메뉴 건너뛰기




Volumn 22, Issue 19, 2015, Pages 2392-2403

Therapeutic effects of herbal chemicals in traditional Chinese medicine on Alzheimer's disease

Author keywords

Alzheimer's disease; Beta amyloid; Therapeutic potential; Traditional Chinese Medicine; secretases; secretases

Indexed keywords

ALPHA SECRETASE; ALPHA SECRETASE INHIBITOR; AMYLOID BETA PROTEIN; ASPARTIC PROTEINASE INHIBITOR; BAICALEIN; BETA SECRETASE; BETA SECRETASE INHIBITOR; CHOLINESTERASE INHIBITOR; COPTIS CHINENSIS EXTRACT; CRYPTOTANSHINONE; DAVUNETIDE; DONEPEZIL; GALANTAMINE; GINKGO BILOBA EXTRACT; HEAT SHOCK PROTEIN; HEME OXYGENASE; HUPERZINE A; MEMANTINE; MITOCHONDRIAL DNA; N METHYL DEXTRO ASPARTIC ACID RECEPTOR BLOCKING AGENT; PYRUVATE DEHYDROGENASE; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE; RIVASTIGMINE; SALVIANOLIC ACID B; TACRINE; UNCLASSIFIED DRUG; HERBACEOUS AGENT;

EID: 84937132147     PISSN: 09298673     EISSN: 1875533X     Source Type: Journal    
DOI: 10.2174/0929867322666150520095509     Document Type: Article
Times cited : (28)

References (140)
  • 1
    • 0037072064 scopus 로고    scopus 로고
    • Alzheimer's disease
    • Burns, A.; Byrne, E. J.; Maurer, K. Alzheimer's disease. Lancet, 2002, 360, 163-165.
    • (2002) Lancet , vol.360 , pp. 163-165
    • Burns, A.1    Byrne, E.J.2    Maurer, K.3
  • 2
    • 84875354777 scopus 로고    scopus 로고
    • 2013 Alzheimer's disease facts and figures
    • Association, A. 2013 Alzheimer's disease facts and figures. Alzheimer's Dement., 2013, 9(2), 208-245.
    • (2013) Alzheimer's Dement. , vol.9 , Issue.2 , pp. 208-245
    • Association, A.1
  • 5
    • 0033977086 scopus 로고    scopus 로고
    • Amyloid fibrillogenesis: Themes and variations
    • Rochet, J. C.; Lansbury, P. T. Amyloid fibrillogenesis: themes and variations. Curr. Opin. Struct. Biol., 2000, 10(1), 60-68.
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , Issue.1 , pp. 60-68
    • Rochet, J.C.1    Lansbury, P.T.2
  • 7
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy, J.; Selkoe, D. J. The amyloid hypothesis of alzheimer's disease: progress and problems on the road to therapeutics. Science, 2002, 297(5580), 353-356.
    • (2002) Science , vol.297 , Issue.5580 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 8
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the alzheimer's amyloid betapeptide
    • Haass, C.; Selkoe, D. J. Soluble protein oligomers in neurodegeneration: lessons from the alzheimer's amyloid betapeptide. Nat. Rev. Mol. Cell Biol., 2007, 8(2), 101-112.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , Issue.2 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 9
    • 0012194808 scopus 로고
    • A drosophila gene encoding a protein resembling the human betaamyloid protein precursor
    • Rosen, D. R.; Martin-Morris, L.; Luo, L. Q.; White, K. A drosophila gene encoding a protein resembling the human betaamyloid protein precursor. Proc. Natl. Acad. Sci. U. S. A., 1989, 86(7), 2478-2482.
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , Issue.7 , pp. 2478-2482
    • Rosen, D.R.1    Martin-Morris, L.2    Luo, L.Q.3    White, K.4
  • 10
    • 0034644836 scopus 로고    scopus 로고
    • Regulation of app cleavage by alpha-, betaand gamma-secretases
    • Nunan, J.; Small, D. H. Regulation of app cleavage by alpha-, betaand gamma-secretases. FEBS Lett., 2000, 483(1), 6-10.
    • (2000) FEBS Lett. , vol.483 , Issue.1 , pp. 6-10
    • Nunan, J.1    Small, D.H.2
  • 11
    • 15944413832 scopus 로고    scopus 로고
    • The non-amyloidogenic pathway: Structure and function of alpha-secretases
    • Kojro, E.; Fahrenholz, F. The non-amyloidogenic pathway: structure and function of alpha-secretases. Subcell. Biochem., 2005, 38, 105-127.
    • (2005) Subcell. Biochem. , vol.38 , pp. 105-127
    • Kojro, E.1    Fahrenholz, F.2
  • 13
    • 1542275420 scopus 로고    scopus 로고
    • Identification of novel nuclear export and nuclear localization-related signals in human heat shock cognate protein 70
    • Tsukahara, F.; Maru, Y. Identification of novel nuclear export and nuclear localization-related signals in human heat shock cognate protein 70. J. Biol. Chem., 2004, 279(10), 8867-8872.
    • (2004) J. Biol. Chem. , vol.279 , Issue.10 , pp. 8867-8872
    • Tsukahara, F.1    Maru, Y.2
  • 16
    • 34248190279 scopus 로고    scopus 로고
    • A beta oligomers - A decade of discovery
    • Walsh, D. M.; Selkoe, D. J. A beta oligomers - a decade of discovery. J. Neurochem., 2007, 101(5), 1172-1184.
    • (2007) J. Neurochem. , vol.101 , Issue.5 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 17
    • 0037174618 scopus 로고    scopus 로고
    • Alzheimer's disease is a synaptic failure
    • Selkoe, D. J. Alzheimer's disease is a synaptic failure. Science, 2002, 298(5594), 789-791.
    • (2002) Science , vol.298 , Issue.5594 , pp. 789-791
    • Selkoe, D.J.1
  • 18
    • 0036215321 scopus 로고    scopus 로고
    • Betaamyloid peptide induces ultrastructural changes in synaptosomes and potentiates mitochondrial dysfunction in the presence of ryanodine
    • Mungarro-Menchaca, X.; Ferrera, P.; Morán, J.; Arias, C. Betaamyloid peptide induces ultrastructural changes in synaptosomes and potentiates mitochondrial dysfunction in the presence of ryanodine. J. Neurosci. Res., 2002, 68(1), 89-96.
    • (2002) J. Neurosci. Res. , vol.68 , Issue.1 , pp. 89-96
    • Mungarro-Menchaca, X.1    Ferrera, P.2    Morán, J.3    Arias, C.4
  • 20
    • 39149122810 scopus 로고    scopus 로고
    • Amyloid beta, mitochondrial dysfunction and synaptic damage: Implications for cognitive decline in aging and alzheimer's disease
    • Reddy, P. H.; Beal, M. F. Amyloid beta, mitochondrial dysfunction and synaptic damage: implications for cognitive decline in aging and alzheimer's disease. Trends Mol. Med., 2008, 14(2), 45-53.
    • (2008) Trends Mol. Med. , vol.14 , Issue.2 , pp. 45-53
    • Reddy, P.H.1    Beal, M.F.2
  • 23
    • 0035863188 scopus 로고    scopus 로고
    • Decreased nuclear beta-catenin, tau hyperphosphorylation and neurodegeneration in gsk-3beta conditional transgenic mice
    • Lucas, J. J.; Hernández, F.; Gómez-Ramos, P.; Morán, M. A.; Hen, R.; Avila, J. Decreased nuclear beta-catenin, tau hyperphosphorylation and neurodegeneration in gsk-3beta conditional transgenic mice. EMBO J., 2001, 20(1-2), 27-39.
    • (2001) EMBO J. , vol.20 , Issue.1-2 , pp. 27-39
    • Lucas, J.J.1    Hernández, F.2    Gómez-Ramos, P.3    Morán, M.A.4    Hen, R.5    Avila, J.6
  • 24
    • 0026740795 scopus 로고
    • Neurofibrillary tangles but not senile plaques parallel duration and severity of alzheimer's disease
    • Arriagada, P. V; Growdon, J. H.; Hedley-Whyte, E. T.; Hyman, B. T. Neurofibrillary tangles but not senile plaques parallel duration and severity of alzheimer's disease. Neurology, 1992, 42(3 Pt 1), 631-639.
    • (1992) Neurology , vol.42 , Issue.3 , pp. 631-639
    • Arriagada, P.V.1    Growdon, J.H.2    Hedley-Whyte, E.T.3    Hyman, B.T.4
  • 25
    • 0035943436 scopus 로고    scopus 로고
    • Formation of neurofibrillary tangles in p3011 tau transgenic mice induced by abeta 42 fibrils
    • Götz, J.; Chen, F.; van Dorpe, J.; Nitsch, R. M. Formation of neurofibrillary tangles in p3011 tau transgenic mice induced by abeta 42 fibrils. Science, 2001, 293(5534), 1491-1495.
    • (2001) Science , vol.293 , Issue.5534 , pp. 1491-1495
    • Götz, J.1    Chen, F.2    Van Dorpe, J.3    Nitsch, R.M.4
  • 26
    • 33644851265 scopus 로고    scopus 로고
    • Inducible expression of tau repeat domain in cell models of tauopathy: Aggregation is toxic to cells but can be reversed by inhibitor drugs
    • Khlistunova, I.; Biernat, J.; Wang, Y.; Pickhardt, M.; von Bergen, M.; Gazova, Z.; Mandelkow, E.; Mandelkow, E.M. Inducible expression of tau repeat domain in cell models of tauopathy: aggregation is toxic to cells but can be reversed by inhibitor drugs. J. Biol. Chem., 2006, 281(2), 1205-1214.
    • (2006) J. Biol. Chem. , vol.281 , Issue.2 , pp. 1205-1214
    • Khlistunova, I.1    Biernat, J.2    Wang, Y.3    Pickhardt, M.4    Von Bergen, M.5    Gazova, Z.6    Mandelkow, E.7    Mandelkow, E.M.8
  • 28
    • 33846015514 scopus 로고    scopus 로고
    • Reduction of soluble abeta and tau, but not soluble abeta alone, ameliorates cognitive decline in transgenic mice with plaques and tangles
    • Oddo, S.; Vasilevko, V.; Caccamo, A.; Kitazawa, M.; Cribbs, D. H.; LaFerla, F. M. Reduction of soluble abeta and tau, but not soluble abeta alone, ameliorates cognitive decline in transgenic mice with plaques and tangles. J. Biol. Chem., 2006, 281(51), 39413-39423.
    • (2006) J. Biol. Chem. , vol.281 , Issue.51 , pp. 39413-39423
    • Oddo, S.1    Vasilevko, V.2    Caccamo, A.3    Kitazawa, M.4    Cribbs, D.H.5    LaFerla, F.M.6
  • 29
    • 0035830408 scopus 로고    scopus 로고
    • Altered expression of synaptic proteins occurs early during progression of alzheimer's disease
    • Masliah, E.; Mallory, M.; Alford, M.; DeTeresa, R.; Hansen, L. A.; McKeel, D. W.; Morris, J. C. Altered expression of synaptic proteins occurs early during progression of alzheimer's disease. Neurology, 2001, 56(1), 127-129.
    • (2001) Neurology , vol.56 , Issue.1 , pp. 127-129
    • Masliah, E.1    Mallory, M.2    Alford, M.3    DeTeresa, R.4    Hansen, L.A.5    McKeel, D.W.6    Morris, J.C.7
  • 30
    • 0025269152 scopus 로고
    • Synapse loss in frontal cortex biopsies in alzheimer's disease: Correlation with cognitive severity
    • DeKosky, S. T.; Scheff, S. W. Synapse loss in frontal cortex biopsies in alzheimer's disease: correlation with cognitive severity. Ann. Neurol., 1990, 27(5), 457-464.
    • (1990) Ann. Neurol. , vol.27 , Issue.5 , pp. 457-464
    • DeKosky, S.T.1    Scheff, S.W.2
  • 31
    • 0025987048 scopus 로고
    • Physical basis of cognitive alterations in alzheimer's disease: Synapse loss is the major correlate of cognitive impairment
    • Terry, R. D.; Masliah, E.; Salmon, D. P.; Butters, N.; DeTeresa, R.; Hill, R.; Hansen, L. A.; Katzman, R. Physical basis of cognitive alterations in alzheimer's disease: synapse loss is the major correlate of cognitive impairment. Ann. Neurol., 1991, 30(4), 572-580.
    • (1991) Ann. Neurol. , vol.30 , Issue.4 , pp. 572-580
    • Terry, R.D.1    Masliah, E.2    Salmon, D.P.3    Butters, N.4    DeTeresa, R.5    Hill, R.6    Hansen, L.A.7    Katzman, R.8
  • 32
    • 0023106967 scopus 로고
    • A quantitative morphometric analysis of the neuronal and synaptic content of the frontal and temporal cortex in patients with alzheimer's disease
    • Davies, C. A.; Mann, D. M.; Sumpter, P. Q.; Yates, P. O. A quantitative morphometric analysis of the neuronal and synaptic content of the frontal and temporal cortex in patients with alzheimer's disease. J. Neurol. Sci., 1987, 78(2), 151-164.
    • (1987) J. Neurol. Sci. , vol.78 , Issue.2 , pp. 151-164
    • Davies, C.A.1    Mann, D.M.2    Sumpter, P.Q.3    Yates, P.O.4
  • 34
    • 0034006944 scopus 로고    scopus 로고
    • Beta-amyloid(1-42) binds to alpha7 nicotinic acetylcholine receptor with high affinity. Implications for alzheimer's disease pathology
    • Wang, H. Y.; Lee, D. H.; D'Andrea, M. R.; Peterson, P. A.; Shank, R. P.; Reitz, A. B. Beta-amyloid(1-42) binds to alpha7 nicotinic acetylcholine receptor with high affinity. implications for alzheimer's disease pathology. J. Biol. Chem., 2000, 275(8), 5626-5632.
    • (2000) J. Biol. Chem. , vol.275 , Issue.8 , 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
  • 35
    • 3042693940 scopus 로고    scopus 로고
    • Glutamate-mediated excitotoxicity and neurodegeneration in alzheimer's disease
    • Hynd, M. R.; Scott, H. L.; Dodd, P. R. Glutamate-mediated excitotoxicity and neurodegeneration in alzheimer's disease. Neurochem. Int., 2004, 45(5), 583-595.
    • (2004) Neurochem. Int. , vol.45 , Issue.5 , pp. 583-595
    • Hynd, M.R.1    Scott, H.L.2    Dodd, P.R.3
  • 36
    • 84948011844 scopus 로고
    • The toxic effect of sodium l-glutamate on the inner layers of the retina
    • LUCAS, D. R.; NEWHOUSE, J. P. The toxic effect of sodium l-glutamate on the inner layers of the retina. amA. Arch. Ophthalmol., 1957, 58(2), 193-201.
    • (1957) amA. Arch. Ophthalmol. , vol.58 , Issue.2 , pp. 193-201
    • Lucas, D.R.1    Newhouse, J.P.2
  • 37
    • 0043172479 scopus 로고    scopus 로고
    • The glutamatergic system and alzheimer's disease: Therapeutic implications
    • Butterfield, D. A.; Pocernich, C. B. The glutamatergic system and alzheimer's disease: therapeutic implications. CNS Drugs, 2003, 17(9), 641-652.
    • (2003) CNS Drugs , vol.17 , Issue.9 , pp. 641-652
    • Butterfield, D.A.1    Pocernich, C.B.2
  • 38
  • 39
    • 0031737226 scopus 로고    scopus 로고
    • Abnormalities of mitochondrial enzymes in alzheimer disease
    • Gibson, G. E.; Sheu, K. F.; Blass, J. P. Abnormalities of mitochondrial enzymes in alzheimer disease. J. Neural Transm., 1998, 105(8-9), 855-870.
    • (1998) J. Neural Transm. , vol.105 , Issue.8-9 , pp. 855-870
    • Gibson, G.E.1    Sheu, K.F.2    Blass, J.P.3
  • 40
    • 0020685951 scopus 로고
    • Decreased pyruvate dehydrogenase complex activity in huntington and alzheimer brain
    • Sorbi, S.; Bird, E. D.; Blass, J. P. Decreased pyruvate dehydrogenase complex activity in huntington and alzheimer brain. Ann. Neurol., 1983, 13(1), 72-78.
    • (1983) Ann. Neurol. , vol.13 , Issue.1 , pp. 72-78
    • Sorbi, S.1    Bird, E.D.2    Blass, J.P.3
  • 42
    • 2442482592 scopus 로고    scopus 로고
    • Free radicals: Key to brain aging and heme oxygenase as a cellular response to oxidative stress
    • Poon, H. F.; Calabrese, V.; Scapagnini, G.; Butterfield, D. A. Free radicals: key to brain aging and heme oxygenase as a cellular response to oxidative stress. J. Gerontol. A. Biol. Sci. Med. Sci., 2004, 59(5), 478-493.
    • (2004) J. Gerontol. A. Biol. Sci. Med. Sci. , vol.59 , Issue.5 , pp. 478-493
    • Poon, H.F.1    Calabrese, V.2    Scapagnini, G.3    Butterfield, D.A.4
  • 44
    • 84861601576 scopus 로고    scopus 로고
    • Heme oxygenase-1 posttranslational modifications in the brain of subjects with alzheimer disease and mild cognitive impairment
    • Barone, E.; Di Domenico, F.; Sultana, R.; Coccia, R.; Mancuso, C.; Perluigi, M.; Butterfield, D. A. Heme oxygenase-1 posttranslational modifications in the brain of subjects with alzheimer disease and mild cognitive impairment. Free Radic. Biol. Med., 52(11-12), 2292-2301.
    • Free Radic. Biol. Med. , vol.52 , Issue.11-12 , pp. 2292-2301
    • Barone, E.1    Di Domenico, F.2    Sultana, R.3    Coccia, R.4    Mancuso, C.5    Perluigi, M.6    Butterfield, D.A.7
  • 45
    • 0032487648 scopus 로고    scopus 로고
    • Amyloid beta-peptide induces apoptosis-related events in synapses and dendrites
    • Mattson, M. P.; Partin, J.; Begley, J. G. Amyloid beta-peptide induces apoptosis-related events in synapses and dendrites. Brain Res., 1998, 807(1-2), 167-176.
    • (1998) Brain Res. , vol.807 , Issue.1-2 , pp. 167-176
    • Mattson, M.P.1    Partin, J.2    Begley, J.G.3
  • 47
    • 0036724204 scopus 로고    scopus 로고
    • Iron (iii) induces aggregation of hyperphosphorylated tau and its reduction to iron (ii) reverses the aggregation: Implications in the formation of neurofibrillary tangles of alzheimer's disease
    • Yamamoto, A.; Shin, R.-W.; Hasegawa, K.; Naiki, H.; Sato, H.; Yoshimasu, F.; Kitamoto, T. Iron (iii) induces aggregation of hyperphosphorylated tau and its reduction to iron (ii) reverses the aggregation: implications in the formation of neurofibrillary tangles of alzheimer's disease. J. Neurochem., 2002, 82(5), 1137-1147.
    • (2002) J. Neurochem. , vol.82 , Issue.5 , pp. 1137-1147
    • Yamamoto, A.1    Shin, R.-W.2    Hasegawa, K.3    Naiki, H.4    Sato, H.5    Yoshimasu, F.6    Kitamoto, T.7
  • 48
    • 80051710827 scopus 로고    scopus 로고
    • Pharmacologists and alzheimer disease therapy: To boldly go where no scientist has gone before
    • Mancuso, C.; Siciliano, R.; Barone, E.; Butterfield, D. A.; Preziosi, P. Pharmacologists and alzheimer disease therapy: to boldly go where no scientist has gone before. Expert Opin. Investig. Drugs, 2011, 20(9), 1243-1261.
    • (2011) Expert Opin. Investig. Drugs , vol.20 , Issue.9 , pp. 1243-1261
    • Mancuso, C.1    Siciliano, R.2    Barone, E.3    Butterfield, D.A.4    Preziosi, P.5
  • 49
    • 0028316959 scopus 로고
    • Hepatotoxic Effects of tacrine administration in patients with alzheimer's disease
    • Watkins, P. B.; Zimmerman, H. J.; Knapp, M. J.; Gracon, S. I.; Lewis, K. W. Hepatotoxic Effects of tacrine administration in patients with alzheimer's disease. JAMA, 1994, 271(13), 992-998.
    • (1994) JAMA , vol.271 , Issue.13 , pp. 992-998
    • Watkins, P.B.1    Zimmerman, H.J.2    Knapp, M.J.3    Gracon, S.I.4    Lewis, K.W.5
  • 51
    • 15044338779 scopus 로고    scopus 로고
    • Failures and successes of nmda receptor antagonists: Molecular basis for the use of open-channel blockers like memantine in the treatment of acute and chronic neurologic insults
    • Lipton, S. A. Failures and successes of nmda receptor antagonists: molecular basis for the use of open-channel blockers like memantine in the treatment of acute and chronic neurologic insults. NeuroRx., 2004, 1(1), 101-110.
    • (2004) NeuroRx. , vol.1 , Issue.1 , pp. 101-110
    • Lipton, S.A.1
  • 52
    • 68149108466 scopus 로고    scopus 로고
    • Semagacestat, a gamma-secretase inhibitor for the potential treatment of alzheimer's disease
    • Imbimbo, B. P.; Peretto, I. Semagacestat, a gamma-secretase inhibitor for the potential treatment of alzheimer's disease. Curr. Opin. Investig. Drugs, 2009, 10(7), 721-730.
    • (2009) Curr. Opin. Investig. Drugs , vol.10 , Issue.7 , pp. 721-730
    • Imbimbo, B.P.1    Peretto, I.2
  • 55
    • 77957361080 scopus 로고    scopus 로고
    • Alzheimer's failure raises questions about diseasemodifying strategies
    • Extance, A. Alzheimer's failure raises questions about diseasemodifying strategies. Nat. Rev. Drug Discov., 2010, 9(10), 749-751.
    • (2010) Nat. Rev. Drug Discov. , vol.9 , Issue.10 , pp. 749-751
    • Extance, A.1
  • 56
    • 72549105935 scopus 로고    scopus 로고
    • Effect of tarenflurbil on cognitive decline and activities of daily living in patients with mild alzheimer disease: A randomized controlled trial
    • Green, R. C.; Schneider, L. S.; Amato, D. A.; Beelen, A. P.; Wilcock, G.; Swabb, E. A.; Zavitz, K. H. Effect of tarenflurbil on cognitive decline and activities of daily living in patients with mild alzheimer disease: a randomized controlled trial. JAMA, 2009, 302(23), 2557-2564.
    • (2009) JAMA , vol.302 , Issue.23 , pp. 2557-2564
    • Green, R.C.1    Schneider, L.S.2    Amato, D.A.3    Beelen, A.P.4    Wilcock, G.5    Swabb, E.A.6    Zavitz, K.H.7
  • 57
    • 84925279976 scopus 로고    scopus 로고
    • Immunotherapeutic approaches for alzheimer's disease
    • Wisniewski, T.; Goñi, F. Immunotherapeutic approaches for alzheimer's disease. Neuron, 2015, 85, 1162-1176.
    • (2015) Neuron , vol.85 , pp. 1162-1176
    • Wisniewski, T.1    Goñi, F.2
  • 62
    • 84899594297 scopus 로고    scopus 로고
    • Davunetide: A review of safety and efficacy data with a focus on neurodegenerative diseases
    • Morimoto, B. H.; Fox, A. W.; Stewart, A. J.; Gold, M. Davunetide: A review of safety and efficacy data with a focus on neurodegenerative diseases. Expert Rev. Clin. Pharmacol., 2013, 6(5), 483-502.
    • (2013) Expert Rev. Clin. Pharmacol. , vol.6 , Issue.5 , pp. 483-502
    • Morimoto, B.H.1    Fox, A.W.2    Stewart, A.J.3    Gold, M.4
  • 63
    • 84925423182 scopus 로고    scopus 로고
    • Effects of vitamin e on cognitive performance during ageing and in alzheimer's disease
    • La Fata, G.; Weber, P.; Mohajeri, M. H. Effects of vitamin e on cognitive performance during ageing and in alzheimer's disease. Nutrients, 2014, 6 (12), 5453-5472.
    • (2014) Nutrients , vol.6 , Issue.12 , pp. 5453-5472
    • La Fata, G.1    Weber, P.2    Mohajeri, M.H.3
  • 65
    • 67650921433 scopus 로고    scopus 로고
    • Vitamin e paradox in alzheimer's disease: It does not prevent loss of cognition and may even be detrimental
    • Lloret, A.; Badía, M.-C.; Mora, N. J.; Pallardó, F. V; Alonso, M.- D.; Viña, J. Vitamin e paradox in alzheimer's disease: it does not prevent loss of cognition and may even be detrimental. J. Alzheimers. Dis., 2009, 17(1), 143-149.
    • (2009) J. Alzheimers. Dis. , vol.17 , Issue.1 , pp. 143-149
    • Lloret, A.1    Badía, M.-C.2    Mora, N.J.3    Pallardó, F.V.4    Alonso, M.-D.5    Viña, J.6
  • 67
    • 84877966990 scopus 로고    scopus 로고
    • From traditional european medicine to discovery of new drug candidates for the treatment of dementia and alzheimer's disease: Acetylcholinesterase inhibitors
    • Russo, P.; Frustaci, A.; Del Bufalo, A.; Fini, M.; Cesario, A. from traditional european medicine to discovery of new drug candidates for the treatment of dementia and alzheimer's disease: acetylcholinesterase inhibitors. Curr. Med. Chem, 2013, 20(8), 976-983.
    • (2013) Curr. Med. Chem , vol.20 , Issue.8 , pp. 976-983
    • Russo, P.1    Frustaci, A.2    Del Bufalo, A.3    Fini, M.4    Cesario, A.5
  • 68
    • 79959922360 scopus 로고    scopus 로고
    • Nutritional approaches to modulate oxidative stress in alzheimer's disease
    • Pocernich, C. B.; Lange, M. L. B.; Sultana, R.; Butterfield, D. A. Nutritional approaches to modulate oxidative stress in alzheimer's disease. Curr. Alzheimer Res., 2011, 8(5), 452-469.
    • (2011) Curr. Alzheimer Res. , vol.8 , Issue.5 , pp. 452-469
    • Pocernich, C.B.1    Lange, M.L.B.2    Sultana, R.3    Butterfield, D.A.4
  • 69
    • 84866004507 scopus 로고    scopus 로고
    • Pharmacological actions and therapeutic applications of salvia miltiorrhiza depside salt and its active components
    • Wu, W.; Wang, Y. Pharmacological actions and therapeutic applications of salvia miltiorrhiza depside salt and its active components. Acta Pharmacol. Sin., 2012, 33(9), 1119-1130.
    • (2012) Acta Pharmacol. Sin. , vol.33 , Issue.9 , pp. 1119-1130
    • Wu, W.1    Wang, Y.2
  • 71
    • 60249088016 scopus 로고    scopus 로고
    • Cryptotanshinone, a compound from salvia miltiorrhiza modulates amyloid precursor protein metabolism and attenuates beta-amyloid deposition through upregulating alpha-secretase in vivo and in vitro
    • Mei, Z.; Zhang, F.; Tao, L.; Zheng, W.; Cao, Y.; Wang, Z.; Tang, S.; Le, K.; Chen, S.; Pi, R.; Liu, P. Cryptotanshinone, a compound from salvia miltiorrhiza modulates amyloid precursor protein metabolism and attenuates beta-amyloid deposition through upregulating alpha-secretase in vivo and in vitro. Neurosci. Lett.,2009, 452(2), 90-95.
    • (2009) Neurosci. Lett. , vol.452 , Issue.2 , pp. 90-95
    • Mei, Z.1    Zhang, F.2    Tao, L.3    Zheng, W.4    Cao, Y.5    Wang, Z.6    Tang, S.7    Le, K.8    Chen, S.9    Pi, R.10    Liu, P.11
  • 72
    • 0001294345 scopus 로고    scopus 로고
    • Ginkgo biloba extract (egb 761). State of knowledge in the dawn of the year 2000
    • Clostre, F. Ginkgo biloba extract (egb 761). state of knowledge in the dawn of the year 2000. Ann. Pharm. françaises, 1999, 57(Suppl 1), 1S8-S88.
    • (1999) Ann. Pharm. Françaises , vol.57 , pp. 1S8-S88
    • Clostre, F.1
  • 73
    • 79955011062 scopus 로고    scopus 로고
    • Drug Discovery from chinese medicine against neurodegeneration in alzheimer's and vascular dementia
    • Ho, Y.S.; So, K.F.; Chang, R. C.C. Drug Discovery from chinese medicine against neurodegeneration in alzheimer's and vascular dementia. Chin. Med., 2011, 6, 15.
    • (2011) Chin. Med. , vol.6 , pp. 15
    • Ho, Y.S.1    So, K.F.2    Chang, R.C.C.3
  • 75
    • 0034121829 scopus 로고    scopus 로고
    • The ginkgo biloba extract (egb 761) protects hippocampal neurons against cell death induced by beta-amyloid
    • Bastianetto, S.; Ramassamy, C.; Doré, S.; Christen, Y.; Poirier, J.; Quirion, R. The ginkgo biloba extract (egb 761) protects hippocampal neurons against cell death induced by beta-amyloid. Eur. J. Neurosci., 2000, 12(6), 1882-1890.
    • (2000) Eur. J. Neurosci. , vol.12 , Issue.6 , pp. 1882-1890
    • Bastianetto, S.1    Ramassamy, C.2    Doré, S.3    Christen, Y.4    Poirier, J.5    Quirion, R.6
  • 76
    • 0035910374 scopus 로고    scopus 로고
    • The Ginkgo biloba extract egb 761 rescues the pc12 neuronal cells from beta-amyloid-induced cell death by inhibiting the formation of beta-amyloid-derived diffusible neurotoxic ligands
    • Yao, Z.; Drieu, K.; Papadopoulos, V. The Ginkgo biloba extract egb 761 rescues the pc12 neuronal cells from beta-amyloid-induced cell death by inhibiting the formation of beta-amyloid-derived diffusible neurotoxic ligands. Brain Res., 2001, 889(1-2), 181-190.
    • (2001) Brain Res. , vol.889 , Issue.1-2 , pp. 181-190
    • Yao, Z.1    Drieu, K.2    Papadopoulos, V.3
  • 77
    • 0030039729 scopus 로고    scopus 로고
    • Ginkgo biloba extract (egb 761) independently improves changes in passive avoidance learning and brain membrane fluidity in the aging mouse
    • Stoll, S.; Scheuer, K.; Pohl, O.; Müller, W. E. Ginkgo biloba extract (egb 761) independently improves changes in passive avoidance learning and brain membrane fluidity in the aging mouse. Pharmacopsychiatry, 1996, 29(4), 144-149.
    • (1996) Pharmacopsychiatry , vol.29 , Issue.4 , pp. 144-149
    • Stoll, S.1    Scheuer, K.2    Pohl, O.3    Müller, W.E.4
  • 79
    • 70549108840 scopus 로고    scopus 로고
    • Gene regulatory effects of ginkgo biloba extract and its flavonol and terpenelactone fractions in mouse brain
    • Augustin, S.; Rimbach, G.; Augustin, K.; Cermak, R.; Wolffram, S. Gene regulatory effects of ginkgo biloba extract and its flavonol and terpenelactone fractions in mouse brain. J. Clin. Biochem. Nutr., 2009, 45(3), 315-321.
    • (2009) J. Clin. Biochem. Nutr. , vol.45 , Issue.3 , pp. 315-321
    • Augustin, S.1    Rimbach, G.2    Augustin, K.3    Cermak, R.4    Wolffram, S.5
  • 80
    • 0030775196 scopus 로고    scopus 로고
    • Clinical efficacy of ginkgo biloba special extract egb 761 in dementia of the alzheimer type
    • Maurer, K.; Ihl, R.; Dierks, T.; Frölich, L. Clinical efficacy of ginkgo biloba special extract egb 761 in dementia of the alzheimer type. J. Psychiatr. Res., 31(6), 645-655.
    • J. Psychiatr. Res. , vol.31 , Issue.6 , pp. 645-655
    • Maurer, K.1    Ihl, R.2    Dierks, T.3    Frölich, L.4
  • 81
    • 28244446721 scopus 로고    scopus 로고
    • A randomized, double-blind, placebocontrolled trial of two doses of ginkgo biloba extract in dementia of the alzheimer's type
    • Schneider, L. S.; DeKosky, S. T.; Farlow, M. R.; Tariot, P. N.; Hoerr, R.; Kieser, M. A randomized, double-blind, placebocontrolled trial of two doses of ginkgo biloba extract in dementia of the alzheimer's type. Curr. Alzheimer Res., 2005, 2(5), 541-551.
    • (2005) Curr. Alzheimer Res. , vol.2 , Issue.5 , pp. 541-551
    • Schneider, L.S.1    DeKosky, S.T.2    Farlow, M.R.3    Tariot, P.N.4    Hoerr, R.5    Kieser, M.6
  • 82
    • 33747823312 scopus 로고    scopus 로고
    • Ginkgo biloba and donepezil: A comparison in the treatment of alzheimer's dementia in a randomized placebo-controlled double-blind study
    • Mazza, M.; Capuano, A.; Bria, P.; Mazza, S. Ginkgo biloba and donepezil: a comparison in the treatment of alzheimer's dementia in a randomized placebo-controlled double-blind study. Eur. J. Neurol., 2006, 13(9), 981-985.
    • (2006) Eur. J. Neurol. , vol.13 , Issue.9 , pp. 981-985
    • Mazza, M.1    Capuano, A.2    Bria, P.3    Mazza, S.4
  • 83
    • 0033837006 scopus 로고    scopus 로고
    • The Ameliorating effects of the cognitive-enhancing chinese herbs on scopolamine-induced amnesia in rats
    • Hsieh, M. T.; Peng, W. H.; Wu, C. R.; Wang, W. H. The Ameliorating effects of the cognitive-enhancing chinese herbs on scopolamine-induced amnesia in rats. Phytother. Res., 2000, 14(5), 375-377.
    • (2000) Phytother. Res. , vol.14 , Issue.5 , pp. 375-377
    • Hsieh, M.T.1    Peng, W.H.2    Wu, C.R.3    Wang, W.H.4
  • 84
    • 38049001548 scopus 로고    scopus 로고
    • Protective effects of berberine against low-density lipoprotein (ldl) oxidation and oxidized ldl-induced cytotoxicity on endothelial cells
    • Hsieh, Y.S.; Kuo, W.H.; Lin, T.W.; Chang, H.-R.; Lin, T.H.; Chen, P.N.; Chu, S.C. Protective effects of berberine against low-density lipoprotein (ldl) oxidation and oxidized ldl-induced cytotoxicity on endothelial cells. J. Agric. Food Chem., 2007, 55(25), 10437-10445.
    • (2007) J. Agric. Food Chem. , vol.55 , Issue.25 , pp. 10437-10445
    • Hsieh, Y.S.1    Kuo, W.H.2    Lin, T.W.3    Chang, H.-R.4    Lin, T.H.5    Chen, P.N.6    Chu, S.C.7
  • 85
    • 3843065565 scopus 로고    scopus 로고
    • Antiradical and antioxidant activities of alkaloids isolated from mahonia aquifolium. Structural aspects
    • Racková, L.; Májeková, M.; Kost'álová, D.; Stefek, M. Antiradical and antioxidant activities of alkaloids isolated from mahonia aquifolium. structural aspects. Bioorg. Med. Chem., 2004, 12(17), 4709-4715.
    • (2004) Bioorg. Med. Chem. , vol.12 , Issue.17 , pp. 4709-4715
    • Racková, L.1    Májeková, M.2    Kost'álová, D.3    Stefek, M.4
  • 86
    • 69149104713 scopus 로고    scopus 로고
    • Anti-alzheimer and antioxidant activities of coptidis rhizoma alkaloids
    • Jung, H. A.; Min, B.-S.; Yokozawa, T.; Lee, J.H.; Kim, Y. S.; Choi, J. S. Anti-alzheimer and antioxidant activities of coptidis rhizoma alkaloids. Biol. Pharm. Bull, 2009, 32(8), 1433-1438.
    • (2009) Biol. Pharm. Bull , vol.32 , Issue.8 , pp. 1433-1438
    • Jung, H.A.1    Min, B.-S.2    Yokozawa, T.3    Lee, J.H.4    Kim, Y.S.5    Choi, J.S.6
  • 87
    • 79952697907 scopus 로고    scopus 로고
    • Polygalae radix inhibits toxin-induced neuronal death in the parkinson's disease models
    • Choi, J. G.; Kim, H. G.; Kim, M. C.; Yang, W. M.; Huh, Y.; Kim, S. Y.; Oh, M. S. Polygalae radix inhibits toxin-induced neuronal death in the parkinson's disease models. J. Ethnopharmacol., 2011, 134 (2), 414-421.
    • (2011) J. Ethnopharmacol. , vol.134 , Issue.2 , pp. 414-421
    • Choi, J.G.1    Kim, H.G.2    Kim, M.C.3    Yang, W.M.4    Huh, Y.5    Kim, S.Y.6    Oh, M.S.7
  • 88
    • 16344389225 scopus 로고    scopus 로고
    • Pharmacological properties of n-095, a drug containing red ginseng, polygala root, saffron, antelope horn and aloe wood
    • Inoue, E.; Shimizu, Y.; Shoji, M.; Tsuchida, H.; Sano, Y.; Ito, C. Pharmacological properties of n-095, a drug containing red ginseng, polygala root, saffron, antelope horn and aloe wood. Am. J. Chin. Med., 2005, 33(1), 49-60.
    • (2005) Am. J. Chin. Med. , vol.33 , Issue.1 , pp. 49-60
    • Inoue, E.1    Shimizu, Y.2    Shoji, M.3    Tsuchida, H.4    Sano, Y.5    Ito, C.6
  • 89
    • 4043151473 scopus 로고    scopus 로고
    • Tenuigenin treatment decreases secretion of the alzheimer's disease amyloid beta-protein in cultured cells
    • Jia, H.; Jiang, Y.; Ruan, Y.; Zhang, Y.; Ma, X.; Zhang, J.; Beyreuther, K.; Tu, P.; Zhang, D. Tenuigenin treatment decreases secretion of the alzheimer's disease amyloid beta-protein in cultured cells. Neurosci. Lett, 2004, 367(1), 123-128.
    • (2004) Neurosci. Lett , vol.367 , Issue.1 , pp. 123-128
    • Jia, H.1    Jiang, Y.2    Ruan, Y.3    Zhang, Y.4    Ma, X.5    Zhang, J.6    Beyreuther, K.7    Tu, P.8    Zhang, D.9
  • 90
    • 67650470744 scopus 로고    scopus 로고
    • Tenuifolin, an extract derived from tenuigenin, inhibits amyloid-β secretion in vitro
    • Lv, J.; Jia, H.; Jiang, Y.; Ruan, Y.; Liu, Z.; Yue, W.; Beyreuther, K.; Tu, P.; Zhang, D. Tenuifolin, an extract derived from tenuigenin, inhibits amyloid-β secretion in vitro. Acta Physiol., 2009, 196, 419-425.
    • (2009) Acta Physiol. , vol.196 , pp. 419-425
    • Lv, J.1    Jia, H.2    Jiang, Y.3    Ruan, Y.4    Liu, Z.5    Yue, W.6    Beyreuther, K.7    Tu, P.8    Zhang, D.9
  • 91
    • 0025779179 scopus 로고
    • Solution structures of beta peptide and its constituent fragments: Relation to amyloid deposition
    • Barrow, C. J.; Zagorski, M. G. Solution structures of beta peptide and its constituent fragments: relation to amyloid deposition. Science, 1991, 253(5016), 179-182.
    • (1991) Science , vol.253 , Issue.5016 , pp. 179-182
    • Barrow, C.J.1    Zagorski, M.G.2
  • 92
    • 0031695652 scopus 로고    scopus 로고
    • Activation of tau protein kinase i/glycogen synthase kinase-3beta by amyloid beta peptide (25-35) enhances phosphorylation of tau in hippocampal neurons
    • Takashima, A.; Honda, T.; Yasutake, K.; Michel, G.; Murayama, O.; Murayama, M.; Ishiguro, K.; Yamaguchi, H. Activation of tau protein kinase i/glycogen synthase kinase-3beta by amyloid beta peptide (25-35) enhances phosphorylation of tau in hippocampal neurons. Neurosci. Res., 1998, 31(4), 317-323.
    • (1998) Neurosci. Res. , vol.31 , Issue.4 , pp. 317-323
    • Takashima, A.1    Honda, T.2    Yasutake, K.3    Michel, G.4    Murayama, O.5    Murayama, M.6    Ishiguro, K.7    Yamaguchi, H.8
  • 93
    • 7244236841 scopus 로고    scopus 로고
    • A modified beta-amyloid hypothesis: Intraneuronal accumulation of the beta-amyloid peptide - The first step of a fatal cascade
    • Wirths, O.; Multhaup, G.; Bayer, T. A. A modified beta-amyloid hypothesis: intraneuronal accumulation of the beta-amyloid peptide - the first step of a fatal cascade. J. Neurochem., 2004, 91(3), 513-520.
    • (2004) J. Neurochem. , vol.91 , Issue.3 , pp. 513-520
    • Wirths, O.1    Multhaup, G.2    Bayer, T.A.3
  • 94
    • 0041667974 scopus 로고    scopus 로고
    • Anti-inflammatory and analgesic effects of paeonol in carrageenan-evoked thermal hyperalgesia
    • Chou, T.C. Anti-inflammatory and analgesic effects of paeonol in carrageenan-evoked thermal hyperalgesia. Br. J. Pharmacol., 2003, 139(6), 1146-1152.
    • (2003) Br. J. Pharmacol. , vol.139 , Issue.6 , pp. 1146-1152
    • Chou, T.C.1
  • 96
    • 79952010449 scopus 로고    scopus 로고
    • Baicalein inhibits formation of α -synuclein oligomers within living cells and prevents aβ peptide fibrillation and oligomerisation
    • Lu, J.H.; Ardah, M. T.; Durairajan, S. S. K.; Liu, L.F.; Xie, L.X.; Fong, W.F. D.; Hasan, M. Y.; Huang, J.D.; El-Agnaf, O. M. A.; Li, M. Baicalein inhibits formation of α -synuclein oligomers within living cells and prevents aβ peptide fibrillation and oligomerisation. Chembiochem., 2011, 12(4), 615-624.
    • (2011) Chembiochem. , vol.12 , Issue.4 , pp. 615-624
    • Lu, J.H.1    Ardah, M.T.2    Durairajan, S.S.K.3    Liu, L.F.4    Xie, L.X.5    Fong, W.F.D.6    Hasan, M.Y.7    Huang, J.D.8    El-Agnaf, O.M.A.9    Li, M.10
  • 97
    • 11844260060 scopus 로고    scopus 로고
    • Chemistry and biological activities of caffeic acid derivatives from salvia miltiorrhiza
    • Jiang, R.-W.; Lau, K.-M.; Hon, P.-M.; Mak, T. C. W.; Woo, K.-S.; Fung, K.-P. Chemistry and biological activities of caffeic acid derivatives from salvia miltiorrhiza. Curr. Med. Chem. 2005, 12 (2), 237-246.
    • (2005) Curr. Med. Chem. , vol.12 , Issue.2 , pp. 237-246
    • Jiang, R.-W.1    Lau, K.-M.2    Hon, P.-M.3    Mak, T.C.W.4    Woo, K.-S.5    Fung, K.-P.6
  • 98
    • 33746891189 scopus 로고    scopus 로고
    • Salvianolic acid b, an antioxidant from salvia miltiorrhiza, prevents abeta(25-35)-induced reduction in bprp in pC12 Cells
    • Lin, Y.H.; Liu, A.H.; Wu, H.L.; Westenbroek, C.; Song, Q.L.; Yu, H.M.; Ter Horst, G. J.; Li, X.J. Salvianolic acid b, an antioxidant from salvia miltiorrhiza, prevents abeta(25-35)-induced reduction in bprp in pC12 Cells. Biochem. Biophys. Res. Commun., 2006, 348(2), 593-599.
    • (2006) Biochem. Biophys. Res. Commun. , vol.348 , Issue.2 , pp. 593-599
    • Lin, Y.H.1    Liu, A.H.2    Wu, H.L.3    Westenbroek, C.4    Song, Q.L.5    Yu, H.M.6    Ter Horst, G.J.7    Li, X.J.8
  • 99
    • 38349160407 scopus 로고    scopus 로고
    • Salvianolic Acid B Inhibits aβ fibril formation and disaggregates preformed fibrils and protects against aβ-induced cytotoxicty
    • Durairajan, S. S. K.; Yuan, Q.; Xie, L.; Chan, W. S.; Kum, W. F.; Koo, I.; Liu, C.; Song, Y.; Huang, J. D.; Klein, W. L.; Li, M. Salvianolic Acid B Inhibits aβ fibril formation and disaggregates preformed fibrils and protects against aβ-induced cytotoxicty. Neurochem. Int., 2008, 52, 741-750.
    • (2008) Neurochem. Int. , vol.52 , pp. 741-750
    • Durairajan, S.S.K.1    Yuan, Q.2    Xie, L.3    Chan, W.S.4    Kum, W.F.5    Koo, I.6    Liu, C.7    Song, Y.8    Huang, J.D.9    Klein, W.L.10    Li, M.11
  • 101
    • 33645058893 scopus 로고    scopus 로고
    • Use of ginseng in medicine with emphasis on neurodegenerative disorders
    • Radad, K.; Gille, G.; Liu, L.; Rausch, W.-D. Use of ginseng in medicine with emphasis on neurodegenerative disorders. J. Pharmacol. Sci. 2006, 100 (3), 175-186.
    • (2006) J. Pharmacol. Sci. , vol.100 , Issue.3 , pp. 175-186
    • Radad, K.1    Gille, G.2    Liu, L.3    Rausch, W.-D.4
  • 102
    • 0025753762 scopus 로고
    • Anti-Lipid Peroxilative Effect of Ginsenoside Rb1 and Rg1
    • Deng, H. L.; Zhang, J. T. Anti-Lipid Peroxilative Effect of Ginsenoside Rb1 and Rg1. Chin. Med. J. (Engl). 1991, 104(5), 395-398.
    • (1991) Chin. Med. J. (Engl) , vol.104 , Issue.5 , pp. 395-398
    • Deng, H.L.1    Zhang, J.T.2
  • 103
    • 0029456090 scopus 로고
    • Protective effects of ginsenoside rb1 and rg1 on cultured hippocampal neurons
    • Liu, M.; Zhang, J. T. Protective effects of ginsenoside rb1 and rg1 on cultured hippocampal neurons. Yao Xue Xue Bao, 1995, 30(9), 674-678.
    • (1995) Yao Xue Xue Bao , vol.30 , Issue.9 , pp. 674-678
    • Liu, M.1    Zhang, J.T.2
  • 104
    • 0031596324 scopus 로고    scopus 로고
    • Ginsenosides rb1 and rg3 protect cultured rat cortical cells from glutamateinduced neurodegeneration
    • Kim, Y. C.; Kim, S. R.; Markelonis, G. J.; Oh, T. H. Ginsenosides rb1 and rg3 protect cultured rat cortical cells from glutamateinduced neurodegeneration. J. Neurosci. Res., 1998, 53(4), 426-432.
    • (1998) J. Neurosci. Res. , vol.53 , Issue.4 , pp. 426-432
    • Kim, Y.C.1    Kim, S.R.2    Markelonis, G.J.3    Oh, T.H.4
  • 105
    • 33745820864 scopus 로고    scopus 로고
    • Ginsenoside re attenuate beta-amyloid and serum-free induced neurotoxicity in pc12 cells
    • Ji, Z. N.; Dong, T. T. X.; Ye, W. C.; Choi, R. C.; Lo, C. K.; Tsim, K. W. K. Ginsenoside re attenuate beta-amyloid and serum-free induced neurotoxicity in pc12 cells. J. Ethnopharmacol., 2006, 107(1), 48-52.
    • (2006) J. Ethnopharmacol. , vol.107 , Issue.1 , pp. 48-52
    • Ji, Z.N.1    Dong, T.T.X.2    Ye, W.C.3    Choi, R.C.4    Lo, C.K.5    Tsim, K.W.K.6
  • 106
    • 34247230363 scopus 로고    scopus 로고
    • Protective effects of ginsenoside rg2 against glutamate-induced neurotoxicity in pc12 cells
    • Li, N.; Liu, B.; Dluzen, D. E.; Jin, Y. Protective effects of ginsenoside rg2 against glutamate-induced neurotoxicity in pc12 cells. J. Ethnopharmacol., 2007, 111(3), 458-463.
    • (2007) J. Ethnopharmacol. , vol.111 , Issue.3 , pp. 458-463
    • Li, N.1    Liu, B.2    Dluzen, D.E.3    Jin, Y.4
  • 107
    • 75149115354 scopus 로고    scopus 로고
    • Icariin inhibits neurotoxicity of beta-amyloid by upregulating cocaine-regulated and amphetamine-regulated transcripts
    • Sha, D.; Li, L.; Ye, L.; Liu, R.; Xu, Y. Icariin inhibits neurotoxicity of beta-amyloid by upregulating cocaine-regulated and amphetamine-regulated transcripts. Neuroreport, 2009, 20(17), 1564-1567.
    • (2009) Neuroreport , vol.20 , Issue.17 , pp. 1564-1567
    • Sha, D.1    Li, L.2    Ye, L.3    Liu, R.4    Xu, Y.5
  • 108
    • 77951218076 scopus 로고    scopus 로고
    • Icariin inhibits the increased inward calcium currents induced by amyloid-beta(25-35) peptide in ca1 pyramidal neurons of neonatal rat hippocampal slice
    • Li, L.; Tsai, H.-J.; Li, L.; Wang, X.M. Icariin inhibits the increased inward calcium currents induced by amyloid-beta(25-35) peptide in ca1 pyramidal neurons of neonatal rat hippocampal slice. Am. J. Chin. Med., 2010, 38(1), 113-125.
    • (2010) Am. J. Chin. Med. , vol.38 , Issue.1 , pp. 113-125
    • Li, L.1    Tsai, H.-J.2    Li, L.3    Wang, X.M.4
  • 109
    • 67650690570 scopus 로고    scopus 로고
    • Protective effects of ginkgo biloba extract (egb761) and its constituents quercetin and ginkgolide b against beta-amyloid peptide-induced toxicity in sh-sy5Y Cells
    • Shi, C.; Zhao, L.; Zhu, B.; Li, Q.; Yew, D. T.; Yao, Z.; Xu, J. Protective effects of ginkgo biloba extract (egb761) and its constituents quercetin and ginkgolide b against beta-amyloid peptide-induced toxicity in sh-sy5Y Cells. Chem. Biol. Interact., 2009, 181(1), 115-123.
    • (2009) Chem. Biol. Interact. , vol.181 , Issue.1 , pp. 115-123
    • Shi, C.1    Zhao, L.2    Zhu, B.3    Li, Q.4    Yew, D.T.5    Yao, Z.6    Xu, J.7
  • 110
    • 77349087319 scopus 로고    scopus 로고
    • Inhibitory effect of ethanol extract of magnolia officinalis and 4-o-methylhonokiol on memory impairment and neuronal toxicity induced by beta-amyloid
    • Lee, J. W.; Lee, Y. K.; Lee, B. J.; Nam, S.Y.; Lee, S. Il; Kim, Y. H.; Kim, K. H.; Oh, K.W.; Hong, J. T. Inhibitory effect of ethanol extract of magnolia officinalis and 4-o-methylhonokiol on memory impairment and neuronal toxicity induced by beta-amyloid. Pharmacol. Biochem. Behav., 2010, 95(1), 31-40.
    • (2010) Pharmacol. Biochem. Behav. , vol.95 , Issue.1 , pp. 31-40
    • Lee, J.W.1    Lee, Y.K.2    Lee, B.J.3    Nam, S.Y.4    Lee Il, S.5    Kim, Y.H.6    Kim, K.H.7    Oh, K.W.8    Hong, J.T.9
  • 111
    • 42149162262 scopus 로고    scopus 로고
    • Protective effect of (-) clausenamide against neurotoxicity induced by okadaic acid and beta-amyloid peptide 25-35
    • Zhang, J.; Cheng, Y.; Zhang, J.T. Protective effect of (-) clausenamide against neurotoxicity induced by okadaic acid and beta-amyloid peptide 25-35. Yao Xue Xue Bao, 2007, 42(9), 935-942.
    • (2007) Yao Xue Xue Bao , vol.42 , Issue.9 , pp. 935-942
    • Zhang, J.1    Cheng, Y.2    Zhang, J.T.3
  • 112
    • 0031902295 scopus 로고    scopus 로고
    • Alzheimer's disease: Etiologies, pathophysiology, cognitive reserve, and treatment opportunities
    • discussion S65-S67
    • Cummings, J. L.; Vinters, H. V; Cole, G. M.; Khachaturian, Z. S. Alzheimer's disease: etiologies, pathophysiology, cognitive reserve, and treatment opportunities. Neurology, 1998, 51(1 Suppl 1), S2-S17; discussion S65-S67.
    • (1998) Neurology , vol.51 , Issue.1 , pp. S2-S17
    • Cummings, J.L.1    Vinters, H.V.2    Cole, G.M.3    Khachaturian, Z.S.4
  • 113
    • 33747177369 scopus 로고    scopus 로고
    • Signaling mechanisms underlying abeta toxicity: Potential therapeutic targets for alzheimer's disease
    • Smith, W. W.; Gorospe, M.; Kusiak, J. W. Signaling mechanisms underlying abeta toxicity: potential therapeutic targets for alzheimer's disease. CNS Neurol. Disord. Drug Targets, 2006, 5(3), 355-361.
    • (2006) CNS Neurol. Disord. Drug Targets , vol.5 , Issue.3 , pp. 355-361
    • Smith, W.W.1    Gorospe, M.2    Kusiak, J.W.3
  • 114
    • 0030248270 scopus 로고    scopus 로고
    • Microglial cells internalize aggregates of the alzheimer's disease amyloid betaprotein via a scavenger receptor
    • Paresce, D. M.; Ghosh, R. N.; Maxfield, F. R. Microglial cells internalize aggregates of the alzheimer's disease amyloid betaprotein via a scavenger receptor. Neuron, 1996, 17(3), 553-565.
    • (1996) Neuron , vol.17 , Issue.3 , pp. 553-565
    • Paresce, D.M.1    Ghosh, R.N.2    Maxfield, F.R.3
  • 115
    • 0041926623 scopus 로고    scopus 로고
    • A new role for astrocytes: Betaamyloid homeostasis and degradation
    • Nicoll, J. A. R.; Weller, R. O. A new role for astrocytes: betaamyloid homeostasis and degradation. Trends Mol. Med., 2003, 9(7), 281-282.
    • (2003) Trends Mol. Med. , vol.9 , Issue.7 , pp. 281-282
    • Nicoll, J.A.R.1    Weller, R.O.2
  • 116
    • 0036685522 scopus 로고    scopus 로고
    • Inflammation in neurodegenerative disease - A double-edged sword
    • Wyss-Coray, T.; Mucke, L. Inflammation in neurodegenerative disease - a double-edged sword. Neuron, 2002, 35(3), 419-432.
    • (2002) Neuron , vol.35 , Issue.3 , pp. 419-432
    • Wyss-Coray, T.1    Mucke, L.2
  • 118
    • 0037336701 scopus 로고    scopus 로고
    • Interleukin-1 mediates pathological effects of microglia on tau phosphorylation and on synaptophysin synthesis in cortical neurons through a p38- mapk pathway
    • Li, Y.; Liu, L.; Barger, S. W.; Griffin, W. S. T. Interleukin-1 mediates pathological effects of microglia on tau phosphorylation and on synaptophysin synthesis in cortical neurons through a p38- mapk pathway. J. Neurosci., 2003, 23(5), 1605-1611.
    • (2003) J. Neurosci. , vol.23 , Issue.5 , pp. 1605-1611
    • Li, Y.1    Liu, L.2    Barger, S.W.3    Griffin, W.S.T.4
  • 120
    • 0035903037 scopus 로고    scopus 로고
    • The plant flavonoid wogonin suppresses death of activated c6 rat glial cells by inhibiting nitric oxide production
    • Kim, H.; Kim, Y. S.; Kim, S. Y.; Suk, K. The plant flavonoid wogonin suppresses death of activated c6 rat glial cells by inhibiting nitric oxide production. Neurosci. Lett., 2001, 309 (1), 67-71.
    • (2001) Neurosci. Lett. , vol.309 , Issue.1 , pp. 67-71
    • Kim, H.1    Kim, Y.S.2    Kim, S.Y.3    Suk, K.4
  • 121
    • 1642553221 scopus 로고    scopus 로고
    • Flavonoid wogonin from medicinal herb is neuroprotective by inhibiting inflammatory activation of microglia
    • Lee, H.; Kim, Y. O.; Kim, H.; Kim, S. Y.; Noh, H. S.; Kang, S. S.; Cho, G. J.; Choi, W. S.; Suk, K. Flavonoid wogonin from medicinal herb is neuroprotective by inhibiting inflammatory activation of microglia. FASEB J., 2003, 17(13), 1943-1944.
    • (2003) FASEB J. , vol.17 , Issue.13 , pp. 1943-1944
    • Lee, H.1    Kim, Y.O.2    Kim, H.3    Kim, S.Y.4    Noh, H.S.5    Kang, S.S.6    Cho, G.J.7    Choi, W.S.8    Suk, K.9
  • 122
    • 20044389086 scopus 로고    scopus 로고
    • Inhibition of microglial activation by the herbal flavonoid baicalein attenuates inflammation-mediated degeneration of dopaminergic neurons
    • Li, F.Q.; Wang, T.; Pei, Z.; Liu, B.; Hong, J.S. Inhibition of microglial activation by the herbal flavonoid baicalein attenuates inflammation-mediated degeneration of dopaminergic neurons. J. Neural Transm., 2005, 112(3), 331-347.
    • (2005) J. Neural Transm. , vol.112 , Issue.3 , pp. 331-347
    • Li, F.Q.1    Wang, T.2    Pei, Z.3    Liu, B.4    Hong, J.S.5
  • 123
    • 0037404413 scopus 로고    scopus 로고
    • Flavonoid baicalein attenuates activation-induced cell death of brain microglia
    • Suk, K.; Lee, H.; Kang, S. S.; Cho, G. J.; Choi, W. S. Flavonoid baicalein attenuates activation-induced cell death of brain microglia. J. Pharmacol. Exp. Ther., 2003, 305(2), 638-645.
    • (2003) J. Pharmacol. Exp. Ther. , vol.305 , Issue.2 , pp. 638-645
    • Suk, K.1    Lee, H.2    Kang, S.S.3    Cho, G.J.4    Choi, W.S.5
  • 124
    • 0042662901 scopus 로고    scopus 로고
    • Immunosuppressive and anti-inflammatory mechanisms of triptolide, the principal active diterpenoid from the chinese medicinal herb tripterygium wilfordii hook. f
    • Qiu, D.; Kao, P. N. Immunosuppressive and anti-inflammatory mechanisms of triptolide, the principal active diterpenoid from the chinese medicinal herb tripterygium wilfordii hook. f. Drugs R. D., 2003, 4(1), 1-18.
    • (2003) Drugs R. D. , vol.4 , Issue.1 , pp. 1-18
    • Qiu, D.1    Kao, P.N.2
  • 125
    • 14744284455 scopus 로고    scopus 로고
    • Triptolide Protects dopaminergic neurons from inflammationmediated damage induced by lipopolysaccharide intranigral injection
    • Zhou, H.F.; Liu, X.Y.; Niu, D.B.; Li, F.Q.; He, Q.H.; Wang, X.M. Triptolide Protects dopaminergic neurons from inflammationmediated damage induced by lipopolysaccharide intranigral injection. Neurobiol. Dis., 2005, 18 (3), 441-449.
    • (2005) Neurobiol. Dis. , vol.18 , Issue.3 , pp. 441-449
    • Zhou, H.F.1    Liu, X.Y.2    Niu, D.B.3    Li, F.Q.4    He, Q.H.5    Wang, X.M.6
  • 126
    • 53749093009 scopus 로고    scopus 로고
    • Triptolide inhibits cox-2 expression and pge2 release by suppressing the activity of nfkappab and jnk in lps-treated microglia
    • Gong, Y.; Xue, B.; Jiao, J.; Jing, L.; Wang, X. Triptolide inhibits cox-2 expression and pge2 release by suppressing the activity of nfkappab and jnk in lps-treated microglia. J. Neurochem., 2008, 107(3), 779-788.
    • (2008) J. Neurochem. , vol.107 , Issue.3 , pp. 779-788
    • Gong, Y.1    Xue, B.2    Jiao, J.3    Jing, L.4    Wang, X.5
  • 127
    • 31144450053 scopus 로고    scopus 로고
    • Current pharmacotherapy for alzheimer's Disease
    • Lleó, A.; Greenberg, S. M.; Growdon, J. H. Current pharmacotherapy for alzheimer's Disease. Annu. Rev. Med., 2006, 57, 513-533.
    • (2006) Annu. Rev. Med. , vol.57 , pp. 513-533
    • Lleó, A.1    Greenberg, S.M.2    Growdon, J.H.3
  • 128
    • 84922342912 scopus 로고
    • The structures of huperzine a and b, two new alkaloids exhibiting marked anticholinesterase activity
    • Liu, J.S.; Zhu, Y.L.; Yu, C.M.; Zhou, Y.Z.; Han, Y.Y.; Wu, F.W.; Qi, B.F. The structures of huperzine a and b, two new alkaloids exhibiting marked anticholinesterase activity. Can. J. Chem., 1986, 64(lc), 837-839.
    • (1986) Can. J. Chem. , vol.64 , Issue.LC , pp. 837-839
    • Liu, J.S.1    Zhu, Y.L.2    Yu, C.M.3    Zhou, Y.Z.4    Han, Y.Y.5    Wu, F.W.6    Qi, B.F.7
  • 129
    • 4444293556 scopus 로고    scopus 로고
    • Anticholinesterase activity in an alkaloid extract of huperzia saururus
    • Ortega, M. G.; Agnese, A. M.; Cabrera, J. L. Anticholinesterase activity in an alkaloid extract of huperzia saururus. Phytomedicine, 2004, 11(6), 539-543.
    • (2004) Phytomedicine , vol.11 , Issue.6 , pp. 539-543
    • Ortega, M.G.1    Agnese, A.M.2    Cabrera, J.L.3
  • 130
    • 0037195557 scopus 로고    scopus 로고
    • Effects of huperzine a on acetylcholinesterase isoforms in vitro: Comparison with tacrine, donepezil, rivastigmine and physostigmine
    • Zhao, Q.; Tang, X. C. Effects of huperzine a on acetylcholinesterase isoforms in vitro: comparison with tacrine, donepezil, rivastigmine and physostigmine. Eur. J. Pharmacol., 2002, 455(2-3), 101-107.
    • (2002) Eur. J. Pharmacol. , vol.455 , Issue.2-3 , pp. 101-107
    • Zhao, Q.1    Tang, X.C.2
  • 131
    • 0026752611 scopus 로고
    • Mechanism of Inhibition of Cholinesterases by Huperzine A
    • Ashani, Y.; Peggins, J. O.; Doctor, B. P. Mechanism of Inhibition of Cholinesterases by Huperzine A. Biochem. Biophys. Res. Commun., 1992, 184(2), 719-726.
    • (1992) Biochem. Biophys. Res. Commun. , vol.184 , Issue.2 , pp. 719-726
    • Ashani, Y.1    Peggins, J.O.2    Doctor, B.P.3
  • 133
    • 34248589627 scopus 로고    scopus 로고
    • Huperzine a in rat plasma and csf following intranasal administration
    • Yue, P.; Tao, T.; Zhao, Y.; Ren, J.; Chai, X. Huperzine a in rat plasma and csf following intranasal administration. Int. J. Pharm., 2007, 337(1-2), 127-132.
    • (2007) Int. J. Pharm. , vol.337 , Issue.1-2 , pp. 127-132
    • Yue, P.1    Tao, T.2    Zhao, Y.3    Ren, J.4    Chai, X.5
  • 134
    • 33744931940 scopus 로고    scopus 로고
    • Pharmacokinetics of huperzine a in dogs following single intravenous and oral administrations
    • Chu, D.; Liu, W.; Li, Y.; Li, P.; Gu, J.; Liu, K. Pharmacokinetics of huperzine a in dogs following single intravenous and oral administrations. Planta Med., 2006, 72(6), 552-555.
    • (2006) Planta Med. , vol.72 , Issue.6 , pp. 552-555
    • Chu, D.1    Liu, W.2    Li, Y.3    Li, P.4    Gu, J.5    Liu, K.6
  • 135
    • 73349120649 scopus 로고    scopus 로고
    • Pharmacokinetic behavior of huperzine a in plasma and cerebrospinal fluid after intranasal administration in rats
    • Wang, Q.; Chen, G. Pharmacokinetic behavior of huperzine a in plasma and cerebrospinal fluid after intranasal administration in rats. Biopharm. Drug Dispos., 2009, 30(9), 551-555.
    • (2009) Biopharm. Drug Dispos. , vol.30 , Issue.9 , pp. 551-555
    • Wang, Q.1    Chen, G.2
  • 136
    • 0034625561 scopus 로고    scopus 로고
    • Protective effects of huperzine a on beta-amyloid(25-35) induced oxidative injury in rat pheochromocytoma cells
    • Xiao, X. Q.; Wang, R.; Han, Y. F.; Tang, X. C. Protective effects of huperzine a on beta-amyloid(25-35) induced oxidative injury in rat pheochromocytoma cells. Neurosci. Lett., 2000, 286(3), 155-158.
    • (2000) Neurosci. Lett. , vol.286 , Issue.3 , pp. 155-158
    • Xiao, X.Q.1    Wang, R.2    Han, Y.F.3    Tang, X.C.4
  • 137
    • 0035876056 scopus 로고    scopus 로고
    • Huperzine a attenuates cognitive dysfunction and neuronal degeneration caused by betaamyloid protein-(1-40) in rat
    • Wang, R.; Zhang, H. Y.; Tang, X. C. Huperzine a attenuates cognitive dysfunction and neuronal degeneration caused by betaamyloid protein-(1-40) in rat. Eur. J. Pharmacol. 2001, 421(3), 149-156.
    • (2001) Eur. J. Pharmacol. , vol.421 , Issue.3 , pp. 149-156
    • Wang, R.1    Zhang, H.Y.2    Tang, X.C.3
  • 138
    • 84884528895 scopus 로고    scopus 로고
    • Huperzine a for alzheimer's disease: A systematic review and meta-analysis of randomized clinical trials
    • Yang, G.; Wang, Y.; Tian, J.; Liu, J.P. Huperzine a for alzheimer's disease: a systematic review and meta-analysis of randomized clinical trials. PLoS One, 2013, 8(9), e74916.
    • (2013) PLoS One , vol.8 , Issue.9
    • Yang, G.1    Wang, Y.2    Tian, J.3    Liu, J.P.4
  • 139
    • 20944446415 scopus 로고    scopus 로고
    • Neuroprotective effects of huperzine a
    • Wang, R.; Tang, X. C. Neuroprotective effects of huperzine a. Neurosignals, 2005, 14(1-2), 71-82.
    • (2005) Neurosignals , vol.14 , Issue.1-2 , pp. 71-82
    • Wang, R.1    Tang, X.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.