.144 , pp. 1075-1085
    • Hurd, D.D.1    Saxton, W.M.2
  • 41
    • 0026096809 scopus 로고
    • Kinesin heavy chain is essential for viability and neuromuscular functions in Drosophila, but mutants show no defects in mitosis
    • Saxton WM, Hicks J, Goldstein LS, Raff EC (1991) Kinesin heavy chain is essential for viability and neuromuscular functions in Drosophila, but mutants show no defects in mitosis. Cell 64: 1093-1102.
    • (1991) Cell , vol.64 , pp. 1093-1102
    • Saxton, W.M.1    Hicks, J.2    Goldstein, L.S.3    Raff, E.C.4
  • 43
    • 6344225310 scopus 로고    scopus 로고
    • A high-affinity interaction with ADP-actin monomers underlies the mechanism and in vivo function of Srv2/cyclase-associated protein
    • Mattila PK, Quintero-Monzon O, Kugler J, Moseley JB, Almo SC, et al. (2004) A high-affinity interaction with ADP-actin monomers underlies the mechanism and in vivo function of Srv2/cyclase-associated protein. Mol Biol Cell 15: 5158-5171.
    • (2004) Mol Biol Cell , vol.15 , pp. 5158-5171
    • Mattila, P.K.1    Quintero-Monzon, O.2    Kugler, J.3    Moseley, J.B.4    Almo, S.C.5
  • 44
    • 34848873760 scopus 로고    scopus 로고
    • Capu and Spire assemble a cytoplasmic actin mesh that maintains microtubule organization in the Drosophila oocyte
    • Dahlgaard K, Raposo AA, Niccoli T, St Johnston D (2007) Capu and Spire assemble a cytoplasmic actin mesh that maintains microtubule organization in the Drosophila oocyte. Dev Cell 13: 539-553.
    • (2007) Dev Cell , vol.13 , pp. 539-553
    • Dahlgaard, K.1    Raposo, A.A.2    Niccoli, T.3    St Johnston, D.4
  • 45
    • 0032559260 scopus 로고    scopus 로고
    • Kinesin and dynein superfamily proteins and the mechanism of organelle transport
    • Hirokawa N (1998) Kinesin and dynein superfamily proteins and the mechanism of organelle transport. Science 279: 519-526.
    • (1998) Science , vol.279 , pp. 519-526
    • Hirokawa, N.1
  • 46
    • 33745780575 scopus 로고    scopus 로고
    • Phosphorylation of actin-depolymerizing factor/cofilin by LIM-kinase mediates amytoid beta-induced degeneration: A potential mechanism of neuronal dystrophy in Alzheimer's disease
    • Heredia L, Helguera P, de Olmos S, Kedikian G, Sola Vigo F, et al. (2006) Phosphorylation of actin-depolymerizing factor/cofilin by LIM-kinase mediates amytoid beta-induced degeneration: a potential mechanism of neuronal dystrophy in Alzheimer's disease. J Neurosci 26: 6533-6542.
    • (2006) J Neurosci , vol.26 , pp. 6533-6542
    • Heredia, L.1    Helguera, P.2    de Olmos, S.3    Kedikian, G.4    Sola Vigo, F.5
  • 47
    • 33947230065 scopus 로고    scopus 로고
    • Tau is actin up in Alzheimer's disease
    • Gallo G (2007) Tau is actin up in Alzheimer's disease. Nat Cell Biol 9: 133-134.
    • (2007) Nat Cell Biol , vol.9 , pp. 133-134
    • Gallo, G.1
  • 48
    • 33947286683 scopus 로고    scopus 로고
    • Abnormal bundling and accumulation of F-actin mediates tau-induced neuronal degeneration in vivo
    • Fulga TA, Elson-Schwab I, Khurana V, Steinhilb ML, Spires TL, et al. (2007) Abnormal bundling and accumulation of F-actin mediates tau-induced neuronal degeneration in vivo. Nat Cell Biol 9: 139-148.
    • (2007) Nat Cell Biol , vol.9 , pp. 139-148
    • Fulga, T.A.1    Elson-Schwab, I.2    Khurana, V.3    Steinhilb, M.L.4    Spires, T.L.5
  • 49
    • 0035829720 scopus 로고    scopus 로고
    • Disruption of axonal transport and neuronal viability by annyloid precursor protein mutations in Drosophila
    • Gunawardena S, Goldstein LS (2001) Disruption of axonal transport and neuronal viability by annyloid precursor protein mutations in Drosophila. Neuron 32: 3889-401.
    • (2001) Neuron , vol.32 , pp. 3889-4401
    • Gunawardena, S.1    Goldstein, L.S.2
  • 50
    • 0035818998 scopus 로고    scopus 로고
    • Kinesin-mediated axonal transport of a membrane compartment containing beta-secretase and presenilin-1 requires APP
    • Kamal A, Almenar-Queralt A, LeBlane JF, Roberts EA, Goldstein LS (2001) Kinesin-mediated axonal transport of a membrane compartment containing beta-secretase and presenilin-1 requires APP. Nature 414: 643-648.
    • (2001) Nature , vol.414 , pp. 643-648
    • Kamal, A.1    Almenar-Queralt, A.2    LeBlane, J.F.3    Roberts, E.A.4    Goldstein, L.S.5
  • 51
    • 34548036227 scopus 로고    scopus 로고
    • Tau-mediated neurodegeneration in Alzheimer's disease and related disorders
    • Ballatore C, Lee VM, Trojanowski JQ (2007) Tau-mediated neurodegeneration in Alzheimer's disease and related disorders. Nat Rev Neurosci 8: 663-672.
    • (2007) Nat Rev Neurosci , vol.8 , pp. 663-672
    • Ballatore, C.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 52
    • 33947101532 scopus 로고    scopus 로고
    • A brief history of tau: The evolving view of the microtubule-associated protein tau in neurodegenerative diseases
    • Lace GL, Wharton SB, Ince PG (2007) A brief history of tau: the evolving view of the microtubule-associated protein tau in neurodegenerative diseases. Clin Neuropathol 26: 43-58.
    • (2007) Clin Neuropathol , vol.26 , pp. 43-58
    • Lace, G.L.1    Wharton, S.B.2    Ince, P.G.3
  • 53
    • 0023387681 scopus 로고
    • Cofilin is a component of intranuclear and cytoplasmic actin rods induced in cultured cells
    • Nishida E, Iida K, Yonezawa N, Koyasu S, Yahara I, et al. (1987) Cofilin is a component of intranuclear and cytoplasmic actin rods induced in cultured cells. Proc Natl Acad Sci U S A 84: 5262-5266.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 5262-5266
    • Nishida, E.1    Iida, K.2    Yonezawa, N.3    Koyasu, S.4    Yahara, I.5
  • 55
    • 24344468669 scopus 로고    scopus 로고
    • Martin M, Ahern-Djamali SM, Hoffmann FM, Saxton WM (2005) Ab1 tyrosine kinase and its substrate Ena/VASP have functional interactions with kinesin-1. Mot Biol Cell 16: 4225-4230.
    • Martin M, Ahern-Djamali SM, Hoffmann FM, Saxton WM (2005) Ab1 tyrosine kinase and its substrate Ena/VASP have functional interactions with kinesin-1. Mot Biol Cell 16: 4225-4230.
  • 56
    • 34648843067 scopus 로고    scopus 로고
    • Mitochondrial cascade hypothesis of Alzheimer's disease: Myth or reality?
    • Mancuso M, Coppede F, Murri L, Siciliano G (2007) Mitochondrial cascade hypothesis of Alzheimer's disease: myth or reality? Antioxid Redox Signal 9: 1631-1646.
    • (2007) Antioxid Redox Signal , vol.9 , pp. 1631-1646
    • Mancuso, M.1    Coppede, F.2    Murri, L.3    Siciliano, G.4
  • 57
    • 37349004102 scopus 로고    scopus 로고
    • Parkinson's disease
    • Thomas B, Beal MF (2007) Parkinson's disease. Hum Mol Genet 16 Spec No. 2: R183-194.
    • (2007) Hum Mol Genet , vol.16 , Issue.SPEC 2
    • Thomas, B.1    Beal, M.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.