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Volumn 14, Issue 6, 1999, Pages 437-446

The biochemistry of Alzheimer's disease

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID; AMYLOID PRECURSOR PROTEIN; APOLIPOPROTEIN E; MUTANT PROTEIN; PRESENILIN 1; PRESENILIN 2; TAU PROTEIN;

EID: 0032972031     PISSN: 1170229X     EISSN: None     Source Type: Journal    
DOI: 10.2165/00002512-199914060-00004     Document Type: Review
Times cited : (10)

References (106)
  • 1
    • 0030774535 scopus 로고    scopus 로고
    • The genetics of Alzheimer's disease
    • 1. Rubinstein DC. The genetics of Alzheimer's disease. Prog Neuobiol 1997; 52: 447-54
    • (1997) Prog Neuobiol , vol.52 , pp. 447-454
    • Rubinstein, D.C.1
  • 2
    • 0028267440 scopus 로고
    • Normal and abnormal biology of the β-amyloid precursor protein
    • 2. Selkoe DJ. Normal and abnormal biology of the β-amyloid precursor protein. Annu Rev Neurosci 1994; 17: 489-517
    • (1994) Annu Rev Neurosci , vol.17 , pp. 489-517
    • Selkoe, D.J.1
  • 3
    • 0028286131 scopus 로고
    • Alzheimer's disease. Clinical molecular genetics
    • 3. Hardy J. Alzheimer's disease. Clinical molecular genetics. Clin Geriatr Med 1994; 10:239-47
    • (1994) Clin Geriatr Med , vol.10 , pp. 239-247
    • Hardy, J.1
  • 4
    • 0022614193 scopus 로고
    • Down's syndrome and Alzheimer's disease: A review
    • 4. Oliver C, Holland AJ. Down's syndrome and Alzheimer's disease: a review. Psychol Med 1986; 16: 307-22
    • (1986) Psychol Med , vol.16 , pp. 307-322
    • Oliver, C.1    Holland, A.J.2
  • 5
    • 0025773225 scopus 로고
    • Neuritic pathology and dementia in Alzheimer's disease
    • 5. McKee AC, Kosik KS, Kowall NW. Neuritic pathology and dementia in Alzheimer's disease. Ann Neurol 1991; 30: 156-65
    • (1991) Ann Neurol , vol.30 , pp. 156-165
    • McKee, A.C.1    Kosik, K.S.2    Kowall, N.W.3
  • 6
    • 0019935804 scopus 로고
    • Plaques, tangles and dementia
    • 6. Wilcock GK, Esiri MM. Plaques, tangles and dementia. J Neurol Sci 1982; 56: 343-56
    • (1982) J Neurol Sci , vol.56 , pp. 343-356
    • Wilcock, G.K.1    Esiri, M.M.2
  • 7
    • 0031596261 scopus 로고    scopus 로고
    • The neuropathological diagnosis of Alzheimer disease
    • 7. Jellinger KA. The neuropathological diagnosis of Alzheimer disease. J Neural Transm Suppl 1998; 53: 97-118
    • (1998) J Neural Transm Suppl , vol.53 , pp. 97-118
    • Jellinger, K.A.1
  • 8
    • 0028972701 scopus 로고
    • Image analysis of β-amyloid load in Alzheimer's disease and relation to dementia severity
    • 8. Cummings BJ, Cotman CW. Image analysis of β-amyloid load in Alzheimer's disease and relation to dementia severity. Lancet 1995; 346: 1524-8
    • (1995) Lancet , vol.346 , pp. 1524-1528
    • Cummings, B.J.1    Cotman, C.W.2
  • 9
    • 6844258835 scopus 로고    scopus 로고
    • Frameshift mutations of β amyloid precursor protein and ubiquitin-B in Alzheimer's and down patients
    • 9. Van Leeuwen FW, De Kleijn DPV, Van den Hurk HH, et al. Frameshift mutations of β amyloid precursor protein and ubiquitin-B in Alzheimer's and Down patients. Science 1998; 279: 242-7
    • (1998) Science , vol.279 , pp. 242-247
    • Van Leeuwen, F.W.1    De Kleijn, D.P.V.2    Van Den Hurk, H.H.3
  • 10
    • 0028985574 scopus 로고
    • Alzheimer-type neuropathology in transgenic mice overexpressing 717VxF β-amyloid precursor protein
    • 10. Games D, Adams D, Alessandrini R, et al. Alzheimer-type neuropathology in transgenic mice overexpressing 717VxF β-amyloid precursor protein: Nature 1995; 373: 523-7
    • (1995) Nature , vol.373 , pp. 523-527
    • Games, D.1    Adams, D.2    Alessandrini, R.3
  • 11
    • 0032006678 scopus 로고    scopus 로고
    • The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways
    • 11. Kelly JW, The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. Curr Opin Struct Biol 1998; 8: 101-6
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 101-106
    • Kelly, J.W.1
  • 12
    • 0026713423 scopus 로고
    • β-amyloid neurotoxicity: A discussion of in vitro findings
    • 12. Cotman CW, Pike CJ, Copani A. β-amyloid neurotoxicity: a discussion of in vitro findings. Neurobiol Aging 1992; 13: 587-90
    • (1992) Neurobiol Aging , vol.13 , pp. 587-590
    • Cotman, C.W.1    Pike, C.J.2
  • 13
    • 0027447286 scopus 로고
    • Neurodegeneration induced by β-amyloid peptides in vitro: The role of peptide assembly state
    • 13. Pike CJ, Burdick D, Walencewicz AJ, et al. Neurodegeneration induced by β-amyloid peptides in vitro: the role of peptide assembly state. J Neurosci 1993; 13: 1676-87
    • (1993) J Neurosci , vol.13 , pp. 1676-1687
    • Pike, C.J.1    Burdick, D.2    Walencewicz, A.J.3
  • 14
    • 0029964207 scopus 로고    scopus 로고
    • Amyloid fibril toxicity in Alzheimer's disease and diabetes
    • 14. Yankner BA, Lorenzo A. Amyloid fibril toxicity in Alzheimer's disease and diabetes. Ann N Y Acad Sci 1996; 777: 89-95
    • (1996) Ann N Y Acad Sci , vol.777 , pp. 89-95
    • Yankner, B.A.1    Lorenzo, A.2
  • 15
    • 0027970307 scopus 로고
    • Acceleration of Alzheimer's fibril formation by apolipoprotein E in vitro
    • 15. Wisniewski T, Castano EM, Golabek A, et al. Acceleration of Alzheimer's fibril formation by Apolipoprotein E in vitro. Am J Pathol 1994; 145: 1030-5
    • (1994) Am J Pathol , vol.145 , pp. 1030-1035
    • Wisniewski, T.1    Castano, E.M.2    Golabek, A.3
  • 16
    • 0029863697 scopus 로고    scopus 로고
    • Acetylcholinesterase accelerates assembly of amyloid-β-peptides into Alzheimer's fibrils: Possible role of the peripheral site of the enzyme
    • 16. Inestrosa NC, Alvarez A, Perez CA, et al. Acetylcholinesterase accelerates assembly of amyloid-β-peptides into Alzheimer's fibrils: possible role of the peripheral site of the enzyme. Neuron 1996; 16: 881-91
    • (1996) Neuron , vol.16 , pp. 881-891
    • Inestrosa, N.C.1    Alvarez, A.2    Perez, C.A.3
  • 17
    • 0028986858 scopus 로고
    • Alpha l-antichymotrypsin regulates Alzheimer β-amyloid peptide fibril formation
    • 17. Eriksson S, Janciauskiene S, Lannfelt T. Alpha l-antichymotrypsin regulates Alzheimer β-amyloid peptide fibril formation. Proc Natl Acad Sci USA 1995; 92: 2313-7
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 2313-2317
    • Eriksson, S.1    Janciauskiene, S.2    Lannfelt, T.3
  • 18
    • 0028965513 scopus 로고
    • The NACP/synuclein gene: Chromosomal assignment and screening for alterations in Alzheimer disease
    • 18. Campion D, Martin C, Heilig R. et al. The NACP/synuclein gene: chromosomal assignment and screening for alterations in Alzheimer disease. Genomics 1995; 26: 254-7
    • (1995) Genomics , vol.26 , pp. 254-257
    • Campion, D.1    Martin, C.2    Heilig, R.3
  • 19
    • 0030025635 scopus 로고    scopus 로고
    • Altered presynaptic protein NACP is associated with plaque formation and neurodegeneration in Alzheimer's disease
    • 19. Masliah E, Iwai A, Mallory M, et al. Altered presynaptic protein NACP is associated with plaque formation and neurodegeneration in Alzheimer's disease. Am J Pathol 1996; 148: 201-10
    • (1996) Am J Pathol , vol.148 , pp. 201-210
    • Masliah, E.1    Iwai, A.2    Mallory, M.3
  • 20
    • 0029820770 scopus 로고    scopus 로고
    • Characterization of the precursor of the non-Aβ component of senile plaques (NACP) in the human central nervous system
    • 20. Irizarry MC, Tim TW, McNamara M, et al. Characterization of the precursor of the non-Aβ component of senile plaques (NACP) in the human central nervous system. J Neuropathol Exp Neurol 1996; 55: 889-95
    • (1996) J Neuropathol Exp Neurol , vol.55 , pp. 889-895
    • Irizarry, M.C.1    Tim, T.W.2    McNamara, M.3
  • 21
    • 0028985267 scopus 로고
    • The precursor protein of non-Aβ component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system
    • 21. Iwai A, Masliah E, Yoshimato M, et al. The precursor protein of non-Aβ component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system. Neuron 1995; 14:467-75
    • (1995) Neuron , vol.14 , pp. 467-475
    • Iwai, A.1    Masliah, E.2    Yoshimato, M.3
  • 22
    • 0029938770 scopus 로고    scopus 로고
    • The synaptic protein NACP is abnormally expressed during the progression of Alzheimer's disease
    • 22. Iwai A, Masliah E, Sundsmo MP, et al. The synaptic protein NACP is abnormally expressed during the progression of Alzheimer's disease. Brain Res 1996; 720: 230-4
    • (1996) Brain Res , vol.720 , pp. 230-234
    • Iwai, A.1    Masliah, E.2    Sundsmo, M.P.3
  • 23
    • 0029904487 scopus 로고    scopus 로고
    • NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded
    • 23. Weinreb PH, Zhen W, Poon AW, et al. NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded. Biochemistry 1996; 35: 13709-15
    • (1996) Biochemistry , vol.35 , pp. 13709-13715
    • Weinreb, P.H.1    Zhen, W.2    Poon, A.W.3
  • 24
    • 0031588598 scopus 로고    scopus 로고
    • Evidence that the precursor protein of non Aβ component of Alzheimer's disease amyloid (NACP) has an extended structure primarily composed of random-coil
    • 24. Kim J. Evidence that the precursor protein of non Aβ component of Alzheimer's disease amyloid (NACP) has an extended structure primarily composed of random-coil. Mol Cells 1997; 7: 78-83
    • (1997) Mol Cells , vol.7 , pp. 78-83
    • Kim, J.1
  • 25
    • 0029056115 scopus 로고
    • NACP, the precursor protein of the non-amyloid β/A4 protein (A beta) component of Alzheimer disease amyloid, binds A beta and stimulates a beta aggregation
    • 25. Yoshimoto M, Iwai A, Kang D, et al. NACP, the precursor protein of the non-amyloid β/A4 protein (A beta) component of Alzheimer disease amyloid, binds A beta and stimulates A beta aggregation. Proc Natl Acad Sci USA 1995; 92: 9141-5
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 9141-9145
    • Yoshimoto, M.1    Iwai, A.2    Kang, D.3
  • 26
    • 0028984925 scopus 로고
    • Non-a beta component of Alzheimer's disease amyloid (NAC) is amyloidogenic
    • 26. Iwai A, Yoshimoto M, Masliah E, et al. Non-A beta component of Alzheimer's disease amyloid (NAC) is amyloidogenic. Biochemistry 1995; 34: 10139-45
    • (1995) Biochemistry , vol.34 , pp. 10139-10145
    • Iwai, A.1    Yoshimoto, M.2    Masliah, E.3
  • 27
    • 0030741131 scopus 로고    scopus 로고
    • Presenilins and early-onset familial Alzheimer's disease
    • 27. Rohan de Silva HAR, Patel AJ. Presenilins and early-onset familial Alzheimer's disease. Neuroreport 1997; 8: 1-12
    • (1997) Neuroreport , vol.8 , pp. 1-12
    • Rohan De Silva, H.A.R.1    Patel, A.J.2
  • 28
    • 0030922146 scopus 로고    scopus 로고
    • Evidence for a six-transmembrane domain structure of presenilin 1
    • 28. Lehmann S, Chiesa R, Harris DA. Evidence for a six-transmembrane domain structure of presenilin 1. J Biol Chem 1997; 272: 12047-51
    • (1997) J Biol Chem , vol.272 , pp. 12047-12051
    • Lehmann, S.1    Chiesa, R.2    Harris, D.A.3
  • 29
    • 0031442678 scopus 로고    scopus 로고
    • The seven-transmembrane spanning topography of the Alzheimer disease-related presenilin proteins in the plasma membranes of cultured cells
    • 29. Dewji NN, Singer SJ. The seven-transmembrane spanning topography of the Alzheimer disease-related presenilin proteins in the plasma membranes of cultured cells. Proc Natl Acad Sci USA 1997; 94: 14025-30
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 14025-14030
    • Dewji, N.N.1    Singer, S.J.2
  • 30
    • 0031473796 scopus 로고    scopus 로고
    • On the spurious endoproteolytic processing of the presenilin proteins in cultured cells and tissue
    • 30. Dewji NN, Do C, Singer SJ. On the spurious endoproteolytic processing of the presenilin proteins in cultured cells and tissue. Proc Natl Acad Sci USA 1997; 94: 14031-6
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 14031-14036
    • Dewji, N.N.1    Do, C.2    Singer, S.J.3
  • 31
    • 0030992087 scopus 로고    scopus 로고
    • Processing of presenilin 1 in brains of patients with Alzheimer's disease and controls
    • 31. Hendriks L, Thinakuran G, Harris CL, et al. Processing of presenilin 1 in brains of patients with Alzheimer's disease and controls. Neuroreport 1997; 8: 1717-21
    • (1997) Neuroreport , vol.8 , pp. 1717-1721
    • Hendriks, L.1    Thinakuran, G.2    Harris, C.L.3
  • 32
    • 13344282063 scopus 로고
    • Alzheimer-associated presenilins 1 and 2: Neuronal expression in brain and localization to intracellular membranes in mammalian cells
    • 32. Kovacs DM, Fausett HJ, Page KJ, et al. Alzheimer-associated presenilins 1 and 2: neuronal expression in brain and localization to intracellular membranes in mammalian cells. Nat Med 1496; 2: 224-9
    • (1496) Nat Med , vol.2 , pp. 224-229
    • Kovacs, D.M.1    Fausett, H.J.2    Page, K.J.3
  • 33
    • 0030753089 scopus 로고    scopus 로고
    • Interaction between amyloid precursor protein and presenilins in mammalian cells, implications for the pathogenesis of Alzheimer disease
    • 33. Xia W, Zhang J, Perez R, et al. Interaction between amyloid precursor protein and presenilins in mammalian cells, implications for the pathogenesis of Alzheimer disease. Proc Natl Acad Sci USA 1997; 94: 8208-13
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 8208-8213
    • Xia, W.1    Zhang, J.2    Perez, R.3
  • 34
    • 0030761059 scopus 로고    scopus 로고
    • Alzheimer presenilins in the nuclear membrane, interphase kinetochores, and centrosomes suggest a role in chromosome segregation
    • 34. Li J, Xu M, Zhou Z, et al. Alzheimer presenilins in the nuclear membrane, interphase kinetochores, and centrosomes suggest a role in chromosome segregation. Cell 1997; 90: 917-27
    • (1997) Cell , vol.90 , pp. 917-927
    • Li, J.1    Xu, M.2    Zhou, Z.3
  • 35
    • 0030922421 scopus 로고    scopus 로고
    • Presenilins: Genes for life and death
    • 35. Haass C, Presenilins: genes for life and death. Neuron 1997; 18: 687-90
    • (1997) Neuron , vol.18 , pp. 687-690
    • Haass, C.1
  • 36
    • 16944362157 scopus 로고    scopus 로고
    • Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid beta-protein in both transfected cells and transgenic mice
    • 36. Citron M, Westaway D, Xia W, et al. Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid beta-protein in both transfected cells and transgenic mice. Nat Med 1997; 3: 67-72
    • (1997) Nat Med , vol.3 , pp. 67-72
    • Citron, M.1    Westaway, D.2    Xia, W.3
  • 37
    • 0031031120 scopus 로고    scopus 로고
    • Presenilins, amyloid-β and Alzheimer's disease
    • 37. Lamb BT. Presenilins, amyloid-β and Alzheimer's disease. Nat Med 1997; 3: 28-9
    • (1997) Nat Med , vol.3 , pp. 28-29
    • Lamb, B.T.1
  • 38
    • 10544224542 scopus 로고    scopus 로고
    • Participation of presenilin 2 in apoptosis: Enhanced basal activity conferred by an Alzheimer mutation
    • 38. Wolozin B, Iwasaki K, Vito P, et al. Participation of Presenilin 2 in apoptosis: enhanced basal activity conferred by an Alzheimer mutation. Science 1996; 274: 1710-13
    • (1996) Science , vol.274 , pp. 1710-1713
    • Wolozin, B.1    Iwasaki, K.2    Vito, P.3
  • 39
    • 0030868903 scopus 로고    scopus 로고
    • Alternative cleavage of Alzheimer-associated presenilins during apoplosis by a caspase-3 family protease
    • 39. Kim T-W, Pettingell WH, Jung Y-K, et al. Alternative cleavage of Alzheimer-associated presenilins during apoplosis by a caspase-3 family protease. Science 1997; 277: 373-6
    • (1997) Science , vol.277 , pp. 373-376
    • Kim, T.-W.1    Pettingell, W.H.2    Jung, Y.-K.3
  • 40
    • 0029975481 scopus 로고    scopus 로고
    • Age, neurofibrillary changes, a beta-amyloid and the onset of Alzheimer's disease
    • 40. Braak H, Braak F, Bohl J, et al. Age, neurofibrillary changes, A beta-amyloid and the onset of Alzheimer's disease. Neurosci Lett 1996; 210; 87-90
    • (1996) Neurosci Lett , vol.210 , pp. 87-90
    • Braak, H.1    Braak, F.2    Bohl, J.3
  • 41
    • 0029940510 scopus 로고    scopus 로고
    • Pattern of brain destruction in Parkinson's and Alzheimer's diseases
    • 41. Braak H, Braak E, Yilmazer D, et al. Pattern of brain destruction in Parkinson's and Alzheimer's diseases. J Neural Transm 1996; 103: 455-90
    • (1996) J Neural Transm , vol.103 , pp. 455-490
    • Braak, H.1    Braak, E.2    Yilmazer, D.3
  • 42
    • 0030937952 scopus 로고    scopus 로고
    • The phosphorylation of tau: A critical singe in neurodevelopment and neurodegenerative processes
    • 42. Lovestone S, Reynolds CH. The phosphorylation of tau: a critical singe in neurodevelopment and neurodegenerative processes. Neuroscience 1997; 78: 309-24
    • (1997) Neuroscience , vol.78 , pp. 309-324
    • Lovestone, S.1    Reynolds, C.H.2
  • 43
    • 0031007546 scopus 로고    scopus 로고
    • Regulated phosphorylation and dephosphorylation of tau prolein: Effects on microtubule interaction, intracellular trafficking and neurodegeneration
    • 43. Billingsley ML, Kincaid RL. Regulated phosphorylation and dephosphorylation of tau prolein: effects on microtubule interaction, intracellular trafficking and neurodegeneration. Biochem J 1997; 323: 577-91
    • (1997) Biochem J , vol.323 , pp. 577-591
    • Billingsley, M.L.1    Kincaid, R.L.2
  • 44
    • 0030840778 scopus 로고    scopus 로고
    • Two-dimensional characterization of paired helical filament-tau from Alzheimer's disease: Demonstration of an additional 74-kDa component and age-related biochemical modifications
    • 44. Sergeant N, David JP, Goedert M, et al. Two-dimensional characterization of paired helical filament-tau from Alzheimer's disease: demonstration of an additional 74-kDa component and age-related biochemical modifications. J Neurochem 1997; 69: 834-44
    • (1997) J Neurochem , vol.69 , pp. 834-844
    • Sergeant, N.1    David, J.P.2    Goedert, M.3
  • 45
    • 0032543684 scopus 로고    scopus 로고
    • Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17
    • 45. Hutton M, Lendon CL, Rizzu P, et al. Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17. Nature 1998; 393: 702-5
    • (1998) Nature , vol.393 , pp. 702-705
    • Hutton, M.1    Lendon, C.L.2    Rizzu, P.3
  • 46
    • 0030005627 scopus 로고    scopus 로고
    • Apolipoprotein E alleles as risk factors in Alzheimer's disease
    • 46. Roses AD. Apolipoprotein E alleles as risk factors in Alzheimer's disease. Annu Rev Med 1996; 47: 387-400
    • (1996) Annu Rev Med , vol.47 , pp. 387-400
    • Roses, A.D.1
  • 47
    • 0030933095 scopus 로고    scopus 로고
    • Apolipoprotein E and Alzheimer's disease: A review of recent studies
    • 47. Higgins GA, Large CM, Rupniak HT, et al. Apolipoprotein E and Alzheimer's disease: a review of recent studies. Pharmacol Biochem Behav 1997; 56: 675-85
    • (1997) Pharmacol Biochem Behav , vol.56 , pp. 675-685
    • Higgins, G.A.1    Large, C.M.2    Rupniak, H.T.3
  • 48
    • 17744410836 scopus 로고    scopus 로고
    • ApoE-4 and age at onset of Alzheimer's disease: The NIMH genetics initiative
    • 48. Blacker D, Haines JL, Rodes L, et al. ApoE-4 and age at onset of Alzheimer's disease: the NIMH genetics initiative. Neurology 1997; 48: 139-47
    • (1997) Neurology , vol.48 , pp. 139-147
    • Blacker, D.1    Haines, J.L.2    Rodes, L.3
  • 49
    • 0027933984 scopus 로고
    • Apo E allele frequencies in Alzheimer's disease, Lewy body dementia, Alzheimer's disease with cercbrovascular disease and vascular dementia
    • 49. Betard C, Robitaille Y, Gee M, et al. Apo E allele frequencies in Alzheimer's disease, Lewy body dementia, Alzheimer's disease with cercbrovascular disease and vascular dementia. Neuroreport 1994; 5: 1893-6
    • (1994) Neuroreport , vol.5 , pp. 1893-1896
    • Betard, C.1    Robitaille, Y.2    Gee, M.3
  • 50
    • 0028146969 scopus 로고
    • Lipoproteins, neurobiology, and Alzheimer's disease: Structure and function of apolipoprotein E
    • 50. Weisgraber KH, Pitas RE, Mahley RW. Lipoproteins, neurobiology, and Alzheimer's disease: structure and function of apolipoprotein E. Curr Opin Struct Biol 1994; 4: 507-15
    • (1994) Curr Opin Struct Biol , vol.4 , pp. 507-515
    • Weisgraber, K.H.1    Pitas, R.E.2    Mahley, R.W.3
  • 51
    • 0027994092 scopus 로고
    • Apolipoprotein e is localized to the cytoplasm of human cortical neurons: A light and electron microscopic study
    • 51. Han S-H, Einstein G, Weisgraber KH, et al. Apolipoprotein E is localized to the cytoplasm of human cortical neurons: a light and electron microscopic study. J Neuropathol Exp Neurol 1994; 53:535-44
    • (1994) J Neuropathol Exp Neurol , vol.53 , pp. 535-544
    • Han, S.-H.1    Einstein, G.2    Weisgraber, K.H.3
  • 52
    • 0029119868 scopus 로고
    • Apolipoprotein E increases the fibrillogenic potential of synthetic peptides derived from Alzheimer's, gelsolin and AA amyloids
    • 52. Soto C, Castano EM, Prelli F, et al. Apolipoprotein E increases the fibrillogenic potential of synthetic peptides derived from Alzheimer's, gelsolin and AA amyloids. FEBS Lett 1995; 371: 110-14
    • (1995) FEBS Lett , vol.371 , pp. 110-114
    • Soto, C.1    Castano, E.M.2    Prelli, F.3
  • 53
    • 0030610645 scopus 로고    scopus 로고
    • Microglial activation by Alzheimer amyloid precursor protein and modulation by apolipoprotein e
    • 53. Barger SW, Harmon AD. Microglial activation by Alzheimer amyloid precursor protein and modulation by apolipoprotein E. Nature 1997, 388: 878-81
    • (1997) Nature , vol.388 , pp. 878-881
    • Barger, S.W.1    Harmon, A.D.2
  • 54
    • 0030977663 scopus 로고    scopus 로고
    • Concentration-dependent inhibitory effects of apolipoprotein E on Alzheimer's beta-amyloid fibril formation in vitro
    • 54. Naiki H, Gejyo F, Nakakuki K. Concentration-dependent inhibitory effects of apolipoprotein E on Alzheimer's beta-amyloid fibril formation in vitro. Biochemistry 1997; 36: 6243-50
    • (1997) Biochemistry , vol.36 , pp. 6243-6250
    • Naiki, H.1    Gejyo, F.2    Nakakuki, K.3
  • 55
    • 0030867936 scopus 로고    scopus 로고
    • Imeraction of nascent apoE2, apoE3, and apoE4 isolorms expressed in mammalian cells with amyloid peptide beta (1-40)
    • 55. Aleshkov S, Abraham CR, Zannis VI. Imeraction of nascent apoE2, apoE3, and apoE4 isolorms expressed in mammalian cells with amyloid peptide beta (1-40). Biochemistry 1997; 36: 10571-80
    • (1997) Biochemistry , vol.36 , pp. 10571-10580
    • Aleshkov, S.1    Abraham, C.R.2    Zannis, V.I.3
  • 56
    • 0027931854 scopus 로고
    • Isoform-specific binding of apolipoprotein E to beta-amyloid
    • 56. LaDu MJ, Falduto MT, Manelli AM, et al. Isoform-specific binding of apolipoprotein E to beta-amyloid. J Biol Chem 1994; 269: 23403-6
    • (1994) J Biol Chem , vol.269 , pp. 23403-23406
    • Ladu, M.J.1    Falduto, M.T.2    Manelli, A.M.3
  • 57
    • 0030851335 scopus 로고    scopus 로고
    • Alzheimer transgenic mouse models come of age
    • 57. Duff K. Alzheimer transgenic mouse models come of age. Trends Neurosci 1997; 20: 279-80
    • (1997) Trends Neurosci , vol.20 , pp. 279-280
    • Duff, K.1
  • 58
    • 0030764732 scopus 로고    scopus 로고
    • Amyloidogenic role of eytokine TGF-β1 in transgenic mice in Alzheimer's disease
    • 58. Wyss-Coray T, Masliah E, Mallory M, et al. Amyloidogenic role of eytokine TGF-β1 in transgenic mice in Alzheimer's disease. Nature 1997; 389: 603-6
    • (1997) Nature , vol.389 , pp. 603-606
    • Wyss-Coray, T.1    Masliah, E.2    Mallory, M.3
  • 59
    • 0031020909 scopus 로고    scopus 로고
    • Amyloid precursor protein processing and Aβ42 deposition in a transgenic mouse model of Alzheimer disease
    • 59. Johnson-Wood K, Lee M, Motter R, et al. Amyloid precursor protein processing and Aβ42 deposition in a transgenic mouse model of Alzheimer disease. Proc Natl Acad Sci USA 1997; 94: 1550-5
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 1550-1555
    • Johnson-Wood, K.1    Lee, M.2    Motter, R.3
  • 60
    • 0030611097 scopus 로고    scopus 로고
    • Aβ deposition is associated with neuropil changes, but not with overt neuronal loss in the human amyloid precursor protein V717F(PDAPP) transgenic mouse
    • 60. Irizarry MC, Soriano F, McNamara M, et al. Aβ deposition is associated with neuropil changes, but not with overt neuronal loss in the human amyloid precursor protein V717F(PDAPP) transgenic mouse. J Neurosci 1997; 17: 7053-9
    • (1997) J Neurosci , vol.17 , pp. 7053-7059
    • Irizarry, M.C.1    Soriano, F.2    McNamara, M.3
  • 61
    • 0030612033 scopus 로고    scopus 로고
    • APPSw transgenic mice develop age related A beta deposits and neuropil abnormalities, but no neuronal loss in CAI
    • 61. Irizarry MC, McNamara M, Fedorchak K, et al. APPSw transgenic mice develop age related A beta deposits and neuropil abnormalities, but no neuronal loss in CAI. J Neuropathol Exp Neurol 1997; 56: 965-73
    • (1997) J Neuropathol Exp Neurol , vol.56 , pp. 965-973
    • Irizarry, M.C.1    McNamara, M.2    Fedorchak, K.3
  • 62
    • 16044366039 scopus 로고    scopus 로고
    • Increased amyloid-beta42(43) in brains of mice expressing mutant presenilin 1
    • 62. Duff K, Eckman C, Zehr C, et al. Increased amyloid-beta42(43) in brains of mice expressing mutant presenilin 1. Nature 1996; 383: 710-3
    • (1996) Nature , vol.383 , pp. 710-713
    • Duff, K.1    Eckman, C.2    Zehr, C.3
  • 63
    • 0030293676 scopus 로고    scopus 로고
    • Familial alzheimer's disease linked presenilin 1 variants elevate abeta1-42/1-40 ratio in vitro and in vivo
    • 63. Borehelt DR, Thinakaran G, Eckman CB, et al. Familial Alzheimer's disease linked presenilin 1 variants elevate Abeta1-42/1-40 ratio in vitro and in vivo. Neuron 1996; 17: 1005-13
    • (1996) Neuron , vol.17 , pp. 1005-1013
    • Borehelt, D.R.1    Thinakaran, G.2    Eckman, C.B.3
  • 64
    • 0030833055 scopus 로고    scopus 로고
    • Accelerated amyloid depositions in the brains of transgenic mice coexpressing mutant presenilin 1 and amyloid precursor proteins
    • 64. Borchelt DR, Ratovitski T, van Lare J, et al. Accelerated amyloid depositions in the brains of transgenic mice coexpressing mutant presenilin 1 and amyloid precursor proteins. Neuron 1997; 19: 939-45
    • (1997) Neuron , vol.19 , pp. 939-945
    • Borchelt, D.R.1    Ratovitski, T.2    Van Lare, J.3
  • 65
    • 0031914718 scopus 로고    scopus 로고
    • Accelerated Alzheimer-type phenotype in transgenic mice carrying both mutant amyloid precursor protein and presenilin 1 transgenes
    • 65. Holcomb L, Gordon MN, McGowan E, et al. Accelerated Alzheimer-type phenotype in transgenic mice carrying both mutant amyloid precursor protein and presenilin 1 transgenes. Nat Med 1998; 4:97-100
    • (1998) Nat Med , vol.4 , pp. 97-100
    • Holcomb, L.1    Gordon, M.N.2    McGowan, E.3
  • 66
    • 0029742199 scopus 로고    scopus 로고
    • Correlative memory deficits, Abeta elevation, and amyloid plaques in transgenic mite
    • 66. Hsiao K, Chapman P, Nilsen S, et al. Correlative memory deficits, Abeta elevation, and amyloid plaques in transgenic mite. Science 1996; 274: 99-102
    • (1996) Science , vol.274 , pp. 99-102
    • Hsiao, K.1    Chapman, P.2    Nilsen, S.3
  • 67
    • 0028786849 scopus 로고
    • Paired helical filament-like phosphorylation of tau, deposition of β/A4-amyloid and memory impairment in rat induced by chronic inhibition of phosphatase 1 and 2A
    • 67. Arendt T, Holzer M, Fruth R, et al. Paired helical filament-like phosphorylation of tau, deposition of β/A4-amyloid and memory impairment in rat induced by chronic inhibition of phosphatase 1 and 2A. Neuroscience 1995, 69: 691-8
    • (1995) Neuroscience , vol.69 , pp. 691-698
    • Arendt, T.1    Holzer, M.2    Fruth, R.3
  • 68
    • 0028577208 scopus 로고
    • Immunohistochemical evidence for apoptosis in Alzheimer's disease
    • 68. Su JH, Anderson AJ, Cummings BJ, et al. Immunohistochemical evidence for apoptosis in Alzheimer's disease. Neuroreport 1994; 5: 2529-33
    • (1994) Neuroreport , vol.5 , pp. 2529-2533
    • Su, J.H.1    Anderson, A.J.2    Cummings, B.J.3
  • 69
    • 0029040355 scopus 로고
    • In situ evidence for DNA fragmentation in Huntington's disease striatum and Alzheimer's disease temporal lobes
    • 69. Dragunow M, Faull RLM, Lawlor P, et al. In situ evidence for DNA fragmentation in Huntington's disease striatum and Alzheimer's disease temporal lobes. Neuroreport 1995; 6: 1053-7
    • (1995) Neuroreport , vol.6 , pp. 1053-1057
    • Dragunow, M.1    Faull, R.L.M.2    Lawlor, P.3
  • 70
    • 0028833215 scopus 로고
    • Cell death in Alzheimer's disease evaluated by DNA fragmentation in situ
    • 70. Lassmann H, Bancher C, Breitschopf H, et al. Cell death in Alzheimer's disease evaluated by DNA fragmentation in situ. Acta Neuropathol 1995; 89: 35-41
    • (1995) Acta Neuropathol , vol.89 , pp. 35-41
    • Lassmann, H.1    Bancher, C.2    Breitschopf, H.3
  • 71
    • 0030831489 scopus 로고    scopus 로고
    • Correlates of p53-and Fas (CD95)-mediated apoplosis in Alzheimer's disease
    • 71. De la Monte SM, Sohn YK, Wands JR. Correlates of p53-and Fas (CD95)-mediated apoplosis in Alzheimer's disease. J Neurol Sci 1997; 152:73-83
    • (1997) J Neurol Sci , vol.152 , pp. 73-83
    • De La Monte, S.M.1    Sohn, Y.K.2    Wands, J.R.3
  • 72
    • 0029983170 scopus 로고    scopus 로고
    • Up-regulalion of Bcl-2 is associated with neuronal DNA damage in Alzheimer's disease
    • 72. Su JH, Satou T, Anderson AJ, et al. Up-regulalion of Bcl-2 is associated with neuronal DNA damage in Alzheimer's disease. Neuroreport 1996; 7: 437-40
    • (1996) Neuroreport , vol.7 , pp. 437-440
    • Su, J.H.1    Satou, T.2    Anderson, A.J.3
  • 73
    • 0027191973 scopus 로고
    • Apoptosis mediated neurotoxicity induced by chronic application of β amyloid fragment 25-35
    • 73. Forloni G, Chiesa R, Smiroldo S, et al. Apoptosis mediated neurotoxicity induced by chronic application of β amyloid fragment 25-35. Neuroreport 1993; 4: 523-6
    • (1993) Neuroreport , vol.4 , pp. 523-526
    • Forloni, G.1    Chiesa, R.2    Smiroldo, S.3
  • 74
    • 0027257708 scopus 로고
    • Apoptosis is induced by β-amyloid in cultured central nervous system neurons
    • 74. Loo DT, Copani A, Pike CJ, et al. Apoptosis is induced by β-amyloid in cultured central nervous system neurons. Proc Natl Acad Sci USA 1993; 90: 7951-5
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 7951-7955
    • Loo, D.T.1    Copani, A.2    Pike, C.J.3
  • 75
    • 0029133850 scopus 로고
    • Differential induction of immediate early gene proteins in cultured neurons by beta-amyloid (Abeta): Association of c-Jun with Abeta-induced aoptosis
    • 75. Anderson AJ, Pike CJ, Cotman CW. Differential induction of immediate early gene proteins in cultured neurons by beta-amyloid (Abeta): association of c-Jun with Abeta-induced aoptosis. J Neurochem 1995; 65: 1487-98
    • (1995) J Neurochem , vol.65 , pp. 1487-1498
    • Anderson, A.J.1    Pike, C.J.2    Cotman, C.W.3
  • 76
    • 0028982522 scopus 로고
    • Shift from fetal-type to Alzheimer-type phosphorylated tau proteins in SKNSH SY 5Y cells treated with okadaic acid
    • 76. Dupont-Wallois L, Sautiere PE, Cocquerelle C, et al. Shift from fetal-type to Alzheimer-type phosphorylated tau proteins in SKNSH SY 5Y cells treated with okadaic acid. FEBS Lett 1995; 357: 197-201
    • (1995) FEBS Lett , vol.357 , pp. 197-201
    • Dupont-Wallois, L.1    Sautiere, P.E.2    Cocquerelle, C.3
  • 77
    • 0025002021 scopus 로고
    • Acute phase proteins are present in amorphous plaques in the cerebral but not in the cerebellar cortex of patients with Alzheimer's disease
    • 77. Rozemuller JM, Stam FC, Eikelenboom P. Acute phase proteins are present in amorphous plaques in the cerebral but not in the cerebellar cortex of patients with Alzheimer's disease. Neurosci Lett 1990; 119: 75-8
    • (1990) Neurosci Lett , vol.119 , pp. 75-78
    • Rozemuller, J.M.1    Stam, F.C.2    Eikelenboom, P.3
  • 78
    • 0027354835 scopus 로고
    • Microglia in degenerative neurological disease
    • 78. McGeer PL, Kawamata T, Walker DC, et al. Microglia in degenerative neurological disease. Glia 1993; 7: 84-92
    • (1993) Glia , vol.7 , pp. 84-92
    • McGeer, P.L.1    Kawamata, T.2    Walker, D.C.3
  • 79
    • 0029971210 scopus 로고    scopus 로고
    • Amyloid β protein (Aβ) primes cultured rat microglial cells for an enhanced phorhol-myristate-acetate induced respiratory burst activity
    • 79. Van Muiswinkel FL, Veerhuis K, Eikelenboom P. Amyloid β protein (Aβ) primes cultured rat microglial cells for an enhanced phorhol-myristate-acetate induced respiratory burst activity. J Neurochem 1996, 66: 2468-76
    • (1996) J Neurochem , vol.66 , pp. 2468-2476
    • Van Muiswinkel, F.L.1    Veerhuis, K.2    Eikelenboom, P.3
  • 80
    • 0007692414 scopus 로고    scopus 로고
    • In vivo and in vitro evidence supporting a role for the inflammatory cytokine interleukin-1 as a driving force in Alzheimer pathogenesis
    • 80. Sheng JG, Ito K, Skinner RD, et al. In vivo and in vitro evidence supporting a role for the inflammatory cytokine interleukin-1 as a driving force in Alzheimer pathogenesis. Neurobiol Aging 1996; 17: 761-6
    • (1996) Neurobiol Aging , vol.17 , pp. 761-766
    • Sheng, J.G.1    Ito, K.2    Skinner, R.D.3
  • 81
    • 0029976439 scopus 로고    scopus 로고
    • Neurocytopathic effects of β-amyloid-stimulated monocytes: A potential mechanism for central nervous system damage in Alzheimer disease
    • 81. London JA, Biegel D, Pachter JS. Neurocytopathic effects of β-amyloid-stimulated monocytes: a potential mechanism for central nervous system damage in Alzheimer disease. Proc Natl Acad Sci USA 1996; 93: 4147-52
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 4147-4152
    • London, J.A.1    Biegel, D.2    Pachter, J.S.3
  • 82
    • 0029795517 scopus 로고    scopus 로고
    • Inflammation, Aβ deposition, and neurofibrillary tangle formation as correlates of Alzheimer's disease neurodegeneration
    • 82. Lue L-F, Bruchova L, Civin WH, et al. Inflammation, Aβ deposition, and neurofibrillary tangle formation as correlates of Alzheimer's disease neurodegeneration. J Neuropathol Exp Neurol 1996; 55: 1083-8
    • (1996) J Neuropathol Exp Neurol , vol.55 , pp. 1083-1088
    • Lue, L.-F.1    Bruchova, L.2    Civin, W.H.3
  • 83
    • 0029614765 scopus 로고
    • Neural apoptosis
    • 83. Bredesen DE. Neural apoptosis. Ann Neurol 1995; 38: 839-51
    • (1995) Ann Neurol , vol.38 , pp. 839-851
    • Bredesen, D.E.1
  • 84
    • 0029058742 scopus 로고
    • The Alzheimer amyloid precursor proteoglycan (appican) is present in brain and is produced by astrocytes but not by neurons in primary neural cultures
    • 84. Shioi J, Pangalos MN, Ripellino JA, et al. The Alzheimer amyloid precursor proteoglycan (appican) is present in brain and is produced by astrocytes but not by neurons in primary neural cultures. J Biol Chem 1995; 270: 11839-44
    • (1995) J Biol Chem , vol.270 , pp. 11839-11844
    • Shioi, J.1    Pangalos, M.N.2    Ripellino, J.A.3
  • 85
    • 0030944118 scopus 로고    scopus 로고
    • Metabotropic glutamate receptors increase amyloid precursor protein processing in astrocytes: Inhibition by cyclic AMP
    • 85. Lee RKK, Wurtman RJ. Metabotropic glutamate receptors increase amyloid precursor protein processing in astrocytes: inhibition by cyclic AMP. J Neurochem 1997; 68: 1830-5
    • (1997) J Neurochem , vol.68 , pp. 1830-1835
    • Lee, R.K.K.1    Wurtman, R.J.2
  • 87
    • 0029076362 scopus 로고
    • Microglia: Intrinsic immunoeffector cell of the brain
    • 87. Gehrmann J, Matsumoto Y, Kreutzberg GW. Microglia: intrinsic immunoeffector cell of the brain. Brain Res Rev 1995; 20: 269-87
    • (1995) Brain Res Rev , vol.20 , pp. 269-287
    • Gehrmann, J.1    Matsumoto, Y.2    Kreutzberg, G.W.3
  • 88
    • 0030222037 scopus 로고    scopus 로고
    • Microglia: A sensor for pathological events in the CNS
    • 88. Kreutzberg GW. Microglia: a sensor for pathological events in the CNS. Trends Neurosci 1996; 19: 312-8
    • (1996) Trends Neurosci , vol.19 , pp. 312-318
    • Kreutzberg, G.W.1
  • 89
    • 0025580779 scopus 로고
    • Ultrastructure of the cells forming amyloid fibers in Alzheimer disease and scrapie
    • 89. Wisniewski HM, Vorbrodt AW, Wegiel J, et al. Ultrastructure of the cells forming amyloid fibers in Alzheimer disease and scrapie. Am J Med Genet 1990; 7: 287-97
    • (1990) Am J Med Genet , vol.7 , pp. 287-297
    • Wisniewski, H.M.1    Vorbrodt, A.W.2    Wegiel, J.3
  • 90
    • 0029811901 scopus 로고    scopus 로고
    • Arthritis and antiinflammatury agents as possible protective factors for Alzheimer's disease: A review of 17 epidemiologic studies
    • 90. McGeer PL, Schulzer M, McGeer EG. Arthritis and antiinflammatury agents as possible protective factors for Alzheimer's disease: a review of 17 epidemiologic studies. Neurology 1996; 47: 425-32
    • (1996) Neurology , vol.47 , pp. 425-432
    • McGeer, P.L.1    Schulzer, M.2    McGeer, E.G.3
  • 91
    • 0030250758 scopus 로고    scopus 로고
    • Neuroglial-mediated immunoinflammatory responses in Alzheimer's disease: Complement activation and therapeutic approaches
    • 91. Chen S, Frederickson RCA, Brunden KR. Neuroglial-mediated immunoinflammatory responses in Alzheimer's disease: complement activation and therapeutic approaches. Neurobiol Aging 1996; 17: 781-7
    • (1996) Neurobiol Aging , vol.17 , pp. 781-787
    • Chen, S.1    Frederickson, R.C.A.2    Brunden, K.R.3
  • 92
    • 0031031747 scopus 로고    scopus 로고
    • Aspartate residue 7 in amyloid beta protein is critical for classical complement pathway activation: Implications for Alzheimer's disease progress
    • 92. Velazquez P, Cribbs DH, Poulos TL, et al. Aspartate residue 7 in amyloid beta protein is critical for classical complement pathway activation: implications for Alzheimer's disease progress. Nat Med 1997; 3: 77-9
    • (1997) Nat Med , vol.3 , pp. 77-79
    • Velazquez, P.1    Cribbs, D.H.2    Poulos, T.L.3
  • 93
    • 0030248270 scopus 로고    scopus 로고
    • Microglial cells internalize aggregates of the Alzheimer's disease amyloid beta protein via a scavenger receptor
    • 93. Paresce DM, Ghosh RN, Maxfield FR. Microglial cells internalize aggregates of the Alzheimer's disease amyloid beta protein via a scavenger receptor. Neuron 1996; 17; 553-65
    • (1996) Neuron , vol.17 , pp. 553-565
    • Paresce, D.M.1    Ghosh, R.N.2    Maxfield, F.R.3
  • 94
    • 0026073725 scopus 로고
    • Cellular aging and alzheimer's disease: Membrane-related events as clues to primary mechanisms
    • 94. Busman GJCGM, Bartholomeus IGP, De Grip WJ. Cellular aging and Alzheimer's disease: membrane-related events as clues to primary mechanisms. Gerontology 1991; 37: 95-112
    • (1991) Gerontology , vol.37 , pp. 95-112
    • Busman, G.J.C.G.M.1    Bartholomeus, I.G.P.2    De Grip, W.J.3
  • 95
    • 0027367764 scopus 로고
    • Physiological production of the beta-amyloid protein and the mechanism of alzheimer's disease
    • 95. Selkoe DJ. Physiological production of the beta-amyloid protein and the mechanism of alzheimer's disease. Trends Neurosci 1993; 16:403-9
    • (1993) Trends Neurosci , vol.16 , pp. 403-409
    • Selkoe, D.J.1
  • 96
    • 0029671454 scopus 로고    scopus 로고
    • Cholesterol modulates a-secretase cleavage of amyloid precursor protein
    • 96. Bodovitz S, Klein WL. Cholesterol modulates a-secretase cleavage of amyloid precursor protein. J Biol Chem 1996; 271: 4436-40
    • (1996) J Biol Chem , vol.271 , pp. 4436-4440
    • Bodovitz, S.1    Klein, W.L.2
  • 97
    • 0030596751 scopus 로고    scopus 로고
    • Alzheimer's amyloid precursor protein is expressed on the surface of hematopoietic cells upon activation
    • 97. Bullido MJ, Munoz-Fernandez MA, Recuero M, et al. Alzheimer's amyloid precursor protein is expressed on the surface of hematopoietic cells upon activation. Biochim Biophys Acta 1996; 1313:54-62
    • (1996) Biochim Biophys Acta , vol.1313 , pp. 54-62
    • Bullido, M.J.1    Munoz-Fernandez, M.A.2    Recuero, M.3
  • 98
    • 0028866524 scopus 로고
    • Membrane alterations in Alzheimer's disease and aging
    • 98. Cowburn RF, O'Neill C, Fowler CJ. Membrane alterations in Alzheimer's disease and aging Trends Neurosci 1995; 18: 483-4
    • (1995) Trends Neurosci , vol.18 , pp. 483-484
    • Cowburn, R.F.1    O'Neill, C.2    Fowler, C.J.3
  • 99
    • 0028670272 scopus 로고
    • β-amyloid Ca2-t-channel hypothesis for neuronal death in Alzheimer disease
    • 99. Arispe N, Pollard HB, Rojas E. β-amyloid Ca2-t-channel hypothesis for neuronal death in Alzheimer disease. Mol Cell Biochem 1994; 140; 119-25
    • (1994) Mol Cell Biochem , vol.140 , pp. 119-125
    • Arispe, N.1    Pollard, H.B.2    Rojas, E.3
  • 100
    • 0026495712 scopus 로고
    • Mechanisms of neuronal death in hrain aging and alzheimer's disease: Role of endocrine-mediated calcium dyshomeostasis
    • 100. Landfield PW, Thibault O, Mazzanti ML, et al. Mechanisms of neuronal death in hrain aging and alzheimer's disease: role of endocrine-mediated calcium dyshomeostasis. J Neurobiol 1992; 23: 1247-60
    • (1992) J Neurobiol , vol.23 , pp. 1247-1260
    • Landfield, P.W.1    Thibault, O.2    Mazzanti, M.L.3
  • 101
    • 0028304198 scopus 로고
    • Receptor-mediated activation of G proteins is reduced in postmortem brains from Alzheimer's disease patients
    • 101. Wang H-Y, Friedman E. Receptor-mediated activation of G proteins is reduced in postmortem brains from Alzheimer's disease patients. Neurosci Lett 1994; 173; 37-9
    • (1994) Neurosci Lett , vol.173 , pp. 37-39
    • Wang, H.-Y.1    Friedman, E.2
  • 102
    • 0342940764 scopus 로고    scopus 로고
    • Phospholipase C isozymes in the human brain and their changes in Alzheimer's disease
    • 102. Shimohama S, Sasaki Y, Fujimoto S, et al. Phospholipase C isozymes in the human brain and their changes in Alzheimer's disease. Neuroscience 1998; 82: 999-1007
    • (1998) Neuroscience , vol.82 , pp. 999-1007
    • Shimohama, S.1    Sasaki, Y.2    Fujimoto, S.3
  • 103
    • 0028082136 scopus 로고
    • An important role of heparin sulfate proteoglycan (perlecan) in a model system for the deposition and persistence of fibrillar A beta amyloid in rat brain
    • 103. Snow AD, Sekiguchi R, Nochlin P, et al. An important role of heparin sulfate proteoglycan (perlecan) in a model system for the deposition and persistence of fibrillar A beta amyloid in rat brain. Neuron 1994; 12: 219-34
    • (1994) Neuron , vol.12 , pp. 219-234
    • Snow, A.D.1    Sekiguchi, R.2    Nochlin, P.3
  • 104
    • 0029907548 scopus 로고    scopus 로고
    • Assembly of microbutule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosnminoglycans
    • 104. Goedert M, Jakes R, Spillantini MG, et al. Assembly of microbutule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosnminoglycans. Nature 1996; 383; 550-3
    • (1996) Nature , vol.383 , pp. 550-553
    • Goedert, M.1    Jakes, R.2    Spillantini, M.G.3
  • 105
    • 0027056828 scopus 로고
    • Degradation of proteins in the membrane-eytoskeleton complex in Alzheimer's disease
    • 105. Saitoh T, Masliah E, Baum L, et al. Degradation of proteins in the membrane-eytoskeleton complex in Alzheimer's disease. Ann N Y Acad Sci 1992; 674: 180-92
    • (1992) Ann N Y Acad Sci , vol.674 , pp. 180-192
    • Saitoh, T.1    Masliah, E.2    Baum, L.3
  • 106
    • 0027214115 scopus 로고
    • Proteins immunologically related to erythrocyte anion transporter band 3 are altered in brain areas affected by Alzheimer's disease
    • 106. Bosman GJCGM, Van Workum FPA, Renkawek K, et al. Proteins immunologically related to erythrocyte anion transporter band 3 are altered in brain areas affected by Alzheimer's disease. Acta Neuropathol 1993; 86: 353-9
    • (1993) Acta Neuropathol , vol.86 , pp. 353-359
    • Bosman, G.J.C.G.M.1    Van Workum, F.P.A.2    Renkawek, K.3


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