메뉴 건너뛰기




Volumn , Issue , 2014, Pages 889-920

Alzheimer’s disease

Author keywords

[No Author keywords available]

Indexed keywords

COGNITIVE IMPAIRMENT; ESSENTIAL FEATURES; HYPERPHOSPHORYLATED; NEURODEGENERATION; NEURODEGENERATIVE DISORDERS; NEUROFIBRILLARY TANGLES; RESEARCH FRAMEWORKS; UNIFIED MODELING;

EID: 84919452903     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-3-642-30574-0_51     Document Type: Chapter
Times cited : (2)

References (255)
  • 1
    • 81855183715 scopus 로고    scopus 로고
    • Probabilistic computational neurogenetic modeling: From cognitive systems to Alzheimer’s disease
    • N.K. Kasabov, R. Schliebs, H. Kojima: Probabilistic computational neurogenetic modeling: From cognitive systems to Alzheimer’s disease, IEEE Trans. Auton. Mental Dev. 3, 1-12 (2011)
    • (2011) IEEE Trans. Auton. Mental Dev. , vol.3 , pp. 1-12
    • Kasabov, N.K.1    Schliebs, R.2    Kojima, H.3
  • 3
    • 0021207461 scopus 로고
    • Alzheimer’s disease and Down’s syndrome: Sharing of a unique cerebrovascular amyloid fibril protein
    • G.G. Glenner, C.W. Wong: Alzheimer’s disease and Down’s syndrome: Sharing of a unique cerebrovascular amyloid fibril protein, Biochem. Biophys. Res. Commun. 122, 1131-1135 (1984)
    • (1984) Biochem. Biophys. Res. Commun. , vol.122 , pp. 1131-1135
    • Glenner, G.G.1    Wong, C.W.2
  • 6
    • 0023132387 scopus 로고    scopus 로고
    • (1987) Characterization and chromosomal localization of a cDNA encoding brain amyloid of Alzheimer’s disease
    • D. Goldgaber, M.I. Lerman, O.W. McBride, U. Saffiotti, D.C. Gajdusek: (1987) Characterization and chromosomal localization of a cDNA encoding brain amyloid of Alzheimer’s disease, Science 235, 877-880 (2006)
    • (2006) Science , vol.235 , pp. 877-880
    • Goldgaber, D.1    Lerman, M.I.2    McBride, O.W.3    Saffiotti, U.4    Gajdusek, D.C.5
  • 7
    • 2142777413 scopus 로고
    • Molecular cloning and characterization of a cDNA encoding the cerebrovascular and the neuritic plaque amyloid peptides
    • N.K. Robakis, N. Ramakrishna, G. Wolfe, H.M. Wisniewski: Molecular cloning and characterization of a cDNA encoding the cerebrovascular and the neuritic plaque amyloid peptides, Proc. Natl. Acad. Sci. USA 84, 4190-4194 (1987)
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 4190-4194
    • Robakis, N.K.1    Ramakrishna, N.2    Wolfe, G.3    Wisniewski, H.M.4
  • 9
    • 85031032764 scopus 로고    scopus 로고
    • Deutsche Alzheimer Gesellschaft e.V., Berlin, available online at
    • H. Bickel: Die Epidemiologie der Demenz, Informationsblatt (Deutsche Alzheimer Gesellschaft e.V., Berlin 2010), available online at www.deutschealzheimer. de/
    • (2010) Die Epidemiologie der Demenz, Informationsblatt
    • Bickel, H.1
  • 10
    • 78650403081 scopus 로고    scopus 로고
    • Reimagining Alzheimer’s disease-an age-based hypothesis
    • K. Herrup: Reimagining Alzheimer’s disease-an age-based hypothesis, J. Neurosci. 30, 16755-16762 (2010)
    • (2010) J. Neurosci. , vol.30 , pp. 16755-16762
    • Herrup, K.1
  • 11
    • 33750334671 scopus 로고    scopus 로고
    • Alzheimer’s disease
    • R.S. Turner: Alzheimer’s disease, Semin. Neurol. 26, 499-506 (2006)
    • (2006) Semin. Neurol. , vol.26 , pp. 499-506
    • Turner, R.S.1
  • 13
    • 0021572660 scopus 로고
    • The amyloid deposits in Alzheimer’s disease: Their nature and pathogenesis
    • G.G. Glenner, C.W. Wong, V. Quaranta, E.D. Eanes: The amyloid deposits in Alzheimer’s disease: Their nature and pathogenesis, Appl. Pathol. 2, 357-369 (1984)
    • (1984) Appl. Pathol. , vol.2 , pp. 357-369
    • Glenner, G.G.1    Wong, C.W.2    Quaranta, V.3    Eanes, E.D.4
  • 17
    • 0035976524 scopus 로고    scopus 로고
    • Regulation of cell survival by secreted proneurotrophins
    • R. Lee, P. Kermani, K.K. Teng, B.L. Hempstead: Regulation of cell survival by secreted proneurotrophins, Science 294, 1945-1948 (2001)
    • (2001) Science , vol.294 , pp. 1945-1948
    • Lee, R.1    Kermani, P.2    Teng, K.K.3    Hempstead, B.L.4
  • 19
    • 0035811050 scopus 로고    scopus 로고
    • Hyperphosphorylation induces self-assembly of tau into tangles of paired helical filaments/straight filaments
    • A. Alonso, T. Zaidi, M. Novak, I. Grundke-Iqbal, K. Iqbal: Hyperphosphorylation induces self-assembly of tau into tangles of paired helical filaments/straight filaments, Proc. Natl. Acad. Sci. USA 98, 6923-6928 (2001)
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 6923-6928
    • Alonso, A.1    Zaidi, T.2    Novak, M.3    Grundke-Iqbal, I.4    Iqbal, K.5
  • 22
    • 65249116483 scopus 로고    scopus 로고
    • Tau mutations in neurodegenerative diseases
    • M.S. Wolfe: Tau mutations in neurodegenerative diseases, J. Biol. Chem. 284, 6021-6025 (2009)
    • (2009) J. Biol. Chem. , vol.284 , pp. 6021-6025
    • Wolfe, M.S.1
  • 23
    • 33750705653 scopus 로고    scopus 로고
    • A century of Alzheimer’s disease
    • M. Goedert, M.G. Spillantini: A century of Alzheimer’s disease, Science 314, 777-781 (2006)
    • (2006) Science , vol.314 , pp. 777-781
    • Goedert, M.1    Spillantini, M.G.2
  • 24
    • 56349119351 scopus 로고    scopus 로고
    • Linking Aβ and tau in late-onset Alzheimer’s disease: A dual pathway hypothesis
    • S.A. Small, K. Duff: Linking Aβ and tau in late-onset Alzheimer’s disease: A dual pathway hypothesis, Neuron 60, 534-542 (2008)
    • (2008) Neuron , vol.60 , pp. 534-542
    • Small, S.A.1    Duff, K.2
  • 25
    • 77957927865 scopus 로고    scopus 로고
    • The genetics of Alzheimer disease: Back to the future
    • L. Bertram, C.M. Lill, R.E. Tanzi: The genetics of Alzheimer disease: Back to the future, Neuron 68, 270-281 (2010)
    • (2010) Neuron , vol.68 , pp. 270-281
    • Bertram, L.1    Lill, C.M.2    Tanzi, R.E.3
  • 28
    • 77953286012 scopus 로고    scopus 로고
    • Aβ-independent roles of apolipoprotein E4 in the pathogenesis of Alzheimer’s disease
    • Y. Huang: Aβ-independent roles of apolipoprotein E4 in the pathogenesis of Alzheimer’s disease, Trends Mol. Med. 16, 287-294 (2010)
    • (2010) Trends Mol. Med. , vol.16 , pp. 287-294
    • Huang, Y.1
  • 30
    • 79959396151 scopus 로고    scopus 로고
    • The three new pathways leading to AD
    • K. Morgan: The three new pathways leading to AD, Neuropathol. Appl. Neurobiol. 37, 353-357 (2011)
    • (2011) Neuropathol. Appl. Neurobiol. , vol.37 , pp. 353-357
    • Morgan, K.1
  • 31
    • 0017133142 scopus 로고
    • Neurotransmitter-related enzymes and indices of hypoxia in senile dementia and other abiotrophies
    • D.M. Bowen, C.B. Smith, P. White, A.N. Davison: Neurotransmitter-related enzymes and indices of hypoxia in senile dementia and other abiotrophies, Brain 99, 459-496 (1976)
    • (1976) Brain , vol.99 , pp. 459-496
    • Bowen, D.M.1    Smith, C.B.2    White, P.3    Davison, A.N.4
  • 32
    • 0011162190 scopus 로고
    • Selective loss of central cholinergic neurons in Alzheimer’s disease
    • P. Davies, A.J. Maloney: Selective loss of central cholinergic neurons in Alzheimer’s disease, Lancet 2, 1403 (1976)
    • (1976) Lancet , vol.2 , pp. 1403
    • Davies, P.1    Maloney, A.J.2
  • 33
    • 84886631402 scopus 로고
    • Neurotransmitter enzyme abnormalities in senile dementia. Choline acetyltransferase and glutamic acid decarboxylase activities in necropsy brain tissue
    • E.K. Perry, P.H. Gibson, G. Blessed, R.H. Perry, B.E. Tomlinson: Neurotransmitter enzyme abnormalities in senile dementia. Choline acetyltransferase and glutamic acid decarboxylase activities in necropsy brain tissue, J. Neurol. Sci. 34, 247-265 (1977)
    • (1977) J. Neurol. Sci. , vol.34 , pp. 247-265
    • Perry, E.K.1    Gibson, P.H.2    Blessed, G.3    Perry, R.H.4    Tomlinson, B.E.5
  • 34
    • 0017360731 scopus 로고
    • Necropsy evidence of central cholinergic deficits in senile dementia
    • E.K. Perry, R.H. Perry, G. Blessed, B.E. Tomlinson: Necropsy evidence of central cholinergic deficits in senile dementia, Lancet. 1, 189 (1977)
    • (1977) Lancet. , vol.1 , pp. 189
    • Perry, E.K.1    Perry, R.H.2    Blessed, G.3    Tomlinson, B.E.4
  • 35
    • 0036810329 scopus 로고    scopus 로고
    • Alzheimer’s disease and the basal forebrain cholinergic system: Relations to β-amyloid peptides, cognition, and treatment strategies
    • D.S. Auld, T.J. Kornecook, S. Bastianetto, R. Quirion: Alzheimer’s disease and the basal forebrain cholinergic system: Relations to β-amyloid peptides, cognition, and treatment strategies, Prog. Neurobiol. 68, 209-245 (2002)
    • (2002) Prog. Neurobiol. , vol.68 , pp. 209-245
    • Auld, D.S.1    Kornecook, T.J.2    Bastianetto, S.3    Quirion, R.4
  • 36
    • 0027031286 scopus 로고
    • Neuroreceptor changes in Alzheimer disease
    • A. Nordberg: Neuroreceptor changes in Alzheimer disease, Cerebrovasc. Brain Metab. Rev. 4, 303-328 (1992)
    • (1992) Cerebrovasc. Brain Metab. Rev. , vol.4 , pp. 303-328
    • Nordberg, A.1
  • 38
    • 0346025493 scopus 로고    scopus 로고
    • Functional neurochemistry of Alzheimer’s disease
    • W. Gsell, G. Jungkunz, P. Riederer: Functional neurochemistry of Alzheimer’s disease, Curr. Pharmacol. Des. 10, 265-293 (2004)
    • (2004) Curr. Pharmacol. Des. , vol.10 , pp. 265-293
    • Gsell, W.1    Jungkunz, G.2    Riederer, P.3
  • 39
    • 0034125843 scopus 로고    scopus 로고
    • On neurodegenerative diseases, models, and treatment strategies: Lessons learned and lessons forgotten a generation following the cholinergic hypothesis
    • R.T. Bartus: On neurodegenerative diseases, models, and treatment strategies: Lessons learned and lessons forgotten a generation following the cholinergic hypothesis, Exp. Neurol. 163, 495-529 (2000)
    • (2000) Exp. Neurol. , vol.163 , pp. 495-529
    • Bartus, R.T.1
  • 40
    • 55849111494 scopus 로고    scopus 로고
    • Cholinergic system during the progression of Alzheimer’s disease: Therapeutic implications
    • E.J. Mufson, S.E. Counts, S.E. Perez, S.D. Ginsberg: Cholinergic system during the progression of Alzheimer’s disease: Therapeutic implications, Exp, Rev. Neurother. 8, 1703-1718 (2008)
    • (2008) Exp, Rev. Neurother. , vol.8 , pp. 1703-1718
    • Mufson, E.J.1    Counts, S.E.2    Perez, S.E.3    Ginsberg, S.D.4
  • 41
    • 34548672350 scopus 로고    scopus 로고
    • Cholinotrophic molecular substrates of mild cognitive impairment in the elderly
    • E.J. Mufson, S.E. Counts, M. Fahnestock, S.D. Ginsberg: Cholinotrophic molecular substrates of mild cognitive impairment in the elderly, Curr. Alzheimer Res. 4, 340-350 (2007)
    • (2007) Curr. Alzheimer Res. , vol.4 , pp. 340-350
    • Mufson, E.J.1    Counts, S.E.2    Fahnestock, M.3    Ginsberg, S.D.4
  • 42
    • 34548699096 scopus 로고    scopus 로고
    • NGF-cholinergic dependency in brain aging, MCI and Alzheimer’s disease
    • A.C. Cuello, M.A. Bruno, K.F. Bell: NGF-cholinergic dependency in brain aging, MCI and Alzheimer’s disease, Curr. Alzheimer Res. 4, 351-358 (2007)
    • (2007) Curr. Alzheimer Res. , vol.4 , pp. 351-358
    • Cuello, A.C.1    Bruno, M.A.2    Bell, K.F.3
  • 43
    • 78650944520 scopus 로고    scopus 로고
    • APP processing in Alzheimer’s disease
    • Y.W. Zhang, R. Thompson, H. Zhang, H. Xu: APP processing in Alzheimer’s disease, Mol. Brain 4, 3 (2011), doi: 10.1186/1756-6606-4-3
    • (2011) Mol. Brain , vol.4 , Issue.3
    • Zhang, Y.W.1    Thompson, R.2    Zhang, H.3    Xu, H.4
  • 44
    • 60549089207 scopus 로고    scopus 로고
    • APP binds DR6 to trigger axon pruning and neuron death via distinct caspases
    • A. Nikolaev, T. McLaughlin, D.D. O’Leary, M. Tessier-Lavigne: APP binds DR6 to trigger axon pruning and neuron death via distinct caspases, Nature 457, 981-989 (2009)
    • (2009) Nature , vol.457 , pp. 981-989
    • Nikolaev, A.1    McLaughlin, T.2    O’Leary, D.D.3    Tessier-Lavigne, M.4
  • 45
    • 78049267204 scopus 로고    scopus 로고
    • Soluble amyloid precursor protein (APP) regulates transthyretin and Klotho gene expression without rescuing the essential function of APP
    • H. Li, B. Wang, Z. Wang, Q. Guo, K. Tabuchi, R.E. Hammer, T.C. Südhof, H. Zheng: Soluble amyloid precursor protein (APP) regulates transthyretin and Klotho gene expression without rescuing the essential function of APP, Proc. Natl. Acad. Sci. USA 107, 17362-17367 (2010)
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 17362-17367
    • Li, H.1    Wang, B.2    Wang, Z.3    Guo, Q.4    Tabuchi, K.5    Hammer, R.E.6    Südhof, T.C.7    Zheng, H.8
  • 46
    • 76849086405 scopus 로고    scopus 로고
    • The secretases: Enzymes with therapeutic potential in Alzheimer disease
    • B. De Strooper, R. Vassar, T. Golde: The secretases: Enzymes with therapeutic potential in Alzheimer disease, Nat. Rev. Neurol. 6, 99-107 (2010)
    • (2010) Nat. Rev. Neurol. , vol.6 , pp. 99-107
    • De Strooper, B.1    Vassar, R.2    Golde, T.3
  • 47
    • 0025899041 scopus 로고
    • Amyloid deposition as the central event in the aetiology of Alzheimer’s disease
    • J. Hardy, D. Allsop: Amyloid deposition as the central event in the aetiology of Alzheimer’s disease, Trends Pharmacol. Sci. 12, 383-388 (1991)
    • (1991) Trends Pharmacol. Sci. , vol.12 , pp. 383-388
    • Hardy, J.1    Allsop, D.2
  • 48
    • 67651180986 scopus 로고    scopus 로고
    • The amyloid hypothesis for Alzheimer’s disease: A critical reappraisal
    • J. Hardy: The amyloid hypothesis for Alzheimer’s disease: A critical reappraisal, J. Neurochem. 110, 1129-1134 (2009)
    • (2009) J. Neurochem. , vol.110 , pp. 1129-1134
    • Hardy, J.1
  • 49
    • 79951674097 scopus 로고    scopus 로고
    • Transgenic animal models of neurodegeneration based on human genetic studies
    • B.K. Harvey, C.T. Richie, B.J. Hoffer, M. Airavaara: Transgenic animal models of neurodegeneration based on human genetic studies, J. Neural Transm. 118, 27-45 (2011)
    • (2011) J. Neural Transm. , vol.118 , pp. 27-45
    • Harvey, B.K.1    Richie, C.T.2    Hoffer, B.J.3    Airavaara, M.4
  • 50
    • 78751662442 scopus 로고    scopus 로고
    • The role of G proteincoupled receptors in the pathology of Alzheimer’s disease
    • A. Thathiah, B. De Strooper: The role of G proteincoupled receptors in the pathology of Alzheimer’s disease, Nat. Rev. Neurosci. 12, 73-87 (2011)
    • (2011) Nat. Rev. Neurosci. , vol.12 , pp. 73-87
    • Thathiah, A.1    De Strooper, B.2
  • 51
    • 52049105166 scopus 로고    scopus 로고
    • Interactions between the amyloid and cholinergic mechanisms in Alzheimer’s disease
    • M. Pákáski, J. Kálmán: Interactions between the amyloid and cholinergic mechanisms in Alzheimer’s disease, Neurochem. Int. 53, 103-111 (2008)
    • (2008) Neurochem. Int. , vol.53 , pp. 103-111
    • Pákáski, M.1    Kálmán, J.2
  • 52
    • 77949681543 scopus 로고    scopus 로고
    • Nicotinic acetylcholine receptor interaction with beta-amyloid: Molecular, cellular, and physiological consequences
    • R.H. Parri, T.K. Dineley: Nicotinic acetylcholine receptor interaction with beta-amyloid: Molecular, cellular, and physiological consequences, Curr. Alzheimer Res. 7, 27-39 (2010)
    • (2010) Curr. Alzheimer Res. , vol.7 , pp. 27-39
    • Parri, R.H.1    Dineley, T.K.2
  • 53
    • 0022616589 scopus 로고
    • Alzheimer plaques and cortical cholinergic innervation
    • M.M. Mesulam: Alzheimer plaques and cortical cholinergic innervation, Neuroscience 17, 275-276 (1986)
    • (1986) Neuroscience , vol.17 , pp. 275-276
    • Mesulam, M.M.1
  • 54
    • 0027514286 scopus 로고
    • Colocalization of cholinesterases with β-amyloid protein in aged and Alzheimer’s brain
    • M.A. Moran, E.J. Mufson, P. Gomez-Ramos: Colocalization of cholinesterases with β-amyloid protein in aged and Alzheimer’s brain, Acta Neuropathol. 85, 362-369 (1993)
    • (1993) Acta Neuropathol. , vol.85 , pp. 362-369
    • Moran, M.A.1    Mufson, E.J.2    Gomez-Ramos, P.3
  • 55
    • 0026476297 scopus 로고
    • Release of Alzheimer amyloid precursor derivatives stimulated by activation of muscarinic acetylcholine receptors
    • R.M. Nitsch, B.E. Slack, R.J. Wurtman, J.H. Growdon: Release of Alzheimer amyloid precursor derivatives stimulated by activation of muscarinic acetylcholine receptors, Science 258, 304-307 (1992)
    • (1992) Science , vol.258 , pp. 304-307
    • Nitsch, R.M.1    Slack, B.E.2    Wurtman, R.J.3    Growdon, J.H.4
  • 57
    • 0027209083 scopus 로고
    • Release of amyloid beta-protein precursor derivatives by electrical depolarization of rat hippocampal slices
    • R.M. Nitsch, S.A. Farber, J.H. Growdon, R.J. Wurtman: Release of amyloid beta-protein precursor derivatives by electrical depolarization of rat hippocampal slices, Proc. Natl. Acad. Sci. USA 90, 5191-5193 (1993)
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5191-5193
    • Nitsch, R.M.1    Farber, S.A.2    Growdon, J.H.3    Wurtman, R.J.4
  • 59
    • 0028971033 scopus 로고
    • Regulated secretion of beta-amyloid precursor protein in rat brain
    • S.A. Farber, R.M. Nitsch, J.G. Schulz, R.J. Wurtman: Regulated secretion of beta-amyloid precursor protein in rat brain, J. Neurosci. 15, 7442-7451 (1995)
    • (1995) J. Neurosci. , vol.15 , pp. 7442-7451
    • Farber, S.A.1    Nitsch, R.M.2    Schulz, J.G.3    Wurtman, R.J.4
  • 60
    • 0030609970 scopus 로고    scopus 로고
    • In vivo consequences of M1-receptor activation by talsaclidine
    • A. Walland, S. Burkard, R. Hammer, W. Troger: In vivo consequences of M1-receptor activation by talsaclidine, Life Sci. 60, 977-984 (1997)
    • (1997) Life Sci. , vol.60 , pp. 977-984
    • Walland, A.1    Burkard, S.2    Hammer, R.3    Troger, W.4
  • 61
    • 0343811715 scopus 로고    scopus 로고
    • Muscarinic M1 receptor agonists increase the secretion of the amyloid precursor protein ectodomain
    • D.M. Müller, K. Mendla, S.A. Farber, R.M. Nitsch: Muscarinic M1 receptor agonists increase the secretion of the amyloid precursor protein ectodomain, Life Sci. 60, 985-991 (1997)
    • (1997) Life Sci. , vol.60 , pp. 985-991
    • Müller, D.M.1    Mendla, K.2    Farber, S.A.3    Nitsch, R.M.4
  • 63
    • 12444313989 scopus 로고    scopus 로고
    • Treatment with the selective muscarinic m1 agonist talsaclidine decreases cerebrospinal fluid levels of Aβ42 in patients with Alzheimer’s disease
    • R.M. Nitsch: Treatment with the selective muscarinic m1 agonist talsaclidine decreases cerebrospinal fluid levels of Aβ42 in patients with Alzheimer’s disease, Amyloid 10, 1-6 (2003)
    • (2003) Amyloid , vol.10 , pp. 1-6
    • Nitsch, R.M.1
  • 65
    • 79957646992 scopus 로고    scopus 로고
    • ERK1-independent α-secretase cut of β-amyloid precursor protein via M1 muscarinic receptors and PKCα/ε
    • M. Cisse, U. Braun, M. Leitges, A. Fisher, G. Pages, F. Checler, B. Vincent: ERK1-independent α-secretase cut of β-amyloid precursor protein via M1 muscarinic receptors and PKCα/ε, Mol. Cell Neurosci. 47, 223-232 (2011)
    • (2011) Mol. Cell Neurosci. , vol.47 , pp. 223-232
    • Cisse, M.1    Braun, U.2    Leitges, M.3    Fisher, A.4    Pages, G.5    Checler, F.6    Vincent, B.7
  • 66
    • 0028935040 scopus 로고
    • Tyrosine phosphorylationdependent stimulation of amyloid precursor protein secretion by the m3 muscarinic acetylcholine receptor
    • B.E. Slack, J. Breu, M.A. Petryniak, K. Srivastava, R.J. Wurtman: Tyrosine phosphorylationdependent stimulation of amyloid precursor protein secretion by the m3 muscarinic acetylcholine receptor, J. Biol. Chem. 270, 8337-8344 (1995)
    • (1995) J. Biol. Chem. , vol.270 , pp. 8337-8344
    • Slack, B.E.1    Breu, J.2    Petryniak, M.A.3    Srivastava, K.4    Wurtman, R.J.5
  • 67
    • 0031751761 scopus 로고    scopus 로고
    • Mitogenactivated protein kinase-dependent and protein kinase C-dependent pathways link the m1 muscarinic receptor to beta-amyloid precursor protein secretion
    • R. Haring, A. Fisher, D. Marciano, Z. Pittel, Y. Kloog, A. Zuckerman, N. Eshhar, E. Heldman: Mitogenactivated protein kinase-dependent and protein kinase C-dependent pathways link the m1 muscarinic receptor to beta-amyloid precursor protein secretion, J. Neurochem. 71, 2094-2103 (1998)
    • (1998) J. Neurochem. , vol.71 , pp. 2094-2103
    • Haring, R.1    Fisher, A.2    Marciano, D.3    Pittel, Z.4    Kloog, Y.5    Zuckerman, A.6    Eshhar, N.7    Heldman, E.8
  • 68
    • 0001059974 scopus 로고    scopus 로고
    • The regulation of amyloid precursor protein metabolism by cholinergic mechanisms and neurotrophin receptor signaling
    • S. Roßner, U. Ueberham, R. Schliebs, J.R. Perez-Polo, V. Bigl: The regulation of amyloid precursor protein metabolism by cholinergic mechanisms and neurotrophin receptor signaling, Prog. Neurobiol. 56, 541-569 (1998)
    • (1998) Prog. Neurobiol. , vol.56 , pp. 541-569
    • Roßner, S.1    Ueberham, U.2    Schliebs, R.3    Perez-Polo, J.R.4    Bigl, V.5
  • 69
    • 0032693398 scopus 로고    scopus 로고
    • Cognitive changes and modified processing of amyloid precursor protein in the cortical and hippocampal system after cholinergic synapse loss and muscarinic receptor activation
    • L. Lin, B. Georgievska, A. Mattsson, O. Isacson: Cognitive changes and modified processing of amyloid precursor protein in the cortical and hippocampal system after cholinergic synapse loss and muscarinic receptor activation, Proc. Natl. Acad. Sci. USA 96, 12108-12113 (1999)
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 12108-12113
    • Lin, L.1    Georgievska, B.2    Mattsson, A.3    Isacson, O.4
  • 70
    • 0036454306 scopus 로고    scopus 로고
    • Corticohippocampal APP and NGF levels are dynamically altered by cholinergic muscarinic antagonist or M1 agonist treatment in normal mice
    • H. Seo, A.W. Ferree, O. Isacson: Corticohippocampal APP and NGF levels are dynamically altered by cholinergic muscarinic antagonist or M1 agonist treatment in normal mice, Eur J. Neurosci. 15, 498-505 (2002)
    • (2002) Eur J. Neurosci. , vol.15 , pp. 498-505
    • Seo, H.1    Ferree, A.W.2    Isacson, O.3
  • 71
    • 33644535477 scopus 로고    scopus 로고
    • Muscarinic acetylcholine receptor inhibition in transgenic Alzheimer-like Tg2576 mice by scopolamine favours the amyloidogenic route of processing of amyloid precursor protein
    • W. Liskowsky, R. Schliebs: Muscarinic acetylcholine receptor inhibition in transgenic Alzheimer-like Tg2576 mice by scopolamine favours the amyloidogenic route of processing of amyloid precursor protein, Int. J. Devl. Neurosci. 24, 149-156 (2006)
    • (2006) Int. J. Devl. Neurosci. , vol.24 , pp. 149-156
    • Liskowsky, W.1    Schliebs, R.2
  • 72
    • 77949826581 scopus 로고    scopus 로고
    • Deletion of M1 muscarinic acetylcholine receptors increases amyloid pathology in vitro and in vivo
    • A.A. Davis, J.J. Fritz, J. Wess, J.J. Lah, A.I. Levey: Deletion of M1 muscarinic acetylcholine receptors increases amyloid pathology in vitro and in vivo, J. Neurosci. 30, 4190-4196 (2010)
    • (2010) J. Neurosci. , vol.30 , pp. 4190-4196
    • Davis, A.A.1    Fritz, J.J.2    Wess, J.3    Lah, J.J.4    Levey, A.I.5
  • 75
    • 3042712380 scopus 로고    scopus 로고
    • β-secretase BACE1 is differentially controlled through muscarinic acetylcholine receptor signaling
    • T. Züchner, J.R. Perez-Polo, R. Schliebs: β-secretase BACE1 is differentially controlled through muscarinic acetylcholine receptor signaling, J. Neurosci. Res. 77, 250-257 (2004)
    • (2004) J. Neurosci. Res. , vol.77 , pp. 250-257
    • Züchner, T.1    Perez-Polo, J.R.2    Schliebs, R.3
  • 76
    • 0037223063 scopus 로고    scopus 로고
    • Regulation of G protein-coupled receptor kinases and arrestins during receptor desensitization
    • T.A. Kohout, R.J. Lefkowitz: Regulation of G protein-coupled receptor kinases and arrestins during receptor desensitization, Mol. Pharmacol. 63, 9-18 (2003)
    • (2003) Mol. Pharmacol. , vol.63 , pp. 9-18
    • Kohout, T.A.1    Lefkowitz, R.J.2
  • 77
    • 67749145689 scopus 로고    scopus 로고
    • GRK5 deficiency leads to reduced hippocampal acetylcholine level via impaired presynaptic M2/M4 autoreceptor desensitization
    • J. Liu, I. Rasul, Y. Sun, G. Wu, L. Li, R.T. Premont, W.Z. Suo: GRK5 deficiency leads to reduced hippocampal acetylcholine level via impaired presynaptic M2/M4 autoreceptor desensitization, J. Biol. Chem. 284, 19564-19571 (2009)
    • (2009) J. Biol. Chem. , vol.284 , pp. 19564-19571
    • Liu, J.1    Rasul, I.2    Sun, Y.3    Wu, G.4    Li, L.5    Premont, R.T.6    Suo, W.Z.7
  • 78
    • 0036522982 scopus 로고    scopus 로고
    • Characterization of central inhibitory muscarinic autoreceptors by the use of muscarinic acetylcholine receptor knock-out mice
    • W. Zhang, A.S. Basile, J. Gomeza, L.A. Volpicelli, A.I. Levey, J. Wess: Characterization of central inhibitory muscarinic autoreceptors by the use of muscarinic acetylcholine receptor knock-out mice, J. Neurosci. 22, 1709-1717 (2002)
    • (2002) J. Neurosci. , vol.22 , pp. 1709-1717
    • Zhang, W.1    Basile, A.S.2    Gomeza, J.3    Volpicelli, L.A.4    Levey, A.I.5    Wess, J.6
  • 79
    • 1842506382 scopus 로고    scopus 로고
    • Abnormality of G-protein-coupled receptor kinases at prodromala and early stages of Alzheimer’s disease: An association with early beta-amyloid accumulation
    • Z. Suo, M.Wu, B.A. Citron, G.T.Wong, B.W. Festoff: Abnormality of G-protein-coupled receptor kinases at prodromal and early stages of Alzheimer’s disease: An association with early beta-amyloid accumulation, J. Neurosci. 24, 3444-3452 (2004)
    • (2004) J. Neurosci. , vol.24 , pp. 3444-3452
    • Suo, Z.1    Wu, M.2    Citron, B.A.3    Wong, G.T.4    Festoff, B.W.5
  • 80
    • 78650631014 scopus 로고    scopus 로고
    • GRK5 deficiency accelerates β-amyloid accumulation in Tg2576 mice via impaired cholinergic activity
    • S. Cheng, L. Li, S. He, J. Liu, Y. Sun, M. He, K. Grasing, R.T. Premont, W.Z. Suo: GRK5 deficiency accelerates β-amyloid accumulation in Tg2576 mice via impaired cholinergic activity, J. Biol. Chem. 285, 41541-41548 (2010)
    • (2010) J. Biol. Chem. , vol.285 , pp. 41541-41548
    • Cheng, S.1    Li, L.2    He, S.3    Liu, J.4    Sun, Y.5    He, M.6    Grasing, K.7    Premont, R.T.8    Suo, W.Z.9
  • 82
    • 0030880424 scopus 로고    scopus 로고
    • Enhanced release of secreted form of Alzheimer’s amyloid precursor protein from PC12 cells by nicotine
    • S.H. Kim, Y.K. Kim, S.J. Jeong, C. Haass, Y.H. Kim, Y.H. Suh: Enhanced release of secreted form of Alzheimer’s amyloid precursor protein from PC12 cells by nicotine, Mol. Pharmacol. 52, 430-436 (1997)
    • (1997) Mol. Pharmacol. , vol.52 , pp. 430-436
    • Kim, S.H.1    Kim, Y.K.2    Jeong, S.J.3    Haass, C.4    Kim, Y.H.5    Suh, Y.H.6
  • 84
    • 34848913464 scopus 로고    scopus 로고
    • The consequences of reducing expression of the alpha7 nicotinic receptor by RNA interference and of stimulating its activity with an alpha7 agonist in SH-SY5Y cells indicate that this receptor plays a neuroprotective role in connection with the pathogenesis of Alzheimer’s disease
    • X.L. Qi, A. Nordberg, J. Xiu, Z.Z. Guan: The consequences of reducing expression of the alpha7 nicotinic receptor by RNA interference and of stimulating its activity with an alpha7 agonist in SH-SY5Y cells indicate that this receptor plays a neuroprotective role in connection with the pathogenesis of Alzheimer’s disease, Neurochem. Int. 51, 377-383 (2007)
    • (2007) Neurochem. Int. , vol.51 , pp. 377-383
    • Qi, X.L.1    Nordberg, A.2    Xiu, J.3    Guan, Z.Z.4
  • 86
    • 0036295594 scopus 로고    scopus 로고
    • Nicotine reduces the secretion of Alzheimer’s β-amyloid precursor protein containing β-amyloid peptide in the rat without altering synaptic proteins
    • D.K. Lahiri, T. Utsuki, D. Chen, M.R. Farlow, M. Shoaib, D.K. Ingram, N.H. Greig: Nicotine reduces the secretion of Alzheimer’s β-amyloid precursor protein containing β-amyloid peptide in the rat without altering synaptic proteins, Ann. N. Y. Acad. Sci. 965, 364-372 (2002)
    • (2002) Ann. N. Y. Acad. Sci. , vol.965 , pp. 364-372
    • Lahiri, D.K.1    Utsuki, T.2    Chen, D.3    Farlow, M.R.4    Shoaib, M.5    Ingram, D.K.6    Greig, N.H.7
  • 87
    • 60949111629 scopus 로고    scopus 로고
    • Nicotinic receptor agonists and antagonists increase sAPPalpha secretion and decrease Abeta levels in vitro
    • M. Mousavi, E. Hellström-Lindahl: Nicotinic receptor agonists and antagonists increase sAPPalpha secretion and decrease Abeta levels in vitro, Neurochem. Int. 54, 237-244 (2009)
    • (2009) Neurochem. Int. , vol.54 , pp. 237-244
    • Mousavi, M.1    Hellström-Lindahl, E.2
  • 88
    • 77956871554 scopus 로고    scopus 로고
    • Activation of α7 nicotinic receptor affects APP processing by regulating secretase activity in SH-EP1-α7 nAChR-hAPP695 cells
    • H.Z. Nie, S. Shi, R.J. Lukas, W.J. Zhao, Y.N. Sun, M. Yin: Activation of α7 nicotinic receptor affects APP processing by regulating secretase activity in SH-EP1-α7 nAChR-hAPP695 cells, Brain Res. 1356, 112-120 (2010)
    • (2010) Brain Res. , vol.1356 , pp. 112-120
    • Nie, H.Z.1    Shi, S.2    Lukas, R.J.3    Zhao, W.J.4    Sun, Y.N.5    Yin, M.6
  • 89
    • 79954434338 scopus 로고    scopus 로고
    • Nicotine decreases beta-amyloid through regulating BACE1 transcription in SH-EP1-α4β2 nAChR-APP695 cells
    • H.Z. Nie, Z.Q. Li, Q.X. Yan, Z.J. Wang, W.J. Zhao, L.C. Guo, M. Yin: Nicotine decreases beta-amyloid through regulating BACE1 transcription in SH-EP1-α4β2 nAChR-APP695 cells, Neurochem. Res. 36, 904-912 (2011)
    • (2011) Neurochem. Res. , vol.36 , pp. 904-912
    • Nie, H.Z.1    Li, Z.Q.2    Yan, Q.X.3    Wang, Z.J.4    Zhao, W.J.5    Guo, L.C.6    Yin, M.7
  • 91
    • 79954594758 scopus 로고    scopus 로고
    • Chronic nicotine restores normal Aβ levels and prevents short-term memory and E-LTP impairment in Aβ ratmodel of Alzheimer’s disease
    • M. Srivareerat, T.T. Tran, S. Salim, A.M. Aleisa, K.A. Alkadhi: Chronic nicotine restores normal Aβ levels and prevents short-term memory and E-LTP impairment in Aβ ratmodel of Alzheimer’s disease, Neurobiol. Aging 32, 834-844 (2011)
    • (2011) Neurobiol. Aging , vol.32 , pp. 834-844
    • Srivareerat, M.1    Tran, T.T.2    Salim, S.3    Aleisa, A.M.4    Alkadhi, K.A.5
  • 93
    • 0033385632 scopus 로고    scopus 로고
    • Neurotoxicity and oxidative damage of β-amyloid 1-42 versus β-amyloid 1-40 in themouse cerebral cortex
    • A.M. Klein, N.W. Kowall, R.J. Ferrante: Neurotoxicity and oxidative damage of β-amyloid 1-42 versus β-amyloid 1-40 in themouse cerebral cortex, Ann. N. Y. Acad. Sci. 893, 314-320 (1999)
    • (1999) Ann. N. Y. Acad. Sci. , vol.893 , pp. 314-320
    • Klein, A.M.1    Kowall, N.W.2    Ferrante, R.J.3
  • 95
    • 34248190279 scopus 로고    scopus 로고
    • Aβ oligomers-a decade of discovery
    • D.M. Walsh, D.J. Selkoe: Aβ oligomers-a decade of discovery, J. Neurochem. 101, 1172-1184 (2007)
    • (2007) J. Neurochem. , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 96
    • 64149132721 scopus 로고    scopus 로고
    • Amyloid β-protein toxicity and the pathogenesis of Alzheimer disease
    • B.A. Yankner, T. Lu: Amyloid β-protein toxicity and the pathogenesis of Alzheimer disease, J. Biol. Chem. 284, 4755-4759 (2009)
    • (2009) J. Biol. Chem. , vol.284 , pp. 4755-4759
    • Yankner, B.A.1    Lu, T.2
  • 97
    • 79955727727 scopus 로고    scopus 로고
    • The cholinergic system in aging and neuronal degeneration
    • R. Schliebs, T. Arendt: The cholinergic system in aging and neuronal degeneration, Behav. Brain Res. 221, 555-563 (2011)
    • (2011) Behav. Brain Res. , vol.221 , pp. 555-563
    • Schliebs, R.1    Arendt, T.2
  • 99
    • 78650637178 scopus 로고    scopus 로고
    • Amyloid beta as a modulator of synaptic plasticity
    • M.S. Parihar, G.J. Brewer: Amyloid beta as a modulator of synaptic plasticity, J. Alzheimers Dis. 22, 741-763 (2010)
    • (2010) J. Alzheimers Dis. , vol.22 , pp. 741-763
    • Parihar, M.S.1    Brewer, G.J.2
  • 103
    • 0037145719 scopus 로고    scopus 로고
    • Impairment of cholinergic neurotransmission in adult and aged transgenic Tg2576 mouse brain expressing the Swedish mutation of human beta-amyloid precursor protein
    • J. Apelt, A. Kumar, R. Schliebs: Impairment of cholinergic neurotransmission in adult and aged transgenic Tg2576 mouse brain expressing the Swedish mutation of human beta-amyloid precursor protein, Brain Res. 953, 17-30 (2002)
    • (2002) Brain Res. , vol.953 , pp. 17-30
    • Apelt, J.1    Kumar, A.2    Schliebs, R.3
  • 104
    • 0038360763 scopus 로고    scopus 로고
    • Degeneration of β-amyloid-associated cholinergic structures in transgenic APPSW mice
    • H.J. Lüth, J. Apelt, A. Ihunwo, R. Schliebs: Degeneration of β-amyloid-associated cholinergic structures in transgenic APPSW mice, Brain Res. 977, 16-22 (2003)
    • (2003) Brain Res. , vol.977 , pp. 16-22
    • Lüth, H.J.1    Apelt, J.2    Ihunwo, A.3    Schliebs, R.4
  • 105
    • 0242383891 scopus 로고    scopus 로고
    • Alterations in cholinergic and non-cholinergic neurotransmitter receptor densities in transgenic Tg2576 mouse brain with β-amyloid plaque pathology
    • M. Klingner, J. Apelt, A. Kumar, D. Sorger, O. Sabri, J. Steinbach, M. Scheunemann, R. Schliebs: Alterations in cholinergic and non-cholinergic neurotransmitter receptor densities in transgenic Tg2576 mouse brain with β-amyloid plaque pathology, Int. J. Devl. Neurosci. 21, 357-369 (2003)
    • (2003) Int. J. Devl. Neurosci. , vol.21 , pp. 357-369
    • Klingner, M.1    Apelt, J.2    Kumar, A.3    Sorger, D.4    Sabri, O.5    Steinbach, J.6    Scheunemann, M.7    Schliebs, R.8
  • 107
    • 14344263222 scopus 로고    scopus 로고
    • Analysis of cholinergic markers, biogenic amines, and amino acids in the CNS of two APP overexpression mouse models
    • D. Van Dam, B. Marescau, S. Engelborghs, T. Cremers, J. Mulder, M. Staufenbiel, P.P. De Deyn: Analysis of cholinergic markers, biogenic amines, and amino acids in the CNS of two APP overexpression mouse models, Neurochem. Int. 46, 409-422 (2005)
    • (2005) Neurochem. Int. , vol.46 , pp. 409-422
    • Van Dam, D.1    Marescau, B.2    Engelborghs, S.3    Cremers, T.4    Mulder, J.5    Staufenbiel, M.6    De Deyn, P.P.7
  • 108
  • 112
    • 84856971964 scopus 로고    scopus 로고
    • Different β-amyloid oligomer assemblies in Alzheimer brains correlate with age of disease onset and impaired cholinergic activity
    • F. Bao, L. Wicklund, P.N. Lacor, W.L. Klein, A. Nordberg, A. Marutle: Different β-amyloid oligomer assemblies in Alzheimer brains correlate with age of disease onset and impaired cholinergic activity, Neurobiol. Aging. 33, 825.e1-825.e13 (2012)
    • (2012) Neurobiol. Aging. , vol.33 , pp. 825.e1-825.e13
    • Bao, F.1    Wicklund, L.2    Lacor, P.N.3    Klein, W.L.4    Nordberg, A.5    Marutle, A.6
  • 113
    • 0027333557 scopus 로고
    • Cellular processing of betaamyloid precursor protein and the genesis of amyloid beta-peptide
    • C. Haass, D.J. Selkoe: Cellular processing of betaamyloid precursor protein and the genesis of amyloid beta-peptide, Cell 75, 1039-1042 (1993)
    • (1993) Cell , vol.75 , pp. 1039-1042
    • Haass, C.1    Selkoe, D.J.2
  • 115
    • 11344265672 scopus 로고    scopus 로고
    • Interactions between β-amyloida and central cholinergic neurons: Implications for Alzheimer’s disease
    • S. Kar, S.P. Slowikowski, D. Westaway, H.T. Mount: Interactions between β-amyloid and central cholinergic neurons: Implications for Alzheimer’s disease, J. Psychiatry Neurosci. 29, 427-441 (2004)
    • (2004) J. Psychiatry Neurosci. , vol.29 , pp. 427-441
    • Kar, S.1    Slowikowski, S.P.2    Westaway, D.3    Mount, H.T.4
  • 116
    • 0026502543 scopus 로고
    • Choline metabolism as a basis for the selective vulnerability of cholinergic neurons
    • R.J. Wurtman: Choline metabolism as a basis for the selective vulnerability of cholinergic neurons, Trends Neurosci. 15, 117-122 (1992)
    • (1992) Trends Neurosci. , vol.15 , pp. 117-122
    • Wurtman, R.J.1
  • 118
    • 0029795254 scopus 로고    scopus 로고
    • Amyloid β-protein reduces acetylcholine synthesis in a cell line derived from cholinergic neurons of the basal forebrain
    • W.A. Pedersen, M.A. Kloczewiak, J.K. Blusztajn: Amyloid β-protein reduces acetylcholine synthesis in a cell line derived from cholinergic neurons of the basal forebrain, Proc. Natl. Acad. Sci. USA 93, 8068-8071 (1996)
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8068-8071
    • Pedersen, W.A.1    Kloczewiak, M.A.2    Blusztajn, J.K.3
  • 121
    • 35348889638 scopus 로고    scopus 로고
    • Amyolid precursor protein mediates presynaptic localization and activity of the high-affinity choline transporter
    • B. Wang, L. Yang, Z. Wang, H. Zheng: Amyolid precursor protein mediates presynaptic localization and activity of the high-affinity choline transporter, Proc. Natl. Acad. Sci. USA 104, 14140-14145 (2007)
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 14140-14145
    • Wang, B.1    Yang, L.2    Wang, Z.3    Zheng, H.4
  • 122
    • 0033988554 scopus 로고    scopus 로고
    • Repeated intracerebroventricular administration of beta-amyloid (25-35) to rats decreases muscarinic receptors in cerebral cortex
    • J. Pavia, J. Alberch, I. Alvárez, A. Toledano, M.L. de Ceballos: Repeated intracerebroventricular administration of beta-amyloid (25-35) to rats decreases muscarinic receptors in cerebral cortex, Neurosci. Lett. 278, 69-72 (2000)
    • (2000) Neurosci. Lett. , vol.278 , pp. 69-72
    • Pavia, J.1    Alberch, J.2    Alvárez, I.3    Toledano, A.4    de Ceballos, M.L.5
  • 123
    • 77952351441 scopus 로고    scopus 로고
    • G protein-coupled receptors, cholinergic dysfunction, and Aβ toxicity in Alzheimer’s disease
    • A. Thathiah, B. De Strooper: G protein-coupled receptors, cholinergic dysfunction, and Aβ toxicity in Alzheimer’s disease, Sci. Signal. 2(93), re8 (2009)
    • (2009) Sci. Signal. , vol.2 , Issue.93
    • Thathiah, A.1    De Strooper, B.2
  • 124
  • 126
    • 0242486453 scopus 로고    scopus 로고
    • Protein andmRNA levels of nicotinic receptors in brain of tobacco using controls and patients with Alzheimer’s disease
    • M. Mousavi, E. Hellström-Lindahl, Z.Z. Guan, K.R. Shan, R. Ravid, A. Nordberg: Protein andmRNA levels of nicotinic receptors in brain of tobacco using controls and patients with Alzheimer’s disease, Neuroscience 122, 515-520 (2003)
    • (2003) Neuroscience , vol.122 , pp. 515-520
    • Mousavi, M.1    Hellström-Lindahl, E.2    Guan, Z.Z.3    Shan, K.R.4    Ravid, R.5    Nordberg, A.6
  • 128
    • 0033302309 scopus 로고    scopus 로고
    • Nicotinic acetylcholine receptors in Alzheimer’s disease
    • A. Wevers, H. Schröder: Nicotinic acetylcholine receptors in Alzheimer’s disease, J. Alzheimers Dis. 1, 207-219 (1999)
    • (1999) J. Alzheimers Dis. , vol.1 , pp. 207-219
    • Wevers, A.1    Schröder, H.2
  • 129
    • 0035251677 scopus 로고    scopus 로고
    • Nicotinic receptor abnormalities of Alzheimer’s disease: Therapeutic implications
    • A. Nordberg: Nicotinic receptor abnormalities of Alzheimer’s disease: Therapeutic implications, Biol. Psychiatry 49, 200-210 (2001)
    • (2001) Biol. Psychiatry , vol.49 , pp. 200-210
    • Nordberg, A.1
  • 130
    • 63849213473 scopus 로고    scopus 로고
    • Nicotinic acetylcholine receptor signalling: Roles in Alzheimer’s disease and amyloid neuroprotection
    • S.D. Buckingham, A.K. Jones, L.A. Brown, D.B. Sattelle: Nicotinic acetylcholine receptor signalling: Roles in Alzheimer’s disease and amyloid neuroprotection, Pharmacol. Rev. 61, 39-61 (2009)
    • (2009) Pharmacol. Rev. , vol.61 , pp. 39-61
    • Buckingham, S.D.1    Jones, A.K.2    Brown, L.A.3    Sattelle, D.B.4
  • 131
    • 75049085411 scopus 로고    scopus 로고
    • Nicotinic receptors, amaloid-β, and synaptic failure in Alzheimer’s disease
    • S. Jürgensen, S. Ferreira: Nicotinic receptors, amaloid-β, and synaptic failure in Alzheimer’s disease, J. Mol. Neurosci. 40, 221-229 (2010)
    • (2010) J. Mol. Neurosci. , vol.40 , pp. 221-229
    • Jürgensen, S.1    Ferreira, S.2
  • 132
    • 0037066072 scopus 로고    scopus 로고
    • Intracellular accumulation of betaamyloid (1-42) in neurons is facilitated by the alpha 7 nicotinic acetylcholine receptor in Alzheimer’s disease
    • R.G. Nagele, M.R. D’Andrea, W.J. Anderson, H.Y. Wang: Intracellular accumulation of betaamyloid (1-42) in neurons is facilitated by the alpha 7 nicotinic acetylcholine receptor in Alzheimer’s disease, Neuroscience 110, 199-211 (2002)
    • (2002) Neuroscience , vol.110 , pp. 199-211
    • Nagele, R.G.1    D’Andrea, M.R.2    Anderson, W.J.3    Wang, H.Y.4
  • 133
    • 77951904180 scopus 로고    scopus 로고
    • Neuronal nicotinic acetylcholine receptor-cholesterol crosstalk in Alzheimer’s disease
    • F.J. Barrantes, V. Borroni, S. Vallés: Neuronal nicotinic acetylcholine receptor-cholesterol crosstalk in Alzheimer’s disease, FEBS Lett. 584, 1856-1863 (2010)
    • (2010) FEBS Lett. , vol.584 , pp. 1856-1863
    • Barrantes, F.J.1    Borroni, V.2    Vallés, S.3
  • 134
    • 0035666459 scopus 로고    scopus 로고
    • Suppressed expression of nicotinic acetylcholine receptors by nanomolar β-amyloid peptides in PC12 cells
    • Z.Z. Guan, H. Miao, J.Y. Tian, C. Unger, A. Nordberg, X. Zhang: Suppressed expression of nicotinic acetylcholine receptors by nanomolar β-amyloid peptides in PC12 cells, J. Neural Transm. 108, 1417-1433 (2001)
    • (2001) J. Neural Transm. , vol.108 , pp. 1417-1433
    • Guan, Z.Z.1    Miao, H.2    Tian, J.Y.3    Unger, C.4    Nordberg, A.5    Zhang, X.6
  • 135
    • 0035836747 scopus 로고    scopus 로고
    • β-amyloid peptide blocks the response of α7-containing nicotinic receptors on hippocampal neurons
    • Q. Liu, H. Kawai, D.K. Berg: β-amyloid peptide blocks the response of α7-containing nicotinic receptors on hippocampal neurons, Proc. Natl. Acad. Sci. USA 98, 4734-4739 (2001)
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 4734-4739
    • Liu, Q.1    Kawai, H.2    Berg, D.K.3
  • 136
    • 84862851690 scopus 로고    scopus 로고
    • Elevation of BACE in an Aβ rat model of Alzheimer’s disease: Exacerbation by chronic stress and prevention by nicotine
    • K.A. Alkadhi, K.H. Alzoubi, M. Srivareerat, T.T. Tran: Elevation of BACE in an Aβ rat model of Alzheimer’s disease: Exacerbation by chronic stress and prevention by nicotine, Int. J. Neuropsychopharmacol. 28, 1-11 (2011)
    • (2011) Int. J. Neuropsychopharmacol. , vol.28 , pp. 1-11
    • Alkadhi, K.A.1    Alzoubi, K.H.2    Srivareerat, M.3    Tran, T.T.4
  • 137
    • 0034006944 scopus 로고    scopus 로고
    • β-Amyloid(1-42) binds to α7 nicotinic acetylcholine receptor with high affinity, Implications for Alzheimer’s disease pathology
    • H.Y. Wang, D.H. Lee, M.R. D’Andrea, P.A. Peterson, R.P. Shank, A.B. Reitz: β-Amyloid(1-42) binds to α7 nicotinic acetylcholine receptor with high affinity, Implications for Alzheimer’s disease pathology, J. Biol. Chem. 275, 5626-5632 (2000)
    • (2000) J. Biol. Chem. , vol.275 , pp. 5626-5632
    • Wang, H.Y.1    Lee, D.H.2    D’Andrea, M.R.3    Peterson, P.A.4    Shank, R.P.5    Reitz, A.B.6
  • 138
    • 0033624509 scopus 로고    scopus 로고
    • Amyloid peptide Aβ (1-42) binds selectively and with picomolar affinity to α7 nicotinic acetylcholine receptors
    • H.Y. Wang, D.H. Lee, C.B. Davis, R.P. Shank: Amyloid peptide Aβ (1-42) binds selectively and with picomolar affinity to α7 nicotinic acetylcholine receptors, J. Neurochem. 75, 1155-1161 (2000)
    • (2000) J. Neurochem. , vol.75 , pp. 1155-1161
    • Wang, H.Y.1    Lee, D.H.2    Davis, C.B.3    Shank, R.P.4
  • 140
    • 18144392979 scopus 로고    scopus 로고
    • Oxidative stress induced by β-amyloid peptide (1-42) is involved in the altered composition of cellular membrane lipids and the decreased expression of nicotinic receptors in human SH-SY5Y neuroblastoma cells
    • X.L. Qi, J. Xiu, K.R. Shan, Y. Xiao, R. Gu, R.Y. Liu, Z.Z. Guan: Oxidative stress induced by β-amyloid peptide (1-42) is involved in the altered composition of cellular membrane lipids and the decreased expression of nicotinic receptors in human SH-SY5Y neuroblastoma cells, Neurochem. Int. 46, 613-621 (2005)
    • (2005) Neurochem. Int. , vol.46 , pp. 613-621
    • Qi, X.L.1    Xiu, J.2    Shan, K.R.3    Xiao, Y.4    Gu, R.5    Liu, R.Y.6    Guan, Z.Z.7
  • 141
    • 0037308415 scopus 로고    scopus 로고
    • Loss of nicotinic receptors induced by β-amyloid peptides in PC12 cells: Possible mechanism involving lipid peroxidation
    • Z.Z. Guan, W.F. Yu, K.R. Shan, T. Nordman, J. Olsson, A. Nordberg: Loss of nicotinic receptors induced by β-amyloid peptides in PC12 cells: Possible mechanism involving lipid peroxidation, J. Neurosci. Res. 71, 397-406 (2003)
    • (2003) J. Neurosci. Res. , vol.71 , pp. 397-406
    • Guan, Z.Z.1    Yu, W.F.2    Shan, K.R.3    Nordman, T.4    Olsson, J.5    Nordberg, A.6
  • 142
    • 0035875962 scopus 로고    scopus 로고
    • β-amyloid activates the mitogen-activated protein kinase cascade via hippocampal α7 nicotinic acetylcholine receptors: In vitro and in vivo mechanisms related to Alzheimer’s disease
    • K.T. Dineley, M. Westerman, D. Bui, K. Bell, K.H. Ashe, J.D. Sweatt: β-amyloid activates the mitogen-activated protein kinase cascade via hippocampal α7 nicotinic acetylcholine receptors: In vitro and in vivo mechanisms related to Alzheimer’s disease, J. Neurosci. 21, 4125-4133 (2001)
    • (2001) J. Neurosci. , vol.21 , pp. 4125-4133
    • Dineley, K.T.1    Westerman, M.2    Bui, D.3    Bell, K.4    Ashe, K.H.5    Sweatt, J.D.6
  • 143
    • 0042357192 scopus 로고    scopus 로고
    • α7 nicotinic acetylcholine receptors mediate β-amyloid peptide-induced tau protein phosphorylation
    • H.Y. Wang, W. Li, N.J. Benedetti, D.H. Lee: α7 nicotinic acetylcholine receptors mediate β-amyloid peptide-induced tau protein phosphorylation, J. Biol. Chem. 278, 31547-31553 (2003)
    • (2003) J. Biol. Chem. , vol.278 , pp. 31547-31553
    • Wang, H.Y.1    Li, W.2    Benedetti, N.J.3    Lee, D.H.4
  • 144
    • 0037067717 scopus 로고    scopus 로고
    • β-Amyloid peptide activates α7 nicotinic acetylcholine receptors expressed in Xenopus oocytes
    • K.T. Dineley, K.A. Bell, D. Bui, J.D. Sweatt: β-Amyloid peptide activates α7 nicotinic acetylcholine receptors expressed in Xenopus oocytes, J. Biol. Chem. 277, 25056-25061 (2002)
    • (2002) J. Biol. Chem , vol.277 , pp. 25056-25061
    • Dineley, K.T.1    Bell, K.A.2    Bui, D.3    Sweatt, J.D.4
  • 145
    • 72449129007 scopus 로고    scopus 로고
    • α7 neuronal nicotinic receptors: The missing link to understanding Alzheimer’s etiopathology?
    • M. Bencherif, P. Lippiello: α7 neuronal nicotinic receptors: The missing link to understanding Alzheimer’s etiopathology?, Med. Hypotheses 74, 281-285 (2010)
    • (2010) Med. Hypotheses , vol.74 , pp. 281-285
    • Bencherif, M.1    Lippiello, P.2
  • 147
    • 67650484613 scopus 로고    scopus 로고
    • Deletion of the α7 nicotinic acetylcholine receptor gene improves cognitive deficits and synaptic pathology in a mouse model of Alzheimer’s disease
    • G. Dziewczapolski, C.M. Glogowski, E. Masliah, S.F. Heinemann: Deletion of the α7 nicotinic acetylcholine receptor gene improves cognitive deficits and synaptic pathology in a mouse model of Alzheimer’s disease, J. Neurosci. 29, 8805-8815 (2009)
    • (2009) J. Neurosci. , vol.29 , pp. 8805-8815
    • Dziewczapolski, G.1    Glogowski, C.M.2    Masliah, E.3    Heinemann, S.F.4
  • 148
    • 79951567728 scopus 로고    scopus 로고
    • Functional interactions of fibrillar and oligomeric amyloid-β with alpha7 nicotinic receptors in Alzheimer’s disease
    • A.M. Lilja, O. Porras, E. Storelli, A. Nordberg, A. Marutle: Functional interactions of fibrillar and oligomeric amyloid-β with alpha7 nicotinic receptors in Alzheimer’s disease, J. Alzheimers Dis. 23, 335-347 (2011)
    • (2011) J. Alzheimers Dis. , vol.23 , pp. 335-347
    • Lilja, A.M.1    Porras, O.2    Storelli, E.3    Nordberg, A.4    Marutle, A.5
  • 149
    • 77957019415 scopus 로고    scopus 로고
    • Amyloid precursor protein gene mutated at Swedish 670/671 sites in vitro induces changed expression of nicotinic acetylcholine receptors and neurotoxicity
    • Y. An, X.L. Qi, J.J. Pei, Z. Tang, Y. Xiao, Z.Z. Guan: Amyloid precursor protein gene mutated at Swedish 670/671 sites in vitro induces changed expression of nicotinic acetylcholine receptors and neurotoxicity, Neurochem. Int. 57, 647-654 (2010)
    • (2010) Neurochem. Int. , vol.57 , pp. 647-654
    • An, Y.1    Qi, X.L.2    Pei, J.J.3    Tang, Z.4    Xiao, Y.5    Guan, Z.Z.6
  • 151
    • 79959985280 scopus 로고    scopus 로고
    • A dual mechanism linking NGF/proNGF imbalance and early inflammation to Alzheimer’s disease neurodegeneration in the AD11 Anti-NGF mouse model
    • S. Capsoni, R. Brandi, I. Arisi, M. D’Onofrio, A. Cattaneo: A dual mechanism linking NGF/proNGF imbalance and early inflammation to Alzheimer’s disease neurodegeneration in the AD11 Anti-NGF mouse model, CNS Neurol. Disord. Drug Targets, 10, 635-647 (2011)
    • (2011) CNS Neurol. Disord. Drug Targets , vol.10 , pp. 635-647
    • Capsoni, S.1    Brandi, R.2    Arisi, I.3    D’Onofrio, M.4    Cattaneo, A.5
  • 153
    • 65249105453 scopus 로고    scopus 로고
    • Selective vulnerability in Alzheimer’s disease: Amyloid precursor protein and p75(NTR) interaction
    • J. Fombonne, S. Rabizadeh, S. Banwait, P. Mehlen, D.E. Bredesen: Selective vulnerability in Alzheimer’s disease: Amyloid precursor protein and p75(NTR) interaction, Ann. Neurol. 65, 294-303 (2009)
    • (2009) Ann. Neurol. , vol.65 , pp. 294-303
    • Fombonne, J.1    Rabizadeh, S.2    Banwait, S.3    Mehlen, P.4    Bredesen, D.E.5
  • 154
    • 77949729496 scopus 로고    scopus 로고
    • Understanding proneurotrophin actions: Recent advances and challenges
    • K.K. Teng, S. Felice, T. Kim, B.L. Hempstead: Understanding proneurotrophin actions: Recent advances and challenges, Dev. Neurobiol. 70, 350-359 (2010)
    • (2010) Dev. Neurobiol. , vol.70 , pp. 350-359
    • Teng, K.K.1    Felice, S.2    Kim, T.3    Hempstead, B.L.4
  • 155
    • 0348110429 scopus 로고    scopus 로고
    • ProNGF: A neurotrophic or an apoptotic molecule?
    • M. Fahnestock, G. Yu, M.D. Coughlin: ProNGF: A neurotrophic or an apoptotic molecule?, Prog. Brain Res. 146, 101-110 (2004)
    • (2004) Prog. Brain Res. , vol.146 , pp. 101-110
    • Fahnestock, M.1    Yu, G.2    Coughlin, M.D.3
  • 157
    • 68949124786 scopus 로고    scopus 로고
    • The role of the p75 neurotrophin receptor in choplinergic dysfunction in Alzheimer’s disease
    • E.J. Coulson, L.M. May, A.M. Sykes, A.S. Hamlin: The role of the p75 neurotrophin receptor in choplinergic dysfunction in Alzheimer’s disease, Neuroscientist 15, 317-322 (2009)
    • (2009) Neuroscientist , vol.15 , pp. 317-322
    • Coulson, E.J.1    May, L.M.2    Sykes, A.M.3    Hamlin, A.S.4
  • 158
    • 22244466071 scopus 로고    scopus 로고
    • Characterization of the signaling pathway downstream p75 neurotrophin receptor involved in β-amyloid peptidedependent cell death
    • C. Costantini, F. Rossi, E. Formaggio, R. Bernardoni, D. Cecconi, V. Della-Bianca: Characterization of the signaling pathway downstream p75 neurotrophin receptor involved in β-amyloid peptidedependent cell death, J. Mol. Neurosci. 25, 141-156 (2005)
    • (2005) J. Mol. Neurosci. , vol.25 , pp. 141-156
    • Costantini, C.1    Rossi, F.2    Formaggio, E.3    Bernardoni, R.4    Cecconi, D.5    Della-Bianca, V.6
  • 159
    • 33745894132 scopus 로고    scopus 로고
    • Does the p75 neurotrophin receptor mediate Aβ-induced toxicity in Alzheimer’s disease?
    • E.J. Coulson: Does the p75 neurotrophin receptor mediate Aβ-induced toxicity in Alzheimer’s disease?, J. Neurochem. 98, 654-660 (2006)
    • (2006) J. Neurochem. , vol.98 , pp. 654-660
    • Coulson, E.J.1
  • 164
    • 77149138009 scopus 로고    scopus 로고
    • Amyloid-β peptides stimulate the expression of the p75(NTR) neurotrophin receptor in SHSY5Y human neuroblastoma cells and AD transgenic mice
    • B. Chakravarthy, C. Gaudet, M. Ménard, T. Atkinson, L. Brown, F.M. Laferla, U. Armato, J. Whitfield: Amyloid-β peptides stimulate the expression of the p75(NTR) neurotrophin receptor in SHSY5Y human neuroblastoma cells and AD transgenic mice, J. Alzheimers Dis. 19, 915-925 (2010)
    • (2010) J. Alzheimers Dis. , vol.19 , pp. 915-925
    • Chakravarthy, B.1    Gaudet, C.2    Ménard, M.3    Atkinson, T.4    Brown, L.5    Laferla, F.M.6    Armato, U.7    Whitfield, J.8
  • 165
    • 11144258263 scopus 로고    scopus 로고
    • Mutations causing neurodegenerative tauopathies
    • M. Goedert, R. Jakes: Mutations causing neurodegenerative tauopathies, Biochim. Biophys. Acta 1739, 240-250 (2005)
    • (2005) Biochim. Biophys. Acta , vol.1739 , pp. 240-250
    • Goedert, M.1    Jakes, R.2
  • 166
    • 0344845132 scopus 로고    scopus 로고
    • Amyloid deposition precedes tangle formation in a triple transgenic model of Alzheimer’s disease
    • S. Oddo, A. Caccamo, M. Kitazawa, B.P. Tseng, F.M. LaFerla: Amyloid deposition precedes tangle formation in a triple transgenic model of Alzheimer’s disease, Neurobiol. Aging 24, 1063-1070 (2003)
    • (2003) Neurobiol. Aging , vol.24 , pp. 1063-1070
    • Oddo, S.1    Caccamo, A.2    Kitazawa, M.3    Tseng, B.P.4    LaFerla, F.M.5
  • 167
    • 14644442872 scopus 로고    scopus 로고
    • Intraneuronal Aβ causes the onset of early Alzheimer’s disease-related cognitive deficits in transgenic mice
    • L.M. Billings, S. Oddo, K.N. Green, J.L. McGaugh, F.M. LaFerla: Intraneuronal Aβ causes the onset of early Alzheimer’s disease-related cognitive deficits in transgenic mice, Neuron 45, 675-688 (2005)
    • (2005) Neuron , vol.45 , pp. 675-688
    • Billings, L.M.1    Oddo, S.2    Green, K.N.3    McGaugh, J.L.4    LaFerla, F.M.5
  • 168
    • 25644456097 scopus 로고    scopus 로고
    • Lipopolysaccharide-induced inflammation exacerbates tau pathology by a cyclindependent kinase 5-mediated pathway in a transgenic model of Alzheimer’s disease
    • M. Kitazawa, S. Oddo, T.R. Yamasaki, K.N. Green, F.M. LaFerla: Lipopolysaccharide-induced inflammation exacerbates tau pathology by a cyclindependent kinase 5-mediated pathway in a transgenic model of Alzheimer’s disease, J. Neurosci. 25, 8843-8853 (2005)
    • (2005) J. Neurosci. , vol.25 , pp. 8843-8853
    • Kitazawa, M.1    Oddo, S.2    Yamasaki, T.R.3    Green, K.N.4    LaFerla, F.M.5
  • 169
    • 33645102446 scopus 로고    scopus 로고
    • Shift in the ratio of three-repeat tau and four-repeat tau mRNAs in individual cholinergic basal forebrain neurons in mild cognitive impairment and Alzheimer’s disease
    • S.D. Ginsberg, S. Che, S.E. Counts, E.J. Mufson: Shift in the ratio of three-repeat tau and four-repeat tau mRNAs in individual cholinergic basal forebrain neurons in mild cognitive impairment and Alzheimer’s disease, J. Neurochem. 96, 1401-1408 (2006)
    • (2006) J. Neurochem. , vol.96 , pp. 1401-1408
    • Ginsberg, S.D.1    Che, S.2    Counts, S.E.3    Mufson, E.J.4
  • 170
    • 0842304284 scopus 로고    scopus 로고
    • The cholinergic lesion of Alzheimer’s disease: Pivotal factor or side show
    • M. Mesulam: The cholinergic lesion of Alzheimer’s disease: Pivotal factor or side show, Learn Mem. 11, 43-49 (2004)
    • (2004) Learn Mem. , vol.11 , pp. 43-49
    • Mesulam, M.1
  • 171
    • 41949104908 scopus 로고    scopus 로고
    • Cholinergic neuronal and axonal abnormalities are present early in aging and in Alzheimer disease
    • C. Geula, N. Nagykery, A. Nicholas, C.K. Wu: Cholinergic neuronal and axonal abnormalities are present early in aging and in Alzheimer disease, J. Neuropathol. Exp. Neurol. 67, 309-318 (2008)
    • (2008) J. Neuropathol. Exp. Neurol. , vol.67 , pp. 309-318
    • Geula, C.1    Nagykery, N.2    Nicholas, A.3    Wu, C.K.4
  • 173
    • 77952547828 scopus 로고    scopus 로고
    • Vascular risk factor detection and control may prevent Alzheimer’s disease
    • J.C. de la Torre: Vascular risk factor detection and control may prevent Alzheimer’s disease, Ageing Res. Rev. 9, 218-225 (2010)
    • (2010) Ageing Res. Rev. , vol.9 , pp. 218-225
    • de la Torre, J.C.1
  • 174
    • 62949149460 scopus 로고    scopus 로고
    • Threats to themind: Aging, amyloid, and hypertension
    • C. Iadecola, L. Park, C. Capone: Threats to themind: Aging, amyloid, and hypertension, Stroke. 40(3 Suppl), S40-44 (2009)
    • (2009) Stroke. , vol.40 , Issue.3 , pp. S40-S44
    • Iadecola, C.1    Park, L.2    Capone, C.3
  • 175
    • 0027314240 scopus 로고
    • Can disturbed brain microcirculation cause Alzheimer’s disease?
    • J.C. de la Torre, T. Mussivand: Can disturbed brain microcirculation cause Alzheimer’s disease?, Neurol. Res. 15, 146-153 (1993)
    • (1993) Neurol. Res. , vol.15 , pp. 146-153
    • de la Torre, J.C.1    Mussivand, T.2
  • 176
    • 78649427539 scopus 로고    scopus 로고
    • Vascular basis for brain degeneration: Faltering controls and risk factors for dementia
    • R.N. Kalaria: Vascular basis for brain degeneration: Faltering controls and risk factors for dementia, Nutr. Rev. 68(Suppl.), S74-87 (2010)
    • (2010) Nutr. Rev. , vol.68 , pp. S74-S87
    • Kalaria, R.N.1
  • 177
    • 79957946047 scopus 로고    scopus 로고
    • Neurovascular function in Alzheimer’s disease patients and experimental models
    • N. Nicolakakis, E. Hamel: Neurovascular function in Alzheimer’s disease patients and experimental models, Cereb. Blood Flow Metab. 31, 1354-1370 (2011)
    • (2011) Cereb. Blood Flow Metab. , vol.31 , pp. 1354-1370
    • Nicolakakis, N.1    Hamel, E.2
  • 178
    • 67349118757 scopus 로고    scopus 로고
    • Microvasculature changes and cerebral amyloid angiopathy in Alzheimer’s disease and their potential impact on therapy
    • R.O. Weller, D. Boche, J.A.R. Nicoll: Microvasculature changes and cerebral amyloid angiopathy in Alzheimer’s disease and their potential impact on therapy, Acta Neuropathol. 119, 87-102 (2009)
    • (2009) Acta Neuropathol. , vol.119 , pp. 87-102
    • Weller, R.O.1    Boche, D.2    Nicoll, J.A.R.3
  • 179
    • 79551713201 scopus 로고    scopus 로고
    • Brain microbleeds and Alzheimer’s disease: Innocent observation or key player?
    • C. Cordonnier, W.M. van der Flier: Brain microbleeds and Alzheimer’s disease: Innocent observation or key player?, Brain 134, 335-344 (2011)
    • (2011) Brain , vol.134 , pp. 335-344
    • Cordonnier, C.1    van der Flier, W.M.2
  • 180
    • 46749099351 scopus 로고    scopus 로고
    • New therapeutic targets in the neurovascular pathway in Alzheimer’s disease
    • B.V. Zlokovic: New therapeutic targets in the neurovascular pathway in Alzheimer’s disease, Neurotherapeutics 5, 409-414 (2008)
    • (2008) Neurotherapeutics , vol.5 , pp. 409-414
    • Zlokovic, B.V.1
  • 181
    • 79954623282 scopus 로고    scopus 로고
    • Perivascular drainage of solutes is impaired in the ageing mouse brain and in the presence of cerebral amyloid angiopathy
    • C.A. Hawkes, W. Härtig, J. Kacza, R. Schliebs, R.O. Weller, J.A. Nicoll, R.O. Carare: Perivascular drainage of solutes is impaired in the ageing mouse brain and in the presence of cerebral amyloid angiopathy, Acta Neuropathol. 121, 431-443 (2011)
    • (2011) Acta Neuropathol. , vol.121 , pp. 431-443
    • Hawkes, C.A.1    Härtig, W.2    Kacza, J.3    Schliebs, R.4    Weller, R.O.5    Nicoll, J.A.6    Carare, R.O.7
  • 182
    • 80054711185 scopus 로고    scopus 로고
    • Vascular β-amyloid and early astrocyte alterations impair cerebrovascular function and cerebral metabolism in transgenic arcAβ mice
    • M. Merlini, E.P. Meyer, A. Ulmann-Schuler, R.M. Nitsch: Vascular β-amyloid and early astrocyte alterations impair cerebrovascular function and cerebral metabolism in transgenic arcAβ mice, Acta Neuropathol. 122, 293-311 (2011)
    • (2011) Acta Neuropathol. , vol.122 , pp. 293-311
    • Merlini, M.1    Meyer, E.P.2    Ulmann-Schuler, A.3    Nitsch, R.M.4
  • 183
    • 0042387969 scopus 로고    scopus 로고
    • Vasoactive effects of Aβ in isolated human cerebrovessels and in a transgenic mouse model of Alzheimer’s disease: Role of inflammation
    • D. Paris, J. Humphrey, A. Quadros, N. Patel, R. Crescentini, F. Crawford, M. Mullan: Vasoactive effects of Aβ in isolated human cerebrovessels and in a transgenic mouse model of Alzheimer’s disease: Role of inflammation, Neurol. Res. 25, 642-651 (2003)
    • (2003) Neurol. Res. , vol.25 , pp. 642-651
    • Paris, D.1    Humphrey, J.2    Quadros, A.3    Patel, N.4    Crescentini, R.5    Crawford, F.6    Mullan, M.7
  • 184
    • 2342614850 scopus 로고    scopus 로고
    • Neurovascular regulation in the normal brain and in Alzheimer’s disease
    • C. Iadecola: Neurovascular regulation in the normal brain and in Alzheimer’s disease, Nat Rev. Neurosci. 5, 347-360 (2004)
    • (2004) Nat Rev. Neurosci. , vol.5 , pp. 347-360
    • Iadecola, C.1
  • 185
    • 67149139988 scopus 로고    scopus 로고
    • The role of vascular factors in late-onset sporadic Alzheimer’s disease. Genetic and molecular aspects
    • A. Rocchi, D. Orsucci, G. Tognoni, R. Ceravolo, G. Siciliano: The role of vascular factors in late-onset sporadic Alzheimer’s disease. Genetic and molecular aspects, Curr. Alzheimer Res. 6, 224-237 (2009)
    • (2009) Curr. Alzheimer Res. , vol.6 , pp. 224-237
    • Rocchi, A.1    Orsucci, D.2    Tognoni, G.3    Ceravolo, R.4    Siciliano, G.5
  • 186
    • 51049085039 scopus 로고    scopus 로고
    • Metabolic syndrome and Alzheimer’s disease: A link to a vascular hypothesis?
    • H.J. Milionis, M. Florentin, S. Giannopoulos: Metabolic syndrome and Alzheimer’s disease: A link to a vascular hypothesis?, CNS Spectrums 13, 606-613 (2008)
    • (2008) CNS Spectrums , vol.13 , pp. 606-613
    • Milionis, H.J.1    Florentin, M.2    Giannopoulos, S.3
  • 188
    • 69249212436 scopus 로고    scopus 로고
    • Linking vascular disorders and Alzheimer’s disease: Potential involvement of BACE1
    • S.L. Cole, R. Vassar: Linking vascular disorders and Alzheimer’s disease: Potential involvement of BACE1, Neurbiol. Aging 30, 1535-1544 (2009)
    • (2009) Neurbiol. Aging , vol.30 , pp. 1535-1544
    • Cole, S.L.1    Vassar, R.2
  • 189
    • 67650069539 scopus 로고    scopus 로고
    • β-amyloid, blood vessels and brain function
    • E.E. Smith, S.M. Greenberg: β-amyloid, blood vessels and brain function, Stroke 40, 2601-2606 (2009)
    • (2009) Stroke , vol.40 , pp. 2601-2606
    • Smith, E.E.1    Greenberg, S.M.2
  • 194
    • 12244268644 scopus 로고    scopus 로고
    • Molecular and cellular mechanisms of neuroprotection by vascular endothelial growth factor
    • F.Y. Sun, X. Guo: Molecular and cellular mechanisms of neuroprotection by vascular endothelial growth factor, J. Neurosci. Res. 79, 180-184 (2005)
    • (2005) J. Neurosci. Res. , vol.79 , pp. 180-184
    • Sun, F.Y.1    Guo, X.2
  • 195
    • 0037699954 scopus 로고    scopus 로고
    • The biology of VEGF and its receptors
    • N. Ferrara, H.P. Gerber, J. LeCouter: The biology of VEGF and its receptors, Nat. Med. 9, 669-676 (2003)
    • (2003) Nat. Med. , vol.9 , pp. 669-676
    • Ferrara, N.1    Gerber, H.P.2    LeCouter, J.3
  • 196
    • 0032512124 scopus 로고    scopus 로고
    • Vascular endothelial growth factor in Alzheimer’s disease and experimental cerebral ischemia
    • R.N. Kalaria, D.L. Cohen, D.R. Premkumar, S. Nag, J.C. LaManna, W.D. Lust: Vascular endothelial growth factor in Alzheimer’s disease and experimental cerebral ischemia, Mol. Brain Res. 62, 101-105 (1998)
    • (1998) Mol. Brain Res. , vol.62 , pp. 101-105
    • Kalaria, R.N.1    Cohen, D.L.2    Premkumar, D.R.3    Nag, S.4    LaManna, J.C.5    Lust, W.D.6
  • 197
    • 0036167595 scopus 로고    scopus 로고
    • Increased intrathecal levels of the angiogenic factors VEGF and TGFbeta in Alzheimer’s disease and vascular dementia
    • E. Tarkowski, R. Issa, M. Sjogren, A. Wallin, K. Blennow, A. Tarkowski: Increased intrathecal levels of the angiogenic factors VEGF and TGFbeta in Alzheimer’s disease and vascular dementia, Neurobiol. Aging 23, 237-243 (2002)
    • (2002) Neurobiol. Aging , vol.23 , pp. 237-243
    • Tarkowski, E.1    Issa, R.2    Sjogren, M.3    Wallin, A.4    Blennow, K.5    Tarkowski, A.6
  • 198
    • 1242338809 scopus 로고    scopus 로고
    • Co-accumulation of vascular endothelial growth factor with β-amyloid in the brain of patients with Alzheimer’s disease
    • S.P. Yang, D.G. Bae, H.J. Kang, B.J. Gwag, Y.S. Gho, C.B. Chae: Co-accumulation of vascular endothelial growth factor with β-amyloid in the brain of patients with Alzheimer’s disease, Neurobiol. Aging 25, 283-290 (2004)
    • (2004) Neurobiol. Aging , vol.25 , pp. 283-290
    • Yang, S.P.1    Bae, D.G.2    Kang, H.J.3    Gwag, B.J.4    Gho, Y.S.5    Chae, C.B.6
  • 199
    • 58149383380 scopus 로고    scopus 로고
    • Microglial VEGF receptor response is an integral chemotactic component in Alzheimer’s disease pathology
    • J.K. Ryu, T. Cho, H.B. Choi, Y.T. Wang, J.G. Mc-Larnon: Microglial VEGF receptor response is an integral chemotactic component in Alzheimer’s disease pathology, J. Neurosci. 29, 3-13 (2009)
    • (2009) J. Neurosci. , vol.29 , pp. 3-13
    • Ryu, J.K.1    Cho, T.2    Choi, H.B.3    Wang, Y.T.4    Mc-Larnon, J.G.5
  • 200
    • 3142673338 scopus 로고    scopus 로고
    • Angiogenic signaling in Alzheimer’s disease
    • A.I. Pogue, W.J. Lukiw: Angiogenic signaling in Alzheimer’s disease, Neuroreport 15, 1507-1510 (2004)
    • (2004) Neuroreport , vol.15 , pp. 1507-1510
    • Pogue, A.I.1    Lukiw, W.J.2
  • 201
  • 202
    • 0037442177 scopus 로고    scopus 로고
    • Alzheimer’s disease and angiogenesis
    • A.H. Vagnucci, W.W. Li: Alzheimer’s disease and angiogenesis, Lancet 361, 605-608 (2003)
    • (2003) Lancet , vol.361 , pp. 605-608
    • Vagnucci, A.H.1    Li, W.W.2
  • 204
    • 0033902012 scopus 로고    scopus 로고
    • Hypoxia-induced vascular endothelial growth factor expression precedes neovascularization after cerebral ischemia
    • H.J. Marti, M. Bernaudin, A. Bellail, H. Schoch, M. Euler, W. Petit: Hypoxia-induced vascular endothelial growth factor expression precedes neovascularization after cerebral ischemia, Am. J. Pathol. 156, 965-976 (2000)
    • (2000) Am. J. Pathol. , vol.156 , pp. 965-976
    • Marti, H.J.1    Bernaudin, M.2    Bellail, A.3    Schoch, H.4    Euler, M.5    Petit, W.6
  • 205
    • 0029082384 scopus 로고
    • Stabilization of vascular endothelial growth factor mRNA by hypoxia and hypoglycemia and coregulation with other ischemia-induced genes
    • I. Stein, M. Neeman, D. Shweiki, A. Itin, E. Keshet: Stabilization of vascular endothelial growth factor mRNA by hypoxia and hypoglycemia and coregulation with other ischemia-induced genes, Mol. Cell Biol. 15, 5363-5368 (1995)
    • (1995) Mol. Cell Biol. , vol.15 , pp. 5363-5368
    • Stein, I.1    Neeman, M.2    Shweiki, D.3    Itin, A.4    Keshet, E.5
  • 208
    • 0032923562 scopus 로고    scopus 로고
    • Thrombin induces surface and intracellular secretion of amyloid precursor protein from human endothelial cells
    • J.R. Ciallella, H. Figueiredo, V. Smith-Swintosky, J.P. McGillis: Thrombin induces surface and intracellular secretion of amyloid precursor protein from human endothelial cells, Thromb. Haemost. 81, 630-637 (1999)
    • (1999) Thromb. Haemost. , vol.81 , pp. 630-637
    • Ciallella, J.R.1    Figueiredo, H.2    Smith-Swintosky, V.3    McGillis, J.P.4
  • 209
    • 68549086855 scopus 로고    scopus 로고
    • Vascular endothelial growth factor (VEGF) affects processing of the amyloid precursor protein and β-amyloidogenesis in brain slice cultures derived from transgenic Tg2576 mouse brain
    • S. Bürger, M. Noack, L.P. Kirazov, E.P. Kirazov, C.L. Naydenov, E. Kouznetsova, Y. Yafai, R. Schliebs: Vascular endothelial growth factor (VEGF) affects processing of the amyloid precursor protein and β-amyloidogenesis in brain slice cultures derived from transgenic Tg2576 mouse brain, Int. J. Dev. Neurosci. 27, 517-523 (2009)
    • (2009) Int. J. Dev. Neurosci. , vol.27 , pp. 517-523
    • Bürger, S.1    Noack, M.2    Kirazov, L.P.3    Kirazov, E.P.4    Naydenov, C.L.5    Kouznetsova, E.6    Yafai, Y.7    Schliebs, R.8
  • 210
    • 79955577637 scopus 로고    scopus 로고
    • Effect of VEGF and its receptor antagonist SU-5416, an inhibitor of angiogenesis, on processing of the β-amyloid precursor protein in primary neuronal cells derived from brain tissue of Tg2576 mice
    • S. Bürger, Y. Yafai, M. Bigl, P. Wiedemann, R. Schliebs: Effect of VEGF and its receptor antagonist SU-5416, an inhibitor of angiogenesis, on processing of the β-amyloid precursor protein in primary neuronal cells derived from brain tissue of Tg2576 mice, Int. J. Dev. Neurosci. 28, 597-604 (2010)
    • (2010) Int. J. Dev. Neurosci. , vol.28 , pp. 597-604
    • Bürger, S.1    Yafai, Y.2    Bigl, M.3    Wiedemann, P.4    Schliebs, R.5
  • 211
    • 33644649803 scopus 로고    scopus 로고
    • Neurovascular coupling in the normal brain and in hypertension, stroke, and Alzheimer disease
    • H. Girouard, C. Iadecola: Neurovascular coupling in the normal brain and in hypertension, stroke, and Alzheimer disease, J. Appl. Physiol. 100, 328-335 (2006)
    • (2006) J. Appl. Physiol. , vol.100 , pp. 328-335
    • Girouard, H.1    Iadecola, C.2
  • 212
    • 33645809129 scopus 로고    scopus 로고
    • Perivascular nerves and the regulation of cerebrovascular tone
    • E. Hamel: Perivascular nerves and the regulation of cerebrovascular tone, J. Appl. Physiol. 100, 1059-1064 (2006)
    • (2006) J. Appl. Physiol. , vol.100 , pp. 1059-1064
    • Hamel, E.1
  • 213
    • 79955735314 scopus 로고    scopus 로고
    • The cerebrovascular role of the cholinergic neural system in Alzheimer’s disease
    • A.H. VanBeek, J.A. Claassen: The cerebrovascular role of the cholinergic neural system in Alzheimer’s disease, Behav. Brain Res. 221, 537-542 (2003)
    • (2003) Behav. Brain Res. , vol.221 , pp. 537-542
    • VanBeek, A.H.1    Claassen, J.A.2
  • 214
    • 0028800951 scopus 로고
    • Cholinergic basal forebrain neurons project to cortical microvessels in the rat: Electron microscopic study with anterogradely transported Phaseolus vulgaris leucoagglutinin and choline acetyltransferase immunocytochemistry
    • E. Vaucher, E. Hamel: Cholinergic basal forebrain neurons project to cortical microvessels in the rat: Electron microscopic study with anterogradely transported Phaseolus vulgaris leucoagglutinin and choline acetyltransferase immunocytochemistry, J. Neurosci. 15, 7427-7441 (1995)
    • (1995) J. Neurosci. , vol.15 , pp. 7427-7441
    • Vaucher, E.1    Hamel, E.2
  • 215
    • 0344441268 scopus 로고    scopus 로고
    • Cholinergic modulation of the cortical microvascular bed
    • E. Hamel: Cholinergic modulation of the cortical microvascular bed, Prog. Brain Res. 145, 171-178 (2004)
    • (2004) Prog. Brain Res. , vol.145 , pp. 171-178
    • Hamel, E.1
  • 216
    • 0033969655 scopus 로고    scopus 로고
    • Muscarinic-but not nicotinic-acetylcholine receptors mediate a nitric oxide-dependent dilation in brain cortical arterioles: A possible role for the M5 receptor subtype
    • A. Elhusseiny, E. Hamel: Muscarinic-but not nicotinic-acetylcholine receptors mediate a nitric oxide-dependent dilation in brain cortical arterioles: A possible role for the M5 receptor subtype, J. Cereb. Blood Flow Metab. 20, 298-305 (2000)
    • (2000) J. Cereb. Blood Flow Metab. , vol.20 , pp. 298-305
    • Elhusseiny, A.1    Hamel, E.2
  • 217
    • 0035047718 scopus 로고    scopus 로고
    • Cerebral microvascular pathology in aging and Alzheimer’s disease
    • E. Farkas, P.G. Luiten: Cerebral microvascular pathology in aging and Alzheimer’s disease, Prog. Neurobiol. 64, 575-611 (2001)
    • (2001) Prog. Neurobiol. , vol.64 , pp. 575-611
    • Farkas, E.1    Luiten, P.G.2
  • 218
    • 5644289368 scopus 로고    scopus 로고
    • Cortical GABA interneurons in neurovascular coupling: Relays for subcortical vasoactive pathways
    • B. Cauli, X.K. Tong, A. Rancillac, N. Serluca, B. Lambolez, J. Rossier, E. Hamel: Cortical GABA interneurons in neurovascular coupling: Relays for subcortical vasoactive pathways, J. Neurosci. 24, 8940-8949 (2004)
    • (2004) J. Neurosci. , vol.24 , pp. 8940-8949
    • Cauli, B.1    Tong, X.K.2    Rancillac, A.3    Serluca, N.4    Lambolez, B.5    Rossier, J.6    Hamel, E.7
  • 219
    • 24744449326 scopus 로고    scopus 로고
    • Cerebrovascular damage as a cause for Alzheimer’s disease
    • C. Humpel, J. Marksteiner: Cerebrovascular damage as a cause for Alzheimer’s disease, Curr. Neurovasc. Res. 2, 341-347 (2005)
    • (2005) Curr. Neurovasc. Res. , vol.2 , pp. 341-347
    • Humpel, C.1    Marksteiner, J.2
  • 220
    • 33646009985 scopus 로고    scopus 로고
    • Cholinergically mediated augmentation of cerebral perfusion in Alzheimer’s disease and related cognitive disorders: The cholinergic-vascular hypothesis
    • J.A. Claassen, R.W. Jansen: Cholinergically mediated augmentation of cerebral perfusion in Alzheimer’s disease and related cognitive disorders: The cholinergic-vascular hypothesis, J. Gerontol. A Biol. Sci. Med. Sci. 61, 267-271 (2006)
    • (2006) J. Gerontol. A Biol. Sci. Med. Sci. , vol.61 , pp. 267-271
    • Claassen, J.A.1    Jansen, R.W.2
  • 221
    • 79955741185 scopus 로고    scopus 로고
    • Role of cholinergic system in β-amyloid related changes of perivascular innervation of cerebral microvessels in transgenic Tg2576 Alzheimer-like mice
    • E. Kouznetsova, R. Schliebs: Role of cholinergic system in β-amyloid related changes of perivascular innervation of cerebral microvessels in transgenic Tg2576 Alzheimer-like mice, J. Neurochem. 101(Suppl. 1), 63 (2007)
    • (2007) J. Neurochem. , vol.101 , pp. 63
    • Kouznetsova, E.1    Schliebs, R.2
  • 222
    • 12244307865 scopus 로고    scopus 로고
    • Nerve growth factor and acetyl-l-carnitine evoked shifts in acetyl-CoA and cholinergic SN56 cell Vulnerability to neurotoxic inputs
    • A. Szutowicz, H. Bielarczyk, S. Gul, P. Zieliński, T. Pawełczyk, M. Tomaszewicz: Nerve growth factor and acetyl-l-carnitine evoked shifts in acetyl-CoA and cholinergic SN56 cell Vulnerability to neurotoxic inputs, J. Neurosci. Res. 79, 185-192 (2005)
    • (2005) J. Neurosci. Res. , vol.79 , pp. 185-192
    • Szutowicz, A.1    Bielarczyk, H.2    Gul, S.3    Zieliński, P.4    Pawełczyk, T.5    Tomaszewicz, M.6
  • 224
    • 12244312497 scopus 로고    scopus 로고
    • Cortical glucose metabolism is altered in aged transgenic Tg2576 mice that demonstrate Alzheimer plaque pathology
    • M. Bigl, J. Apelt, K. Eschrich, R. Schliebs: Cortical glucose metabolism is altered in aged transgenic Tg2576 mice that demonstrate Alzheimer plaque pathology, J. Neural Transm. 110, 77-94 (2003)
    • (2003) J. Neural Transm. , vol.110 , pp. 77-94
    • Bigl, M.1    Apelt, J.2    Eschrich, K.3    Schliebs, R.4
  • 225
    • 77957713248 scopus 로고    scopus 로고
    • Dynamics of protofibril elongation and association involved in Aβ42 peptide aggregation in Alzheimer’s disease
    • P. Ghosh, A. Kumar, B. Datta, V. Rangachari: Dynamics of protofibril elongation and association involved in Aβ42 peptide aggregation in Alzheimer’s disease, BMC Bioinformatics 11(Suppl 6), S24 (2010)
    • (2010) BMC Bioinformatics , vol.11 , pp. S24
    • Ghosh, P.1    Kumar, A.2    Datta, B.3    Rangachari, V.4
  • 227
    • 0032729982 scopus 로고    scopus 로고
    • Computationally derived structural models of the beta-amyloid found in Alzheimer’s disease plaques and the interaction with possible aggregation inhibitors
    • A.R. George, D.R. Howlett: Computationally derived structural models of the beta-amyloid found in Alzheimer’s disease plaques and the interaction with possible aggregation inhibitors, Biopolymers 50, 733-741 (1999)
    • (1999) Biopolymers , vol.50 , pp. 733-741
    • George, A.R.1    Howlett, D.R.2
  • 228
    • 79954465027 scopus 로고    scopus 로고
    • Computational prediction and analysis of the DR6-NAPP interaction
    • S.Y. Ponomarev, J. Audie: Computational prediction and analysis of the DR6-NAPP interaction, Proteins. 79, 1376-1395 (2011)
    • (2011) Proteins. , vol.79 , pp. 1376-1395
    • Ponomarev, S.Y.1    Audie, J.2
  • 229
    • 77649226785 scopus 로고    scopus 로고
    • In silico analysis of the apolipoprotein E and the amyloid beta peptide interaction: Misfolding induced by frustration of the salt bridge network
    • J. Luo, J.D. Maréchal, S. Wärmländer, A. Gräslund, A. Perálvarez-Marín: In silico analysis of the apolipoprotein E and the amyloid beta peptide interaction: Misfolding induced by frustration of the salt bridge network, PLoS Comput. Biol. 6(2), e1000663 (2010)
    • (2010) PLoS Comput. Biol. , vol.6 , Issue.2
    • Luo, J.1    Maréchal, J.D.2    Wärmländer, S.3    Gräslund, A.4    Perálvarez-Marín, A.5
  • 230
    • 67149088375 scopus 로고    scopus 로고
    • Connecting protein interaction data, mutations
    • J.Y. Chen, E. Youn, S.D. Mooney: Connecting protein interaction data, mutations, Methods Mol. Biol. 541, 449-461 (2009)
    • (2009) Methods Mol. Biol. , vol.541 , pp. 449-461
    • Chen, J.Y.1    Youn, E.2    Mooney, S.D.3
  • 231
    • 0033532596 scopus 로고    scopus 로고
    • A model of the complex between cyclin-dependent kinase 5 and the activation domain of neuronal Cdk5 activator
    • K.C. Chou, K.D. Watenpaugh, R.L. Heinrikson: A model of the complex between cyclin-dependent kinase 5 and the activation domain of neuronal Cdk5 activator, Biochem. Biophys. Res. Commun. 259, 420-428 (1999)
    • (1999) Biochem. Biophys. Res. Commun. , vol.259 , pp. 420-428
    • Chou, K.C.1    Watenpaugh, K.D.2    Heinrikson, R.L.3
  • 232
    • 79953312851 scopus 로고    scopus 로고
    • An integrated genetics approach for identifying protein signal pathways of Alzheimer’s disease
    • Y. Huang, X. Sun, G. Hu: An integrated genetics approach for identifying protein signal pathways of Alzheimer’s disease, Comput. Methods Biomech. Biomed. Engin. 14, 371-378 (2011)
    • (2011) Comput. Methods Biomech. Biomed. Engin. , vol.14 , pp. 371-378
    • Huang, Y.1    Sun, X.2    Hu, G.3
  • 233
    • 38449089399 scopus 로고    scopus 로고
    • Chalkboard: Ontology-based pathway modeling and qualitative inference of disease mechanisms
    • D.L. Cook, J.C. Wiley, J.H. Gennari: Chalkboard: Ontology-based pathway modeling and qualitative inference of disease mechanisms, Pac. Symp. Biocomput. 2007, 16-27 (2007)
    • (2007) Pac. Symp. Biocomput. , vol.2007 , pp. 16-27
    • Cook, D.L.1    Wiley, J.C.2    Gennari, J.H.3
  • 234
    • 80051566363 scopus 로고    scopus 로고
    • First computational chemistry multi-target model for anti-Alzheimer, anti-parasitic, anti-fungi, and anti-bacterial activity of GSK-3 inhibitors in vitro, in vivo, and in different cellular lines
    • I. García, Y. Fall, G. Gómez, H. González-Díaz: First computational chemistry multi-target model for anti-Alzheimer, anti-parasitic, anti-fungi, and anti-bacterial activity of GSK-3 inhibitors in vitro, in vivo, and in different cellular lines, Mol. Divers. 15, 561-567 (2011)
    • (2011) Mol. Divers. , vol.15 , pp. 561-567
    • García, I.1    Fall, Y.2    Gómez, G.3    González-Díaz, H.4
  • 235
    • 22444440903 scopus 로고    scopus 로고
    • Computational studies of Cu(II)/Met and Cu(I)/Met binding motifs relevant for the chemistry of Alzheimer’s disease
    • R. Gómez-Balderas, D.F. Raffa, G.A. Rickard, P. Brunelle, A. Rauk: Computational studies of Cu(II)/Met and Cu(I)/Met binding motifs relevant for the chemistry of Alzheimer’s disease, J. Phys. Chem. A 109, 5498-5508 (2005)
    • (2005) J. Phys. Chem. A , vol.109 , pp. 5498-5508
    • Gómez-Balderas, R.1    Raffa, D.F.2    Rickard, G.A.3    Brunelle, P.4    Rauk, A.5
  • 236
    • 65249160667 scopus 로고    scopus 로고
    • Computational insights into aspartyl protease activity of presenilin 1 (PS1) generating Alzheimer amyloid β-peptides (Aβ40 and Aβ42)
    • R. Singh, A. Barman, R. Prabhakar: Computational insights into aspartyl protease activity of presenilin 1 (PS1) generating Alzheimer amyloid β-peptides (Aβ40 and Aβ42), J. Phys. Chem. B. 113, 2990-2999 (2009)
    • (2009) J. Phys. Chem. B. , vol.113 , pp. 2990-2999
    • Singh, R.1    Barman, A.2    Prabhakar, R.3
  • 237
    • 79960345867 scopus 로고    scopus 로고
    • Genetics: Finding risk factors
    • M. Eisenstein: Genetics: Finding risk factors, Nature 475, S20-S22 (2011)
    • (2011) Nature , vol.475 , pp. S20-S22
    • Eisenstein, M.1
  • 238
    • 0037310257 scopus 로고    scopus 로고
    • Power of multifactor dimensionality reduction for detecting gene-gene interactions in the presence of genotyping error, missing data, phenocopy, and genetic heterogeneity
    • M.D. Ritchie, L.W. Hahn, J.H. Moore: Power of multifactor dimensionality reduction for detecting gene-gene interactions in the presence of genotyping error, missing data, phenocopy, and genetic heterogeneity, Genet. Epidemiol. 24, 150-157 (2003)
    • (2003) Genet. Epidemiol. , vol.24 , pp. 150-157
    • Ritchie, M.D.1    Hahn, L.W.2    Moore, J.H.3
  • 239
    • 35748972938 scopus 로고    scopus 로고
    • Loglinear model-based multifactor dimensionality reduction method to detect gene gene interactions
    • S.Y. Lee, Y. Chung, R.C. Elston, Y. Kim, T. Park: Loglinear model-based multifactor dimensionality reduction method to detect gene gene interactions, Bioinformatics. 23, 2589-2595 (2007)
    • (2007) Bioinformatics. , vol.23 , pp. 2589-2595
    • Lee, S.Y.1    Chung, Y.2    Elston, R.C.3    Kim, Y.4    Park, T.5
  • 241
    • 33748787676 scopus 로고    scopus 로고
    • Exploring candidate genes for human brain diseases from a brain-specific gene network
    • B. Liu, T. Jiang, S. Ma, H. Zhao, J. Li, X. Jiang, J. Zhang: Exploring candidate genes for human brain diseases from a brain-specific gene network, Biochem. Biophys. Res. Commun. 349, 1308-1314 (2006)
    • (2006) Biochem. Biophys. Res. Commun. , vol.349 , pp. 1308-1314
    • Liu, B.1    Jiang, T.2    Ma, S.3    Zhao, H.4    Li, J.5    Jiang, X.6    Zhang, J.7
  • 242
    • 33748069154 scopus 로고    scopus 로고
    • Toxicity mediated by soluble oligomers of β-amyloid (1-42) on cholinergic SN56.B5.G4 cells
    • K. Heinitz, M. Beck, R. Schliebs, J.R. Perez-Polo: Toxicity mediated by soluble oligomers of β-amyloid (1-42) on cholinergic SN56.B5.G4 cells, J. Neurochem. 98, 1930-1945 (2006)
    • (2006) J. Neurochem. , vol.98 , pp. 1930-1945
    • Heinitz, K.1    Beck, M.2    Schliebs, R.3    Perez-Polo, J.R.4
  • 243
    • 41649106212 scopus 로고    scopus 로고
    • Oligomeric β-amyloid (1-42) induces the expression of Alzheimer disease-relevant proteins in cholinergic SN56.B5.G4 cells as revealed by proteomic analysis
    • S. Joerchel, M. Raap, M. Bigl, K. Eschrich, R. Schliebs: Oligomeric β-amyloid (1-42) induces the expression of Alzheimer disease-relevant proteins in cholinergic SN56.B5.G4 cells as revealed by proteomic analysis, Int. J. Dev. Neurosci. 26, 301-308 (2006)
    • (2006) Int. J. Dev. Neurosci. , vol.26 , pp. 301-308
    • Joerchel, S.1    Raap, M.2    Bigl, M.3    Eschrich, K.4    Schliebs, R.5
  • 244
    • 68249111344 scopus 로고    scopus 로고
    • Building disease-specific drug-protein connectivity maps from molecular interaction networks and PubMed abstracts
    • J. Li, X. Zhu, J.Y. Chen: Building disease-specific drug-protein connectivity maps from molecular interaction networks and PubMed abstracts, PLoS Comput. Biol. 5(7), e1000450 (2009)
    • (2009) PLoS Comput. Biol. , vol.5 , Issue.7
    • Li, J.1    Zhu, X.2    Chen, J.Y.3
  • 245
    • 68949098594 scopus 로고    scopus 로고
    • Neuronal networks in Alzheimer’s disease
    • Y. He, Z. Chen, G. Gong, A. Evans: Neuronal networks in Alzheimer’s disease, Neuroscientist 15, 333-350 (2009)
    • (2009) Neuroscientist , vol.15 , pp. 333-350
    • He, Y.1    Chen, Z.2    Gong, G.3    Evans, A.4
  • 246
    • 0032482432 scopus 로고    scopus 로고
    • Collective dynamics of ‘small-world’ networks
    • D.J. Watts, S.H. Strogatz: Collective dynamics of ‘small-world’ networks, Nature 393, 440-442 (1998)
    • (1998) Nature , vol.393 , pp. 440-442
    • Watts, D.J.1    Strogatz, S.H.2
  • 247
    • 33845742477 scopus 로고    scopus 로고
    • Small-world networks and functional connectivity in Alzheimer’s disease
    • C.J. Stam, B.F. Jones, G. Nolte, M. Breakspear, P. Scheltens: Small-world networks and functional connectivity in Alzheimer’s disease, Cereb. Cortex 17, 92-99 (2007)
    • (2007) Cereb. Cortex , vol.17 , pp. 92-99
    • Stam, C.J.1    Jones, B.F.2    Nolte, G.3    Breakspear, M.4    Scheltens, P.5
  • 248
    • 33644857555 scopus 로고    scopus 로고
    • Neural networks for longitudinal studies in Alzheimer’s disease
    • R. Tandon, S. Adak, J.A. Kaye: Neural networks for longitudinal studies in Alzheimer’s disease, Artif. Intell. Med. 36, 245-255 (2006)
    • (2006) Artif. Intell. Med. , vol.36 , pp. 245-255
    • Tandon, R.1    Adak, S.2    Kaye, J.A.3
  • 249
    • 0031134367 scopus 로고    scopus 로고
    • A computational model of the progression of Alzheimer’s disease
    • M.E. Hasselmo: A computational model of the progression of Alzheimer’s disease, M.D. Computing 14, 181-191 (1997)
    • (1997) M.D. Computing , vol.14 , pp. 181-191
    • Hasselmo, M.E.1
  • 250
    • 0028958196 scopus 로고
    • Neuromodulation and cortical function: Modeling the physiological basis of behavior
    • M.E. Hasselmo: Neuromodulation and cortical function: Modeling the physiological basis of behavior, Behav. Brain Res. 67, 1-27 (1995)
    • (1995) Behav. Brain Res. , vol.67 , pp. 1-27
    • Hasselmo, M.E.1
  • 251
    • 0030586660 scopus 로고    scopus 로고
    • Neuronal-based synaptic compensation: A computational study in Alzheimer’s disease
    • D. Horn, N. Levy, E. Ruppin: Neuronal-based synaptic compensation: A computational study in Alzheimer’s disease, Neural Comput. 8, 1227-1243 (1996)
    • (1996) Neural Comput. , vol.8 , pp. 1227-1243
    • Horn, D.1    Levy, N.2    Ruppin, E.3
  • 253
    • 39049196051 scopus 로고    scopus 로고
    • Computational representation of Alzheimer’s disease evolution applied to a cooking activity
    • A. Serna, V. Rialle, H. Pigot: Computational representation of Alzheimer’s disease evolution applied to a cooking activity, Stud. Health Technol. Inform. 124, 587-592 (2006)
    • (2006) Stud. Health Technol. Inform. , vol.124 , pp. 587-592
    • Serna, A.1    Rialle, V.2    Pigot, H.3
  • 254
    • 34047139812 scopus 로고    scopus 로고
    • Path planning in the hippocampo-prefrontal cortex pathway: An adaptive model based receding horizon planner
    • M.A. Ahmadi-Pajouh, F. Towhidkhah, S. Gharibzadeh, M. Mashhadimalek: Path planning in the hippocampo-prefrontal cortex pathway: An adaptive model based receding horizon planner, Med. Hypotheses 68, 1411-1415 (2007)
    • (2007) Med. Hypotheses , vol.68 , pp. 1411-1415
    • Ahmadi-Pajouh, M.A.1    Towhidkhah, F.2    Gharibzadeh, S.3    Mashhadimalek, M.4
  • 255
    • 0028834147 scopus 로고
    • A neural model of memory impairment in diffuse cerebral atrophy
    • E. Ruppin, J.A. Reggia: A neural model of memory impairment in diffuse cerebral atrophy, Br. J. Psychiatry. 166, 19-28 (1995)
    • (1995) Br. J. Psychiatry. , vol.166 , pp. 19-28
    • Ruppin, E.1    Reggia, J.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.