메뉴 건너뛰기




Volumn 35, Issue 1, 2007, Pages 21-43

Cofilin-mediated neurodegeneration in Alzheimer's disease and other amyloidopathies

Author keywords

Actin; ADF cofilin; Alzheimer's disease; Amyloid ; Down syndrome; Inclusions; Neurodegeneration; Stroke; Transport

Indexed keywords

ACTIN; ACTIN DEPOLYMERIZING FACTOR; AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; AMYLOID BETA PROTEIN[25-35]; AMYLOID PRECURSOR PROTEIN; APOLIPOPROTEIN E; CHOLESTEROL; COFILIN; F ACTIN; G ACTIN;

EID: 34347347236     PISSN: 08937648     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF02700622     Document Type: Article
Times cited : (97)

References (159)
  • 1
    • 0036773010 scopus 로고    scopus 로고
    • Hypoxia signaling to genes: Significance in Alzheimer's disease
    • Bazan, N. G., Palacios-Pelaez, R., and Lukiw, W. J. (2002). Hypoxia signaling to genes: significance in Alzheimer's disease. Mol Neurobiol. 26(2-3), 283-298.
    • (2002) Mol Neurobiol , vol.26 , Issue.2-3 , pp. 283-298
    • Bazan, N.G.1    Palacios-Pelaez, R.2    Lukiw, W.J.3
  • 2
    • 0025269152 scopus 로고
    • Synapse loss in frontal cortex biopsies in Alzheimer's disease: Correlation with cognitive severity
    • DeKosky, S. T. and Scheff, S. W. (1990). Synapse loss in frontal cortex biopsies in Alzheimer's disease: correlation with cognitive severity. Ann Neurol. 27(5), 457-464.
    • (1990) Ann Neurol , vol.27 , Issue.5 , pp. 457-464
    • DeKosky, S.T.1    Scheff, S.W.2
  • 3
    • 0025987048 scopus 로고
    • Physical basis of cognitive alterations in Alzheimer's disease; synapse loss is the major correlate of cognitive impairment
    • Terry, R. D., Masliah, E., Salmon, D. P., et al. (1991). Physical basis of cognitive alterations in Alzheimer's disease; synapse loss is the major correlate of cognitive impairment. Ann Neurol. 30(4), 572-580.
    • (1991) Ann Neurol , vol.30 , Issue.4 , pp. 572-580
    • Terry, R.D.1    Masliah, E.2    Salmon, D.P.3
  • 4
    • 0345276572 scopus 로고    scopus 로고
    • Synaptic slaughter in Alzheimer's disease
    • Coleman, P. D. and Yao, P. J. (2003). Synaptic slaughter in Alzheimer's disease. Neurobiol Aging 24(8), 1023-1027.
    • (2003) Neurobiol Aging , vol.24 , Issue.8 , pp. 1023-1027
    • Coleman, P.D.1    Yao, P.J.2
  • 5
    • 0023106967 scopus 로고
    • A quantitative morphometric analysis of the neuronal and synaptic content of the frontal and temporal cortex in patients with Alzheimer's Disease
    • Davies, C. A., Mann, D. M., Sumpter, P. Q., and Yates, P. O. (1987). A quantitative morphometric analysis of the neuronal and synaptic content of the frontal and temporal cortex in patients with Alzheimer's Disease. J Neurol Sci. 78(2), 151-164.
    • (1987) J Neurol Sci , vol.78 , Issue.2 , pp. 151-164
    • Davies, C.A.1    Mann, D.M.2    Sumpter, P.Q.3    Yates, P.O.4
  • 6
    • 0034282106 scopus 로고    scopus 로고
    • Neurodegenerative stimuli induce persistent ADF/cofilin-actin rods that disrupt distal neurite function
    • Minamide, L. S., Striegl, A.M., Boyle, J. A., Meberg, P. J., and Bamburg, J. R. (2000). Neurodegenerative stimuli induce persistent ADF/cofilin-actin rods that disrupt distal neurite function. Nat Cell Biol. 2(9), 628-636.
    • (2000) Nat Cell Biol , vol.2 , Issue.9 , pp. 628-636
    • Minamide, L.S.1    Striegl, A.M.2    Boyle, J.A.3    Meberg, P.J.4    Bamburg, J.R.5
  • 8
    • 33644849690 scopus 로고    scopus 로고
    • Amyloidogenic processing of beta-amyloid precursor protein in intracellular compartments
    • Vetrivel, K. S. and Thinakaran, G. (2006). Amyloidogenic processing of beta-amyloid precursor protein in intracellular compartments. Neurology 66(2 Suppl 1), S69-S73.
    • (2006) Neurology , vol.66 , Issue.2 SUPPL. 1
    • Vetrivel, K.S.1    Thinakaran, G.2
  • 9
    • 14244268498 scopus 로고    scopus 로고
    • Gamma-secretase exists on the plasma membrane as an intact complex that accepts substrates and effects intramembrane cleavage
    • Chyung, J. H., Raper, D. M., and Selkoe, D. J. (2005). Gamma-secretase exists on the plasma membrane as an intact complex that accepts substrates and effects intramembrane cleavage. J Biol Chem. 280(6), 4383-4392.
    • (2005) J Biol Chem , vol.280 , Issue.6 , pp. 4383-4392
    • Chyung, J.H.1    Raper, D.M.2    Selkoe, D.J.3
  • 10
    • 0037421206 scopus 로고    scopus 로고
    • Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts
    • Ehehalt, R., Keller, P., Haass, C., Thiele, C., and Simons, K. (2003). Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts. J Cell Biol. 160(1), 113-123.
    • (2003) J Cell Biol , vol.160 , Issue.1 , pp. 113-123
    • Ehehalt, R.1    Keller, P.2    Haass, C.3    Thiele, C.4    Simons, K.5
  • 11
    • 0021207461 scopus 로고
    • Alzheimer's disease and Down's syndrome: Sharing of a unique cerebrovascular amyloid fibril protein
    • Glenner, G. G., and Wong, C. W. (1984). Alzheimer's disease and Down's syndrome: sharing of a unique cerebrovascular amyloid fibril protein. Biochem Biophys Res Commun. 122(3), 1131-1135.
    • (1984) Biochem Biophys Res Commun , vol.122 , Issue.3 , pp. 1131-1135
    • Glenner, G.G.1    Wong, C.W.2
  • 12
    • 3943092621 scopus 로고    scopus 로고
    • Pathways towards and away from Alzheimer's disease
    • Mattson, M. P. (2004). Pathways towards and away from Alzheimer's disease. Nature 430, 631-639.
    • (2004) Nature , vol.430 , pp. 631-639
    • Mattson, M.P.1
  • 13
    • 13944276825 scopus 로고    scopus 로고
    • Twenty years of the Alzheimer's Disease hypothesis: A genetic perspective
    • Tanzi, R. E. and Bertram, L. (2005). Twenty years of the Alzheimer's Disease hypothesis: A genetic perspective. Cell 120, 545-555.
    • (2005) Cell , vol.120 , pp. 545-555
    • Tanzi, R.E.1    Bertram, L.2
  • 14
    • 0027365822 scopus 로고    scopus 로고
    • Schmechel, D. E., Saunders, A. M., Strittmatter, W. J., et al. (1993). Increased amyloid beta-peptide deposition in cerebral cortex as a consequence of apolipoprotein E genotype in lateonset Alzheimer disease. Proc Natl Acad Sci U S A 90, 9649-9653.
    • Schmechel, D. E., Saunders, A. M., Strittmatter, W. J., et al. (1993). Increased amyloid beta-peptide deposition in cerebral cortex as a consequence of apolipoprotein E genotype in lateonset Alzheimer disease. Proc Natl Acad Sci U S A 90, 9649-9653.
  • 15
    • 0027407565 scopus 로고
    • Apolipoprotein E: High-avidity binding to beta-amyloid and increased frequency of type 4 allele in late-onset familial Alzheimer disease
    • Strittmatter, W. J., Saunders, A. M., Schmechel, D., et al. (1993). Apolipoprotein E: high-avidity binding to beta-amyloid and increased frequency of type 4 allele in late-onset familial Alzheimer disease. Proc Natl Acad Sci U S A 90(5), 1977-1981.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , Issue.5 , pp. 1977-1981
    • Strittmatter, W.J.1    Saunders, A.M.2    Schmechel, D.3
  • 16
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner, G. G. and Wong, C. W. (1984). Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem Biophys Res Commun. 120(3), 885-890.
    • (1984) Biochem Biophys Res Commun , vol.120 , Issue.3 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 17
    • 0037220750 scopus 로고    scopus 로고
    • Actin-ATP hydrolysis is a major energy drain for neurons
    • Bernstein, B. W. and Bamburg, J. R. (2003). Actin-ATP hydrolysis is a major energy drain for neurons. J Neurosci. 23(1), 1-6.
    • (2003) J Neurosci , vol.23 , Issue.1 , pp. 1-6
    • Bernstein, B.W.1    Bamburg, J.R.2
  • 18
    • 0037169335 scopus 로고    scopus 로고
    • Control of actin reorganization by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin
    • Niwa, R., Nagata-Ohashi, K., Takeichi, M., Mizuno, K., and Uemura, T. (2002). Control of actin reorganization by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin. Cell 108(2), 233-246.
    • (2002) Cell , vol.108 , Issue.2 , pp. 233-246
    • Niwa, R.1    Nagata-Ohashi, K.2    Takeichi, M.3    Mizuno, K.4    Uemura, T.5
  • 19
    • 12344250639 scopus 로고    scopus 로고
    • Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics
    • Ghola, A., Birkenfield, J., and Bokoch, G. M. (2005). Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics. Nature Cell Biol. 7(1), 21-29.
    • (2005) Nature Cell Biol , vol.7 , Issue.1 , pp. 21-29
    • Ghola, A.1    Birkenfield, J.2    Bokoch, G.M.3
  • 20
    • 30844443048 scopus 로고    scopus 로고
    • Cofilin phosphatases and regulation of actin dynamics
    • Huang, T. Y., DerMardirossian, C., and Bokoch, G. M. (2006). Cofilin phosphatases and regulation of actin dynamics. Curr Opin Cell Biol. 18(1), 26-31.
    • (2006) Curr Opin Cell Biol , vol.18 , Issue.1 , pp. 26-31
    • Huang, T.Y.1    DerMardirossian, C.2    Bokoch, G.M.3
  • 21
    • 0027439319 scopus 로고
    • The interaction of human actin depolymerizing factor with actin is pH regulated
    • Hawkins, M., Pope, B., Maciver, S. K., and Weeds, A. G. (1993). The interaction of human actin depolymerizing factor with actin is pH regulated. Biochemistry 32(38), 9985-9993.
    • (1993) Biochemistry , vol.32 , Issue.38 , pp. 9985-9993
    • Hawkins, M.1    Pope, B.2    Maciver, S.K.3    Weeds, A.G.4
  • 22
    • 0027494863 scopus 로고
    • Analysis of the interactions of actin depolymerizing factor with G- and F-actin
    • 9994-10,004
    • Hayden, S. M., Miller, P. S., Brauweiler, A., and Bamburg, J. R. (1993). Analysis of the interactions of actin depolymerizing factor with G- and F-actin. Biochemistry 32(38), 9994-10,004.
    • (1993) Biochemistry , vol.32 , Issue.38
    • Hayden, S.M.1    Miller, P.S.2    Brauweiler, A.3    Bamburg, J.R.4
  • 23
    • 0030843484 scopus 로고    scopus 로고
    • Actin Depolymerizing Factor (ADF/cofilin) enhances the rate of filament turnover: Implication in actin-based motility
    • Carlier, M. -F., Laurent. V., Santolini, J., et al. (1997). Actin Depolymerizing Factor (ADF/cofilin) enhances the rate of filament turnover: implication in actin-based motility. J Cell Biol. 136(6), 1307-1322.
    • (1997) J Cell Biol , vol.136 , Issue.6 , pp. 1307-1322
    • Carlier, M.-F.1    Laurent, V.2    Santolini, J.3
  • 24
    • 0030820734 scopus 로고    scopus 로고
    • Cofilin changes the twist of F-actin: Implications for actin dynamics and cellular function
    • McGough, A., Pope. B., Chiu, W., and Weeds, A. (1997). Cofilin changes the twist of F-actin: implications for actin dynamics and cellular function. J Cell Biol. 138(4), 771-781.
    • (1997) J Cell Biol , vol.138 , Issue.4 , pp. 771-781
    • McGough, A.1    Pope, B.2    Chiu, W.3    Weeds, A.4
  • 25
    • 30744462047 scopus 로고    scopus 로고
    • Cooperative effects of cofilin (ADF) on actin structure suggest allosteric mechanism of cofilin function
    • Bobokov, A. A., Muhlrad, A., Pavlov, D. A., Kokabi, K., Yilmaz, A., and Reisler, E. (2006). Cooperative effects of cofilin (ADF) on actin structure suggest allosteric mechanism of cofilin function. J Mol Biol. 256(2), 325-334.
    • (2006) J Mol Biol , vol.256 , Issue.2 , pp. 325-334
    • Bobokov, A.A.1    Muhlrad, A.2    Pavlov, D.A.3    Kokabi, K.4    Yilmaz, A.5    Reisler, E.6
  • 26
    • 0033194037 scopus 로고    scopus 로고
    • Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signaling to actin cytoskeletal dynamics
    • Edwards, D. C., Sanders, L. C., Bokoch, G. M., and Gill, G. N. (1999). Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signaling to actin cytoskeletal dynamics. Nature Cell Biol. 1(5), 253-259.
    • (1999) Nature Cell Biol , vol.1 , Issue.5 , pp. 253-259
    • Edwards, D.C.1    Sanders, L.C.2    Bokoch, G.M.3    Gill, G.N.4
  • 27
    • 0035943704 scopus 로고    scopus 로고
    • Cytoskeletal changes regulated by the PAK4 serine/threonine kinase are mediated by LIM kinase 1 and cofilin
    • Dan, C., Kelly, A., Bernard, O., and Minden, A. (2001). Cytoskeletal changes regulated by the PAK4 serine/threonine kinase are mediated by LIM kinase 1 and cofilin. J Biol Chem. 276(34), 32,115-32,121.
    • (2001) J Biol Chem , vol.276 , Issue.34
    • Dan, C.1    Kelly, A.2    Bernard, O.3    Minden, A.4
  • 28
    • 0032565962 scopus 로고    scopus 로고
    • Regulation of actin dynamics through phosphorylation of cofilin by LIM-kinase
    • Arber, S., Barbayannis, F. A., Hanser, H., et al. (1998). Regulation of actin dynamics through phosphorylation of cofilin by LIM-kinase. Nature 393(6687), 805-809.
    • (1998) Nature , vol.393 , Issue.6687 , pp. 805-809
    • Arber, S.1    Barbayannis, F.A.2    Hanser, H.3
  • 29
    • 0032565769 scopus 로고    scopus 로고
    • Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization
    • Yang, N., Higuchi, O., Ohashi, K., et al. (1998). Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization. Nature 393(6687), 809-812.
    • (1998) Nature , vol.393 , Issue.6687 , pp. 809-812
    • Yang, N.1    Higuchi, O.2    Ohashi, K.3
  • 30
    • 14844286389 scopus 로고    scopus 로고
    • Interplay between components of a novel LIM kinase-slingshot phosphatase complex regulates cofilin
    • Soosairajah, J., Maiti, S., Wiggan, O., et al. (2005). Interplay between components of a novel LIM kinase-slingshot phosphatase complex regulates cofilin. EMBO J. 24(3), 473-486.
    • (2005) EMBO J , vol.24 , Issue.3 , pp. 473-486
    • Soosairajah, J.1    Maiti, S.2    Wiggan, O.3
  • 31
    • 18444372636 scopus 로고    scopus 로고
    • Abnormal spine morphology and enhanced LTP in LIMK-1 knockout mice
    • Meng, Y., Zhang, Y., Tregoubov, V., et al. (2002). Abnormal spine morphology and enhanced LTP in LIMK-1 knockout mice. Neuron 35(1), 121-133.
    • (2002) Neuron , vol.35 , Issue.1 , pp. 121-133
    • Meng, Y.1    Zhang, Y.2    Tregoubov, V.3
  • 32
    • 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(12), 598-605.
    • (2002) Trends Cell Biol , vol.12 , Issue.12 , pp. 598-605
    • Bamburg, J.R.1    Wiggan, O.P.2
  • 33
    • 0033134860 scopus 로고    scopus 로고
    • Bridging cognition, the brain and molecular genetics: Evidence from William's syndrome
    • Bellugi, U., Lichtenberger, L., Mills. D., Galaburda, A., and Korenberg, J. R. (1999). Bridging cognition, the brain and molecular genetics: evidence from William's syndrome. Trends Neurosci. 22, 197-207.
    • (1999) Trends Neurosci , vol.22 , pp. 197-207
    • Bellugi, U.1    Lichtenberger, L.2    Mills, D.3    Galaburda, A.4    Korenberg, J.R.5
  • 34
    • 31544476561 scopus 로고    scopus 로고
    • Role of p21-activated kinase pathway defects in the cognitive deficits of Alzheimer disease
    • Zhao, L., Ma, Q. L., Calon, F., et al. (2006). Role of p21-activated kinase pathway defects in the cognitive deficits of Alzheimer disease. Nat Neurosci. 9(2), 234-242.
    • (2006) Nat Neurosci , vol.9 , Issue.2 , pp. 234-242
    • Zhao, L.1    Ma, Q.L.2    Calon, F.3
  • 35
    • 0002428026 scopus 로고
    • Histochemical changes induced in sympathetic, motor, and sensory nerve cells by functional activity
    • Mann, G., (1894). Histochemical changes induced in sympathetic, motor, and sensory nerve cells by functional activity. J Anat Physiol. London 19, 100-108.
    • (1894) J Anat Physiol. London , vol.19 , pp. 100-108
    • Mann, G.1
  • 36
    • 0018428638 scopus 로고
    • Nuclear actin bundles in Amoeba, Dictyostelium and human HeLa cells induced by dimethyl sulfoxide
    • Fukui, Y., and Katsumaru, H. (1979). Nuclear actin bundles in Amoeba, Dictyostelium and human HeLa cells induced by dimethyl sulfoxide. Exp Cell Res. 120(2), 451-455.
    • (1979) Exp Cell Res , vol.120 , Issue.2 , pp. 451-455
    • Fukui, Y.1    Katsumaru, H.2
  • 37
    • 0022510684 scopus 로고
    • Heat shock induction of intranuclear actin rods in cultured mammalian cells
    • Iida, K., Iida, H., and Yahara, I. (1986). Heat shock induction of intranuclear actin rods in cultured mammalian cells. Exp Cell Res. 165(1), 207-215.
    • (1986) Exp Cell Res , vol.165 , Issue.1 , pp. 207-215
    • Iida, K.1    Iida, H.2    Yahara, I.3
  • 38
    • 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., and Sakai, H. (1987). Cofilin is a component of intranuclear and cytoplasmic actin rods induced in cultured cells. Proc Natl Acad Sci U S A 84(15), 5262-5266.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , Issue.15 , pp. 5262-5266
    • Nishida, E.1    Iida, K.2    Yonezawa, N.3    Koyasu, S.4    Yahara, I.5    Sakai, H.6
  • 39
    • 0024429070 scopus 로고
    • Dephosphorylation of cofilin accompanies heat shock-induced nuclear accumulation of cofilin
    • Ohta, Y., Nishida, E., Sakai, H., and Miyamoto, E. (1989). Dephosphorylation of cofilin accompanies heat shock-induced nuclear accumulation of cofilin. J Biol Chem. 264(27), 16,143-16,148.
    • (1989) J Biol Chem , vol.264 , Issue.27
    • Ohta, Y.1    Nishida, E.2    Sakai, H.3    Miyamoto, E.4
  • 40
    • 0026550804 scopus 로고
    • The KKRKK sequence is involved in heat shock-induced nuclear translocation of the 18-kDa actin-binding protein, cofilin
    • Iida, K., Matsumoto, S., and Yahara, I. (1992). The KKRKK sequence is involved in heat shock-induced nuclear translocation of the 18-kDa actin-binding protein, cofilin. Cell Struct Funct. 17(1), 39-46.
    • (1992) Cell Struct Funct , vol.17 , Issue.1 , pp. 39-46
    • Iida, K.1    Matsumoto, S.2    Yahara, I.3
  • 41
    • 0027258440 scopus 로고
    • Colocalization of ADF and cofilin in intranuclear actin rods of cultured muscle cells
    • Ono, S., Abe, H., Nagaoka, R., and Obinata, T. (1993). Colocalization of ADF and cofilin in intranuclear actin rods of cultured muscle cells. J Muscle Res Cell Motil. 14(2), 195-204.
    • (1993) J Muscle Res Cell Motil , vol.14 , Issue.2 , pp. 195-204
    • Ono, S.1    Abe, H.2    Nagaoka, R.3    Obinata, T.4
  • 42
    • 0029678546 scopus 로고    scopus 로고
    • Phosphorylation of Ser-3 of cofilin regulates its essential function on actin
    • Moriyama, K., Iida, K., and Yahara, I. (1996). Phosphorylation of Ser-3 of cofilin regulates its essential function on actin. Genes Cells 1(1), 73-86.
    • (1996) Genes Cells , vol.1 , Issue.1 , pp. 73-86
    • Moriyama, K.1    Iida, K.2    Yahara, I.3
  • 43
    • 0001081894 scopus 로고    scopus 로고
    • Live dynamics of Dictyostelium cofilin suggests a role in remodeling actin latticework into bundles
    • Aizawa, H., Fukui, Y., and Yahara, I. (1997). Live dynamics of Dictyostelium cofilin suggests a role in remodeling actin latticework into bundles. J Cell Sci. 110 (Pt 19), 2333-2344.
    • (1997) J Cell Sci , vol.110 , Issue.PART 19 , pp. 2333-2344
    • Aizawa, H.1    Fukui, Y.2    Yahara, I.3
  • 45
    • 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 Alzheimer's 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 Alzheimer's disease. J Neurosci. 25(49), 11,313-11,321.
    • (2005) J Neurosci , vol.25 , Issue.49
    • Maloney, M.T.1    Minamide, L.S.2    Kinley, A.W.3    Boyle, J.A.4    Bamburg, J.R.5
  • 46
    • 33745268224 scopus 로고    scopus 로고
    • Different conformations of amyloid beta induce neurotoxicity by distinct mechanisms in human cortical neurons
    • Deshpande. A., Mina, E., Glabe, C., and Busciglio, J. (2006). Different conformations of amyloid beta induce neurotoxicity by distinct mechanisms in human cortical neurons. J. Neurosci. 26(22), 6011-6018.
    • (2006) J. Neurosci , vol.26 , Issue.22 , pp. 6011-6018
    • Deshpande, A.1    Mina, E.2    Glabe, C.3    Busciglio, J.4
  • 47
    • 20844458090 scopus 로고    scopus 로고
    • Synaptic targeting by Alzheimer's-related amyloid beta oligomers
    • Lacor, P. N., Buniel, M. C., Chang, L., et al. (2004). Synaptic targeting by Alzheimer's-related amyloid beta oligomers. J Neurosci. 24(45), 10,191-10,200.
    • (2004) J Neurosci , vol.24 , Issue.45
    • Lacor, P.N.1    Buniel, M.C.2    Chang, L.3
  • 48
    • 0034509452 scopus 로고    scopus 로고
    • The role of synaptic proteins in Alzheimer's disease
    • Masliah, E. (2000). The role of synaptic proteins in Alzheimer's disease. Ann N Y Acad Sci. 924, 68-75.
    • (2000) Ann N Y Acad Sci , vol.924 , pp. 68-75
    • Masliah, E.1
  • 49
    • 0034213718 scopus 로고    scopus 로고
    • High-level neuronal expression of abeta 1-42 in wild-type human amyloid protein precursor transgenic mice: Synaptotoxicity without plaque formation
    • Mucke, L., Masliah, E., Yu, G. Q., et al. (2000). High-level neuronal expression of abeta 1-42 in wild-type human amyloid protein precursor transgenic mice: synaptotoxicity without plaque formation. J Neurosci 20(11), 4050-4058.
    • (2000) J Neurosci , vol.20 , Issue.11 , pp. 4050-4058
    • Mucke, L.1    Masliah, E.2    Yu, G.Q.3
  • 50
    • 27644495116 scopus 로고    scopus 로고
    • Cofilin expression induces cofilin-actin rod formation and disrupts synaptic structure and function in Aplysia synapses
    • Jang, D. H., Han, J. H., Lee, S. H., et al. (2005). Cofilin expression induces cofilin-actin rod formation and disrupts synaptic structure and function in Aplysia synapses. Proc Natl Acad Sci U S A. 102(44), 16,072-16,077.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , Issue.44
    • Jang, D.H.1    Han, J.H.2    Lee, S.H.3
  • 51
    • 0029057814 scopus 로고
    • Intracellular A beta 1-42 aggregates stimulate the accumulation of stable, insoluble amyloidogenic fragments of the amyloid precursor protein in transfected cells
    • Yang, A. J., Knauer, M., Burdick, D.A., and Glabe, C. (1995). Intracellular A beta 1-42 aggregates stimulate the accumulation of stable, insoluble amyloidogenic fragments of the amyloid precursor protein in transfected cells. J Biol Chem. 270(24), 14,786-14,792.
    • (1995) J Biol Chem , vol.270 , Issue.24
    • Yang, A.J.1    Knauer, M.2    Burdick, D.A.3    Glabe, C.4
  • 52
    • 2142707174 scopus 로고    scopus 로고
    • Central cholinergic functions in human amyloid precursor protein knock-in/presenilin-1 transgenic mice
    • Hartmann, J., Erb, C., Ebert, U., et al. (2004). Central cholinergic functions in human amyloid precursor protein knock-in/presenilin-1 transgenic mice. Neuroscience 125(4), 1009-1017.
    • (2004) Neuroscience , vol.125 , Issue.4 , pp. 1009-1017
    • Hartmann, J.1    Erb, C.2    Ebert, U.3
  • 53
    • 11544279355 scopus 로고    scopus 로고
    • Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins
    • Lambert, M. P., Barlow, A. K., Chromy, B. A., et al. (1998). Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins. Proc Natl Acad Sci U S A. 95(11), 6448-6453.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , Issue.11 , pp. 6448-6453
    • Lambert, M.P.1    Barlow, A.K.2    Chromy, B.A.3
  • 54
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh, D. M., Klyubin, I., Fadeeva, J. V., et al. (2002). Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416(6880), 535-539.
    • (2002) Nature , vol.416 , Issue.6880 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3
  • 55
    • 0037059598 scopus 로고    scopus 로고
    • Soluble oligomers of beta amyloid (1-42) inhibit long-term potentiation but not long-term depression in rat dentate gyrus
    • Wang, H. W., Pasternak, J. F., Kuo, H., et al. (2002). Soluble oligomers of beta amyloid (1-42) inhibit long-term potentiation but not long-term depression in rat dentate gyrus. Brain Res. 924(2), 133-140.
    • (2002) Brain Res , vol.924 , Issue.2 , pp. 133-140
    • Wang, H.W.1    Pasternak, J.F.2    Kuo, H.3
  • 56
    • 33645038471 scopus 로고    scopus 로고
    • A specific amyloid-beta protein assembly in the brain impairs memory
    • Lesné, S., Koh, M. T., Kotilinek, L., et al. (2006). A specific amyloid-beta protein assembly in the brain impairs memory. Nature 440(7082), 352-357.
    • (2006) Nature , vol.440 , Issue.7082 , pp. 352-357
    • Lesné, S.1    Koh, M.T.2    Kotilinek, L.3
  • 57
    • 0028952749 scopus 로고
    • Aggregation of secreted amyloid beta-protein into sodium dodecyl sulfatestable oligomers in cell culture
    • Podlisny, M. B., Ostaszewski, B. L., Squazzo, S. L., et al. (1995). Aggregation of secreted amyloid beta-protein into sodium dodecyl sulfatestable oligomers in cell culture. J Biol Chem. 270(16), 9564-9570.
    • (1995) J Biol Chem , vol.270 , Issue.16 , pp. 9564-9570
    • Podlisny, M.B.1    Ostaszewski, B.L.2    Squazzo, S.L.3
  • 58
    • 0032539975 scopus 로고    scopus 로고
    • Oligomerization of endogenous and synthetic amyloid beta-protein at nanomolar levels in cell culture and stabilization of monomer by Congo red
    • Podlisny, M. B., Walsh, D. M., Amarante, P., et al. (1998). Oligomerization of endogenous and synthetic amyloid beta-protein at nanomolar levels in cell culture and stabilization of monomer by Congo red. Biochemistry 37(11), 3602-3611.
    • (1998) Biochemistry , vol.37 , Issue.11 , pp. 3602-3611
    • Podlisny, M.B.1    Walsh, D.M.2    Amarante, P.3
  • 59
    • 27844432223 scopus 로고    scopus 로고
    • The role of cell-derived oligomers of Abeta in Alzheimer's disease and avenues for therapeutic intervention
    • Walsh, D. M., Klyubin, I., Shankar, G. M., et al. (2005). The role of cell-derived oligomers of Abeta in Alzheimer's disease and avenues for therapeutic intervention. Biochem Soc Trans. 33(Pt 5), 1087-1090.
    • (2005) Biochem Soc Trans , vol.33 , Issue.PART 5 , pp. 1087-1090
    • Walsh, D.M.1    Klyubin, I.2    Shankar, G.M.3
  • 60
    • 16644379264 scopus 로고    scopus 로고
    • Natural oligomers of the amyloid-beta protein specifically disrupt cognitive function
    • Cleary, J. P., Walsh, D. M., Hofmeister, J. J., et al. (2005). Natural oligomers of the amyloid-beta protein specifically disrupt cognitive function. Nat Neurosci. 8(1), 79-84.
    • (2005) Nat Neurosci , vol.8 , Issue.1 , pp. 79-84
    • Cleary, J.P.1    Walsh, D.M.2    Hofmeister, J.J.3
  • 61
    • 21044453723 scopus 로고    scopus 로고
    • Amyloid beta protein immunotherapy neutralizes Abeta oligomers that disrupt synaptic plasticity in vivo
    • Klyubin, I., Walsh, D. M., Lemere, C. A., et al. (2005). Amyloid beta protein immunotherapy neutralizes Abeta oligomers that disrupt synaptic plasticity in vivo. Nat Med. 11(5), 556-561.
    • (2005) Nat Med , vol.11 , Issue.5 , pp. 556-561
    • Klyubin, I.1    Walsh, D.M.2    Lemere, C.A.3
  • 62
    • 0026756887 scopus 로고
    • Methodological variables in the assessment of beta amyloid neurotoxicity
    • Busciglio, J., Lorenzo, A., and Yankner, B. A. (1992). Methodological variables in the assessment of beta amyloid neurotoxicity. Neurobiol Aging 13(5), 609-612.
    • (1992) Neurobiol Aging , vol.13 , Issue.5 , pp. 609-612
    • Busciglio, J.1    Lorenzo, A.2    Yankner, B.A.3
  • 63
    • 0037130570 scopus 로고    scopus 로고
    • Characterization of neuronal dystrophy induced by fibrillar amyloid beta: Implications for Alzheimer's disease
    • Grace, E. A., Rabiner, C. A., and Busciglio, J. (2002). Characterization of neuronal dystrophy induced by fibrillar amyloid beta: implications for Alzheimer's disease. Neuroscience 114(1), 265-273.
    • (2002) Neuroscience , vol.114 , Issue.1 , pp. 265-273
    • Grace, E.A.1    Rabiner, C.A.2    Busciglio, J.3
  • 64
    • 0037439642 scopus 로고    scopus 로고
    • Aberrant activation of focal adhesion proteins mediates fibrillar amyloid beta-induced neuronal dystrophy
    • Grace, E. A. and Busciglio, J. (2003). Aberrant activation of focal adhesion proteins mediates fibrillar amyloid beta-induced neuronal dystrophy. J Neurosci. 23(2), 493-502.
    • (2003) J Neurosci , vol.23 , Issue.2 , pp. 493-502
    • Grace, E.A.1    Busciglio, J.2
  • 65
    • 0034725593 scopus 로고    scopus 로고
    • Integrins and actin filaments: Reciprocal regulation of cell adhesion and signaling
    • Calderwood, D. A., Shattil, S. J., and Ginsberg, M. H. (2000). Integrins and actin filaments: reciprocal regulation of cell adhesion and signaling. J Biol Chem. 275(30), 22,607-22,610.
    • (2000) J Biol Chem , vol.275 , Issue.30
    • Calderwood, D.A.1    Shattil, S.J.2    Ginsberg, M.H.3
  • 66
    • 0033551899 scopus 로고    scopus 로고
    • Integrin signaling
    • Giancotti, F. G. and Ruoslahti, E. (1999). Integrin signaling. Science 285(5430), 1028-1032.
    • (1999) Science , vol.285 , Issue.5430 , pp. 1028-1032
    • Giancotti, F.G.1    Ruoslahti, E.2
  • 67
    • 0033666291 scopus 로고    scopus 로고
    • Paxillin and focal adhesion signaling
    • Turner, C. E. (2000). Paxillin and focal adhesion signaling. Nat Cell Biol, 2(12), E231-E236.
    • (2000) Nat Cell Biol , vol.2 , Issue.12
    • Turner, C.E.1
  • 68
    • 12844269955 scopus 로고    scopus 로고
    • Regulation of Rho and Rac signaling to the actin cytoskeleton by paxillin during Drosophila development
    • Chen, G. C., Turano, B., Ruest, P. J., Hagel, M., Settleman, J., and Thomas, S. M. (2005). Regulation of Rho and Rac signaling to the actin cytoskeleton by paxillin during Drosophila development. Mol Cell Biol. 25(3), 979-987.
    • (2005) Mol Cell Biol , vol.25 , Issue.3 , pp. 979-987
    • Chen, G.C.1    Turano, B.2    Ruest, P.J.3    Hagel, M.4    Settleman, J.5    Thomas, S.M.6
  • 69
    • 33745780575 scopus 로고    scopus 로고
    • Phosphorylation of ADF/cofilin by LIM-kinase mediates amyloid β-induced degeneration: A potential mechanism of neuronal dystrophy in Alzheimer's disease
    • Heredia, L., Helguera, P., de Olmos, S., et al. (2006). Phosphorylation of ADF/cofilin by LIM-kinase mediates amyloid β-induced degeneration: A potential mechanism of neuronal dystrophy in Alzheimer's disease. J Neurosci. 26(24), 6533-6542.
    • (2006) J Neurosci , vol.26 , Issue.24 , pp. 6533-6542
    • Heredia, L.1    Helguera, P.2    de Olmos, S.3
  • 70
    • 0042838303 scopus 로고    scopus 로고
    • Alzheimer's disease-affected brain: Presence of oligomeric A beta ligands (ADDLs) suggests a molecular basis for reversible memory loss
    • Gong, Y., Chang, L., Viola, K. L., et al. (2003). Alzheimer's disease-affected brain: presence of oligomeric A beta ligands (ADDLs) suggests a molecular basis for reversible memory loss. Proc Natl Acad Sci U S A. 100(18), 10,417-10,422.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , Issue.18
    • Gong, Y.1    Chang, L.2    Viola, K.L.3
  • 71
    • 33644957833 scopus 로고    scopus 로고
    • Temporal memory deficits in Alzheimer's mouse models: Rescue by genetic deletion of BACE1
    • Ohno, M., Chang, L., Tseng, W., et al. (2006). Temporal memory deficits in Alzheimer's mouse models: rescue by genetic deletion of BACE1. Eur J Neurosci 23(1), 251-260.
    • (2006) Eur J Neurosci , vol.23 , Issue.1 , pp. 251-260
    • Ohno, M.1    Chang, L.2    Tseng, W.3
  • 72
    • 16844372470 scopus 로고    scopus 로고
    • Calcium signal-induced cofilin dephosphorylation is mediated by Slingshot via calcineurin
    • Wang, Y., Shibasaki, F., and Mizuno, K. (2005). Calcium signal-induced cofilin dephosphorylation is mediated by Slingshot via calcineurin. J Biol Chem. 280(13), 12,683-12,689.
    • (2005) J Biol Chem , vol.280 , Issue.13
    • Wang, Y.1    Shibasaki, F.2    Mizuno, K.3
  • 73
    • 20444496481 scopus 로고    scopus 로고
    • Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers
    • Demuro, A., Mina, E., Kayed, R., Milton, S. C., Parker, I., and Glabe, C. G. (2005). Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers. J Biol Chem. 280(17), 17,294-17,300.
    • (2005) J Biol Chem , vol.280 , Issue.17
    • Demuro, A.1    Mina, E.2    Kayed, R.3    Milton, S.C.4    Parker, I.5    Glabe, C.G.6
  • 74
    • 30644475475 scopus 로고    scopus 로고
    • Soluble beta-amyloid 1-40 induces NMDA-dependent degradation of postsynaptic density-95 at glutamatergic synapses
    • Roselli, F., Tirard, M., Lu, J., et al. (2005). Soluble beta-amyloid 1-40 induces NMDA-dependent degradation of postsynaptic density-95 at glutamatergic synapses. J Neurosci. 25(48), 11,061-11,070.
    • (2005) J Neurosci , vol.25 , Issue.48
    • Roselli, F.1    Tirard, M.2    Lu, J.3
  • 75
    • 25444457995 scopus 로고    scopus 로고
    • Calcium-regulated signaling pathways: Role in amyloid beta-induced synaptic dysfunction
    • Xie, C. W. (2004). Calcium-regulated signaling pathways: role in amyloid beta-induced synaptic dysfunction. Neuromolecular Med. 6(1), 53-64.
    • (2004) Neuromolecular Med , vol.6 , Issue.1 , pp. 53-64
    • Xie, C.W.1
  • 76
    • 24644499539 scopus 로고    scopus 로고
    • Expression of calcipressin1, an inhibitor of the phosphatase calcineurin, is altered with aging and Alzheimer's disease
    • Cook, C. N., Hejna, M. J., Magnuson, D. J., and Lee, J. M. (2005). Expression of calcipressin1, an inhibitor of the phosphatase calcineurin, is altered with aging and Alzheimer's disease. J Alzheimers Dis. 8(1), 63-73.
    • (2005) J Alzheimers Dis , vol.8 , Issue.1 , pp. 63-73
    • Cook, C.N.1    Hejna, M.J.2    Magnuson, D.J.3    Lee, J.M.4
  • 77
    • 20044385920 scopus 로고    scopus 로고
    • Axonopathy and transport deficits early in the pathogenesis of Alzheimer's disease
    • Stokin, G. B., Lillo, C., Falzone, T. L., et al. (2005). Axonopathy and transport deficits early in the pathogenesis of Alzheimer's disease. Science 307(5713), 1282-1288.
    • (2005) Science , vol.307 , Issue.5713 , pp. 1282-1288
    • Stokin, G.B.1    Lillo, C.2    Falzone, T.L.3
  • 78
    • 1842732209 scopus 로고    scopus 로고
    • Oligomerization of Alzheimer's beta-amyloid within processes and synapses of cultured neurons and brain
    • Takahashi, R. H., Almeida, C. G., Kearney, P.F., et al. (2004). Oligomerization of Alzheimer's beta-amyloid within processes and synapses of cultured neurons and brain. J Neurosci. 24(14), 3592-3599.
    • (2004) J Neurosci , vol.24 , Issue.14 , pp. 3592-3599
    • Takahashi, R.H.1    Almeida, C.G.2    Kearney, P.F.3
  • 79
    • 0041632362 scopus 로고    scopus 로고
    • App gene dosage modulates endosomal abnormalities of Alzheimer's disease in a segmental trisomy 16 mouse model of down syndrome
    • Cataldo, A. M., Petanceska, S., Peterhoff, C. M., et al. (2003). App gene dosage modulates endosomal abnormalities of Alzheimer's disease in a segmental trisomy 16 mouse model of down syndrome. J Neurosci. 23(17), 6788-6792.
    • (2003) J Neurosci , vol.23 , Issue.17 , pp. 6788-6792
    • Cataldo, A.M.1    Petanceska, S.2    Peterhoff, C.M.3
  • 80
    • 0030836345 scopus 로고    scopus 로고
    • Increased neuronal endocytosis and protease delivery to early endosomes in sporadic Alzheimer's disease: Neuropathologic evidence for a mechanism of increased beta-amyloidogenesis
    • Cataldo, A. M., Barnett, J. L., Pieroni, C., and Nixon, R. A. (1997). Increased neuronal endocytosis and protease delivery to early endosomes in sporadic Alzheimer's disease: neuropathologic evidence for a mechanism of increased beta-amyloidogenesis. J Neurosci. 17(16), 6142-6151.
    • (1997) J Neurosci , vol.17 , Issue.16 , pp. 6142-6151
    • Cataldo, A.M.1    Barnett, J.L.2    Pieroni, C.3    Nixon, R.A.4
  • 81
    • 0033869715 scopus 로고    scopus 로고
    • Endocytic pathway abnormalities precede amyloid-β deposition in sporadic Alzheimer's disease and Down syndrome. Differential effects of ApoE genotype and presenilin mutations
    • Cataldo, A. M., Peterhoff, C. M., Troncoso, J. C., Gomez-Isla, T., Hyman, B. T., and Nixon, R. A. (2000). Endocytic pathway abnormalities precede amyloid-β deposition in sporadic Alzheimer's disease and Down syndrome. Differential effects of ApoE genotype and presenilin mutations. Am J Pathol. 157(1), 277-286.
    • (2000) Am J Pathol , vol.157 , Issue.1 , pp. 277-286
    • Cataldo, A.M.1    Peterhoff, C.M.2    Troncoso, J.C.3    Gomez-Isla, T.4    Hyman, B.T.5    Nixon, R.A.6
  • 82
    • 4644319713 scopus 로고    scopus 로고
    • Abeta localization in abnormal endosomes: Association with earliest Abeta elevations in AD and Down syndrome
    • Cataldo, A. M., Petanceska, S., Terio, N. B., et al. (2004). Abeta localization in abnormal endosomes: association with earliest Abeta elevations in AD and Down syndrome. Neurobiol Aging 25(10), 1263-1272.
    • (2004) Neurobiol Aging , vol.25 , Issue.10 , pp. 1263-1272
    • Cataldo, A.M.1    Petanceska, S.2    Terio, N.B.3
  • 83
    • 18244411249 scopus 로고
    • Alzheimer disease: Plaques, tangles, and the basal forebrain
    • Whitehouse P. J., Struble, R. G., Clark, A. W., and Price, D. L. (1982). Alzheimer disease: plaques, tangles, and the basal forebrain. Ann Neurol. 12(5), 494.
    • (1982) Ann Neurol , vol.12 , Issue.5 , pp. 494
    • Whitehouse, P.J.1    Struble, R.G.2    Clark, A.W.3    Price, D.L.4
  • 84
    • 0021264594 scopus 로고
    • Alzheimer's presenile dementia, senile dementia of Alzheimer type and Down's syndrome in middle age form an age related continuum of pathological changes
    • Mann, D. M., Yates, P. O., and Marcyniuk, B. (1984). Alzheimer's presenile dementia, senile dementia of Alzheimer type and Down's syndrome in middle age form an age related continuum of pathological changes. Neuropathol Appl Neurobiol. 10(3), 185-207.
    • (1984) Neuropathol Appl Neurobiol , vol.10 , Issue.3 , pp. 185-207
    • Mann, D.M.1    Yates, P.O.2    Marcyniuk, B.3
  • 85
    • 0021827834 scopus 로고
    • Abnormalities of the nucleus basalis in Down's syndrome
    • Casanova, M. F., Walker, L. C., Whitehouse, P. J., and Price, D. L. (1985). Abnormalities of the nucleus basalis in Down's syndrome. Ann Neurol. 18(3), 310-313.
    • (1985) Ann Neurol , vol.18 , Issue.3 , pp. 310-313
    • Casanova, M.F.1    Walker, L.C.2    Whitehouse, P.J.3    Price, D.L.4
  • 86
    • 0024449354 scopus 로고
    • Loss of nerve growth factor receptor-containing neurons in Alzheimer's disease: A quantitative analysis across subregions of the basal forebrain
    • Mufson, E. J., Bothwell, M., and Kordower, J. H. (1989). Loss of nerve growth factor receptor-containing neurons in Alzheimer's disease: a quantitative analysis across subregions of the basal forebrain. Exp Neurol 105(3), 221-232.
    • (1989) Exp Neurol , vol.105 , Issue.3 , pp. 221-232
    • Mufson, E.J.1    Bothwell, M.2    Kordower, J.H.3
  • 87
    • 0034843660 scopus 로고    scopus 로고
    • Cellular mechanisms for amyloid beta-protein activation of rat cholinergic basal forebrain neurons
    • Jhamandas, J. H., Cho, C., Jassar, B., Harris, K., MacTavish, D., and Easaw, J. (2001). Cellular mechanisms for amyloid beta-protein activation of rat cholinergic basal forebrain neurons. J Neurophysiol. 86(3), 1312-1320.
    • (2001) J Neurophysiol , vol.86 , Issue.3 , pp. 1312-1320
    • Jhamandas, J.H.1    Cho, C.2    Jassar, B.3    Harris, K.4    MacTavish, D.5    Easaw, J.6
  • 88
    • 2942591228 scopus 로고    scopus 로고
    • Failed retrograde transport of NGF in a mouse model of Down's syndrome: Reversal of cholinergic neurodegenerative phenotypes following NGF infusion
    • Cooper, J. D., Salehi, A., Delcroix, J. D., et al. (2001). Failed retrograde transport of NGF in a mouse model of Down's syndrome: reversal of cholinergic neurodegenerative phenotypes following NGF infusion. Proc Natl Acad Sci U S A. 98(18), 10,439-10,444.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , Issue.18
    • Cooper, J.D.1    Salehi, A.2    Delcroix, J.D.3
  • 89
    • 0034941330 scopus 로고    scopus 로고
    • Nerve growth factor signaling, neuroprotection, and neural repair
    • Sofroniew, M. V., Howe, C. L., and Mobley, W. C. (2001). Nerve growth factor signaling, neuroprotection, and neural repair. Annu Rev Neurosci. 24, 1217-1281.
    • (2001) Annu Rev Neurosci , vol.24 , pp. 1217-1281
    • Sofroniew, M.V.1    Howe, C.L.2    Mobley, W.C.3
  • 90
    • 0141864562 scopus 로고    scopus 로고
    • Glutamate and amyloid beta-protein rapidly inhibit fast axonal transport in cultured rat hippocampal neurons by different mechanisms
    • Hiruma, H., Katakura, T., Takahashi, S., Ichikawa, T., and Kawakami, T. (2003). Glutamate and amyloid beta-protein rapidly inhibit fast axonal transport in cultured rat hippocampal neurons by different mechanisms. J Neurosci. 23(26), 8967-8977.
    • (2003) J Neurosci , vol.23 , Issue.26 , pp. 8967-8977
    • Hiruma, H.1    Katakura, T.2    Takahashi, S.3    Ichikawa, T.4    Kawakami, T.5
  • 91
  • 92
    • 0031765270 scopus 로고    scopus 로고
    • Glutamate toxicity in chronic neurodegenerative disease
    • Lancelot, E., and Beal, M. F. (1998). Glutamate toxicity in chronic neurodegenerative disease. Prog Brain Res. 116, 331-347.
    • (1998) Prog Brain Res , vol.116 , pp. 331-347
    • Lancelot, E.1    Beal, M.F.2
  • 93
    • 0024990330 scopus 로고
    • Neurotoxic effect of amyloid beta protein: Reversal by tachykinin neuropeptides
    • Yankner, B. A., Duffy, L. K., and Kirschnur, D. A. (1990). Neurotoxic effect of amyloid beta protein: reversal by tachykinin neuropeptides. Science 250(4978), 279-282.
    • (1990) Science , vol.250 , Issue.4978 , pp. 279-282
    • Yankner, B.A.1    Duffy, L.K.2    Kirschnur, D.A.3
  • 94
    • 0037375473 scopus 로고    scopus 로고
    • C-terminal fragments of amyloid-beta peptide cause cholinergic axonal degeneration by a toxic effect rather than by physical injury in the nondemented human brain
    • Kasa, P., Papp, H., Zombori, J., Mayer, P., and Checler, F. (2003). C-terminal fragments of amyloid-beta peptide cause cholinergic axonal degeneration by a toxic effect rather than by physical injury in the nondemented human brain. Neurochem Res. 28(3-4), 493-498.
    • (2003) Neurochem Res , vol.28 , Issue.3-4 , pp. 493-498
    • Kasa, P.1    Papp, H.2    Zombori, J.3    Mayer, P.4    Checler, F.5
  • 95
    • 33745512851 scopus 로고    scopus 로고
    • Increased APP expression in a mouse model of Down's syndrome disrupts NGF transport and causes cholinergic neuron degeneration
    • Salehi, A., Delcroix, J. D., Belichenko, P. V., et al. (2006). Increased APP expression in a mouse model of Down's syndrome disrupts NGF transport and causes cholinergic neuron degeneration. Neuron 51, 29-42.
    • (2006) Neuron , vol.51 , pp. 29-42
    • Salehi, A.1    Delcroix, J.D.2    Belichenko, P.V.3
  • 96
    • 33746572249 scopus 로고    scopus 로고
    • Increased BACE1 maturation contributes to the pathogenesis of Alzheimer's disease in Down syndrome
    • Sun, X., Tong, Y., Qing, H., Chen, C. H., Song, W. (2006). Increased BACE1 maturation contributes to the pathogenesis of Alzheimer's disease in Down syndrome. FASEB J. 20(9), 1361-1368.
    • (2006) FASEB J , vol.20 , Issue.9 , pp. 1361-1368
    • Sun, X.1    Tong, Y.2    Qing, H.3    Chen, C.H.4    Song, W.5
  • 97
    • 33746549926 scopus 로고    scopus 로고
    • BACE2, as a novel APP theta-secretase, is not responsible for the pathogenesis of Alzheimer's disease in Down syndrome
    • Sun, X., He, G., and Song, W. (2006). BACE2, as a novel APP theta-secretase, is not responsible for the pathogenesis of Alzheimer's disease in Down syndrome. FASEB J. 20(9), 1369-1376.
    • (2006) FASEB J , vol.20 , Issue.9 , pp. 1369-1376
    • Sun, X.1    He, G.2    Song, W.3
  • 98
    • 33646171446 scopus 로고    scopus 로고
    • NFAT dysregulation by increased dosage of DSCR1 and DYRK1A on chromosome 21
    • Arron, J. R., Winslow, M. M., Polleri, A., et al. (2006). NFAT dysregulation by increased dosage of DSCR1 and DYRK1A on chromosome 21. Nature 441(7093), 595-600.
    • (2006) Nature , vol.441 , Issue.7093 , pp. 595-600
    • Arron, J.R.1    Winslow, M.M.2    Polleri, A.3
  • 99
    • 0033636136 scopus 로고    scopus 로고
    • Axonal transport of amyloid precursor protein is mediated by direct binding to the kinesin light chain subunit of kinesin-I
    • Kamal, A., Stokin, G. B., Yang, Z., Xia, C. H., and Goldstein, L. S. (2000). Axonal transport of amyloid precursor protein is mediated by direct binding to the kinesin light chain subunit of kinesin-I. Neuron 28(2), 449-459.
    • (2000) Neuron , vol.28 , Issue.2 , pp. 449-459
    • Kamal, A.1    Stokin, G.B.2    Yang, Z.3    Xia, C.H.4    Goldstein, L.S.5
  • 100
    • 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., LeBlanc, J. F., Roberts, E. A., and Goldstein, L. S. (2001). Kinesin-mediated axonal transport of a membrane compartment containing beta-secretase and presenilin-1 requires APP. Nature 414(6864), 643-648.
    • (2001) Nature , vol.414 , Issue.6864 , pp. 643-648
    • Kamal, A.1    Almenar-Queralt, A.2    LeBlanc, J.F.3    Roberts, E.A.4    Goldstein, L.S.5
  • 101
    • 0036883539 scopus 로고    scopus 로고
    • Presenilin-1 and the amyloid precursor protein are transported bidirectionally in the sciatic nerve of adult rat
    • Papp, H., Pakaski, M., and Kasa, P. (2002). Presenilin-1 and the amyloid precursor protein are transported bidirectionally in the sciatic nerve of adult rat. Neurochem Int. 41(6), 429-435.
    • (2002) Neurochem Int , vol.41 , Issue.6 , pp. 429-435
    • Papp, H.1    Pakaski, M.2    Kasa, P.3
  • 102
    • 0842320909 scopus 로고    scopus 로고
    • The beta-amyloid-related proteins presenilin 1 and BACE1 are axonally transported to nerve terminals in the brain
    • Sheng, J. G., Price, D.L., and Koliatsos, V. E. (2003). The beta-amyloid-related proteins presenilin 1 and BACE1 are axonally transported to nerve terminals in the brain. Exp Neurol. 184(2), 1053-1057.
    • (2003) Exp Neurol , vol.184 , Issue.2 , pp. 1053-1057
    • Sheng, J.G.1    Price, D.L.2    Koliatsos, V.E.3
  • 103
    • 0038603918 scopus 로고    scopus 로고
    • A scaffold protein JIP-1b enhances amyloid precursor protein phosphorylation by JNK and its association with kinesin light chain 1
    • Inomata, H., Nakamura, Y., Hayakawa, A., et al. (2003). A scaffold protein JIP-1b enhances amyloid precursor protein phosphorylation by JNK and its association with kinesin light chain 1. J Biol Chem. 278(25), 22,946-22,955.
    • (2003) J Biol Chem , vol.278 , Issue.25
    • Inomata, H.1    Nakamura, Y.2    Hayakawa, A.3
  • 104
    • 0141532147 scopus 로고    scopus 로고
    • Amyloid beta protein precursor (AbetaPP), but not AbetaPP-like protein 2, is bridged to the kinesin light chain by the scaffold protein JNK-interacting protein 1
    • Matsuda, S., Matsuda, Y., and D'Adamio, L. (2003). Amyloid beta protein precursor (AbetaPP), but not AbetaPP-like protein 2, is bridged to the kinesin light chain by the scaffold protein JNK-interacting protein 1. J Biol Chem. 278(40), 38,601-38,606.
    • (2003) J Biol Chem , vol.278 , Issue.40
    • Matsuda, S.1    Matsuda, Y.2    D'Adamio, L.3
  • 105
    • 0027322761 scopus 로고
    • Amyloid beta protein precursor accumulates in swollen neurites throughout rat brain with aging
    • Kawarabayashi, T., Shoji, M., Yamaguchi, H., et al. (1993). Amyloid beta protein precursor accumulates in swollen neurites throughout rat brain with aging. Neurosci Lett. 153(1), 73-76.
    • (1993) Neurosci Lett , vol.153 , Issue.1 , pp. 73-76
    • Kawarabayashi, T.1    Shoji, M.2    Yamaguchi, H.3
  • 106
    • 0028174629 scopus 로고
    • Beta amyloid protein deposition in the brain after severe head injury: Implications for the pathogenesis of Alzheimer's disease
    • Roberts, G. W., Gentleman, S. M., Lynch, A., Murray, L., Landon, M., and Graham, D. I. (1994). Beta amyloid protein deposition in the brain after severe head injury: implications for the pathogenesis of Alzheimer's disease. J Neurol Neurosurg Psychiatry 57(4), 419-425.
    • (1994) J Neurol Neurosurg Psychiatry , vol.57 , Issue.4 , pp. 419-425
    • Roberts, G.W.1    Gentleman, S.M.2    Lynch, A.3    Murray, L.4    Landon, M.5    Graham, D.I.6
  • 107
    • 0037404532 scopus 로고    scopus 로고
    • Amyloid beta accumulation in axons after traumatic brain injury in humans
    • Smith, D.H., Chen, X. H., Iwata, A., and Graham, D. I. (2003). Amyloid beta accumulation in axons after traumatic brain injury in humans. J Neurosurg. 98(5), 1072-1077.
    • (2003) J Neurosurg , vol.98 , Issue.5 , pp. 1072-1077
    • Smith, D.H.1    Chen, X.H.2    Iwata, A.3    Graham, D.I.4
  • 108
    • 3242770404 scopus 로고    scopus 로고
    • Long-term accumulation of amyloid-beta, beta-secretase, presenilin-1, and caspase-3 in damaged axons following brain trauma
    • Chen, X. H., Siman, R., Iwata, A., Meaney, D. F., Trojanowski, J. Q., and Smith, D. H. (2004). Long-term accumulation of amyloid-beta, beta-secretase, presenilin-1, and caspase-3 in damaged axons following brain trauma. Am J Pathol. 165(2), 357-371.
    • (2004) Am J Pathol , vol.165 , Issue.2 , pp. 357-371
    • Chen, X.H.1    Siman, R.2    Iwata, A.3    Meaney, D.F.4    Trojanowski, J.Q.5    Smith, D.H.6
  • 109
    • 33645019621 scopus 로고    scopus 로고
    • Linking molecular motors to Alzheimer's disease
    • Stokin, G. B. and Goldstein, L. S. (2006). Linking molecular motors to Alzheimer's disease. J Physiol Paris 99(2-3), 193-200.
    • (2006) J Physiol Paris , vol.99 , Issue.2-3 , pp. 193-200
    • Stokin, G.B.1    Goldstein, L.S.2
  • 110
    • 25144501662 scopus 로고    scopus 로고
    • Intraneuronal Abeta accumulation and origin of plaques in Alzheimer's disease
    • Gouras, G. K., Almeida, C.G., and Takahashi, R. H. (2005). Intraneuronal Abeta accumulation and origin of plaques in Alzheimer's disease. Neurobiol Aging. 26(9), 1235-1244.
    • (2005) Neurobiol Aging , vol.26 , Issue.9 , pp. 1235-1244
    • Gouras, G.K.1    Almeida, C.G.2    Takahashi, R.H.3
  • 111
    • 0030833055 scopus 로고    scopus 로고
    • Accelerated amyloid deposition in the brains of transgenic mice coexpressing mutant presenilin 1 and amyloid precursor proteins
    • Borchelt, D. R., Ratovitski, T., van Lare, J., et al. (1997). Accelerated amyloid deposition in the brains of transgenic mice coexpressing mutant presenilin 1 and amyloid precursor proteins. Neuron 19(4), 939-945.
    • (1997) Neuron , vol.19 , Issue.4 , pp. 939-945
    • Borchelt, D.R.1    Ratovitski, T.2    van Lare, J.3
  • 112
    • 0037899137 scopus 로고    scopus 로고
    • NGF signaling in sensory neurons: Evidence that early endosomes cary NGF retrograde signals
    • Delcroix, J. D., Valletta, J., Wu, C., Hunt, S. J., Kowal, A. S., and Mobley, W. C. (2003). NGF signaling in sensory neurons: evidence that early endosomes cary NGF retrograde signals. Neuron 39, 69-84.
    • (2003) Neuron , vol.39 , pp. 69-84
    • Delcroix, J.D.1    Valletta, J.2    Wu, C.3    Hunt, S.J.4    Kowal, A.S.5    Mobley, W.C.6
  • 113
    • 0028276801 scopus 로고
    • Evidence that production and release of amyloid beta-protein involves the endocytic pathway
    • Koo, E. H. and Squazzo, S. L. (1994). Evidence that production and release of amyloid beta-protein involves the endocytic pathway. J Biol Chem. 269(26), 17,386-17,389.
    • (1994) J Biol Chem , vol.269 , Issue.26
    • Koo, E.H.1    Squazzo, S.L.2
  • 114
    • 7244258941 scopus 로고    scopus 로고
    • Association of gamma-secretase with lipid rafts in post-Golgi and endosome membranes
    • Vetrivel, K. S., Cheng, H., Lin, W., et al. (2004). Association of gamma-secretase with lipid rafts in post-Golgi and endosome membranes. J Biol Chem. 279(43), 44,945-44,954.
    • (2004) J Biol Chem , vol.279 , Issue.43
    • Vetrivel, K.S.1    Cheng, H.2    Lin, W.3
  • 115
    • 0031939059 scopus 로고    scopus 로고
    • Molecular mapping of Alzheimer-type dementia in Down's syndrome
    • Prasher, V. P., Farrer, M. J. Kessling, A. M., et al. (1998). Molecular mapping of Alzheimer-type dementia in Down's syndrome. Ann Neurol. 43(3), 380-383.
    • (1998) Ann Neurol , vol.43 , Issue.3 , pp. 380-383
    • Prasher, V.P.1    Farrer, M.J.2    Kessling, A.M.3
  • 116
    • 3042808106 scopus 로고    scopus 로고
    • LIMK1 regulates Golgi dynamics, traffic of Golgi-derived vesicles, and process extension in primary cultured neurons
    • Rosso, S., Bollati, F., Bisbal, M., et al. (2004) LIMK1 regulates Golgi dynamics, traffic of Golgi-derived vesicles, and process extension in primary cultured neurons. Mol Biol Cell. 15(7), 3433-3449.
    • (2004) Mol Biol Cell , vol.15 , Issue.7 , pp. 3433-3449
    • Rosso, S.1    Bollati, F.2    Bisbal, M.3
  • 117
    • 0028204944 scopus 로고
    • Plasma lipids and cholesterol esterification in Alzheimer's disease
    • Knebl, J., DeFazio, P., Clearfield, M. B., et al. (1994). Plasma lipids and cholesterol esterification in Alzheimer's disease. Mech Ageing Dev. 73(1), 69-77.
    • (1994) Mech Ageing Dev , vol.73 , Issue.1 , pp. 69-77
    • Knebl, J.1    DeFazio, P.2    Clearfield, M.B.3
  • 118
    • 0033519601 scopus 로고    scopus 로고
    • The role of cholesterol in the biosynthesis of beta-amyloid
    • Frears, E. R., Stephens, D. J., Walters, C. E., Davies, H., and Austen, B. M. (1999). The role of cholesterol in the biosynthesis of beta-amyloid. Neuroreport 10(8), 1699-1705.
    • (1999) Neuroreport , vol.10 , Issue.8 , pp. 1699-1705
    • Frears, E.R.1    Stephens, D.J.2    Walters, C.E.3    Davies, H.4    Austen, B.M.5
  • 119
    • 0034623284 scopus 로고    scopus 로고
    • Mutant presenilin 2 transgenic mice. A large increase in the levels of Abeta 42 is presumably associated with the low density membrane domain that contains decreased levels of glycerophospholipids and sphingomyelin
    • Sawamura, N., Morishima-Kawashima, M., Waki, H., et al. (2000). Mutant presenilin 2 transgenic mice. A large increase in the levels of Abeta 42 is presumably associated with the low density membrane domain that contains decreased levels of glycerophospholipids and sphingomyelin. J Biol Chem. 275(36), 27,901-27,908.
    • (2000) J Biol Chem , vol.275 , Issue.36
    • Sawamura, N.1    Morishima-Kawashima, M.2    Waki, H.3
  • 120
    • 0036523031 scopus 로고    scopus 로고
    • Inhibition of intracellular cholesterol transport alters presenilin localization and amyloid precursor protein processing in neuronal cells
    • Runz, H., Rietdorf, J., Tomic, I., et al. (2002). Inhibition of intracellular cholesterol transport alters presenilin localization and amyloid precursor protein processing in neuronal cells. J Neurosci. 22(5), 1679-1689.
    • (2002) J Neurosci , vol.22 , Issue.5 , pp. 1679-1689
    • Runz, H.1    Rietdorf, J.2    Tomic, I.3
  • 121
    • 0038045571 scopus 로고    scopus 로고
    • Presenilin redistribution associated with aberrant cholesterol transport enhances beta-amyloid production in vivo
    • Burns, M., Gaynor, K., Olm, V., et al. (2003). Presenilin redistribution associated with aberrant cholesterol transport enhances beta-amyloid production in vivo. J Neurosci. 23(13), 5645-5649.
    • (2003) J Neurosci , vol.23 , Issue.13 , pp. 5645-5649
    • Burns, M.1    Gaynor, K.2    Olm, V.3
  • 122
    • 1242316263 scopus 로고    scopus 로고
    • Jin, L. W., Shie, F. S., Maezawa, I., Vincent, I., and Bird, T. (2004). Intracellular accumulation of amyloidogenic fragments of amyloid-beta precursor protein in neurons with Niemann-Pick type C defects is associated with endosomal abnormalities. Am J Pathol. 164(3), 975-985. Erratum in: Am J Pathol. 165(4), 1447.
    • Jin, L. W., Shie, F. S., Maezawa, I., Vincent, I., and Bird, T. (2004). Intracellular accumulation of amyloidogenic fragments of amyloid-beta precursor protein in neurons with Niemann-Pick type C defects is associated with endosomal abnormalities. Am J Pathol. 164(3), 975-985. Erratum in: Am J Pathol. 165(4), 1447.
  • 123
    • 21444445440 scopus 로고    scopus 로고
    • Statins cause intracellular accumulation of amyloid precursor protein, beta-secretase-cleaved fragments, and amyloid beta-peptide via an isoprenoid-dependent mechanism
    • Cole, S. L., Grudzien, A., Manhart, I. O., Kelly, B. L., Oakley, H., and Vassar, R. (2005). Statins cause intracellular accumulation of amyloid precursor protein, beta-secretase-cleaved fragments, and amyloid beta-peptide via an isoprenoid-dependent mechanism. J Biol Chem. 280(19), 18,755-18,770.
    • (2005) J Biol Chem , vol.280 , Issue.19
    • Cole, S.L.1    Grudzien, A.2    Manhart, I.O.3    Kelly, B.L.4    Oakley, H.5    Vassar, R.6
  • 124
    • 33646137779 scopus 로고    scopus 로고
    • Isoprenoids and Alzheimer's disease: A complex relationship
    • Cole, S. L. and Vassar, R. (2006). Isoprenoids and Alzheimer's disease: A complex relationship. Neurobiol Dis. 22(2), 209-222.
    • (2006) Neurobiol Dis , vol.22 , Issue.2 , pp. 209-222
    • Cole, S.L.1    Vassar, R.2
  • 126
    • 0034990260 scopus 로고    scopus 로고
    • Cholesterol depletion with physiological concentrations of a statin decreases the formation of the Alzheimer amyloid Abeta peptide
    • Buxbaum, J. D., Geoghagen, N. S., and Friedhoff, L. T. (2001). Cholesterol depletion with physiological concentrations of a statin decreases the formation of the Alzheimer amyloid Abeta peptide. J Alzheimers Dis. 3(2), 221-229.
    • (2001) J Alzheimers Dis , vol.3 , Issue.2 , pp. 221-229
    • Buxbaum, J.D.1    Geoghagen, N.S.2    Friedhoff, L.T.3
  • 127
    • 0001504829 scopus 로고    scopus 로고
    • Simvastatin strongly reduces levels of Alzheimer's disease beta -amyloid peptides Abeta 42 and Abeta 40 in vitro and in vivo
    • Fassbender, K., Simons, M., Bergmann, C., et al. (2001). Simvastatin strongly reduces levels of Alzheimer's disease beta -amyloid peptides Abeta 42 and Abeta 40 in vitro and in vivo. Proc Natl Acad Sci U S A. 98(10), 5856-5861.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , Issue.10 , pp. 5856-5861
    • Fassbender, K.1    Simons, M.2    Bergmann, C.3
  • 128
    • 0035826909 scopus 로고    scopus 로고
    • Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the alpha -secretase ADAM 10
    • Kojro, E., Gimpl, G., Lammich, S., Marz, W., and Fahrenholz, F. (2001). Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the alpha -secretase ADAM 10. Proc Natl Acad Sci U S A. 98(10), 5815-5820.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , Issue.10 , pp. 5815-5820
    • Kojro, E.1    Gimpl, G.2    Lammich, S.3    Marz, W.4    Fahrenholz, F.5
  • 129
    • 10344263931 scopus 로고    scopus 로고
    • Neuronal membrane cholesterol loss enhances amyloid peptide generation
    • Abad-Rodriguez, J., Ledesma, M. D., Craessaerts, K., et al. (2004). Neuronal membrane cholesterol loss enhances amyloid peptide generation. J Cell Biol. 167(5), 953-960.
    • (2004) J Cell Biol , vol.167 , Issue.5 , pp. 953-960
    • Abad-Rodriguez, J.1    Ledesma, M.D.2    Craessaerts, K.3
  • 130
    • 0029671454 scopus 로고    scopus 로고
    • Cholesterol modulates alpha-secretase cleavage of amyloid precursor protein
    • Bodovitz, S. and Klein, W. L. (1996). Cholesterol modulates alpha-secretase cleavage of amyloid precursor protein. J Biol Chem. 271(8), 4436-4440.
    • (1996) J Biol Chem , vol.271 , Issue.8 , pp. 4436-4440
    • Bodovitz, S.1    Klein, W.L.2
  • 131
    • 17644429206 scopus 로고    scopus 로고
    • Secretory processing of amyloid precursor protein is inhibited by increase in cellular cholesterol content
    • Racchi, M., Baetta, R., Salvietti, N., et al. (1997). Secretory processing of amyloid precursor protein is inhibited by increase in cellular cholesterol content. Biochem J. 322 (Pt 3), 893-898.
    • (1997) Biochem J , vol.322 , Issue.PART 3 , pp. 893-898
    • Racchi, M.1    Baetta, R.2    Salvietti, N.3
  • 132
    • 0034214328 scopus 로고    scopus 로고
    • Cholesterol decreases secretion of the secreted form of amyloid precursor protein by interfering with glycosylation in the protein secretory pathway
    • Galbete, J. L., Martin, T. R., Peressini, E., Modena, P., Bianchi, R., and Forloni, G. (2000). Cholesterol decreases secretion of the secreted form of amyloid precursor protein by interfering with glycosylation in the protein secretory pathway. Biochem J. 348(Pt 2), 307-313.
    • (2000) Biochem J , vol.348 , Issue.PART 2 , pp. 307-313
    • Galbete, J.L.1    Martin, T.R.2    Peressini, E.3    Modena, P.4    Bianchi, R.5    Forloni, G.6
  • 133
    • 0035928732 scopus 로고    scopus 로고
    • Compartmentalization of beta-secretase (Asp2) into low-buoyant density, noncaveolar lipid rafts
    • Riddell, D. R., Christie, G., Hussain, I., and Dingwall, C. (2001). Compartmentalization of beta-secretase (Asp2) into low-buoyant density, noncaveolar lipid rafts. Curr Biol. 11(16), 1288-1293.
    • (2001) Curr Biol , vol.11 , Issue.16 , pp. 1288-1293
    • Riddell, D.R.1    Christie, G.2    Hussain, I.3    Dingwall, C.4
  • 134
    • 0141482022 scopus 로고    scopus 로고
    • Exclusively targeting beta-secretase to lipid rafts by GPI-anchor addition up-regulates beta-site processing of the amyloid precursor protein
    • Cordy, J. M., Hussain, I., Dingwall, C., Hooper, N. M., and Turner, A. J. (2003). Exclusively targeting beta-secretase to lipid rafts by GPI-anchor addition up-regulates beta-site processing of the amyloid precursor protein. Proc Natl Acad Sci U S A. 100(20), 11,735-11,740.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , Issue.20
    • Cordy, J.M.1    Hussain, I.2    Dingwall, C.3    Hooper, N.M.4    Turner, A.J.5
  • 135
    • 15744397372 scopus 로고    scopus 로고
    • Pedrini, S., Carter, T. L., Prendergast, G., Petanceska, S., Ehrlich, M. E., and Gandy, S. (2005). Modulation of statin-activated shedding of Alzheimer APP ectodomain by ROCK. PLoS Med. 2(1), e18., 0069-0078.
    • Pedrini, S., Carter, T. L., Prendergast, G., Petanceska, S., Ehrlich, M. E., and Gandy, S. (2005). Modulation of statin-activated shedding of Alzheimer APP ectodomain by ROCK. PLoS Med. 2(1), e18., 0069-0078.
  • 136
    • 9144236957 scopus 로고    scopus 로고
    • Inhibition of geranylgeranylation mediates the effects of 3-hydroxy-3-methylglutaryl (HMG)-CoA reductase inhibitors on microglia
    • Bi, X., Baudry, M., Liu, J., et al. (2004). Inhibition of geranylgeranylation mediates the effects of 3-hydroxy-3-methylglutaryl (HMG)-CoA reductase inhibitors on microglia. J Biol Chem. 279(46), 48,238-48,245.
    • (2004) J Biol Chem , vol.279 , Issue.46
    • Bi, X.1    Baudry, M.2    Liu, J.3
  • 137
    • 3242766006 scopus 로고    scopus 로고
    • Statin blocks Rho/Rho-kinase signalling and disrupts the actin cytoskeleton: Relationship to enhancement of LPS-mediated nitric oxide synthesis in vascular smooth muscle cells
    • Kato, T., Hashikabe, H., Iwata, C., Akimoto, K., and Hattori, Y. (2004). Statin blocks Rho/Rho-kinase signalling and disrupts the actin cytoskeleton: relationship to enhancement of LPS-mediated nitric oxide synthesis in vascular smooth muscle cells. Biochim Biophys Acta. 1689(3), 267-272.
    • (2004) Biochim Biophys Acta , vol.1689 , Issue.3 , pp. 267-272
    • Kato, T.1    Hashikabe, H.2    Iwata, C.3    Akimoto, K.4    Hattori, Y.5
  • 138
  • 139
    • 0033998587 scopus 로고    scopus 로고
    • The branch point enzyme of the mevalonate pathway for protein prenylation is overexpressed in the ob/ob mouse and induced by adipogenesis
    • Vicent, D., Maratos-Flier, E., and Kahn, C. R. (2000). The branch point enzyme of the mevalonate pathway for protein prenylation is overexpressed in the ob/ob mouse and induced by adipogenesis. Mol Cell Biol. 20(6), 2158-2166.
    • (2000) Mol Cell Biol , vol.20 , Issue.6 , pp. 2158-2166
    • Vicent, D.1    Maratos-Flier, E.2    Kahn, C.R.3
  • 140
    • 0034997092 scopus 로고    scopus 로고
    • Rho proteins: Linking signaling with membrane trafficking
    • Ridley, A. J. (2001). Rho proteins: linking signaling with membrane trafficking. Traffic 2(5), 303-310.
    • (2001) Traffic , vol.2 , Issue.5 , pp. 303-310
    • Ridley, A.J.1
  • 141
    • 25444474703 scopus 로고    scopus 로고
    • Mitochondria take center stage in aging and neurodegeneration
    • Beal, M. F. (2005). Mitochondria take center stage in aging and neurodegeneration. Ann Neurol. 58(4), 495-505.
    • (2005) Ann Neurol , vol.58 , Issue.4 , pp. 495-505
    • Beal, M.F.1
  • 142
    • 33646922865 scopus 로고    scopus 로고
    • Reduction in mitochondrial superoxide dismutase modulates Alzheimer's disease-like pathology and accelerates the onset of behavioral changes in human amyloid precursor protein transgenic mice
    • Espisoto, L., Raber, J., Kekonius, L., et al. (2006). Reduction in mitochondrial superoxide dismutase modulates Alzheimer's disease-like pathology and accelerates the onset of behavioral changes in human amyloid precursor protein transgenic mice. J. Neurosci. 26(19), 5167-5179.
    • (2006) J. Neurosci , vol.26 , Issue.19 , pp. 5167-5179
    • Espisoto, L.1    Raber, J.2    Kekonius, L.3
  • 143
    • 33751082967 scopus 로고    scopus 로고
    • Formation of Actin-ADF/Cofilin rods transiently retards decline of mitochondrial potential and ATP in stressed neurons
    • Bernstein, B. W., Chen, H., Boyle, J. A., and Bamburg, J. R. (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-C839.
    • (2006) Am. J. Physiol. Cell Physiol , vol.291
    • Bernstein, B.W.1    Chen, H.2    Boyle, J.A.3    Bamburg, J.R.4
  • 144
    • 0018410202 scopus 로고
    • Accelerated ageing or selective neuronal loss as an important cause of dementia?
    • Bowen, D. M., White, P., Spillane, J. A., et al. (1979). Accelerated ageing or selective neuronal loss as an important cause of dementia? Lancet 1(8106), 11-14.
    • (1979) Lancet , vol.1 , Issue.8106 , pp. 11-14
    • Bowen, D.M.1    White, P.2    Spillane, J.A.3
  • 145
    • 0035341254 scopus 로고    scopus 로고
    • Mitochondrial abnormalities in Alzheimer's disease
    • Hirai, K., Aliev, G., Nunomura, A., et al. (2001). Mitochondrial abnormalities in Alzheimer's disease. J Neurosci. 21(9), 3017-3023.
    • (2001) J Neurosci , vol.21 , Issue.9 , pp. 3017-3023
    • Hirai, K.1    Aliev, G.2    Nunomura, A.3
  • 146
    • 0036982389 scopus 로고    scopus 로고
    • Mitochondria in Alzheimer's disease
    • Swerdlow, R. H. and Kish, S. J. (2002). Mitochondria in Alzheimer's disease. Int Rev Neurobiol. 53, 341-385.
    • (2002) Int Rev Neurobiol , vol.53 , pp. 341-385
    • Swerdlow, R.H.1    Kish, S.J.2
  • 147
    • 13844266044 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of mitochondria from primary neuron cultures treated with amyloid beta peptide
    • Lovell, M. A., Xiong, S., Markesbery, W. R., and Lynn, B. C. (2005). Quantitative proteomic analysis of mitochondria from primary neuron cultures treated with amyloid beta peptide. Neurochem Res. 30(1), 113-122.
    • (2005) Neurochem Res , vol.30 , Issue.1 , pp. 113-122
    • Lovell, M.A.1    Xiong, S.2    Markesbery, W.R.3    Lynn, B.C.4
  • 148
    • 0029992233 scopus 로고    scopus 로고
    • Embryonic genes expressed in Alzheimer's disease brains
    • Kondo, T., Shirasawa, T., Itoyama, Y., and Mori, H. (1996). Embryonic genes expressed in Alzheimer's disease brains. Neurosci Lett. 209(3), 157-160.
    • (1996) Neurosci Lett , vol.209 , Issue.3 , pp. 157-160
    • Kondo, T.1    Shirasawa, T.2    Itoyama, Y.3    Mori, H.4
  • 149
    • 33745920512 scopus 로고    scopus 로고
    • Phosphorylation of rat brain mitochondrial voltage-dependent anion as a potential tool to control leakage of cytochrome c
    • Jun 19;
    • Banerjee, J. and Ghosh, S. (2006). Phosphorylation of rat brain mitochondrial voltage-dependent anion as a potential tool to control leakage of cytochrome c. J Neurochem., Jun 19; 98, 670-676.
    • (2006) J Neurochem , vol.98 , pp. 670-676
    • Banerjee, J.1    Ghosh, S.2
  • 150
    • 0344668558 scopus 로고    scopus 로고
    • Mitochondrial translocation of cofilin is an early step in apoptosis induction
    • Chua, B. T., Volbracht, C., Tan, K. O., Li, R., Yu, V. C., and Li, P. (2003). Mitochondrial translocation of cofilin is an early step in apoptosis induction. Nat Cell Biol. 5(12), 1083-1089.
    • (2003) Nat Cell Biol , vol.5 , Issue.12 , pp. 1083-1089
    • Chua, B.T.1    Volbracht, C.2    Tan, K.O.3    Li, R.4    Yu, V.C.5    Li, P.6
  • 151
    • 1842783552 scopus 로고    scopus 로고
    • Overexpression of LIM kinase 1 renders resistance to apoptosis in PC12 cells by inhibition of caspase activation
    • Yang, E., Kim, H., Lee, J., et al. (2004). Overexpression of LIM kinase 1 renders resistance to apoptosis in PC12 cells by inhibition of caspase activation. Cell Mol Neurobiol. 24(2), 181-192.
    • (2004) Cell Mol Neurobiol , vol.24 , Issue.2 , pp. 181-192
    • Yang, E.1    Kim, H.2    Lee, J.3
  • 152
    • 27744577768 scopus 로고    scopus 로고
    • The actin cytoskeleton in ageing and apoptosis
    • Gourlay C. W. and Ayscough, K. R., (2005). The actin cytoskeleton in ageing and apoptosis. FEMS Yeast Res 5(12), 1193-1198.
    • (2005) FEMS Yeast Res , vol.5 , Issue.12 , pp. 1193-1198
    • Gourlay, C.W.1    Ayscough, K.R.2
  • 153
    • 1642277090 scopus 로고    scopus 로고
    • A role for the actin cytoskeleton in cell death and aging in yeast
    • Gourlay, C. W., Carpp, L. N., Timpson, P., Winder, S. J., and Ayschough, K. R. (2004). A role for the actin cytoskeleton in cell death and aging in yeast. J Cell Biol. 164(6), 803-809.
    • (2004) J Cell Biol , vol.164 , Issue.6 , pp. 803-809
    • Gourlay, C.W.1    Carpp, L.N.2    Timpson, P.3    Winder, S.J.4    Ayschough, K.R.5
  • 154
    • 28844492153 scopus 로고    scopus 로고
    • A role for actin in aging and apoptosis
    • Gourlay, C. W. and Ayscough, K. R. (2005). A role for actin in aging and apoptosis. Biochem Soc Trans. 33(6), 1260-1264.
    • (2005) Biochem Soc Trans , vol.33 , Issue.6 , pp. 1260-1264
    • Gourlay, C.W.1    Ayscough, K.R.2
  • 155
    • 21044450363 scopus 로고    scopus 로고
    • Identification of an upstream regulatory pathway controlling actin-mediated apoptosis in yeast
    • Gourlay, C. W. and Ayschogh, K. R. (2005). Identification of an upstream regulatory pathway controlling actin-mediated apoptosis in yeast. J Cell Sci. 118(10), 2119-2132.
    • (2005) J Cell Sci , vol.118 , Issue.10 , pp. 2119-2132
    • Gourlay, C.W.1    Ayschogh, K.R.2
  • 156
    • 0036479011 scopus 로고    scopus 로고
    • The voltage-dependent anion channel: An essential player in apoptosis
    • Tsujimoto, Y. and Shimizu, S. (2002). The voltage-dependent anion channel: an essential player in apoptosis. Biochimie 84, 187-193.
    • (2002) Biochimie , vol.84 , pp. 187-193
    • Tsujimoto, Y.1    Shimizu, S.2
  • 157
    • 14244269224 scopus 로고    scopus 로고
    • Oligomeric states of the voltage-dependent anion channel and cytochrome c release from mitochondria
    • Zalk, R., Israelson, A., Garty, E. S., Azoulay-Zohar, H., and Shoshan-Barmatz, V. (2005). Oligomeric states of the voltage-dependent anion channel and cytochrome c release from mitochondria. Biochem J. 386(Pt 1), 73-83.
    • (2005) Biochem J , vol.386 , Issue.PART 1 , pp. 73-83
    • Zalk, R.1    Israelson, A.2    Garty, E.S.3    Azoulay-Zohar, H.4    Shoshan-Barmatz, V.5
  • 158
    • 0034685808 scopus 로고    scopus 로고
    • Gelsolin inhibits apoptosis by blocking mitochondrial membrane potential loss and cytochrome c release
    • Koya, R. C., Fujita, H., Shimizu, S., et al. (2000). Gelsolin inhibits apoptosis by blocking mitochondrial membrane potential loss and cytochrome c release. J Biol Chem. 275(20), 15,343-15,349.
    • (2000) J Biol Chem , vol.275 , Issue.20
    • Koya, R.C.1    Fujita, H.2    Shimizu, S.3
  • 159
    • 0034609764 scopus 로고    scopus 로고
    • Human gelsolin prevents apoptosis by inhibiting apoptotic mitochondrial changes via closing VDAC
    • Kusano, H., Shimizu, S., Koya, R. C., et al. (2000). Human gelsolin prevents apoptosis by inhibiting apoptotic mitochondrial changes via closing VDAC. Oncogene 19(42), 4807-4814
    • (2000) Oncogene , vol.19 , Issue.42 , pp. 4807-4814
    • Kusano, H.1    Shimizu, S.2    Koya, R.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.