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Volumn 126, Issue 2, 2013, Pages 189-205

N-truncated amyloid β (Aβ) 4-42 forms stable aggregates and induces acute and long-lasting behavioral deficits

Author keywords

Degeneration; Neuron loss; Pyroglutamate Abeta; Spatial reference memory; Toxicity; Transgenic mouse model

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-42]; AMYLOID BETA PROTEIN[3-42]; AMYLOID BETA PROTEIN[4-38]; AMYLOID BETA PROTEIN[4-42]; UNCLASSIFIED DRUG;

EID: 84881099652     PISSN: 00016322     EISSN: 14320533     Source Type: Journal    
DOI: 10.1007/s00401-013-1129-2     Document Type: Article
Times cited : (140)

References (71)
  • 1
    • 80052578595 scopus 로고    scopus 로고
    • Selective Hippocampal neurodegeneration in transgenic mice expressing small amounts of truncated Aβ is induced by pyroglutamate-Aβ formation
    • 21900558 10.1523/JNEUROSCI.1794-11.2011 1:CAS:528:DC%2BC3MXhtFOhtrzI
    • Alexandru A, Jagla W, Graubner S et al (2011) Selective Hippocampal neurodegeneration in transgenic mice expressing small amounts of truncated Aβ is induced by pyroglutamate-Aβ formation. J Neurosci 31:12790-12801
    • (2011) J Neurosci , vol.31 , pp. 12790-12801
    • Alexandru, A.1    Jagla, W.2    Graubner, S.3
  • 2
    • 0025779179 scopus 로고
    • Solution structures of beta peptide and its constituent fragments: Relation to amyloid deposition
    • 1853202 10.1126/science.1853202 1:CAS:528:DyaK3MXlsFegsLo%3D
    • Barrow CJ, Zagorski MG (1991) Solution structures of beta peptide and its constituent fragments: relation to amyloid deposition. Science 253:179-182
    • (1991) Science , vol.253 , pp. 179-182
    • Barrow, C.J.1    Zagorski, M.G.2
  • 3
    • 84857642949 scopus 로고    scopus 로고
    • The toxic A[beta] oligomer and Alzheimer's disease: An emperor in need of clothes
    • 10.1038/nn.3028
    • Benilova I, Karran E, De Strooper B (2012) The toxic A[beta] oligomer and Alzheimer's disease: an emperor in need of clothes. Nat Neurosci 29:349-357
    • (2012) Nat Neurosci , vol.29 , pp. 349-357
    • Benilova, I.1    Karran, E.2    De Strooper, B.3
  • 4
    • 67349160489 scopus 로고    scopus 로고
    • APP/PS1KI bigenic mice develop early synaptic deficits and hippocampus atrophy
    • 19387667 10.1007/s00401-009-0539-7
    • Breyhan H, Wirths O, Duan K, Marcello A, Rettig J, Bayer TA (2009) APP/PS1KI bigenic mice develop early synaptic deficits and hippocampus atrophy. Acta Neuropathol 117:677-685
    • (2009) Acta Neuropathol , vol.117 , pp. 677-685
    • Breyhan, H.1    Wirths, O.2    Duan, K.3    Marcello, A.4    Rettig, J.5    Bayer, T.A.6
  • 5
    • 5144223971 scopus 로고    scopus 로고
    • Spatial memory, recognition memory, and the hippocampus
    • 15452348 10.1073/pnas.0406344101 1:CAS:528:DC%2BD2cXovVeru78%3D
    • Broadbent NJ, Squire LR, Clark RE (2004) Spatial memory, recognition memory, and the hippocampus. Proc Natl Acad Sci USA 101:14515-14520
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 14515-14520
    • Broadbent, N.J.1    Squire, L.R.2    Clark, R.E.3
  • 6
    • 84861914969 scopus 로고    scopus 로고
    • Neurotoxicity and memory deficits induced by soluble low-molecular-weight amyloid-β1-42 oligomers are revealed in vivo by using a novel animal model
    • 22674261 10.1523/JNEUROSCI.5901-11.2012 1:CAS:528:DC%2BC38XovFSmu7k%3D
    • Brouillette J, Caillierez R, Zommer N et al (2012) Neurotoxicity and memory deficits induced by soluble low-molecular-weight amyloid-β1-42 oligomers are revealed in vivo by using a novel animal model. J Neurosci 32:7852-7861
    • (2012) J Neurosci , vol.32 , pp. 7852-7861
    • Brouillette, J.1    Caillierez, R.2    Zommer, N.3
  • 7
    • 4644276796 scopus 로고    scopus 로고
    • Massive CA1/2 neuronal loss with intraneuronal and N-terminal truncated A{beta}42 accumulation in a novel alzheimer transgenic model
    • 15466394 10.1016/S0002-9440(10)63388-3 1:CAS:528:DC%2BD2cXptFSmtbc%3D
    • Casas C, Sergeant N, Itier JM et al (2004) Massive CA1/2 neuronal loss with intraneuronal and N-terminal truncated A{beta}42 accumulation in a novel alzheimer transgenic model. Am J Pathol 165:1289-1300
    • (2004) Am J Pathol , vol.165 , pp. 1289-1300
    • Casas, C.1    Sergeant, N.2    Itier, J.M.3
  • 8
    • 56749152364 scopus 로고    scopus 로고
    • Transient intraneuronal Abeta rather than extracellular plaque pathology correlates with neuron loss in the frontal cortex of APP/PS1KI mice
    • 18974993 10.1007/s00401-008-0451-6 1:CAS:528:DC%2BD1cXhtlyhsbfO
    • Christensen DZ, Kraus SL, Flohr A, Cotel MC, Wirths O, Bayer TA (2008) Transient intraneuronal Abeta rather than extracellular plaque pathology correlates with neuron loss in the frontal cortex of APP/PS1KI mice. Acta Neuropathol 116:647-655
    • (2008) Acta Neuropathol , vol.116 , pp. 647-655
    • Christensen, D.Z.1    Kraus, S.L.2    Flohr, A.3    Cotel, M.C.4    Wirths, O.5    Bayer, T.A.6
  • 9
    • 77952882727 scopus 로고    scopus 로고
    • Intracellular Abeta triggers neuron loss in the cholinergic system of the APP/PS1KI mouse model of Alzheimer's disease
    • 18771817 10.1016/j.neurobiolaging.2008.07.022 1:CAS:528: DC%2BC3cXmtFWit7Y%3D
    • Christensen DZ, Bayer TA, Wirths O (2010) Intracellular Abeta triggers neuron loss in the cholinergic system of the APP/PS1KI mouse model of Alzheimer's disease. Neurobiol Aging 31:1153-1163
    • (2010) Neurobiol Aging , vol.31 , pp. 1153-1163
    • Christensen, D.Z.1    Bayer, T.A.2    Wirths, O.3
  • 10
    • 33749615367 scopus 로고    scopus 로고
    • Inhibition of glutaminyl cyclase alters pyroglutamate formation in mammalian cells
    • 17005457 10.1016/j.bbapap.2006.08.003 1:CAS:528:DC%2BD28XhtVyktrrL
    • Cynis H, Schilling S, Bodnar M et al (2006) Inhibition of glutaminyl cyclase alters pyroglutamate formation in mammalian cells. Biochim Biophys Acta 1764:1618-1625
    • (2006) Biochim Biophys Acta , vol.1764 , pp. 1618-1625
    • Cynis, H.1    Schilling, S.2    Bodnar, M.3
  • 11
    • 0346106076 scopus 로고    scopus 로고
    • Metal binding and oxidation of amyloid-β within isolated senile plaque cores: Raman microscopic evidence
    • 12627941 10.1021/bi0272151 1:CAS:528:DC%2BD3sXht1Oiu7k%3D
    • Dong J, Atwood CS, Anderson VE et al (2003) Metal binding and oxidation of amyloid-β within isolated senile plaque cores: Raman microscopic evidence. Biochemistry 42:2768-2773
    • (2003) Biochemistry , vol.42 , pp. 2768-2773
    • Dong, J.1    Atwood, C.S.2    Anderson, V.E.3
  • 12
    • 33644861975 scopus 로고    scopus 로고
    • Common structure and toxic function of amyloid oligomers implies a common mechanism of pathogenesis
    • 16432151 10.1212/01.wnl.0000192103.24796.42 1:CAS:528: DC%2BD28Xht1Kqsg%3D%3D
    • Glabe CG, Kayed R (2006) Common structure and toxic function of amyloid oligomers implies a common mechanism of pathogenesis. Neurology 66:S74-S78
    • (2006) Neurology , vol.66
    • Glabe, C.G.1    Kayed, R.2
  • 13
    • 33750825049 scopus 로고    scopus 로고
    • High sensitivity analysis of amyloid-beta peptide composition in amyloid deposits from human and PS2APP mouse brain
    • 17008022 10.1016/j.neuroscience.2006.08.027
    • Güntert A, Dobeli H, Bohrmann B (2006) High sensitivity analysis of amyloid-beta peptide composition in amyloid deposits from human and PS2APP mouse brain. Neuroscience 143:461-475
    • (2006) Neuroscience , vol.143 , pp. 461-475
    • Güntert, A.1    Dobeli, H.2    Bohrmann, B.3
  • 14
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid beta-peptide
    • 17245412 10.1038/nrm2101 1:CAS:528:DC%2BD2sXotFKmtw%3D%3D
    • Haass C, Selkoe DJ (2007) Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide. Nat Rev Mol Cell Biol 8:101-112
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 15
    • 0034710784 scopus 로고    scopus 로고
    • Amyloid beta protein starting pyroglutamate at position 3 is a major component of the amyloid deposits in the Alzheimer's disease brain
    • 11027491 10.1006/bbrc.2000.3490 1:CAS:528:DC%2BD3cXntFOrsLY%3D
    • Harigaya Y, Saido TC, Eckman CB, Prada CM, Shoji M, Younkin SG (2000) Amyloid beta protein starting pyroglutamate at position 3 is a major component of the amyloid deposits in the Alzheimer's disease brain. Biochem Biophys Res Commun 276:422-427
    • (2000) Biochem Biophys Res Commun , vol.276 , pp. 422-427
    • Harigaya, Y.1    Saido, T.C.2    Eckman, C.B.3    Prada, C.M.4    Shoji, M.5    Younkin, S.G.6
  • 16
    • 67049087108 scopus 로고    scopus 로고
    • Role of amyloid-beta glycine 33 in oligomerization, toxicity, and neuronal plasticity
    • 19515926 10.1523/JNEUROSCI.1336-09.2009 1:CAS:528:DC%2BD1MXnslSntr0%3D
    • Harmeier A, Wozny C, Rost BR et al (2009) Role of amyloid-beta glycine 33 in oligomerization, toxicity, and neuronal plasticity. J Neurosci 29:7582-7590
    • (2009) J Neurosci , vol.29 , pp. 7582-7590
    • Harmeier, A.1    Wozny, C.2    Rost, B.R.3
  • 17
    • 84856986423 scopus 로고    scopus 로고
    • Structural basis of beta-amyloid-dependent synaptic dysfunctions
    • 22234970 10.1002/anie.201105638 1:CAS:528:DC%2BC38Xksl2rug%3D%3D
    • Haupt C, Leppert J, Ronicke R et al (2012) Structural basis of beta-amyloid-dependent synaptic dysfunctions. Angew Chem Int Ed Engl 51:1576-1579
    • (2012) Angew Chem Int Ed Engl , vol.51 , pp. 1576-1579
    • Haupt, C.1    Leppert, J.2    Ronicke, R.3
  • 18
    • 0031729335 scopus 로고    scopus 로고
    • Quantification of modified amyloid beta peptides in Alzheimer disease and Down syndrome brains
    • 9825946 10.1097/00005072-199811000-00012 1:CAS:528:DyaK1cXnslSnt7s%3D
    • Hosoda R, Saido TC, Otvos L Jr et al (1998) Quantification of modified amyloid beta peptides in Alzheimer disease and Down syndrome brains. J Neuropathol Exp Neurol 57:1089-1095
    • (1998) J Neuropathol Exp Neurol , vol.57 , pp. 1089-1095
    • Hosoda, R.1    Saido, T.C.2    Otvos Jr., L.3
  • 19
    • 0028169925 scopus 로고
    • Visualization of A beta 42(43) and A beta 40 in senile plaques with end-specific A beta monoclonals: Evidence that an initially deposited species is Abeta 42(43)
    • 8043280 10.1016/0896-6273(94)90458-8 1:CAS:528:DyaK2cXlsFCkt74%3D
    • Iwatsubo T, Odaka A, Suzuki N, Mizusawa H, Nukina N, Ihara Y (1994) Visualization of A beta 42(43) and A beta 40 in senile plaques with end-specific A beta monoclonals: evidence that an initially deposited species is Abeta 42(43). Neuron 13:45-53
    • (1994) Neuron , vol.13 , pp. 45-53
    • Iwatsubo, T.1    Odaka, A.2    Suzuki, N.3    Mizusawa, H.4    Nukina, N.5    Ihara, Y.6
  • 20
    • 80655144756 scopus 로고    scopus 로고
    • Pyroglutamate Abeta - A hatchet man in Alzheimer disease
    • 21965666 10.1074/jbc.R111.288308 1:CAS:528:DC%2BC3MXhsVSqt7vE
    • Jawhar S, Wirths O, Bayer TA (2011) Pyroglutamate Abeta - a hatchet man in Alzheimer disease. J Biol Chem 286:38825-38832
    • (2011) J Biol Chem , vol.286 , pp. 38825-38832
    • Jawhar, S.1    Wirths, O.2    Bayer, T.A.3
  • 21
    • 81355124089 scopus 로고    scopus 로고
    • Motor deficits, neuron loss, and reduced anxiety coinciding with axonal degeneration and intraneuronal Abeta aggregation in the 5XFAD mouse model of Alzheimer's disease
    • 20619937 10.1016/j.neurobiolaging.2010.05.027 e129-196.e140
    • Jawhar S, Trawicka A, Jenneckens C, Bayer TA, Wirths O (2012) Motor deficits, neuron loss, and reduced anxiety coinciding with axonal degeneration and intraneuronal Abeta aggregation in the 5XFAD mouse model of Alzheimer's disease. Neurobiol Aging 33:196 e129-196.e140
    • (2012) Neurobiol Aging , vol.33 , pp. 196
    • Jawhar, S.1    Trawicka, A.2    Jenneckens, C.3    Bayer, T.A.4    Wirths, O.5
  • 22
    • 0035863055 scopus 로고    scopus 로고
    • Age-dependent changes in brain, CSF, and plasma amyloid (beta) protein in the Tg2576 transgenic mouse model of Alzheimer's disease
    • 11160418 1:CAS:528:DC%2BD3MXnslCguw%3D%3D
    • Kawarabayashi T, Younkin L, Saido T, Shoji M, Ashe K, Younkin S (2001) Age-dependent changes in brain, CSF, and plasma amyloid (beta) protein in the Tg2576 transgenic mouse model of Alzheimer's disease. J Neurosci 21:372-381
    • (2001) J Neurosci , vol.21 , pp. 372-381
    • Kawarabayashi, T.1    Younkin, L.2    Saido, T.3    Shoji, M.4    Ashe, K.5    Younkin, S.6
  • 23
    • 0035993237 scopus 로고    scopus 로고
    • Abeta toxicity in Alzheimer's disease: Globular oligomers (ADDLs) as new vaccine and drug targets
    • 12176077 10.1016/S0197-0186(02)00050-5 1:CAS:528:DC%2BD38Xmtlemtrc%3D
    • Klein WL (2002) Abeta toxicity in Alzheimer's disease: globular oligomers (ADDLs) as new vaccine and drug targets. Neurochem Int 41:345-352
    • (2002) Neurochem Int , vol.41 , pp. 345-352
    • Klein, W.L.1
  • 24
    • 79957919528 scopus 로고    scopus 로고
    • Extracellular phosphorylation of the amyloid [beta]-peptide promotes formation of toxic aggregates during the pathogenesis of Alzheimer's disease
    • 21527912 10.1038/emboj.2011.138 1:CAS:528:DC%2BC3MXlsVSjtr4%3D
    • Kumar S, Rezaei-Ghaleh N, Terwel D et al (2011) Extracellular phosphorylation of the amyloid [beta]-peptide promotes formation of toxic aggregates during the pathogenesis of Alzheimer's disease. EMBO J 30:2255-2265
    • (2011) EMBO J , vol.30 , pp. 2255-2265
    • Kumar, S.1    Rezaei-Ghaleh, N.2    Terwel, D.3
  • 25
    • 84886703257 scopus 로고    scopus 로고
    • Early intraneuronal accumulation and increased aggregation of phosphorylated Abeta in a mouse model of Alzheimer's disease
    • 23525537 10.1007/s00401-013-1107-8 1:CAS:528:DC%2BC3sXmsFeltb0%3D
    • Kumar S, Wirths O, Theil S, Gerth J, Bayer TA, Walter J (2013) Early intraneuronal accumulation and increased aggregation of phosphorylated Abeta in a mouse model of Alzheimer's disease. Acta Neuropathol 125:699-709
    • (2013) Acta Neuropathol , vol.125 , pp. 699-709
    • Kumar, S.1    Wirths, O.2    Theil, S.3    Gerth, J.4    Bayer, T.A.5    Walter, J.6
  • 26
    • 0031862969 scopus 로고    scopus 로고
    • Irreversible dimerization/tetramerization and post-translational modifications inhibit proteolytic degradation of A beta peptides of Alzheimer's disease
    • 9630681 10.1016/S0925-4439(98)00014-3 1:CAS:528:DyaK1cXjs1ahsLs%3D
    • Kuo YM, Webster S, Emmerling MR, De Lima N, Roher AE (1998) Irreversible dimerization/tetramerization and post-translational modifications inhibit proteolytic degradation of A beta peptides of Alzheimer's disease. Biochim Biophys Acta 1406:291-298
    • (1998) Biochim Biophys Acta , vol.1406 , pp. 291-298
    • Kuo, Y.M.1    Webster, S.2    Emmerling, M.R.3    De Lima, N.4    Roher, A.E.5
  • 27
    • 0035918312 scopus 로고    scopus 로고
    • Comparative analysis of amyloid-beta chemical structure and amyloid plaque morphology of transgenic mouse and Alzheimer's disease brains
    • 11152675 10.1074/jbc.M007859200 1:CAS:528:DC%2BD3MXjtFyms74%3D
    • Kuo YM, Kokjohn TA, Beach TG et al (2001) Comparative analysis of amyloid-beta chemical structure and amyloid plaque morphology of transgenic mouse and Alzheimer's disease brains. J Biol Chem 276:12991-12998
    • (2001) J Biol Chem , vol.276 , pp. 12991-12998
    • Kuo, Y.M.1    Kokjohn, T.A.2    Beach, T.G.3
  • 28
    • 11544279355 scopus 로고    scopus 로고
    • Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins
    • 9600986 10.1073/pnas.95.11.6448 1:STN:280:DyaK1c3mtlektQ%3D%3D
    • Lambert MP, Barlow AK, Chromy BA et al (1998) Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins. Proc Natl Acad Sci USA 95:6448-6453
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6448-6453
    • Lambert, M.P.1    Barlow, A.K.2    Chromy, B.A.3
  • 29
    • 33846135452 scopus 로고    scopus 로고
    • Monoclonal antibodies that target pathological assemblies of Abeta
    • 17116235 10.1111/j.1471-4159.2006.04157.x 1:CAS:528: DC%2BD2sXptlyqtg%3D%3D
    • Lambert MP, Velasco PT, Chang L et al (2007) Monoclonal antibodies that target pathological assemblies of Abeta. J Neurochem 100:23-35
    • (2007) J Neurochem , vol.100 , pp. 23-35
    • Lambert, M.P.1    Velasco, P.T.2    Chang, L.3
  • 30
    • 33645038471 scopus 로고    scopus 로고
    • A specific amyloid-beta protein assembly in the brain impairs memory
    • 16541076 10.1038/nature04533 1:CAS:528:DC%2BD28XitlKgurg%3D
    • Lesne S, Koh MT, Kotilinek L et al (2006) A specific amyloid-beta protein assembly in the brain impairs memory. Nature 440:352-357
    • (2006) Nature , vol.440 , pp. 352-357
    • Lesne, S.1    Koh, M.T.2    Kotilinek, L.3
  • 31
    • 33644942362 scopus 로고    scopus 로고
    • Quantification of Alzheimer pathology in ageing and dementia: Age-related accumulation of amyloid-β(42) peptide in vascular dementia
    • 16599940 10.1111/j.1365-2990.2006.00696.x 1:CAS:528:DC%2BD28XkslantL0%3D
    • Lewis H, Beher D, Cookson N et al (2006) Quantification of Alzheimer pathology in ageing and dementia: age-related accumulation of amyloid-β(42) peptide in vascular dementia. Neuropathol Appl Neurobiol 32:103-118
    • (2006) Neuropathol Appl Neurobiol , vol.32 , pp. 103-118
    • Lewis, H.1    Beher, D.2    Cookson, N.3
  • 32
    • 35348821915 scopus 로고    scopus 로고
    • Longitudinal, quantitative assesment of amyloid, neuroinflammation and anti-amyloid treatment in a living mouse model of Alzheimer's disease enabled by PET
    • 17928437 10.1523/JNEUROSCI.0673-07.2007 1:CAS:528:DC%2BD2sXht1Wnsb7J
    • Maeda J, Ji B, Tomiyama T et al (2007) Longitudinal, quantitative assesment of amyloid, neuroinflammation and anti-amyloid treatment in a living mouse model of Alzheimer's disease enabled by PET. J Neurosci 27:10957-10968
    • (2007) J Neurosci , vol.27 , pp. 10957-10968
    • Maeda, J.1    Ji, B.2    Tomiyama, T.3
  • 34
    • 0032590054 scopus 로고    scopus 로고
    • Soluble pool of Abeta amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease
    • 10589538 10.1002/1531-8249(199912)46:6<860: AID-ANA8>3.0.CO;2-M 1:CAS:528:DC%2BD3cXhsFyrug%3D%3D
    • McLean CA, Cherny RA, Fraser FW et al (1999) Soluble pool of Abeta amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease. Ann Neurol 46:860-866
    • (1999) Ann Neurol , vol.46 , pp. 860-866
    • McLean, C.A.1    Cherny, R.A.2    Fraser, F.W.3
  • 35
    • 0027184611 scopus 로고
    • Peptide compositions of the cerebrovascular and senile plaque core amyloid deposits of Alzheimer's disease
    • 8442665 10.1006/abbi.1993.1112 1:CAS:528:DyaK3sXhs1Klsro%3D
    • Miller DL, Papayannopoulos IA, Styles J et al (1993) Peptide compositions of the cerebrovascular and senile plaque core amyloid deposits of Alzheimer's disease. Arch Biochem Biophys 301:41-52
    • (1993) Arch Biochem Biophys , vol.301 , pp. 41-52
    • Miller, D.L.1    Papayannopoulos, I.A.2    Styles, J.3
  • 36
    • 0035807929 scopus 로고    scopus 로고
    • Phosphorylation of amyloid-[beta] at the serine 26 residue by human cdc2 kinase
    • 11726805 10.1097/00001756-200112040-00047 1:CAS:528:DC%2BD3MXpt1Grt7g%3D
    • Milton NGN (2001) Phosphorylation of amyloid-[beta] at the serine 26 residue by human cdc2 kinase. NeuroReport 12:3839-3844
    • (2001) NeuroReport , vol.12 , pp. 3839-3844
    • Milton, N.G.N.1
  • 37
    • 0026794746 scopus 로고
    • Mass spectrometry of purified amyloid beta protein in Alzheimer's disease
    • 1512246 1:CAS:528:DyaK38Xls1yrsbs%3D
    • Mori H, Takio K, Ogawara M, Selkoe DJ (1992) Mass spectrometry of purified amyloid beta protein in Alzheimer's disease. J Biol Chem 267:17082-17086
    • (1992) J Biol Chem , vol.267 , pp. 17082-17086
    • Mori, H.1    Takio, K.2    Ogawara, M.3    Selkoe, D.J.4
  • 38
    • 0028544334 scopus 로고
    • Racemization: Its biological significance on neuropathogenesis of Alzheimer's disease
    • 7761990 10.1620/tjem.174.251 1:CAS:528:DyaK2MXks1Sitr4%3D
    • Mori H, Ishii K, Tomiyama T et al (1994) Racemization: its biological significance on neuropathogenesis of Alzheimer's disease. Tohoku J Exp Med 174:251-262
    • (1994) Tohoku J Exp Med , vol.174 , pp. 251-262
    • Mori, H.1    Ishii, K.2    Tomiyama, T.3
  • 39
    • 0021173996 scopus 로고
    • Developments of a water-maze procedure for studying spatial learning in the rat
    • 6471907 10.1016/0165-0270(84)90007-4 1:STN:280:DyaL2c3ptl2lug%3D%3D
    • Morris R (1984) Developments of a water-maze procedure for studying spatial learning in the rat. J Neurosci Methods 11:47-60
    • (1984) J Neurosci Methods , vol.11 , pp. 47-60
    • Morris, R.1
  • 40
    • 0028818282 scopus 로고
    • Spatial learning with a minislab in the dorsal hippocampus
    • 7568200 10.1073/pnas.92.21.9697 1:CAS:528:DyaK2MXpsFyrsr4%3D
    • Moser MB, Moser EI, Forrest E, Andersen P, Morris RG (1995) Spatial learning with a minislab in the dorsal hippocampus. Proc Natl Acad Sci USA 92:9697-9701
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 9697-9701
    • Moser, M.B.1    Moser, E.I.2    Forrest, E.3    Andersen, P.4    Morris, R.G.5
  • 41
    • 0028106152 scopus 로고
    • Relative abundance of Alzheimer A beta amyloid peptide variants in Alzheimer disease and normal aging
    • 8078890 10.1073/pnas.91.18.8378
    • Näslund J, Schierhorn A, Hellman U et al (1994) Relative abundance of Alzheimer A beta amyloid peptide variants in Alzheimer disease and normal aging. Proc Natl Acad Sci USA 91:8378-8382
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8378-8382
    • Näslund, J.1    Schierhorn, A.2    Hellman, U.3
  • 42
    • 33749521100 scopus 로고    scopus 로고
    • Intraneuronal beta-amyloid aggregates, neurodegeneration, and neuron loss in transgenic mice with five familial Alzheimer's disease mutations: Potential factors in amyloid plaque formation
    • 17021169 10.1523/JNEUROSCI.1202-06.2006 1:CAS:528:DC%2BD28XhtVymurbK
    • Oakley H, Cole SL, Logan S et al (2006) Intraneuronal beta-amyloid aggregates, neurodegeneration, and neuron loss in transgenic mice with five familial Alzheimer's disease mutations: potential factors in amyloid plaque formation. J Neurosci 26:10129-10140
    • (2006) J Neurosci , vol.26 , pp. 10129-10140
    • Oakley, H.1    Cole, S.L.2    Logan, S.3
  • 43
    • 70349295278 scopus 로고    scopus 로고
    • Structure-neurotoxicity relationships of amyloid β-protein oligomers
    • 19706468 10.1073/pnas.0905127106 1:CAS:528:DC%2BD1MXhtFGrtrfO
    • Ono K, Condron MM, Teplow DB (2009) Structure-neurotoxicity relationships of amyloid β-protein oligomers. Proc Natl Acad Sci USA 106:14745-14750
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 14745-14750
    • Ono, K.1    Condron, M.M.2    Teplow, D.B.3
  • 44
    • 0036581160 scopus 로고    scopus 로고
    • Relative expression software tool (REST) for group-wise comparison and statistical analysis of relative expression results in real-time PCR
    • 11972351 10.1093/nar/30.9.e36
    • Pfaffl MW, Horgan GW, Dempfle L (2002) Relative expression software tool (REST) for group-wise comparison and statistical analysis of relative expression results in real-time PCR. Nucleic Acids Res 30:e36
    • (2002) Nucleic Acids Res , vol.30 , pp. 36
    • Pfaffl, M.W.1    Horgan, G.W.2    Dempfle, L.3
  • 45
    • 0028885682 scopus 로고
    • Amino-terminal deletions enhance aggregation of beta-amyloid peptides in vitro
    • 7592576 10.1074/jbc.270.41.23895 1:CAS:528:DyaK2MXovVSgsL4%3D
    • Pike CJ, Overman MJ, Cotman CW (1995) Amino-terminal deletions enhance aggregation of beta-amyloid peptides in vitro. J Biol Chem 270:23895-23898
    • (1995) J Biol Chem , vol.270 , pp. 23895-23898
    • Pike, C.J.1    Overman, M.J.2    Cotman, C.W.3
  • 46
    • 0032845739 scopus 로고    scopus 로고
    • The nonfibrillar amyloid β-peptide induces apoptotic neuronal cell death
    • 10501209 10.1046/j.1471-4159.1999.0731626.x 1:CAS:528:DyaK1MXmtlOhsb0%3D
    • Pillot T, Drouet B, Queillé S et al (1999) The nonfibrillar amyloid β-peptide induces apoptotic neuronal cell death. J Neurochem 73:1626-1634
    • (1999) J Neurochem , vol.73 , pp. 1626-1634
    • Pillot, T.1    Drouet, B.2    Queillé, S.3
  • 47
    • 77957279325 scopus 로고    scopus 로고
    • Mass spectrometric characterization of brain amyloid beta isoform signatures in familial and sporadic Alzheimer's disease
    • 20419305 10.1007/s00401-010-0690-1 1:CAS:528:DC%2BC3cXotVKnsLY%3D
    • Portelius E, Bogdanovic N, Gustavsson MK et al (2010) Mass spectrometric characterization of brain amyloid beta isoform signatures in familial and sporadic Alzheimer's disease. Acta Neuropathol 120:185-193
    • (2010) Acta Neuropathol , vol.120 , pp. 185-193
    • Portelius, E.1    Bogdanovic, N.2    Gustavsson, M.K.3
  • 48
    • 0023684537 scopus 로고
    • Differences between vascular and plaque core amyloid in Alzheimer's disease
    • 3292706 10.1111/j.1471-4159.1988.tb01087.x 1:CAS:528:DyaL1cXlvVyhtbs%3D
    • Prelli F, Castano E, Glenner GG, Frangione B (1988) Differences between vascular and plaque core amyloid in Alzheimer's disease. J Neurochem 51:648-651
    • (1988) J Neurochem , vol.51 , pp. 648-651
    • Prelli, F.1    Castano, E.2    Glenner, G.G.3    Frangione, B.4
  • 49
    • 77953658771 scopus 로고    scopus 로고
    • Deleterious effects of amyloid [beta] oligomers acting as an extracellular scaffold for mGluR5
    • 20547131 10.1016/j.neuron.2010.04.029 1:CAS:528:DC%2BC3cXnvFaksbk%3D
    • Renner M, Lacor PN, Velasco PT et al (2010) Deleterious effects of amyloid [beta] oligomers acting as an extracellular scaffold for mGluR5. Neuron 66:739-754
    • (2010) Neuron , vol.66 , pp. 739-754
    • Renner, M.1    Lacor, P.N.2    Velasco, P.T.3
  • 50
    • 0027477463 scopus 로고
    • Structural alterations in the peptide backbone of beta-amyloid core protein may account for its deposition and stability in Alzheimer's disease
    • 8428986 1:CAS:528:DyaK3sXhsVGjsb0%3D
    • Roher A, Lowenson J, Clarke S et al (1993) Structural alterations in the peptide backbone of beta-amyloid core protein may account for its deposition and stability in Alzheimer's disease. J Biol Chem 268:3072-3083
    • (1993) J Biol Chem , vol.268 , pp. 3072-3083
    • Roher, A.1    Lowenson, J.2    Clarke, S.3
  • 51
    • 63849197629 scopus 로고    scopus 로고
    • Amyloid beta-protein assembly and Alzheimer disease
    • 18845536 10.1074/jbc.R800036200 1:CAS:528:DC%2BD1MXhvVSgtb0%3D
    • Roychaudhuri R, Yang M, Hoshi MM, Teplow DB (2009) Amyloid beta-protein assembly and Alzheimer disease. J Biol Chem 284:4749-4753
    • (2009) J Biol Chem , vol.284 , pp. 4749-4753
    • Roychaudhuri, R.1    Yang, M.2    Hoshi, M.M.3    Teplow, D.B.4
  • 52
    • 0030742712 scopus 로고    scopus 로고
    • Heterogeneity of water-soluble amyloid beta-peptide in Alzheimer's disease and Down's syndrome brains
    • 9224700 10.1016/S0014-5793(97)00564-4 1:CAS:528:DyaK2sXjslKlsrY%3D
    • Russo C, Saido TC, DeBusk LM, Tabaton M, Gambetti P, Teller JK (1997) Heterogeneity of water-soluble amyloid beta-peptide in Alzheimer's disease and Down's syndrome brains. FEBS Lett 409:411-416
    • (1997) FEBS Lett , vol.409 , pp. 411-416
    • Russo, C.1    Saido, T.C.2    Debusk, L.M.3    Tabaton, M.4    Gambetti, P.5    Teller, J.K.6
  • 53
    • 18744435477 scopus 로고    scopus 로고
    • Presenilin-1 mutations in Alzheimer's disease
    • 10850703 10.1038/35014735 1:CAS:528:DC%2BD3cXktVChtLc%3D
    • Russo C, Schettini G, Saido TC et al (2000) Presenilin-1 mutations in Alzheimer's disease. Nature 405:531-532
    • (2000) Nature , vol.405 , pp. 531-532
    • Russo, C.1    Schettini, G.2    Saido, T.C.3
  • 54
    • 0028855851 scopus 로고
    • Dominant and differential deposition of distinct beta-amyloid peptide species, Abeta N3(pE), in senile plaques
    • 7857653 10.1016/0896-6273(95)90301-1 1:CAS:528:DyaK2MXjvFejsLk%3D
    • Saido TC, Iwatsubo T, Mann DM, Shimada H, Ihara Y, Kawashima S (1995) Dominant and differential deposition of distinct beta-amyloid peptide species, Abeta N3(pE), in senile plaques. Neuron 14:457-466
    • (1995) Neuron , vol.14 , pp. 457-466
    • Saido, T.C.1    Iwatsubo, T.2    Mann, D.M.3    Shimada, H.4    Ihara, Y.5    Kawashima, S.6
  • 55
    • 0023832413 scopus 로고
    • Attenuation of scopolamine-induced impairment of spontaneous alteration behaviour by antagonist but not inverse agonist and agonist beta-carbolines
    • 2836875 10.1007/BF00212843 1:CAS:528:DyaL1cXhvFygsro%3D
    • Sarter M, Bodewitz G, Stephens DN (1988) Attenuation of scopolamine-induced impairment of spontaneous alteration behaviour by antagonist but not inverse agonist and agonist beta-carbolines. Psychopharmacology 94:491-495
    • (1988) Psychopharmacology , vol.94 , pp. 491-495
    • Sarter, M.1    Bodewitz, G.2    Stephens, D.N.3
  • 56
    • 84860519322 scopus 로고    scopus 로고
    • N-terminal pyroglutamate (pGlu) formation of Aβ38 and Aβ40 enforces oligomer formation and potency to disrupt hippocampal LTP
    • 22375951 10.1111/j.1471-4159.2012.07707.x 1:CAS:528:DC%2BC38XhtVGltrvE
    • Schlenzig D, Rönicke R, Cynis H et al (2012) N-terminal pyroglutamate (pGlu) formation of Aβ38 and Aβ40 enforces oligomer formation and potency to disrupt hippocampal LTP. J Neurochem 121:774-784
    • (2012) J Neurochem , vol.121 , pp. 774-784
    • Schlenzig, D.1    Rönicke, R.2    Cynis, H.3
  • 57
    • 12144288683 scopus 로고    scopus 로고
    • Hippocampal neuron loss exceeds amyloid plaque load in a transgenic mouse model of Alzheimer's disease
    • 15039236 10.1016/S0002-9440(10)63235-X
    • Schmitz C, Rutten BP, Pielen A et al (2004) Hippocampal neuron loss exceeds amyloid plaque load in a transgenic mouse model of Alzheimer's disease. Am J Pathol 164:1495-1502
    • (2004) Am J Pathol , vol.164 , pp. 1495-1502
    • Schmitz, C.1    Rutten, B.P.2    Pielen, A.3
  • 58
    • 0032211830 scopus 로고    scopus 로고
    • The cell biology of beta-amyloid precursor protein and presenilin in Alzheimer's disease
    • 9854312 10.1016/S0962-8924(98)01363-4 1:CAS:528:DyaK1MXmsV2m
    • Selkoe DJ (1998) The cell biology of beta-amyloid precursor protein and presenilin in Alzheimer's disease. Trends Cell Biol 8:447-453
    • (1998) Trends Cell Biol , vol.8 , pp. 447-453
    • Selkoe, D.J.1
  • 59
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • 11274343 1:CAS:528:DC%2BD3MXislCrsLc%3D
    • 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
  • 60
    • 33947314641 scopus 로고    scopus 로고
    • Natural oigomers of the Alzheimer amyloid-{beta} protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway
    • 17360908 10.1523/JNEUROSCI.4970-06.2007 1:CAS:528:DC%2BD2sXjs1Wqu7o%3D
    • Shankar GM, Bloodgood BL, Townsend M, Walsh DM, Selkoe DJ, Sabatini BL (2007) Natural oigomers of the Alzheimer amyloid-{beta} protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway. J Neurosci 27:2866-2875
    • (2007) J Neurosci , vol.27 , pp. 2866-2875
    • Shankar, G.M.1    Bloodgood, B.L.2    Townsend, M.3    Walsh, D.M.4    Selkoe, D.J.5    Sabatini, B.L.6
  • 61
    • 49149124343 scopus 로고    scopus 로고
    • Amyloid-beta protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory
    • 18568035 10.1038/nm1782 1:CAS:528:DC%2BD1cXptlKltb0%3D
    • Shankar GM, Li S, Mehta TH et al (2008) Amyloid-beta protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory. Nat Med 14:837-842
    • (2008) Nat Med , vol.14 , pp. 837-842
    • Shankar, G.M.1    Li, S.2    Mehta, T.H.3
  • 62
    • 24944532072 scopus 로고    scopus 로고
    • Biological significance of isoaspartate and its repair system
    • 16141521 10.1248/bpb.28.1590 1:CAS:528:DC%2BD2MXhtFWjurzF
    • Shimizu T, Matsuoka Y, Shirasawa T (2005) Biological significance of isoaspartate and its repair system. Biol Pharm Bull 28:1590-1596
    • (2005) Biol Pharm Bull , vol.28 , pp. 1590-1596
    • Shimizu, T.1    Matsuoka, Y.2    Shirasawa, T.3
  • 63
    • 0030775361 scopus 로고    scopus 로고
    • Amyloid beta-protein (Abeta) 1-40 but not Abeta1-42 contributes to the experimental formation of Alzheimer disease amyloid fibrils in rat brain
    • 9334394 1:CAS:528:DyaK2sXntVyjt7o%3D
    • Shin RW, Ogino K, Kondo A et al (1997) Amyloid beta-protein (Abeta) 1-40 but not Abeta1-42 contributes to the experimental formation of Alzheimer disease amyloid fibrils in rat brain. J Neurosci 17:8187-8193
    • (1997) J Neurosci , vol.17 , pp. 8187-8193
    • Shin, R.W.1    Ogino, K.2    Kondo, A.3
  • 64
    • 0028177534 scopus 로고
    • Racemization of Asp23 residue affects the aggregation properties of Alzheimer amyloid beta protein analogues
    • 8144598 1:CAS:528:DyaK2cXjt1Slsbk%3D
    • Tomiyama T, Asano S, Furiya Y, Shirasawa T, Endo N, Mori H (1994) Racemization of Asp23 residue affects the aggregation properties of Alzheimer amyloid beta protein analogues. J Biol Chem 269:10205-10208
    • (1994) J Biol Chem , vol.269 , pp. 10205-10208
    • Tomiyama, T.1    Asano, S.2    Furiya, Y.3    Shirasawa, T.4    Endo, N.5    Mori, H.6
  • 65
    • 33846461062 scopus 로고    scopus 로고
    • Morris water maze: Procedures for assessing spatial and related forms of learning and memory
    • 17406317 10.1038/nprot.2006.116
    • Vorhees CV, Williams MT (2006) Morris water maze: procedures for assessing spatial and related forms of learning and memory. Nat Protoc 1:848-858
    • (2006) Nat Protoc , vol.1 , pp. 848-858
    • Vorhees, C.V.1    Williams, M.T.2
  • 66
    • 0026339976 scopus 로고
    • Unbiased stereological estimation of the total number of neurons in thesubdivisions of the rat hippocampus using the optical fractionator
    • 1793176 10.1002/ar.1092310411 1:STN:280:DyaK387ntFWrtw%3D%3D
    • West MJ, Slomianka L, Gundersen HJ (1991) Unbiased stereological estimation of the total number of neurons in thesubdivisions of the rat hippocampus using the optical fractionator. Anat Rec 231:482-497
    • (1991) Anat Rec , vol.231 , pp. 482-497
    • West, M.J.1    Slomianka, L.2    Gundersen, H.J.3
  • 67
    • 85027929889 scopus 로고    scopus 로고
    • Aβ oligomer-induced synapse degeneration in Alzheimer's disease
    • 21538118 10.1007/s10571-011-9691-4 1:CAS:528:DC%2BC3MXps1Wit7w%3D
    • Wilcox K, Lacor P, Pitt J, Klein W (2011) Aβ oligomer-induced synapse degeneration in Alzheimer's disease. Cell Mol Neurobiol 31:939-948
    • (2011) Cell Mol Neurobiol , vol.31 , pp. 939-948
    • Wilcox, K.1    Lacor, P.2    Pitt, J.3    Klein, W.4
  • 68
    • 69949135716 scopus 로고    scopus 로고
    • Intraneuronal pyroglutamate-Abeta 3-42 triggers neurodegeneration and lethal neurological deficits in a transgenic mouse model
    • 19547991 10.1007/s00401-009-0557-5
    • Wirths O, Breyhan H, Cynis H, Schilling S, Demuth HU, Bayer TA (2009) Intraneuronal pyroglutamate-Abeta 3-42 triggers neurodegeneration and lethal neurological deficits in a transgenic mouse model. Acta Neuropathol 118:487-496
    • (2009) Acta Neuropathol , vol.118 , pp. 487-496
    • Wirths, O.1    Breyhan, H.2    Cynis, H.3    Schilling, S.4    Demuth, H.U.5    Bayer, T.A.6
  • 69
    • 76949102099 scopus 로고    scopus 로고
    • Pyroglutamate Abeta pathology in APP/PS1KI mice, sporadic and familial Alzheimer's disease cases
    • 19823761 10.1007/s00702-009-0314-x 1:CAS:528:DC%2BD1MXhsFWmurbM
    • Wirths O, Bethge T, Marcello A et al (2010) Pyroglutamate Abeta pathology in APP/PS1KI mice, sporadic and familial Alzheimer's disease cases. J Neural Transm 117:85-96
    • (2010) J Neural Transm , vol.117 , pp. 85-96
    • Wirths, O.1    Bethge, T.2    Marcello, A.3
  • 70
    • 84858040971 scopus 로고    scopus 로고
    • Pyroglutamate amyloid β (Aβ) aggravates behavioral deficits in transgenic amyloid mouse model for Alzheimer disease
    • 22267726 10.1074/jbc.M111.308601 1:CAS:528:DC%2BC38XjsFCrsrw%3D
    • Wittnam JL, Portelius E, Zetterberg H et al (2012) Pyroglutamate amyloid β (Aβ) aggravates behavioral deficits in transgenic amyloid mouse model for Alzheimer disease. J Biol Chem 287:8154-8162
    • (2012) J Biol Chem , vol.287 , pp. 8154-8162
    • Wittnam, J.L.1    Portelius, E.2    Zetterberg, H.3
  • 71
    • 47249113393 scopus 로고    scopus 로고
    • N-truncated amyloid-β oligomers induce learning impairment and neuronal apoptosis
    • 17459527 10.1016/j.neurobiolaging.2007.03.005 1:CAS:528: DC%2BD1cXoslCls7k%3D
    • Youssef I, Florent-Béchard S, Malaplate-Armand C et al (2008) N-truncated amyloid-β oligomers induce learning impairment and neuronal apoptosis. Neurobiol Aging 29:1319-1333
    • (2008) Neurobiol Aging , vol.29 , pp. 1319-1333
    • Youssef, I.1    Florent-Béchard, S.2    Malaplate-Armand, C.3


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