메뉴 건너뛰기




Volumn 5, Issue 2, 2014, Pages 83-92

Flavonoids as therapeutic compounds targeting key proteins involved in Alzheimer's disease

Author keywords

Alzheimer's disease; amyloid beta; amyloid precursor protein; BACE 1; Flavonoids; signaling; tau

Indexed keywords

ALZHEIMER DISEASE; AMYLOID BETA-PEPTIDES; AMYLOID BETA-PROTEIN PRECURSOR; AMYLOID PRECURSOR PROTEIN SECRETASES; FLAVONOIDS; GLYCOGEN SYNTHASE KINASE 3; HUMANS; MITOGEN-ACTIVATED PROTEIN KINASES; PHOSPHATIDYLINOSITOL 3-KINASE; PROTEIN-SERINE-THREONINE KINASES; TAU PROTEINS;

EID: 84894469764     PISSN: None     EISSN: 19487193     Source Type: Journal    
DOI: 10.1021/cn400213r     Document Type: Review
Times cited : (165)

References (127)
  • 1
    • 79953854897 scopus 로고    scopus 로고
    • Alzheimer's disease: The challenge of the second century
    • Holtzman, D. M., Morris, J. C., and Goate, A. M. (2011) Alzheimer's disease: the challenge of the second century Sci. Transl. Med. 3, 77sr71
    • (2011) Sci. Transl. Med. , vol.3
    • Holtzman, D.M.1    Morris, J.C.2    Goate, A.M.3
  • 3
    • 0032211830 scopus 로고    scopus 로고
    • The cell biology of beta-amyloid precursor protein and presenilin in Alzheimer's disease
    • Selkoe, D. J. (1998) The cell biology of beta-amyloid precursor protein and presenilin in Alzheimer's disease Trends Cell Biol. 8, 447-453
    • (1998) Trends Cell Biol. , vol.8 , pp. 447-453
    • Selkoe, D.J.1
  • 4
    • 28944433580 scopus 로고    scopus 로고
    • The interplay of neurotransmitters in Alzheimer's disease
    • Francis, P. T. (2005) The interplay of neurotransmitters in Alzheimer's disease CNS Spectrums 10, 6-9
    • (2005) CNS Spectrums , vol.10 , pp. 6-9
    • Francis, P.T.1
  • 5
    • 0025651974 scopus 로고
    • Neurotransmitter changes in Alzheimer's disease: Implications to diagnostics and therapy
    • Reinikainen, K. J., Soininen, H., and Riekkinen, P. J. (1990) Neurotransmitter changes in Alzheimer's disease: implications to diagnostics and therapy J. Neurosci. Res. 27, 576-586
    • (1990) J. Neurosci. Res. , vol.27 , pp. 576-586
    • Reinikainen, K.J.1    Soininen, H.2    Riekkinen, P.J.3
  • 6
    • 33747760358 scopus 로고    scopus 로고
    • Hippocampal synaptic loss in early Alzheimer's disease and mild cognitive impairment
    • Scheff, S. W., Price, D. A., Schmitt, F. A., and Mufson, E. J. (2006) Hippocampal synaptic loss in early Alzheimer's disease and mild cognitive impairment Neurobiol. Aging 27, 1372-1384
    • (2006) Neurobiol. Aging , vol.27 , pp. 1372-1384
    • Scheff, S.W.1    Price, D.A.2    Schmitt, F.A.3    Mufson, E.J.4
  • 8
    • 0027240503 scopus 로고
    • Isolation and characterization of APLP2 encoding a homologue of the Alzheimer's associated amyloid beta protein precursor
    • Wasco, W., Gurubhagavatula, S., Paradis, M. D., Romano, D. M., Sisodia, S. S., Hyman, B. T., Neve, R. L., and Tanzi, R. E. (1993) Isolation and characterization of APLP2 encoding a homologue of the Alzheimer's associated amyloid beta protein precursor Nat. Genet. 5, 95-100
    • (1993) Nat. Genet. , vol.5 , pp. 95-100
    • Wasco, W.1    Gurubhagavatula, S.2    Paradis, M.D.3    Romano, D.M.4    Sisodia, S.S.5    Hyman, B.T.6    Neve, R.L.7    Tanzi, R.E.8
  • 9
    • 0033972608 scopus 로고    scopus 로고
    • What the evolution of the amyloid protein precursor supergene family tells us about its function
    • Coulson, E. J., Paliga, K., Beyreuther, K., and Masters, C. L. (2000) What the evolution of the amyloid protein precursor supergene family tells us about its function Neurochem. Int. 36, 175-184
    • (2000) Neurochem. Int. , vol.36 , pp. 175-184
    • Coulson, E.J.1    Paliga, K.2    Beyreuther, K.3    Masters, C.L.4
  • 10
    • 0032760270 scopus 로고    scopus 로고
    • It all sticks together - The APP-related family of proteins and Alzheimer's disease
    • Bayer, T. A., Cappai, R., Masters, C. L., Beyreuther, K., and Multhaup, G. (1999) It all sticks together - the APP-related family of proteins and Alzheimer's disease Mol. Psychiatry 4, 524-528
    • (1999) Mol. Psychiatry , vol.4 , pp. 524-528
    • Bayer, T.A.1    Cappai, R.2    Masters, C.L.3    Beyreuther, K.4    Multhaup, G.5
  • 13
    • 0026721943 scopus 로고
    • Beta-amyloid precursor protein cleavage by a membrane-bound protease
    • Sisodia, S. S. (1992) Beta-amyloid precursor protein cleavage by a membrane-bound protease Proc. Natl. Acad. Sci. U.S.A. 89, 6075-6079
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 6075-6079
    • Sisodia, S.S.1
  • 14
    • 0027389118 scopus 로고
    • Identification of the Alzheimer beta/A4 amyloid precursor protein in clathrin-coated vesicles purified from PC12 cells
    • Nordstedt, C., Caporaso, G. L., Thyberg, J., Gandy, S. E., and Greengard, P. (1993) Identification of the Alzheimer beta/A4 amyloid precursor protein in clathrin-coated vesicles purified from PC12 cells J. Biol. Chem. 268, 608-612
    • (1993) J. Biol. Chem. , vol.268 , pp. 608-612
    • Nordstedt, C.1    Caporaso, G.L.2    Thyberg, J.3    Gandy, S.E.4    Greengard, P.5
  • 15
    • 0028351791 scopus 로고
    • Morphologic and biochemical analysis of the intracellular trafficking of the Alzheimer beta/A4 amyloid precursor protein
    • Caporaso, G. L., Takei, K., Gandy, S. E., Matteoli, M., Mundigl, O., Greengard, P., and De Camilli, P. (1994) Morphologic and biochemical analysis of the intracellular trafficking of the Alzheimer beta/A4 amyloid precursor protein J. Neurosci. 14, 3122-3138
    • (1994) J. Neurosci. , vol.14 , pp. 3122-3138
    • Caporaso, G.L.1    Takei, K.2    Gandy, S.E.3    Matteoli, M.4    Mundigl, O.5    Greengard, P.6    De Camilli, P.7
  • 21
    • 0345826094 scopus 로고    scopus 로고
    • BACE1 suppression by RNA interference in primary cortical neurons
    • Kao, S. C., Krichevsky, A. M., Kosik, K. S., and Tsai, L. H. (2004) BACE1 suppression by RNA interference in primary cortical neurons J. Biol. Chem. 279, 1942-1949
    • (2004) J. Biol. Chem. , vol.279 , pp. 1942-1949
    • Kao, S.C.1    Krichevsky, A.M.2    Kosik, K.S.3    Tsai, L.H.4
  • 22
    • 0346055155 scopus 로고    scopus 로고
    • BACE1 deficiency rescues memory deficits and cholinergic dysfunction in a mouse model of Alzheimer's disease
    • Ohno, M., Sametsky, E. A., Younkin, L. H., Oakley, H., Younkin, S. G., Citron, M., Vassar, R., and Disterhoft, J. F. (2004) BACE1 deficiency rescues memory deficits and cholinergic dysfunction in a mouse model of Alzheimer's disease Neuron 41, 27-33
    • (2004) Neuron , vol.41 , pp. 27-33
    • Ohno, M.1    Sametsky, E.A.2    Younkin, L.H.3    Oakley, H.4    Younkin, S.G.5    Citron, M.6    Vassar, R.7    Disterhoft, J.F.8
  • 27
    • 0029894683 scopus 로고    scopus 로고
    • Protein folding, nucleation phenomena and delayed neurodegeneration in Alzheimer's disease
    • Fox, N., Harvey, R. J., and Rossor, M. N. (1996) Protein folding, nucleation phenomena and delayed neurodegeneration in Alzheimer's disease Rev. Neurosci. 7, 21-28
    • (1996) Rev. Neurosci. , vol.7 , pp. 21-28
    • Fox, N.1    Harvey, R.J.2    Rossor, M.N.3
  • 28
    • 11144283513 scopus 로고    scopus 로고
    • Transcriptional and conformational changes of the tau molecule in Alzheimer's disease
    • Hyman, B. T., Augustinack, J. C., and Ingelsson, M. (2005) Transcriptional and conformational changes of the tau molecule in Alzheimer's disease Biochim. Biophys. Acta 1739, 150-157
    • (2005) Biochim. Biophys. Acta , vol.1739 , pp. 150-157
    • Hyman, B.T.1    Augustinack, J.C.2    Ingelsson, M.3
  • 29
    • 0038291981 scopus 로고    scopus 로고
    • Conformational changes and truncation of tau protein during tangle evolution in Alzheimer's disease
    • Garcia-Sierra, F., Ghoshal, N., Quinn, B., Berry, R. W., and Binder, L. I. (2003) Conformational changes and truncation of tau protein during tangle evolution in Alzheimer's disease J. Alzheimer's Dis. 5, 65-77
    • (2003) J. Alzheimer's Dis. , vol.5 , pp. 65-77
    • Garcia-Sierra, F.1    Ghoshal, N.2    Quinn, B.3    Berry, R.W.4    Binder, L.I.5
  • 30
    • 0031012497 scopus 로고    scopus 로고
    • Abnormal phosphorylation of tau and the mechanism of Alzheimer neurofibrillary degeneration: Sequestration of microtubule-associated proteins 1 and 2 and the disassembly of microtubules by the abnormal tau
    • Alonso, A. D., Grundke-Iqbal, I., Barra, H. S., and Iqbal, K. (1997) Abnormal phosphorylation of tau and the mechanism of Alzheimer neurofibrillary degeneration: sequestration of microtubule-associated proteins 1 and 2 and the disassembly of microtubules by the abnormal tau Proc. Natl. Acad. Sci. U.S.A. 94, 298-303
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 298-303
    • Alonso, A.D.1    Grundke-Iqbal, I.2    Barra, H.S.3    Iqbal, K.4
  • 31
    • 0032476645 scopus 로고    scopus 로고
    • Overexpression of tau protein inhibits kinesin-dependent trafficking of vesicles, mitochondria, and endoplasmic reticulum: Implications for Alzheimer's disease
    • Ebneth, A., Godemann, R., Stamer, K., Illenberger, S., Trinczek, B., and Mandelkow, E. (1998) Overexpression of tau protein inhibits kinesin-dependent trafficking of vesicles, mitochondria, and endoplasmic reticulum: implications for Alzheimer's disease J. Cell Biol. 143, 777-794
    • (1998) J. Cell Biol. , vol.143 , pp. 777-794
    • Ebneth, A.1    Godemann, R.2    Stamer, K.3    Illenberger, S.4    Trinczek, B.5    Mandelkow, E.6
  • 34
    • 33646732989 scopus 로고    scopus 로고
    • Role of APP phosphorylation in FE65-dependent gene transactivation mediated by AICD
    • Nakaya, T. and Suzuki, T. (2006) Role of APP phosphorylation in FE65-dependent gene transactivation mediated by AICD Genes Cells 11, 633-645
    • (2006) Genes Cells , vol.11 , pp. 633-645
    • Nakaya, T.1    Suzuki, T.2
  • 37
    • 34347256728 scopus 로고    scopus 로고
    • Tyrosine 687 phosphorylated Alzheimer's amyloid precursor protein is retained intracellularly and exhibits a decreased turnover rate
    • Rebelo, S., Vieira, S. I., Esselmann, H., Wiltfang, J., da Cruz e Silva, E. F., and da Cruz e Silva, O. A. (2007) Tyrosine 687 phosphorylated Alzheimer's amyloid precursor protein is retained intracellularly and exhibits a decreased turnover rate Neurodegener. Dis. 4, 78-87
    • (2007) Neurodegener. Dis. , vol.4 , pp. 78-87
    • Rebelo, S.1    Vieira, S.I.2    Esselmann, H.3    Wiltfang, J.4    Da Cruz Silva E, E.F.5    Da Cruz Silva E, O.A.6
  • 39
    • 0030035749 scopus 로고    scopus 로고
    • In vitro phosphorylation of the cytoplasmic domain of the amyloid precursor protein by glycogen synthase kinase-3beta
    • Aplin, A. E., Gibb, G. M., Jacobsen, J. S., Gallo, J. M., and Anderton, B. H. (1996) In vitro phosphorylation of the cytoplasmic domain of the amyloid precursor protein by glycogen synthase kinase-3beta J. Neurochem. 67, 699-707
    • (1996) J. Neurochem. , vol.67 , pp. 699-707
    • Aplin, A.E.1    Gibb, G.M.2    Jacobsen, J.S.3    Gallo, J.M.4    Anderton, B.H.5
  • 40
    • 0037966577 scopus 로고    scopus 로고
    • Regulation of amyloid precursor protein (APP) phosphorylation and processing by p35/Cdk5 and p25/Cdk5
    • Liu, F., Su, Y., Li, B., Zhou, Y., Ryder, J., Gonzalez-DeWhitt, P., May, P. C., and Ni, B. (2003) Regulation of amyloid precursor protein (APP) phosphorylation and processing by p35/Cdk5 and p25/Cdk5 FEBS Lett. 547, 193-196
    • (2003) FEBS Lett. , vol.547 , pp. 193-196
    • Liu, F.1    Su, Y.2    Li, B.3    Zhou, Y.4    Ryder, J.5    Gonzalez-Dewhitt, P.6    May, P.C.7    Ni, B.8
  • 41
    • 0035166824 scopus 로고    scopus 로고
    • Phosphorylation of thr(668) in the cytoplasmic domain of the Alzheimer's disease amyloid precursor protein by stress-activated protein kinase 1b (Jun N-terminal kinase-3)
    • Standen, C. L., Brownlees, J., Grierson, A. J., Kesavapany, S., Lau, K. F., McLoughlin, D. M., and Miller, C. C. (2001) Phosphorylation of thr(668) in the cytoplasmic domain of the Alzheimer's disease amyloid precursor protein by stress-activated protein kinase 1b (Jun N-terminal kinase-3) J. Neurochem. 76, 316-320
    • (2001) J. Neurochem. , vol.76 , pp. 316-320
    • Standen, C.L.1    Brownlees, J.2    Grierson, A.J.3    Kesavapany, S.4    Lau, K.F.5    McLoughlin, D.M.6    Miller, C.C.7
  • 42
    • 0037205493 scopus 로고    scopus 로고
    • Interaction of Alzheimer's beta -amyloid precursor family proteins with scaffold proteins of the JNK signaling cascade
    • Taru, H., Iijima, K., Hase, M., Kirino, Y., Yagi, Y., and Suzuki, T. (2002) Interaction of Alzheimer's beta -amyloid precursor family proteins with scaffold proteins of the JNK signaling cascade J. Biol. Chem. 277, 20070-20078
    • (2002) J. Biol. Chem. , vol.277 , pp. 20070-20078
    • Taru, H.1    Iijima, K.2    Hase, M.3    Kirino, Y.4    Yagi, Y.5    Suzuki, T.6
  • 45
    • 0033850407 scopus 로고    scopus 로고
    • Tau protein isoforms, phosphorylation and role in neurodegenerative disorders
    • Buee, L., Bussiere, T., Buee-Scherrer, V., Delacourte, A., and Hof, P. R. (2000) Tau protein isoforms, phosphorylation and role in neurodegenerative disorders Brain Res. Rev. 33, 95-130
    • (2000) Brain Res. Rev. , vol.33 , pp. 95-130
    • Buee, L.1    Bussiere, T.2    Buee-Scherrer, V.3    Delacourte, A.4    Hof, P.R.5
  • 46
    • 55249086251 scopus 로고    scopus 로고
    • Hyperphosphorylation of microtubule-associated protein tau: A promising therapeutic target for Alzheimer disease
    • Gong, C. X. and Iqbal, K. (2008) Hyperphosphorylation of microtubule-associated protein tau: a promising therapeutic target for Alzheimer disease Curr. Med. Chem. 15, 2321-2328
    • (2008) Curr. Med. Chem. , vol.15 , pp. 2321-2328
    • Gong, C.X.1    Iqbal, K.2
  • 47
    • 1642289188 scopus 로고    scopus 로고
    • Role of tau protein in both physiological and pathological conditions
    • Avila, J., Lucas, J. J., Perez, M., and Hernandez, F. (2004) Role of tau protein in both physiological and pathological conditions Physiol. Rev. 84, 361-384
    • (2004) Physiol. Rev. , vol.84 , pp. 361-384
    • Avila, J.1    Lucas, J.J.2    Perez, M.3    Hernandez, F.4
  • 48
    • 0027361281 scopus 로고
    • Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease
    • Kopke, E., Tung, Y. C., Shaikh, S., Alonso, A. C., Iqbal, K., and Grundke-Iqbal, I. (1993) Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease J. Biol. Chem. 268, 24374-24384
    • (1993) J. Biol. Chem. , vol.268 , pp. 24374-24384
    • Kopke, E.1    Tung, Y.C.2    Shaikh, S.3    Alonso, A.C.4    Iqbal, K.5    Grundke-Iqbal, I.6
  • 49
    • 0036233802 scopus 로고    scopus 로고
    • Fruit polyphenolics and brain aging: Nutritional interventions targeting age-related neuronal and behavioral deficits
    • Galli, R. L., Shukitt-Hale, B., Youdim, K. A., and Joseph, J. A. (2002) Fruit polyphenolics and brain aging: nutritional interventions targeting age-related neuronal and behavioral deficits Ann. N.Y. Acad. Sci. 959, 128-132
    • (2002) Ann. N.Y. Acad. Sci. , vol.959 , pp. 128-132
    • Galli, R.L.1    Shukitt-Hale, B.2    Youdim, K.A.3    Joseph, J.A.4
  • 50
    • 33645519220 scopus 로고    scopus 로고
    • Long-term administration of green tea catechins improves spatial cognition learning ability in rats
    • Haque, A. M., Hashimoto, M., Katakura, M., Tanabe, Y., Hara, Y., and Shido, O. (2006) Long-term administration of green tea catechins improves spatial cognition learning ability in rats J. Nutr. 136, 1043-1047
    • (2006) J. Nutr. , vol.136 , pp. 1043-1047
    • Haque, A.M.1    Hashimoto, M.2    Katakura, M.3    Tanabe, Y.4    Hara, Y.5    Shido, O.6
  • 52
    • 3242700558 scopus 로고    scopus 로고
    • Suppressive effect of green tea catechins on morphologic and functional regression of the brain in aged mice with accelerated senescence (SAMP10)
    • Unno, K., Takabayashi, F., Kishido, T., and Oku, N. (2004) Suppressive effect of green tea catechins on morphologic and functional regression of the brain in aged mice with accelerated senescence (SAMP10) Exp. Gerontol. 39, 1027-1034
    • (2004) Exp. Gerontol. , vol.39 , pp. 1027-1034
    • Unno, K.1    Takabayashi, F.2    Kishido, T.3    Oku, N.4
  • 53
    • 33745015824 scopus 로고    scopus 로고
    • The in vivo synaptic plasticity mechanism of EGb 761-induced enhancement of spatial learning and memory in aged rats
    • Wang, Y., Wang, L., Wu, J., and Cai, J. (2006) The in vivo synaptic plasticity mechanism of EGb 761-induced enhancement of spatial learning and memory in aged rats Br. J. Pharmacol. 148, 147-153
    • (2006) Br. J. Pharmacol. , vol.148 , pp. 147-153
    • Wang, Y.1    Wang, L.2    Wu, J.3    Cai, J.4
  • 54
    • 0035868503 scopus 로고    scopus 로고
    • A possible emerging role of phytochemicals in improving age-related neurological dysfunctions: A multiplicity of effects
    • Youdim, K. A. and Joseph, J. A. (2001) A possible emerging role of phytochemicals in improving age-related neurological dysfunctions: a multiplicity of effects Free Radical Biol. Med. 30, 583-594
    • (2001) Free Radical Biol. Med. , vol.30 , pp. 583-594
    • Youdim, K.A.1    Joseph, J.A.2
  • 55
    • 84889670328 scopus 로고    scopus 로고
    • Chocolate and the brain: Neurobiological impact of cocoa flavanols on cognition and behavior
    • 10.1016/j.neubiorev.2013.06.013
    • Sokolov, A. N., Pavlova, M. A., Klosterhalfen, S., and Enck, P. (2013) Chocolate and the brain: Neurobiological impact of cocoa flavanols on cognition and behavior Neurosci. Biobehav. Rev. 37 (10 Pt 2) 2445-2453 10.1016/j.neubiorev.2013.06.013
    • (2013) Neurosci. Biobehav. Rev. , vol.37 , Issue.10 PART 2 , pp. 2445-2453
    • Sokolov, A.N.1    Pavlova, M.A.2    Klosterhalfen, S.3    Enck, P.4
  • 56
    • 0141863402 scopus 로고    scopus 로고
    • Overview of dietary flavonoids: Nomenclature, occurrence and intake
    • Beecher, G. R. (2003) Overview of dietary flavonoids: nomenclature, occurrence and intake J. Nutr. 133, 3248S-3254S
    • (2003) J. Nutr. , vol.133
    • Beecher, G.R.1
  • 57
    • 0033859612 scopus 로고    scopus 로고
    • Flavonoids as antioxidants
    • Pietta, P. G. (2000) Flavonoids as antioxidants J. Nat. Prod. 63, 1035-1042
    • (2000) J. Nat. Prod. , vol.63 , pp. 1035-1042
    • Pietta, P.G.1
  • 58
    • 77955498539 scopus 로고    scopus 로고
    • Beyond antioxidants: The cellular and molecular interactions of flavonoids and how these underpin their actions on the brain
    • Spencer, J. P. (2010) Beyond antioxidants: the cellular and molecular interactions of flavonoids and how these underpin their actions on the brain Proc. Nutr. Soc. 69, 244-260
    • (2010) Proc. Nutr. Soc. , vol.69 , pp. 244-260
    • Spencer, J.P.1
  • 59
    • 63049125250 scopus 로고    scopus 로고
    • The impact of flavonoids on memory: Physiological and molecular considerations
    • Spencer, J. P. (2009) The impact of flavonoids on memory: physiological and molecular considerations Chem. Soc. Rev. 38, 1152-1161
    • (2009) Chem. Soc. Rev. , vol.38 , pp. 1152-1161
    • Spencer, J.P.1
  • 60
    • 84870397190 scopus 로고    scopus 로고
    • Anthocyanin-enriched bilberry and blackcurrant extracts modulate amyloid precursor protein processing and alleviate behavioral abnormalities in the APP/PS1 mouse model of Alzheimer's disease
    • Vepsalainen, S., Koivisto, H., Pekkarinen, E., Makinen, P., Dobson, G., McDougall, G. J., Stewart, D., Haapasalo, A., Karjalainen, R. O., Tanila, H., and Hiltunen, M. (2013) Anthocyanin-enriched bilberry and blackcurrant extracts modulate amyloid precursor protein processing and alleviate behavioral abnormalities in the APP/PS1 mouse model of Alzheimer's disease J. Nutr. Biochem. 24, 360-370
    • (2013) J. Nutr. Biochem. , vol.24 , pp. 360-370
    • Vepsalainen, S.1    Koivisto, H.2    Pekkarinen, E.3    Makinen, P.4    Dobson, G.5    McDougall, G.J.6    Stewart, D.7    Haapasalo, A.8    Karjalainen, R.O.9    Tanila, H.10    Hiltunen, M.11
  • 62
    • 46749123053 scopus 로고    scopus 로고
    • Grape-derived polyphenolics prevent Abeta oligomerization and attenuate cognitive deterioration in a mouse model of Alzheimer's disease
    • Wang, J., Ho, L., Zhao, W., Ono, K., Rosensweig, C., Chen, L., Humala, N., Teplow, D. B., and Pasinetti, G. M. (2008) Grape-derived polyphenolics prevent Abeta oligomerization and attenuate cognitive deterioration in a mouse model of Alzheimer's disease J. Neurosci. 28, 6388-6392
    • (2008) J. Neurosci. , vol.28 , pp. 6388-6392
    • Wang, J.1    Ho, L.2    Zhao, W.3    Ono, K.4    Rosensweig, C.5    Chen, L.6    Humala, N.7    Teplow, D.B.8    Pasinetti, G.M.9
  • 64
    • 70349750314 scopus 로고    scopus 로고
    • Consumption of grape seed extract prevents amyloid-beta deposition and attenuates inflammation in brain of an Alzheimer's disease mouse
    • Wang, Y. J., Thomas, P., Zhong, J. H., Bi, F. F., Kosaraju, S., Pollard, A., Fenech, M., and Zhou, X. F. (2009) Consumption of grape seed extract prevents amyloid-beta deposition and attenuates inflammation in brain of an Alzheimer's disease mouse Neurotoxic. Res. 15, 3-14
    • (2009) Neurotoxic. Res. , vol.15 , pp. 3-14
    • Wang, Y.J.1    Thomas, P.2    Zhong, J.H.3    Bi, F.F.4    Kosaraju, S.5    Pollard, A.6    Fenech, M.7    Zhou, X.F.8
  • 65
    • 58049125719 scopus 로고    scopus 로고
    • Effect of a short- and long-term treatment with Ginkgo biloba extract on amyloid precursor protein levels in a transgenic mouse model relevant to Alzheimer's disease
    • Augustin, S., Rimbach, G., Augustin, K., Schliebs, R., Wolffram, S., and Cermak, R. (2009) Effect of a short- and long-term treatment with Ginkgo biloba extract on amyloid precursor protein levels in a transgenic mouse model relevant to Alzheimer's disease Arch. Biochem. Biophys. 481, 177-182
    • (2009) Arch. Biochem. Biophys. , vol.481 , pp. 177-182
    • Augustin, S.1    Rimbach, G.2    Augustin, K.3    Schliebs, R.4    Wolffram, S.5    Cermak, R.6
  • 66
    • 84857497814 scopus 로고    scopus 로고
    • Tannic acid is a natural beta-secretase inhibitor that prevents cognitive impairment and mitigates Alzheimer-like pathology in transgenic mice
    • Mori, T., Rezai-Zadeh, K., Koyama, N., Arendash, G. W., Yamaguchi, H., Kakuda, N., Horikoshi-Sakuraba, Y., Tan, J., and Town, T. (2012) Tannic acid is a natural beta-secretase inhibitor that prevents cognitive impairment and mitigates Alzheimer-like pathology in transgenic mice J. Biol. Chem. 287, 6912-6927
    • (2012) J. Biol. Chem. , vol.287 , pp. 6912-6927
    • Mori, T.1    Rezai-Zadeh, K.2    Koyama, N.3    Arendash, G.W.4    Yamaguchi, H.5    Kakuda, N.6    Horikoshi-Sakuraba, Y.7    Tan, J.8    Town, T.9
  • 67
    • 45049086920 scopus 로고    scopus 로고
    • Flavonols and flavones as BACE-1 inhibitors: Structure-activity relationship in cell-free, cell-based and in silico studies reveal novel pharmacophore features
    • Shimmyo, Y., Kihara, T., Akaike, A., Niidome, T., and Sugimoto, H. (2008) Flavonols and flavones as BACE-1 inhibitors: structure-activity relationship in cell-free, cell-based and in silico studies reveal novel pharmacophore features Biochim. Biophys. Acta 1780, 819-825
    • (2008) Biochim. Biophys. Acta , vol.1780 , pp. 819-825
    • Shimmyo, Y.1    Kihara, T.2    Akaike, A.3    Niidome, T.4    Sugimoto, H.5
  • 68
    • 52649143244 scopus 로고    scopus 로고
    • Epigallocatechin-3-gallate and curcumin suppress amyloid beta-induced beta-site APP cleaving enzyme-1 upregulation
    • Shimmyo, Y., Kihara, T., Akaike, A., Niidome, T., and Sugimoto, H. (2008) Epigallocatechin-3-gallate and curcumin suppress amyloid beta-induced beta-site APP cleaving enzyme-1 upregulation NeuroReport 19, 1329-1333
    • (2008) NeuroReport , vol.19 , pp. 1329-1333
    • Shimmyo, Y.1    Kihara, T.2    Akaike, A.3    Niidome, T.4    Sugimoto, H.5
  • 70
    • 44249116000 scopus 로고    scopus 로고
    • Green tea epigallocatechin-3-gallate (EGCG) reduces beta-amyloid mediated cognitive impairment and modulates tau pathology in Alzheimer transgenic mice
    • Rezai-Zadeh, K., Arendash, G. W., Hou, H., Fernandez, F., Jensen, M., Runfeldt, M., Shytle, R. D., and Tan, J. (2008) Green tea epigallocatechin-3- gallate (EGCG) reduces beta-amyloid mediated cognitive impairment and modulates tau pathology in Alzheimer transgenic mice Brain Res. 1214, 177-187
    • (2008) Brain Res. , vol.1214 , pp. 177-187
    • Rezai-Zadeh, K.1    Arendash, G.W.2    Hou, H.3    Fernandez, F.4    Jensen, M.5    Runfeldt, M.6    Shytle, R.D.7    Tan, J.8
  • 72
    • 77957128191 scopus 로고    scopus 로고
    • EGCG functions through estrogen receptor-mediated activation of ADAM10 in the promotion of non-amyloidogenic processing of APP
    • Fernandez, J. W., Rezai-Zadeh, K., Obregon, D., and Tan, J. (2010) EGCG functions through estrogen receptor-mediated activation of ADAM10 in the promotion of non-amyloidogenic processing of APP FEBS Lett. 584, 4259-4267
    • (2010) FEBS Lett. , vol.584 , pp. 4259-4267
    • Fernandez, J.W.1    Rezai-Zadeh, K.2    Obregon, D.3    Tan, J.4
  • 75
    • 33847025338 scopus 로고    scopus 로고
    • The anti-amyloidogenic effect is exerted against Alzheimer's beta-amyloid fibrils in vitro by preferential and reversible binding of flavonoids to the amyloid fibril structure
    • Hirohata, M., Hasegawa, K., Tsutsumi-Yasuhara, S., Ohhashi, Y., Ookoshi, T., Ono, K., Yamada, M., and Naiki, H. (2007) The anti-amyloidogenic effect is exerted against Alzheimer's beta-amyloid fibrils in vitro by preferential and reversible binding of flavonoids to the amyloid fibril structure Biochemistry 46, 1888-1899
    • (2007) Biochemistry , vol.46 , pp. 1888-1899
    • Hirohata, M.1    Hasegawa, K.2    Tsutsumi-Yasuhara, S.3    Ohhashi, Y.4    Ookoshi, T.5    Ono, K.6    Yamada, M.7    Naiki, H.8
  • 76
    • 0141642253 scopus 로고    scopus 로고
    • Potent anti-amyloidogenic and fibril-destabilizing effects of polyphenols in vitro: Implications for the prevention and therapeutics of Alzheimer's disease
    • Ono, K., Yoshiike, Y., Takashima, A., Hasegawa, K., Naiki, H., and Yamada, M. (2003) Potent anti-amyloidogenic and fibril-destabilizing effects of polyphenols in vitro: implications for the prevention and therapeutics of Alzheimer's disease J. Neurochem. 87, 172-181
    • (2003) J. Neurochem. , vol.87 , pp. 172-181
    • Ono, K.1    Yoshiike, Y.2    Takashima, A.3    Hasegawa, K.4    Naiki, H.5    Yamada, M.6
  • 77
    • 14844303721 scopus 로고    scopus 로고
    • Inhibition of heparin-induced tau filament formation by phenothiazines, polyphenols, and porphyrins
    • Taniguchi, S., Suzuki, N., Masuda, M., Hisanaga, S., Iwatsubo, T., Goedert, M., and Hasegawa, M. (2005) Inhibition of heparin-induced tau filament formation by phenothiazines, polyphenols, and porphyrins J. Biol. Chem. 280, 7614-7623
    • (2005) J. Biol. Chem. , vol.280 , pp. 7614-7623
    • Taniguchi, S.1    Suzuki, N.2    Masuda, M.3    Hisanaga, S.4    Iwatsubo, T.5    Goedert, M.6    Hasegawa, M.7
  • 79
    • 77956314492 scopus 로고    scopus 로고
    • Development of a grape seed polyphenolic extract with anti-oligomeric activity as a novel treatment in progressive supranuclear palsy and other tauopathies
    • Pasinetti, G. M., Ksiezak-Reding, H., Santa-Maria, I., Wang, J., and Ho, L. (2010) Development of a grape seed polyphenolic extract with anti-oligomeric activity as a novel treatment in progressive supranuclear palsy and other tauopathies J. Neurochem. 114, 1557-1568
    • (2010) J. Neurochem. , vol.114 , pp. 1557-1568
    • Pasinetti, G.M.1    Ksiezak-Reding, H.2    Santa-Maria, I.3    Wang, J.4    Ho, L.5
  • 80
    • 60349096854 scopus 로고    scopus 로고
    • Grape seed polyphenolic extract as a potential novel therapeutic agent in tauopathies
    • Ho, L., Yemul, S., Wang, J., and Pasinetti, G. M. (2009) Grape seed polyphenolic extract as a potential novel therapeutic agent in tauopathies J. Alzheimer's Dis. 16, 433-439
    • (2009) J. Alzheimer's Dis. , vol.16 , pp. 433-439
    • Ho, L.1    Yemul, S.2    Wang, J.3    Pasinetti, G.M.4
  • 81
    • 84861195616 scopus 로고    scopus 로고
    • Ultrastructural alterations of Alzheimer's disease paired helical filaments by grape seed-derived polyphenols
    • Ksiezak-Reding, H., Ho, L., Santa-Maria, I., Diaz-Ruiz, C., Wang, J., and Pasinetti, G. M. (2012) Ultrastructural alterations of Alzheimer's disease paired helical filaments by grape seed-derived polyphenols Neurobiol. Aging 33, 1427-1439
    • (2012) Neurobiol. Aging , vol.33 , pp. 1427-1439
    • Ksiezak-Reding, H.1    Ho, L.2    Santa-Maria, I.3    Diaz-Ruiz, C.4    Wang, J.5    Pasinetti, G.M.6
  • 82
    • 38349008651 scopus 로고    scopus 로고
    • The interactions of flavonoids within neuronal signalling pathways
    • Spencer, J. P. (2007) The interactions of flavonoids within neuronal signalling pathways Genes Nutr. 2, 257-273
    • (2007) Genes Nutr. , vol.2 , pp. 257-273
    • Spencer, J.P.1
  • 83
    • 0041816456 scopus 로고    scopus 로고
    • Modulation of pro-survival Akt/protein kinase B and ERK1/2 signaling cascades by quercetin and its in vivo metabolites underlie their action on neuronal viability
    • Spencer, J. P., Rice-Evans, C., and Williams, R. J. (2003) Modulation of pro-survival Akt/protein kinase B and ERK1/2 signaling cascades by quercetin and its in vivo metabolites underlie their action on neuronal viability J. Biol. Chem. 278, 34783-34793
    • (2003) J. Biol. Chem. , vol.278 , pp. 34783-34793
    • Spencer, J.P.1    Rice-Evans, C.2    Williams, R.J.3
  • 84
    • 77954001205 scopus 로고    scopus 로고
    • Involvement of ERK, Akt and JNK signalling in H2O2-induced cell injury and protection by hydroxytyrosol and its metabolite homovanillic alcohol
    • Incani, A., Deiana, M., Corona, G., Vafeiadou, K., Vauzour, D., Dessi, M. A., and Spencer, J. P. (2010) Involvement of ERK, Akt and JNK signalling in H2O2-induced cell injury and protection by hydroxytyrosol and its metabolite homovanillic alcohol Mol. Nutr. Food Res. 54, 788-796
    • (2010) Mol. Nutr. Food Res. , vol.54 , pp. 788-796
    • Incani, A.1    Deiana, M.2    Corona, G.3    Vafeiadou, K.4    Vauzour, D.5    Dessi, M.A.6    Spencer, J.P.7
  • 85
    • 34548250927 scopus 로고    scopus 로고
    • Inhibition of the formation of the neurotoxin 5-S-cysteinyl-dopamine by polyphenols
    • Vauzour, D., Vafeiadou, K., and Spencer, J. P. (2007) Inhibition of the formation of the neurotoxin 5-S-cysteinyl-dopamine by polyphenols Biochem. Biophys. Res. Commun. 362, 340-346
    • (2007) Biochem. Biophys. Res. Commun. , vol.362 , pp. 340-346
    • Vauzour, D.1    Vafeiadou, K.2    Spencer, J.P.3
  • 86
    • 0030051539 scopus 로고    scopus 로고
    • Interactions of flavonoids and other phytochemicals with adenosine receptors
    • Ji, X. D., Melman, N., and Jacobson, K. A. (1996) Interactions of flavonoids and other phytochemicals with adenosine receptors J. Med. Chem. 39, 781-788
    • (1996) J. Med. Chem. , vol.39 , pp. 781-788
    • Ji, X.D.1    Melman, N.2    Jacobson, K.A.3
  • 87
    • 50949103149 scopus 로고    scopus 로고
    • Flavan-3-ol derivatives are positive modulators of GABA(A) receptors with higher efficacy for the alpha(2) subtype and anxiolytic action in mice
    • Fernandez, S. P., Mewett, K. N., Hanrahan, J. R., Chebib, M., and Johnston, G. A. (2008) Flavan-3-ol derivatives are positive modulators of GABA(A) receptors with higher efficacy for the alpha(2) subtype and anxiolytic action in mice Neuropharmacology 55, 900-907
    • (2008) Neuropharmacology , vol.55 , pp. 900-907
    • Fernandez, S.P.1    Mewett, K.N.2    Hanrahan, J.R.3    Chebib, M.4    Johnston, G.A.5
  • 88
    • 32044438645 scopus 로고    scopus 로고
    • (-)-Epigallocatechin gallate attenuates acute stress responses through GABAergic system in the brain
    • Adachi, N., Tomonaga, S., Tachibana, T., Denbow, D. M., and Furuse, M. (2006) (-)-Epigallocatechin gallate attenuates acute stress responses through GABAergic system in the brain Eur. J. Pharmacol. 531, 171-175
    • (2006) Eur. J. Pharmacol. , vol.531 , pp. 171-175
    • Adachi, N.1    Tomonaga, S.2    Tachibana, T.3    Denbow, D.M.4    Furuse, M.5
  • 90
    • 34548620863 scopus 로고    scopus 로고
    • Flavonoids as opioid receptor ligands: Identification and preliminary structure-activity relationships
    • Katavic, P. L., Lamb, K., Navarro, H., and Prisinzano, T. E. (2007) Flavonoids as opioid receptor ligands: identification and preliminary structure-activity relationships J. Nat. Prod. 70, 1278-1282
    • (2007) J. Nat. Prod. , vol.70 , pp. 1278-1282
    • Katavic, P.L.1    Lamb, K.2    Navarro, H.3    Prisinzano, T.E.4
  • 92
    • 78049318379 scopus 로고    scopus 로고
    • Quercetin enhances human alpha7 nicotinic acetylcholine receptor-mediated ion current through interactions with Ca(2+) binding sites
    • Lee, B. H., Choi, S. H., Shin, T. J., Pyo, M. K., Hwang, S. H., Kim, B. R., Lee, S. M., Lee, J. H., Kim, H. C., Park, H. Y., Rhim, H., and Nah, S. Y. (2010) Quercetin enhances human alpha7 nicotinic acetylcholine receptor-mediated ion current through interactions with Ca(2+) binding sites Mol. Cells 30, 245-253
    • (2010) Mol. Cells , vol.30 , pp. 245-253
    • Lee, B.H.1    Choi, S.H.2    Shin, T.J.3    Pyo, M.K.4    Hwang, S.H.5    Kim, B.R.6    Lee, S.M.7    Lee, J.H.8    Kim, H.C.9    Park, H.Y.10    Rhim, H.11    Nah, S.Y.12
  • 96
    • 33745235570 scopus 로고    scopus 로고
    • Specific plasma membrane binding sites for polyphenols, including resveratrol, in the rat brain
    • Han, Y. S., Bastianetto, S., Dumont, Y., and Quirion, R. (2006) Specific plasma membrane binding sites for polyphenols, including resveratrol, in the rat brain J. Pharmacol. Exp. Ther. 318, 238-245
    • (2006) J. Pharmacol. Exp. Ther. , vol.318 , pp. 238-245
    • Han, Y.S.1    Bastianetto, S.2    Dumont, Y.3    Quirion, R.4
  • 99
    • 0035884625 scopus 로고    scopus 로고
    • Flavonoids protect neurons from oxidized low-density-lipoprotein-induced apoptosis involving c-Jun N-terminal kinase (JNK), c-Jun and caspase-3
    • Schroeter, H., Spencer, J. P., Rice-Evans, C., and Williams, R. J. (2001) Flavonoids protect neurons from oxidized low-density-lipoprotein-induced apoptosis involving c-Jun N-terminal kinase (JNK), c-Jun and caspase-3 Biochem. J. 358, 547-557
    • (2001) Biochem. J. , vol.358 , pp. 547-557
    • Schroeter, H.1    Spencer, J.P.2    Rice-Evans, C.3    Williams, R.J.4
  • 100
    • 0026726483 scopus 로고
    • The inhibition of phosphatidylinositol 3-kinase by quercetin and analogs
    • Matter, W. F., Brown, R. F., and Vlahos, C. J. (1992) The inhibition of phosphatidylinositol 3-kinase by quercetin and analogs Biochem. Biophys. Res. Commun. 186, 624-631
    • (1992) Biochem. Biophys. Res. Commun. , vol.186 , pp. 624-631
    • Matter, W.F.1    Brown, R.F.2    Vlahos, C.J.3
  • 101
    • 0030842112 scopus 로고    scopus 로고
    • Relationship between flavonoid structure and inhibition of phosphatidylinositol 3-kinase: A comparison with tyrosine kinase and protein kinase C inhibition
    • Agullo, G., Gamet-Payrastre, L., Manenti, S., Viala, C., Remesy, C., Chap, H., and Payrastre, B. (1997) Relationship between flavonoid structure and inhibition of phosphatidylinositol 3-kinase: a comparison with tyrosine kinase and protein kinase C inhibition Biochem. Pharmacol. 53, 1649-1657
    • (1997) Biochem. Pharmacol. , vol.53 , pp. 1649-1657
    • Agullo, G.1    Gamet-Payrastre, L.2    Manenti, S.3    Viala, C.4    Remesy, C.5    Chap, H.6    Payrastre, B.7
  • 102
    • 0034137655 scopus 로고    scopus 로고
    • Signal transduction events elicited by natural products: Role of MAPK and caspase pathways in homeostatic response and induction of apoptosis
    • Kong, A. N. T., Yu, R., Chen, C., Mandlekar, S., and Primiano, T. (2000) Signal transduction events elicited by natural products: Role of MAPK and caspase pathways in homeostatic response and induction of apoptosis Arch. Pharm. Res. 23, 1-16
    • (2000) Arch. Pharm. Res. , vol.23 , pp. 1-16
    • Kong, A.N.T.1    Yu, R.2    Chen, C.3    Mandlekar, S.4    Primiano, T.5
  • 104
    • 0029043582 scopus 로고
    • How Map Kinases Are Regulated
    • Cobb, M. H. and Goldsmith, E. J. (1995) How Map Kinases Are Regulated J. Biol. Chem. 270, 14843-14846
    • (1995) J. Biol. Chem. , vol.270 , pp. 14843-14846
    • Cobb, M.H.1    Goldsmith, E.J.2
  • 105
    • 79952435349 scopus 로고    scopus 로고
    • Activation and function of the MAPKs and their substrates, the MAPK-activated protein kinases
    • Cargnello, M. and Roux, P. P. (2011) Activation and function of the MAPKs and their substrates, the MAPK-activated protein kinases Microbiol. Mol. Biol. Rev. 75, 50-83
    • (2011) Microbiol. Mol. Biol. Rev. , vol.75 , pp. 50-83
    • Cargnello, M.1    Roux, P.P.2
  • 106
    • 0032862903 scopus 로고    scopus 로고
    • Quercetin inhibits inducible ICAM-1 expression in human endothelial cells through the JNK pathway
    • Kobuchi, H., Roy, S., Sen, C. K., Nguyen, H. G., and Packer, L. (1999) Quercetin inhibits inducible ICAM-1 expression in human endothelial cells through the JNK pathway Am. J. Physiol.: Cell Physiol. 277, C403-C411
    • (1999) Am. J. Physiol.: Cell Physiol. , vol.277
    • Kobuchi, H.1    Roy, S.2    Sen, C.K.3    Nguyen, H.G.4    Packer, L.5
  • 107
    • 34249788691 scopus 로고    scopus 로고
    • (-)Epicatechin stimulates ERK-dependent cyclic AMP response element activity and up-regulates GluR2 in cortical neurons
    • Schroeter, H., Bahia, P., Spencer, J. P., Sheppard, O., Rattray, M., Cadenas, E., Rice-Evans, C., and Williams, R. J. (2007) (-)Epicatechin stimulates ERK-dependent cyclic AMP response element activity and up-regulates GluR2 in cortical neurons J. Neurochem. 101, 1596-1606
    • (2007) J. Neurochem. , vol.101 , pp. 1596-1606
    • Schroeter, H.1    Bahia, P.2    Spencer, J.P.3    Sheppard, O.4    Rattray, M.5    Cadenas, E.6    Rice-Evans, C.7    Williams, R.J.8
  • 108
    • 35448949428 scopus 로고    scopus 로고
    • Activation of pro-survival Akt and ERK1/2 signalling pathways underlie the anti-apoptotic effects of flavanones in cortical neurons
    • Vauzour, D., Vafeiadou, K., Rice-Evans, C., Williams, R. J., and Spencer, J. P. (2007) Activation of pro-survival Akt and ERK1/2 signalling pathways underlie the anti-apoptotic effects of flavanones in cortical neurons J. Neurochem. 103, 1355-1367
    • (2007) J. Neurochem. , vol.103 , pp. 1355-1367
    • Vauzour, D.1    Vafeiadou, K.2    Rice-Evans, C.3    Williams, R.J.4    Spencer, J.P.5
  • 109
    • 33750832268 scopus 로고    scopus 로고
    • Flavonoid fisetin promotes ERK-dependent long-term potentiation and enhances memory
    • Maher, P., Akaishi, T., and Abe, K. (2006) Flavonoid fisetin promotes ERK-dependent long-term potentiation and enhances memory Proc. Natl. Acad. Sci. U.S.A. 103, 16568-16573
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 16568-16573
    • Maher, P.1    Akaishi, T.2    Abe, K.3
  • 110
    • 33748355855 scopus 로고    scopus 로고
    • Modulation of activator protein-1 (AP-1) and MAPK pathway by flavonoids in human prostate cancer PC3 cells
    • Gopalakrishnan, A., Xu, C. J., Nair, S. S., Chen, C., Hebbar, V., and Kong, A. N. (2006) Modulation of activator protein-1 (AP-1) and MAPK pathway by flavonoids in human prostate cancer PC3 cells Arch. Pharm. Res. 29, 633-644
    • (2006) Arch. Pharm. Res. , vol.29 , pp. 633-644
    • Gopalakrishnan, A.1    Xu, C.J.2    Nair, S.S.3    Chen, C.4    Hebbar, V.5    Kong, A.N.6
  • 111
    • 0037116579 scopus 로고    scopus 로고
    • Apigenin and LY294002 prolong EGF-stimulated ERK1/2 activation in PC12 cells but are unable to induce full differentiation
    • Llorens, F., Garcia, L., Itarte, E., and Gomez, N. (2002) Apigenin and LY294002 prolong EGF-stimulated ERK1/2 activation in PC12 cells but are unable to induce full differentiation FEBS Lett. 510, 149-153
    • (2002) FEBS Lett. , vol.510 , pp. 149-153
    • Llorens, F.1    Garcia, L.2    Itarte, E.3    Gomez, N.4
  • 113
    • 0032195577 scopus 로고    scopus 로고
    • Stimulation of cAMP response element (CRE)-mediated transcription during contextual learning
    • Impey, S., Smith, D. M., Obrietan, K., Donahue, R., Wade, C., and Storm, D. R. (1998) Stimulation of cAMP response element (CRE)-mediated transcription during contextual learning Nat. Neurosci. 1, 595-601
    • (1998) Nat. Neurosci. , vol.1 , pp. 595-601
    • Impey, S.1    Smith, D.M.2    Obrietan, K.3    Donahue, R.4    Wade, C.5    Storm, D.R.6
  • 115
    • 46749094132 scopus 로고    scopus 로고
    • Blueberry-induced changes in spatial working memory correlate with changes in hippocampal CREB phosphorylation and brain-derived neurotrophic factor (BDNF) levels
    • Williams, C. M., El Mohsen, M. A., Vauzour, D., Rendeiro, C., Butler, L. T., Ellis, J. A., Whiteman, M., and Spencer, J. P. (2008) Blueberry-induced changes in spatial working memory correlate with changes in hippocampal CREB phosphorylation and brain-derived neurotrophic factor (BDNF) levels Free Radical Biol. Med. 45, 295-305
    • (2008) Free Radical Biol. Med. , vol.45 , pp. 295-305
    • Williams, C.M.1    El Mohsen, M.A.2    Vauzour, D.3    Rendeiro, C.4    Butler, L.T.5    Ellis, J.A.6    Whiteman, M.7    Spencer, J.P.8
  • 116
    • 70149095473 scopus 로고    scopus 로고
    • Long-term green tea catechin administration prevents spatial learning and memory impairment in senescence-accelerated mouse prone-8 mice by decreasing Abeta1-42 oligomers and upregulating synaptic plasticity-related proteins in the hippocampus
    • Li, Q., Zhao, H. F., Zhang, Z. F., Liu, Z. G., Pei, X. R., Wang, J. B., and Li, Y. (2009) Long-term green tea catechin administration prevents spatial learning and memory impairment in senescence-accelerated mouse prone-8 mice by decreasing Abeta1-42 oligomers and upregulating synaptic plasticity-related proteins in the hippocampus Neuroscience 163, 741-749
    • (2009) Neuroscience , vol.163 , pp. 741-749
    • Li, Q.1    Zhao, H.F.2    Zhang, Z.F.3    Liu, Z.G.4    Pei, X.R.5    Wang, J.B.6    Li, Y.7
  • 117
    • 0028170210 scopus 로고
    • A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002)
    • Vlahos, C. J., Matter, W. F., Hui, K. Y., and Brown, R. F. (1994) A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl- 4H-1-benzopyran-4-one (LY294002) J. Biol. Chem. 269, 5241-5248
    • (1994) J. Biol. Chem. , vol.269 , pp. 5241-5248
    • Vlahos, C.J.1    Matter, W.F.2    Hui, K.Y.3    Brown, R.F.4
  • 118
    • 0024550507 scopus 로고
    • Protein kinase C inhibition by plant flavonoids. Kinetic mechanisms and structure-activity relationships
    • Ferriola, P. C., Cody, V., and Middleton, E., Jr. (1989) Protein kinase C inhibition by plant flavonoids. Kinetic mechanisms and structure-activity relationships Biochem. Pharmacol. 38, 1617-1624
    • (1989) Biochem. Pharmacol. , vol.38 , pp. 1617-1624
    • Ferriola, P.C.1    Cody, V.2    Middleton Jr., E.3
  • 119
    • 0033634827 scopus 로고    scopus 로고
    • Structural determinants of phosphoinositide 3-kinase inhibition by wortmannin, LY294002, quercetin, myricetin, and staurosporine
    • Walker, E. H., Pacold, M. E., Perisic, O., Stephens, L., Hawkins, P. T., Wymann, M. P., and Williams, R. L. (2000) Structural determinants of phosphoinositide 3-kinase inhibition by wortmannin, LY294002, quercetin, myricetin, and staurosporine Mol. Cell 6, 909-919
    • (2000) Mol. Cell , vol.6 , pp. 909-919
    • Walker, E.H.1    Pacold, M.E.2    Perisic, O.3    Stephens, L.4    Hawkins, P.T.5    Wymann, M.P.6    Williams, R.L.7
  • 120
    • 0037133172 scopus 로고    scopus 로고
    • The brain-derived neurotrophic factor enhances synthesis of Arc in synaptoneurosomes
    • Yin, Y., Edelman, G. M., and Vanderklish, P. W. (2002) The brain-derived neurotrophic factor enhances synthesis of Arc in synaptoneurosomes Proc. Natl. Acad. Sci. U.S.A. 99, 2368-2373
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 2368-2373
    • Yin, Y.1    Edelman, G.M.2    Vanderklish, P.W.3
  • 121
    • 0035425948 scopus 로고    scopus 로고
    • Arg3.1/Arc mRNA induction by Ca2+ and cAMP requires protein kinase A and mitogen-activated protein kinase/extracellular regulated kinase activation
    • Waltereit, R., Dammermann, B., Wulff, P., Scafidi, J., Staubli, U., Kauselmann, G., Bundman, M., and Kuhl, D. (2001) Arg3.1/Arc mRNA induction by Ca2+ and cAMP requires protein kinase A and mitogen-activated protein kinase/extracellular regulated kinase activation J. Neurosci. 21, 5484-5493
    • (2001) J. Neurosci. , vol.21 , pp. 5484-5493
    • Waltereit, R.1    Dammermann, B.2    Wulff, P.3    Scafidi, J.4    Staubli, U.5    Kauselmann, G.6    Bundman, M.7    Kuhl, D.8
  • 122
    • 0028330166 scopus 로고
    • Dendritic spines: Cellular specializations imparting both stability and flexibility to synaptic function
    • Harris, K. M. and Kater, S. B. (1994) Dendritic spines: cellular specializations imparting both stability and flexibility to synaptic function Annu. Rev. Neurosci. 17, 341-371
    • (1994) Annu. Rev. Neurosci. , vol.17 , pp. 341-371
    • Harris, K.M.1    Kater, S.B.2
  • 124
    • 20144371838 scopus 로고    scopus 로고
    • Green tea polyphenol (-)-epigallocatechin-3-gallate induces neurorescue of long-term serum-deprived PC12 cells and promotes neurite outgrowth
    • Reznichenko, L., Amit, T., Youdim, M. B., and Mandel, S. (2005) Green tea polyphenol (-)-epigallocatechin-3-gallate induces neurorescue of long-term serum-deprived PC12 cells and promotes neurite outgrowth J. Neurochem. 93, 1157-1167
    • (2005) J. Neurochem. , vol.93 , pp. 1157-1167
    • Reznichenko, L.1    Amit, T.2    Youdim, M.B.3    Mandel, S.4
  • 125
    • 0035808457 scopus 로고    scopus 로고
    • Indirubins inhibit glycogen synthase kinase-3 beta and CDK5/p25, two protein kinases involved in abnormal tau phosphorylation in Alzheimer's disease. A property common to most cyclin-dependent kinase inhibitors?
    • Leclerc, S., Garnier, M., Hoessel, R., Marko, D., Bibb, J. A., Snyder, G. L., Greengard, P., Biernat, J., Wu, Y. Z., Mandelkow, E. M., Eisenbrand, G., and Meijer, L. (2001) Indirubins inhibit glycogen synthase kinase-3 beta and CDK5/p25, two protein kinases involved in abnormal tau phosphorylation in Alzheimer's disease. A property common to most cyclin-dependent kinase inhibitors? J. Biol. Chem. 276, 251-260
    • (2001) J. Biol. Chem. , vol.276 , pp. 251-260
    • Leclerc, S.1    Garnier, M.2    Hoessel, R.3    Marko, D.4    Bibb, J.A.5    Snyder, G.L.6    Greengard, P.7    Biernat, J.8    Wu, Y.Z.9    Mandelkow, E.M.10    Eisenbrand, G.11    Meijer, L.12
  • 127
    • 84873060161 scopus 로고    scopus 로고
    • Protective effect of cyanidin 3-O-glucoside on beta-amyloid peptide-induced cognitive impairment in rats
    • Qin, L., Zhang, J., and Qin, M. (2013) Protective effect of cyanidin 3-O-glucoside on beta-amyloid peptide-induced cognitive impairment in rats Neurosci. Lett. 534, 285-288
    • (2013) Neurosci. Lett. , vol.534 , pp. 285-288
    • Qin, L.1    Zhang, J.2    Qin, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.