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Volumn 3, Issue 2, 2008, Pages

Aβ42 mutants with different aggregation profiles induce distinct pathologies in Drosophila

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; COMPLEMENTARY DNA; MUTANT PROTEIN; AMYLOID BETA PROTEIN;

EID: 45949102576     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0001703     Document Type: Article
Times cited : (141)

References (43)
  • 1
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe DJ (2001) Alzheimer's disease: genes, proteins, and therapy. Physiol Rev 81: 741-766.
    • (2001) Physiol Rev , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 3
    • 13944276825 scopus 로고    scopus 로고
    • Twenty years of the Alzheimer's disease amyloid hypothesis: A genetic perspective
    • Tanzi RE, Bertram L (2005) Twenty years of the Alzheimer's disease amyloid hypothesis: a genetic perspective. Cell 120: 545-555.
    • (2005) Cell , vol.120 , pp. 545-555
    • Tanzi, R.E.1    Bertram, L.2
  • 4
    • 17944368176 scopus 로고    scopus 로고
    • The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Abeta protofibril formation
    • Nilsberth C, Westlind-Danielsson A, Eckman CB, Condron MM, Axelman K, et al. (2001) The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Abeta protofibril formation. Nat Neurosci 4: 887-893.
    • (2001) Nat Neurosci , vol.4 , pp. 887-893
    • Nilsberth, C.1    Westlind-Danielsson, A.2    Eckman, C.B.3    Condron, M.M.4    Axelman, K.5
  • 5
    • 33745272215 scopus 로고    scopus 로고
    • Physiochemical characterization of the Alzheimer's disease-related peptides A beta 1-42Arctic and A beta 1-42wt
    • Johansson AS, Berglind-Dehlin F, Karlsson G, Edwards K, Gellerfors P, et al. (2006) Physiochemical characterization of the Alzheimer's disease-related peptides A beta 1-42Arctic and A beta 1-42wt. Febs J 273: 2618-2630.
    • (2006) Febs J , vol.273 , pp. 2618-2630
    • Johansson, A.S.1    Berglind-Dehlin, F.2    Karlsson, G.3    Edwards, K.4    Gellerfors, P.5
  • 6
    • 33750361540 scopus 로고    scopus 로고
    • A century-old debate on protein aggregation and neurodegenerstion enters the clinic
    • Lansbury PT, Lashuel HA (2006) A century-old debate on protein aggregation and neurodegenerstion enters the clinic. Nature 443: 774-779.
    • (2006) Nature , vol.443 , pp. 774-779
    • Lansbury, P.T.1    Lashuel, H.A.2
  • 7
    • 7444221875 scopus 로고    scopus 로고
    • Harnessing chaperones to generate small-molecule inhibitors of amyloid beta aggregation
    • Gestwicki JE, Crabtree GR, Graef IA (2004) Harnessing chaperones to generate small-molecule inhibitors of amyloid beta aggregation. Science 306: 865-869.
    • (2004) Science , vol.306 , pp. 865-869
    • Gestwicki, J.E.1    Crabtree, G.R.2    Graef, I.A.3
  • 8
    • 0024472693 scopus 로고
    • Neurotoxicity of a fragment of the amyloid precursor associated with Alzheimer's disease
    • Yankner BA, Dawes LR, Fisher S, Villa-Komaroff L, Oster-Granite ML, et al. (1989) Neurotoxicity of a fragment of the amyloid precursor associated with Alzheimer's disease. Science 245: 417-420.
    • (1989) Science , vol.245 , pp. 417-420
    • Yankner, B.A.1    Dawes, L.R.2    Fisher, S.3    Villa-Komaroff, L.4    Oster-Granite, M.L.5
  • 9
    • 0242580170 scopus 로고    scopus 로고
    • Neurotoxicity and physicochemical properties of Abeta mutant peptides from cerebral amyloid angiopathy. implication for the pathogenesis of cerebral amyloid angiopathy and Alzheimer's disease
    • Murakami K, Irie K, Morimoto A, Ohigashi H, Shindo M, et al. (2003) Neurotoxicity and physicochemical properties of Abeta mutant peptides from cerebral amyloid angiopathy. implication for the pathogenesis of cerebral amyloid angiopathy and Alzheimer's disease. J Biol Chem 278: 46179-46187.
    • (2003) J Biol Chem , vol.278 , pp. 46179-46187
    • Murakami, K.1    Irie, K.2    Morimoto, A.3    Ohigashi, H.4    Shindo, M.5
  • 10
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • Caughey B, Lansbury PT (2003) Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu Rev Neurosci 26: 267-298.
    • (2003) Annu Rev Neurosci , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 11
    • 2542455537 scopus 로고    scopus 로고
    • Small assemblies of unmodified amyloid beta-protein are the proximate neurotoxin in Alzheimer's disease
    • Klein WJ, Stine WB Jr, Teplow DB (2004) Small assemblies of unmodified amyloid beta-protein are the proximate neurotoxin in Alzheimer's disease. Neurobiol Aging 25: 569-580.
    • (2004) Neurobiol Aging , vol.25 , pp. 569-580
    • Klein, W.J.1    Stine Jr, W.B.2    Teplow, D.B.3
  • 12
    • 12244249201 scopus 로고    scopus 로고
    • Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils
    • Petkova AT, Leapman RD, Guo Z, Yau WM, Mattson MP, et al. (2005) Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils. Science 307: 262-265.
    • (2005) Science , vol.307 , pp. 262-265
    • Petkova, A.T.1    Leapman, R.D.2    Guo, Z.3    Yau, W.M.4    Mattson, M.P.5
  • 13
    • 33746237577 scopus 로고    scopus 로고
    • To be or not to be toxic: Aggregations in Huntington and Alzheimer disease
    • Slow EJ, Graham RK, Hayden MR (2006) To be or not to be toxic: aggregations in Huntington and Alzheimer disease. Trends Genet 22: 4408-411.
    • (2006) Trends Genet , vol.22 , pp. 4408-4411
    • Slow, E.J.1    Graham, R.K.2    Hayden, M.R.3
  • 14
    • 2342473791 scopus 로고    scopus 로고
    • Dissecting the pathological effects of human Abeta40 and Abeta42 in Drosophila: A potential model for Alzheimer's disease
    • Iijima K, Liu HP, Chiang AS, Hearn SA, Konsolaki M, et al. (2004) Dissecting the pathological effects of human Abeta40 and Abeta42 in Drosophila: a potential model for Alzheimer's disease. Proc Natl Acad Sci U S A 101: 6623-6628.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 6623-6628
    • Iijima, K.1    Liu, H.P.2    Chiang, A.S.3    Hearn, S.A.4    Konsolaki, M.5
  • 15
    • 26944437967 scopus 로고    scopus 로고
    • Small non-fibrillar assemblies of amyloid beta-protein bearing the Arctic mutation induce rapid neuritic degeneration
    • Whalen BM, Selkoe DJ, Hartley DM (2005) Small non-fibrillar assemblies of amyloid beta-protein bearing the Arctic mutation induce rapid neuritic degeneration. Neurobiol Dis 20: 254-266.
    • (2005) Neurobiol Dis , vol.20 , pp. 254-266
    • Whalen, B.M.1    Selkoe, D.J.2    Hartley, D.M.3
  • 16
    • 9144272296 scopus 로고    scopus 로고
    • Aggressive amyloidosis in mice expressing human amyloid peptides with the Arctic mutation
    • Cheng IH, Palop JJ, Esposito LA, Bien-Ly N, Yan F, et al. (2004) Aggressive amyloidosis in mice expressing human amyloid peptides with the Arctic mutation. Nat Med 10: 1190-1192.
    • (2004) Nat Med , vol.10 , pp. 1190-1192
    • Cheng, I.H.1    Palop, J.J.2    Esposito, L.A.3    Bien-Ly, N.4    Yan, F.5
  • 17
    • 27744512118 scopus 로고    scopus 로고
    • The Arctic Alzheimer mutation facilitates early intraneuronal Abeta aggregation and senile plaque formation in transgenic mice
    • Lord A, Kalimo H, Eckman C, Zhang XQ, Lannfelt L, et al. (2006) The Arctic Alzheimer mutation facilitates early intraneuronal Abeta aggregation and senile plaque formation in transgenic mice, Neurobiol Aging 27: 67-77.
    • (2006) Neurobiol Aging , vol.27 , pp. 67-77
    • Lord, A.1    Kalimo, H.2    Eckman, C.3    Zhang, X.Q.4    Lannfelt, L.5
  • 18
    • 10644284600 scopus 로고    scopus 로고
    • Analysis of the secondary structure of beta-amyloid (Abeta42) fibrils by systematic proline replacement
    • Morimoto A, Irie K, Murakami K, Masuda Y, Ohigashi H, et al. (2004) Analysis of the secondary structure of beta-amyloid (Abeta42) fibrils by systematic proline replacement. J Biol Chem 279: 52781-52788.
    • (2004) J Biol Chem , vol.279 , pp. 52781-52788
    • Morimoto, A.1    Irie, K.2    Murakami, K.3    Masuda, Y.4    Ohigashi, H.5
  • 19
    • 0031712488 scopus 로고    scopus 로고
    • In vivo aggregation of beta-amyloid peptide variants
    • Fay DS, Fluet A, Johnson CJ, Link CD (1998) In vivo aggregation of beta-amyloid peptide variants. J Neurochem 71: 1616-1625.
    • (1998) J Neurochem , vol.71 , pp. 1616-1625
    • Fay, D.S.1    Fluet, A.2    Johnson, C.J.3    Link, C.D.4
  • 20
    • 0027160708 scopus 로고
    • Targeted gene expression as a means of altering cell fates and generating dominant phenotypes
    • Brand AH, Perrimon N (1993) Targeted gene expression as a means of altering cell fates and generating dominant phenotypes. Development 118: 401-415.
    • (1993) Development , vol.118 , pp. 401-415
    • Brand, A.H.1    Perrimon, N.2
  • 21
    • 0242668337 scopus 로고    scopus 로고
    • Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of Pathogenesis
    • Kayed R, Head E, Thompson JL, McIntire TM, Milton SC, et al. (2003) Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of Pathogenesis. Science 300: 486-489.
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5
  • 22
    • 0018103643 scopus 로고
    • On the relationship between senescence and age-related changes in two wild-type strains of Drosophila melanogaster
    • Ganetzky B, Flanagan JR (1978) On the relationship between senescence and age-related changes in two wild-type strains of Drosophila melanogaster. Exp Gerontol 13: 189-196.
    • (1978) Exp Gerontol , vol.13 , pp. 189-196
    • Ganetzky, B.1    Flanagan, J.R.2
  • 23
    • 0022119763 scopus 로고
    • Classical conditioning and retention in normal and mutant Drosophila melanogaster
    • Tully T, Quinn WG (1985) Classical conditioning and retention in normal and mutant Drosophila melanogaster. J Comp Physiol [A] 157: 263-277.
    • (1985) J Comp Physiol , vol.157 , Issue.A , pp. 263-277
    • Tully, T.1    Quinn, W.G.2
  • 24
    • 0037174618 scopus 로고    scopus 로고
    • Alzheimer's disease is a synaptic failure
    • Selkoe DJ (2002) Alzheimer's disease is a synaptic failure. Science 298: 789-791.
    • (2002) Science , vol.298 , pp. 789-791
    • Selkoe, D.J.1
  • 25
    • 0038439322 scopus 로고    scopus 로고
    • Mushroom body memoir: From maps to models
    • Heisenberg M (2003) Mushroom body memoir: from maps to models. Nat Rev Neurosci 4: 266-275.
    • (2003) Nat Rev Neurosci , vol.4 , pp. 266-275
    • Heisenberg, M.1
  • 26
    • 0038198738 scopus 로고    scopus 로고
    • Axon pruning during Drosophila metamorphosis: Evidence for local degeneration and requirement of the ubiquitin-proteasome system
    • Watts RJ, Hoopler ED, Luo L (2003) Axon pruning during Drosophila metamorphosis: evidence for local degeneration and requirement of the ubiquitin-proteasome system. Neuron 38: 871-885.
    • (2003) Neuron , vol.38 , pp. 871-885
    • Watts, R.J.1    Hoopler, E.D.2    Luo, L.3
  • 27
    • 33846115694 scopus 로고    scopus 로고
    • Genetic and environmental modifiers of Alzheimer's disease phenotypes in the mouse
    • Ryman D, Lamb BT (2006) Genetic and environmental modifiers of Alzheimer's disease phenotypes in the mouse. Curr Alzheimer Res 3: 465-473.
    • (2006) Curr Alzheimer Res , vol.3 , pp. 465-473
    • Ryman, D.1    Lamb, B.T.2
  • 28
    • 33749042749 scopus 로고    scopus 로고
    • Sorting through the cell biology of Alzheimer's disease: Intracellular pathways to pathogenesis
    • Small SA, Gandy S (2006) Sorting through the cell biology of Alzheimer's disease: intracellular pathways to pathogenesis. Neuron 52: 15-31.
    • (2006) Neuron , vol.52 , pp. 15-31
    • Small, S.A.1    Gandy, S.2
  • 29
    • 2142645114 scopus 로고    scopus 로고
    • Age-dependent neurodegeneration and Alzheimer-amyloid plaque formation in transgenic Drosophila
    • Grieve I, Kretzschmar D, Tschape JA, Beyn A, Brellinger C, et al. (2004) Age-dependent neurodegeneration and Alzheimer-amyloid plaque formation in transgenic Drosophila. J Neurosci 24: 3899-3906.
    • (2004) J Neurosci , vol.24 , pp. 3899-3906
    • Grieve, I.1    Kretzschmar, D.2    Tschape, J.A.3    Beyn, A.4    Brellinger, C.5
  • 30
    • 0027407570 scopus 로고
    • Generation of beta-amyloid in the secretory pathway in neuronal and nonneuronal cells
    • Busciglio J, Gabuzda DH, Matsudaira P, Yankner BA (1993) Generation of beta-amyloid in the secretory pathway in neuronal and nonneuronal cells. Proc Natl Acad Sci U S A 90: 2092-2096.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 2092-2096
    • Busciglio, J.1    Gabuzda, D.H.2    Matsudaira, P.3    Yankner, B.A.4
  • 31
    • 0030769092 scopus 로고    scopus 로고
    • Alzheimer's A beta(1-42) is generated in the endoplasmic reticulum/ intermediate compartment of NT2N cells
    • Cook DG, Forman MS, Sung JC, Leight S, Kolson DL, et al. (1997) Alzheimer's A beta(1-42) is generated in the endoplasmic reticulum/ intermediate compartment of NT2N cells. Nat Med 3: 1021-1023.
    • (1997) Nat Med , vol.3 , pp. 1021-1023
    • Cook, D.G.1    Forman, M.S.2    Sung, J.C.3    Leight, S.4    Kolson, D.L.5
  • 32
    • 0031746979 scopus 로고    scopus 로고
    • A detergent-insoluble membrane compartment contains A beta in vivo
    • Lee SJ, Liyanage U, Bickel PE, Xia W, Lansbury PT Jr, et al. (1998) A detergent-insoluble membrane compartment contains A beta in vivo. Nat Med 4: 730-734.
    • (1998) Nat Med , vol.4 , pp. 730-734
    • Lee, S.J.1    Liyanage, U.2    Bickel, P.E.3    Xia, W.4    Lansbury Jr, P.T.5
  • 33
    • 0031781642 scopus 로고    scopus 로고
    • Detection of a novel intraneuronal pool of insoluble amyloid beta protein that accumulates with time in culture
    • Skovronsky DM, Doms RW, Lee VM (1998) Detection of a novel intraneuronal pool of insoluble amyloid beta protein that accumulates with time in culture. J Cell Biol 141: 1031-1039.
    • (1998) J Cell Biol , vol.141 , pp. 1031-1039
    • Skovronsky, D.M.1    Doms, R.W.2    Lee, V.M.3
  • 34
    • 0030952217 scopus 로고    scopus 로고
    • Intracellular generation and accumulation of amyloid beta-peptide terminating at amino acid 42
    • Wild-Bode C, Yamazaki T, Capell A, Leimer U, Steiner H, et al. (1997) Intracellular generation and accumulation of amyloid beta-peptide terminating at amino acid 42. J Biol Chem 272: 16085-16088.
    • (1997) J Biol Chem , vol.272 , pp. 16085-16088
    • Wild-Bode, C.1    Yamazaki, T.2    Capell, A.3    Leimer, U.4    Steiner, H.5
  • 35
    • 33749826587 scopus 로고    scopus 로고
    • p25/ cyclin-dependent kinase 5 induces production and intraneuronal accumulation of amyloid beta in vivo
    • Cruz JC, Kim D, Moy LY, Dobbin MM, Sun X, et al. (2006) p25/ cyclin-dependent kinase 5 induces production and intraneuronal accumulation of amyloid beta in vivo. J Neurosci 26: 10536-10541.
    • (2006) J Neurosci , vol.26 , pp. 10536-10541
    • Cruz, J.C.1    Kim, D.2    Moy, L.Y.3    Dobbin, M.M.4    Sun, X.5
  • 36
    • 13744253923 scopus 로고    scopus 로고
    • Attacking amyloid
    • Kelly JW (2005) Attacking amyloid. N Engl J Med 352: 722-723.
    • (2005) N Engl J Med , vol.352 , pp. 722-723
    • Kelly, J.W.1
  • 37
  • 38
    • 9144224765 scopus 로고    scopus 로고
    • ApoE and clusterin cooperatively suppress Abeta levels and deposition: Evidence that ApoE regulates extracellular Abeta metabolism in vivo
    • DeMattos RB, Cirrito JR, Parsadanian M, May PC, O'Dell MA, et al. (2004) ApoE and clusterin cooperatively suppress Abeta levels and deposition: evidence that ApoE regulates extracellular Abeta metabolism in vivo. Neuron 41: 193-202.
    • (2004) Neuron , vol.41 , pp. 193-202
    • DeMattos, R.B.1    Cirrito, J.R.2    Parsadanian, M.3    May, P.C.4    O'Dell, M.A.5
  • 39
    • 0034964390 scopus 로고    scopus 로고
    • Treatment with a copper-zinc chelator markedly and rapidly inhibits beta-amyloid accumulation in Alzheimer's disease transgenic mice
    • Cherny RA, Atwood CS, Xilinas ME, Gray DN, Jones WD, et al. (2001) Treatment with a copper-zinc chelator markedly and rapidly inhibits beta-amyloid accumulation in Alzheimer's disease transgenic mice. Neuron 30: 665-676.
    • (2001) Neuron , vol.30 , pp. 665-676
    • Cherny, R.A.1    Atwood, C.S.2    Xilinas, M.E.3    Gray, D.N.4    Jones, W.D.5
  • 41
    • 0033637008 scopus 로고    scopus 로고
    • Cognidve and behavioral heterogeneity in Alzheimer's disease: Seeking the neurobiological basis
    • Cummings JL (2000) Cognidve and behavioral heterogeneity in Alzheimer's disease: seeking the neurobiological basis. Neurobiol Aging 21: 845-861.
    • (2000) Neurobiol Aging , vol.21 , pp. 845-861
    • Cummings, J.L.1
  • 42
    • 33749020837 scopus 로고    scopus 로고
    • Exogenous induction of cerebral beta-amyloidogenesis is governed by agent and host
    • Meyer-Luehmann M, Coomaraswamy J, Bolmont T, Kaeser S, Schaefer C, et al. (2006) Exogenous induction of cerebral beta-amyloidogenesis is governed by agent and host. Science 313: 1781-1784.
    • (2006) Science , vol.313 , pp. 1781-1784
    • Meyer-Luehmann, M.1    Coomaraswamy, J.2    Bolmont, T.3    Kaeser, S.4    Schaefer, C.5
  • 43
    • 0030864464 scopus 로고    scopus 로고
    • The swiss cheese mutant causes glial hyperwrapping and brain degeneration in Drosophila
    • Kretzschmar D, Hasan G, Sharma S, Heisenberg M, Benzer S (1997) The swiss cheese mutant causes glial hyperwrapping and brain degeneration in Drosophila. J Neurosci 17: 7425-7432.
    • (1997) J Neurosci , vol.17 , pp. 7425-7432
    • Kretzschmar, D.1    Hasan, G.2    Sharma, S.3    Heisenberg, M.4    Benzer, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.