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Volumn 287, Issue 9, 2012, Pages 6912-6927

Tannic acid is a natural β-secretase inhibitor that prevents cognitive impairment and mitigates Alzheimer-like pathology in transgenic mice

Author keywords

[No Author keywords available]

Indexed keywords

ALZHEIMER DISEASE; AMYLOID DEPOSITS; AMYLOID PLAQUES; AMYLOID PRECURSOR PROTEINS; COGNITIVE FUNCTIONS; COGNITIVE IMPAIRMENT; DIETARY SUPPLEMENTATION; IN-VITRO; MOUSE MODELS; MUTANT HUMAN; NATURALLY OCCURRING; NEUROINFLAMMATION; NEURON-LIKE CELLS; POLYPHENOLS; PROTEIN STABILITY; SECRETASES; SPATIAL REFERENCE; TANNIC ACID; TRANS-GENES; TRANSGENIC MICE; TRANSGENICS;

EID: 84857497814     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.294025     Document Type: Article
Times cited : (160)

References (78)
  • 1
    • 0034660083 scopus 로고    scopus 로고
    • Methods for projecting the incidence and prevalence of chronic diseases in ageing populations: Application to Alzheimer's disease
    • Brookmeyer, R., and Gray, S. (2000) Methods for projecting the incidence and prevalence of chronic diseases in aging populations: application to Alzheimer's disease. Stat. Med. 19, 1481-1493 (Pubitemid 30346241)
    • (2000) Statistics in Medicine , vol.19 , Issue.11-12 , pp. 1481-1493
    • Brookmeyer, R.1
  • 2
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe, D. J. (2001) Alzheimer's disease: genes, proteins, and therapy. Physiol. Rev. 81, 741-766
    • (2001) Physiol. Rev. , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 4
    • 0025899041 scopus 로고
    • Amyloid deposition as the central event in the aetiology of Alzheimer's disease
    • Hardy, J., and Allsop, D. (1991) Amyloid deposition as the central event in the aetiology of Alzheimer's disease. Trends Pharmacol. Sci. 12, 383-388
    • (1991) Trends Pharmacol. Sci. , vol.12 , pp. 383-388
    • Hardy, J.1    Allsop, D.2
  • 8
    • 70350455062 scopus 로고    scopus 로고
    • The β-secretase enzyme BACE in health and Alzheimer's disease: Regulation, cell biology, function, and therapeutic potential
    • Vassar, R., Kovacs, D. M., Yan, R., and Wong, P. C. (2009) The β-secretase enzyme BACE in health and Alzheimer's disease: regulation, cell biology, function, and therapeutic potential. J. Neurosci. 29, 12787-12794
    • (2009) J. Neurosci. , vol.29 , pp. 12787-12794
    • Vassar, R.1    Kovacs, D.M.2    Yan, R.3    Wong, P.C.4
  • 10
    • 0037155581 scopus 로고    scopus 로고
    • Brain to plasma amyloid-β efflux: A measure of brain amyloid burden in a mouse model of Alzheimer's disease
    • DOI 10.1126/science.1067568
    • DeMattos, R. B., Bales, K. R., Cummins, D. J., Paul, S. M., and Holtzman, D. M. (2002) Brain to plasma amyloid-β efflux: a measure of brain amyloid burden in a mouse model of Alzheimer's disease. Science 295, 2264-2267 (Pubitemid 34258840)
    • (2002) Science , vol.295 , Issue.5563 , pp. 2264-2267
    • DeMattos, R.B.1    Bales, K.R.2    Cummins, D.J.3    Paul, S.M.4    Holtzman, D.M.5
  • 11
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
    • DOI 10.1038/416535a
    • Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., and Selkoe, D. J. (2002) Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416, 535-539 (Pubitemid 34288854)
    • (2002) Nature , vol.416 , Issue.6880 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5    Wolfe, M.S.6    Rowan, M.J.7    Selkoe, D.J.8
  • 18
    • 44949173099 scopus 로고    scopus 로고
    • Blocking TGF-β-Smad2/3 innate immune signaling mitigates Alzheimer-like pathology
    • DOI 10.1038/nm1781, PII NM1781
    • Town, T., Laouar, Y., Pittenger, C., Mori, T., Szekely, C.A., Tan, J., Duman, R. S., and Flavell, R. A. (2008) Blocking TGF-β-Smad2/3 innate immune signaling mitigates Alzheimer-like pathology. Nat. Med. 14, 681-687 (Pubitemid 351809551)
    • (2008) Nature Medicine , vol.14 , Issue.6 , pp. 681-687
    • Town, T.1    Laouar, Y.2    Pittenger, C.3    Mori, T.4    Szekely, C.A.5    Tan, J.6    Duman, R.S.7    Flavell, R.A.8
  • 21
    • 77949502713 scopus 로고    scopus 로고
    • Elevated ratio of urinary metabolites of thromboxane and prostacyclin is associated with adverse cardiovascular events in ADAPT
    • Montine, T. J., Sonnen, J. A., Milne, G., Baker, L. D., and Breitner, J. C. (2010) Elevated ratio of urinary metabolites of thromboxane and prostacyclin is associated with adverse cardiovascular events in ADAPT. PLoS One 5, e9340
    • (2010) PLoS One , vol.5
    • Montine, T.J.1    Sonnen, J.A.2    Milne, G.3    Baker, L.D.4    Breitner, J.C.5
  • 22
  • 23
    • 25444500410 scopus 로고    scopus 로고
    • Green tea epigallocatechin-3-gallate (EGCG) modulates amyloid precursor protein cleavage and reduces cerebral amyloidosis in Alzheimer transgenic mice
    • DOI 10.1523/JNEUROSCI.1521-05.2005
    • Rezai-Zadeh, K., Shytle, D., Sun, N., Mori, T., Hou, H., Jeanniton, D., Ehrhart, J., Townsend, K., Zeng, J., Morgan, D., Hardy, J., Town, T., and Tan, J. (2005) Green tea epigallocatechin-3-gallate (EGCG) modulates amyloid precursor protein cleavage and reduces cerebral amyloidosis in Alzheimer transgenic mice. J. Neurosci. 25, 8807-8814 (Pubitemid 41362059)
    • (2005) Journal of Neuroscience , vol.25 , Issue.38 , pp. 8807-8814
    • Rezai-Zadeh, K.1    Shytle, D.2    Sun, N.3    Mori, T.4    Hou, H.5    Jeanniton, D.6    Ehrhart, J.7    Townsend, K.8    Zeng, J.9    Morgan, D.10    Hardy, J.11    Town, T.12    Tan, J.13
  • 26
    • 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
    • DOI 10.1046/j.1471-4159.2003.01976.x
    • 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 (Pubitemid 37210651)
    • (2003) Journal of Neurochemistry , vol.87 , Issue.1 , pp. 172-181
    • Ono, K.1    Yoshiike, Y.2    Takashima, A.3    Hasegawa, K.4    Naiki, H.5    Yamada, M.6
  • 27
    • 27844497059 scopus 로고    scopus 로고
    • Resveratrol promotes clearance of Alzheimer's disease amyloid-β peptides
    • DOI 10.1074/jbc.M508246200
    • Marambaud, P., Zhao, H., and Davies, P. (2005) Resveratrol promotes clearance of Alzheimer's disease amyloid-β peptides. J. Biol. Chem. 280, 37377-37382 (Pubitemid 41642343)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.45 , pp. 37377-37382
    • Marambaud, P.1    Zhao, H.2    Davies, P.3
  • 30
    • 7044286419 scopus 로고    scopus 로고
    • Anti-amyloidogenic activity of tannic acid and its activity to destabilize Alzheimer's β-amyloid fibrils in vitro
    • DOI 10.1016/j.bbadis.2004.06.008, PII S0925443904001024
    • Ono, K., Hasegawa, K., Naiki, H., and Yamada, M. (2004) Anti-amyloidogenic activity of tannic acid and its activity to destabilize Alzheimer's β-amyloid fibrils in vitro. Biochim. Biophys. Acta 1690, 193-202 (Pubitemid 39423614)
    • (2004) Biochimica et Biophysica Acta - Molecular Basis of Disease , vol.1690 , Issue.3 , pp. 193-202
    • Ono, K.1    Hasegawa, K.2    Naiki, H.3    Yamada, M.4
  • 32
    • 77956595088 scopus 로고    scopus 로고
    • The flavanol (-)-epigallocatechin 3-gallate inhibits amyloid formation by islet amyloid polypeptide, disaggregates amyloid fibrils, and protects cultured cells against IAPP-induced toxicity
    • Meng, F., Abedini, A., Plesner, A., Verchere, C. B., and Raleigh, D. P. (2010) The flavanol (-)-epigallocatechin 3-gallate inhibits amyloid formation by islet amyloid polypeptide, disaggregates amyloid fibrils, and protects cultured cells against IAPP-induced toxicity. Biochemistry 49, 8127-8133
    • (2010) Biochemistry , vol.49 , pp. 8127-8133
    • Meng, F.1    Abedini, A.2    Plesner, A.3    Verchere, C.B.4    Raleigh, D.P.5
  • 33
    • 0030833055 scopus 로고    scopus 로고
    • Accelerated amyloid deposition in the brains of transgenic mice coexpressing mutant presenilin 1 and amyloid precursor proteins
    • DOI 10.1016/S0896-6273(00)80974-5
    • Borchelt, D. R., Ratovitski, T., van Lare, J., Lee, M. K., Gonzales, V., Jenkins, N. A., Copeland, N. G., Price, D. L., and Sisodia, S. S. (1997) Accelerated amyloid deposition in the brains of transgenic mice coexpressing mutant presenilin 1 and amyloid precursor proteins. Neuron 19, 939-945 (Pubitemid 27471397)
    • (1997) Neuron , vol.19 , Issue.4 , pp. 939-945
    • Borchelt, D.R.1    Ratovitski, T.2    Van Lare, J.3    Lee, M.K.4    Gonzales, V.5    Jenkins, N.A.6    Copeland, N.G.7    Price, D.L.8    Sisodia, S.S.9
  • 34
    • 0035830686 scopus 로고    scopus 로고
    • Progressive, age-related behavioral impairments in transgenic mice carrying both mutant amyloid precursor protein and presenilin-1 transgenes
    • DOI 10.1016/S0006-8993(00)03186-3, PII S0006899300031863
    • Arendash, G. W., King, D. L., Gordon, M. N., Morgan, D., Hatcher, J. M., Hope, C. E., and Diamond, D. M. (2001) Progressive, age-related behavioral impairments in transgenic mice carrying both mutant amyloid precursor protein and presenilin-1 transgenes. Brain Res. 891, 42-53 (Pubitemid 32115494)
    • (2001) Brain Research , vol.891 , Issue.1-2 , pp. 42-53
    • Arendash, G.W.1    King, D.L.2    Gordon, M.N.3    Morgan, D.4    Hatcher, J.M.5    Hope, C.E.6    Diamond, D.M.7
  • 35
    • 3042651851 scopus 로고    scopus 로고
    • APP processing and amyloid deposition in mice haplo-insufficient for presenilin 1
    • DOI 10.1016/j.neurobiolaging.2003.09.008, PII S0197458003002367
    • Jankowsky, J. L., Slunt, H. H., Gonzales, V., Jenkins, N. A., Copeland, N. G., and Borchelt, D. R. (2004) APP processing and amyloid deposition in mice haplo-insufficient for presenilin 1. Neurobiol. Aging 25, 885-892 (Pubitemid 38813168)
    • (2004) Neurobiology of Aging , vol.25 , Issue.7 , pp. 885-892
    • Jankowsky, J.L.1    Slunt, H.H.2    Gonzales, V.3    Jenkins, N.A.4    Copeland, N.G.5    Borchelt, D.R.6
  • 37
    • 0030969249 scopus 로고    scopus 로고
    • Hippocampal morphology and open-field behavior in Mus musculus domesticus and Mus spretus inbred mice
    • Laghmouch, A., Bertholet, J. Y., and Crusio, W. E. (1997) Hippocampal morphology and open-field behavior in Mus musculus domesticus and Mus spretus inbred mice. Behav. Genet. 27, 67-73 (Pubitemid 27200655)
    • (1997) Behavior Genetics , vol.27 , Issue.1 , pp. 67-73
    • Laghmouch, A.1    Bertholet, J.-Y.2    Crusio, W.E.3
  • 38
    • 31844447417 scopus 로고    scopus 로고
    • Optimization of chronic stress paradigms using anxiety- and depression-like behavioral parameters
    • Kim, K. S., and Han, P. L. (2006) Optimization of chronic stress paradigms using anxiety- and depression-like behavioral parameters. J. Neurosci. Res. 83, 497-507
    • (2006) J. Neurosci. Res. , vol.83 , pp. 497-507
    • Kim, K.S.1    Han, P.L.2
  • 40
    • 0019957779 scopus 로고
    • Place navigation impaired in rats with hippocampal lesions
    • DOI 10.1038/297681a0
    • Morris, R.G., Garrud, P., Rawlins, J. N., and O'Keefe, J. (1982) Place navigation impaired in rats with hippocampal lesions. Nature 297, 681-683 (Pubitemid 12096189)
    • (1982) Nature , vol.297 , Issue.5868 , pp. 681-683
    • Morris, R.G.M.1    Garrud, P.2    Rawlins, J.N.P.3    O'Keefe, J.4
  • 41
    • 0030965113 scopus 로고    scopus 로고
    • Dissociable effects of selective lesions to hippocampal subsystems on exploratory behavior, contextual learning, and spatial learning
    • DOI 10.1037/0735-7044.111.3.487
    • Good, M., and Honey, R. C. (1997) Dissociable effects of selective lesions to hippocampal subsystems on exploratory behavior, contextual learning, and spatial learning. Behav. Neurosci. 111, 487-493 (Pubitemid 27251318)
    • (1997) Behavioral Neuroscience , vol.111 , Issue.3 , pp. 487-493
    • Good, M.1    Honey, R.C.2
  • 43
    • 75849133906 scopus 로고    scopus 로고
    • Overexpression of human S100B exacerbates cerebral amyloidosis and gliosis in the Tg2576 mouse model of Alzheimer's disease
    • Mori, T., Koyama, N., Arendash, G. W., Horikoshi-Sakuraba, Y., Tan, J., and Town, T. (2010) Overexpression of human S100B exacerbates cerebral amyloidosis and gliosis in the Tg2576 mouse model of Alzheimer's disease. Glia 58, 300-314
    • (2010) Glia , vol.58 , pp. 300-314
    • Mori, T.1    Koyama, N.2    Arendash, G.W.3    Horikoshi-Sakuraba, Y.4    Tan, J.5    Town, T.6
  • 45
    • 0034667558 scopus 로고    scopus 로고
    • CD45 opposes β-amyloid peptide-induced microglial activation via inhibition of p44/42 mitogen-activated protein kinase
    • Tan, J., Town, T., Mori, T., Wu, Y., Saxe, M., Crawford, F., and Mullan, M. (2000) CD45 opposes β-amyloid peptide-induced microglial activation via inhibition of p44/42 mitogen-activated protein kinase. J. Neurosci. 20, 7587-7594
    • (2000) J. Neurosci. , vol.20 , pp. 7587-7594
    • Tan, J.1    Town, T.2    Mori, T.3    Wu, Y.4    Saxe, M.5    Crawford, F.6    Mullan, M.7
  • 46
    • 0035863055 scopus 로고    scopus 로고
    • Age-dependent changes in brain, CSF, and plasma amyloid β protein in the Tg2576 transgenic mouse model of Alzheimer's disease
    • Kawarabayashi, T., Younkin, L. H., Saido, T. C., Shoji, M., Ashe, K. H., and Younkin, S. G. (2001) Age-dependent changes in brain, CSF, and plasma amyloid β protein in the Tg2576 transgenic mouse model of Alzheimer's disease. J. Neurosci. 21, 372-381 (Pubitemid 32107428)
    • (2001) Journal of Neuroscience , vol.21 , Issue.2 , pp. 372-381
    • Kawarabayashi, T.1    Younkin, L.H.2    Saido, T.C.3    Shoji, M.4    Ashe, K.H.5    Younkin, S.G.6
  • 49
    • 60549107033 scopus 로고    scopus 로고
    • A specific enzyme-linked immunosorbent assay for measuring β-amyloid protein oligomers in human plasma and brain tissue of patients with Alzheimer disease
    • Xia, W., Yang, T., Shankar, G., Smith, I. M., Shen, Y., Walsh, D. M., and Selkoe, D. J. (2009) A specific enzyme-linked immunosorbent assay for measuring β-amyloid protein oligomers in human plasma and brain tissue of patients with Alzheimer disease. Arch. Neurol. 66, 190-199
    • (2009) Arch. Neurol. , vol.66 , pp. 190-199
    • Xia, W.1    Yang, T.2    Shankar, G.3    Smith, I.M.4    Shen, Y.5    Walsh, D.M.6    Selkoe, D.J.7
  • 52
    • 0029973286 scopus 로고    scopus 로고
    • Cerebral amyloid angiopathy in the brains of patients with Alzheimer's disease: The CERAD experience, part XV
    • Ellis, R. J., Olichney, J. M., Thal, L. J., Mirra, S. S., Morris, J. C., Beekly, D., and Heyman, A. (1996) Cerebral amyloid angiopathy in the brains of patients with Alzheimer's disease: the CERAD experience, Part XV. Neurology 46, 1592-1596 (Pubitemid 26185777)
    • (1996) Neurology , vol.46 , Issue.6 , pp. 1592-1596
    • Ellis, R.J.1    Olichney, J.M.2    Thal, L.J.3    Mirra, S.S.4    Morris, J.C.5    Beekly, D.6    Heyman, A.7
  • 53
  • 55
    • 0033370498 scopus 로고    scopus 로고
    • Evidence for glial-mediated inflammation in aged APP(SW) transgenic mice
    • DOI 10.1016/S0197-4580(99)00065-2, PII S0197458099000652
    • Benzing, W. C., Wujek, J. R., Ward, E. K., Shaffer, D., Ashe, K. H., Younkin, S. G., and Brunden, K. R. (1999) Evidence for glial-mediated inflammation in aged APPsw transgenic mice. Neurobiol. Aging 20, 581-589 (Pubitemid 30064403)
    • (1999) Neurobiology of Aging , vol.20 , Issue.6 , pp. 581-589
    • Benzing, W.C.1    Wujek, J.R.2    Ward, E.K.3    Shaffer, D.4    Ashe, K.H.5    Younkin, S.G.6    Brunden, K.R.7
  • 59
    • 0034845295 scopus 로고    scopus 로고
    • Enhanced expression of Iba1, ionized calcium-binding adapter molecule 1, after transient focal cerebral ischemia in rat brain
    • Ito, D., Tanaka, K., Suzuki, S., Dembo, T., and Fukuuchi, Y. (2001) Enhanced expression of Iba1, ionized calcium-binding adapter molecule 1, after transient focal cerebral ischemia in rat brain. Stroke 32, 1208-1215 (Pubitemid 32825812)
    • (2001) Stroke , vol.32 , Issue.5 , pp. 1208-1215
    • Ito, D.1    Tanaka, K.2    Suzuki, S.3    Dembo, T.4    Fukuuchi, Y.5
  • 60
    • 22144448657 scopus 로고    scopus 로고
    • Kettermann, H., and Ransom, B. R., eds . Oxford University Press, New York
    • Streit, W. J. (2005) in Neuroglia (Kettermann, H., and Ransom, B. R., eds) pp. 60-71, Oxford University Press, New York
    • (2005) Neuroglia , pp. 60-71
    • Streit, W.J.1
  • 62
    • 0033957048 scopus 로고    scopus 로고
    • Mutagenicity and antimutagenicity studies of tannic acid and its related compounds
    • Chen, S. C., and Chung, K. T. (2000) Mutagenicity and antimutagenicity studies of tannic acid and its related compounds. Food Chem. Toxicol. 38, 1-5
    • (2000) Food Chem. Toxicol. , vol.38 , pp. 1-5
    • Chen, S.C.1    Chung, K.T.2
  • 64
    • 58249126953 scopus 로고    scopus 로고
    • Intramyocardial injection of tannic acid attenuates postinfarction remodeling: A novel approach to stabilize the breaking extracellular matrix
    • Zhang, H., Zhu, S. J., Wang, D., Wei, Y. J., and Hu, S. S. (2009) Intramyocardial injection of tannic acid attenuates postinfarction remodeling: a novel approach to stabilize the breaking extracellular matrix. J. Thorac. Cardiovasc. Surg. 137, 216-222, 222e1-2
    • (2009) J. Thorac. Cardiovasc. Surg. , vol.137
    • Zhang, H.1    Zhu, S.J.2    Wang, D.3    Wei, Y.J.4    Hu, S.S.5
  • 66
    • 0005869124 scopus 로고
    • The acute toxicity of tannic acid administered intragastrically
    • Boyd, E. M., Bereczky, K., and Godi, I. (1965) The acute toxicity of tannic acid administered intragastrically. Can. Med. Assoc. J. 92, 1292-1297
    • (1965) Can. Med. Assoc. J. , vol.92 , pp. 1292-1297
    • Boyd, E.M.1    Bereczky, K.2    Godi, I.3
  • 67
    • 63149091662 scopus 로고    scopus 로고
    • Tannic acid facilitates expression of the polypyrimidine tract binding protein and alleviates deleterious inclusion of CHRNA1 exon P3A due to an hnRNP H-disrupting mutation in congenital myasthenic syndrome
    • Bian, Y., Masuda, A., Matsuura, T., Ito, M., Okushin, K., Engel, A. G., and Ohno, K. (2009) Tannic acid facilitates expression of the polypyrimidine tract binding protein and alleviates deleterious inclusion of CHRNA1 exon P3A due to an hnRNP H-disrupting mutation in congenital myasthenic syndrome. Hum. Mol. Genet. 18, 1229-1237
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 1229-1237
    • Bian, Y.1    Masuda, A.2    Matsuura, T.3    Ito, M.4    Okushin, K.5    Engel, A.G.6    Ohno, K.7
  • 68
    • 69949105336 scopus 로고    scopus 로고
    • From functional food to medicinal product: Systematic approach in analysis of polyphenolics from propolis and wine
    • Medić-Sarić, M., Rastija, V., Bojić, M., and Males, Z. (2009) From functional food to medicinal product: systematic approach in analysis of polyphenolics from propolis and wine. Nutr. J. 8, 33
    • (2009) Nutr. J. , vol.8 , pp. 33
    • Medić-Sarić, M.1    Rastija, V.2    Bojić, M.3    Males, Z.4
  • 69
    • 2342588813 scopus 로고    scopus 로고
    • Intestinal absorption of p-coumaric and gallic acids in rats after oral administration
    • Konishi, Y., Hitomi, Y., and Yoshioka, E. (2004) Intestinal absorption of p-coumaric and gallic acids in rats after oral administration. J. Agric. Food Chem. 52, 2527-2532
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 2527-2532
    • Konishi, Y.1    Hitomi, Y.2    Yoshioka, E.3
  • 70
    • 0035069494 scopus 로고    scopus 로고
    • Pharmacokinetics of gallic acid and its relative bioavailability from tea in healthy humans
    • Shahrzad, S., Aoyagi, K., Winter, A., Koyama, A., and Bitsch, I. (2001) Pharmacokinetics of gallic acid and its relative bioavailability from tea in healthy humans. J. Nutr. 131, 1207-1210 (Pubitemid 32275101)
    • (2001) Journal of Nutrition , vol.131 , Issue.4 , pp. 1207-1210
    • Shahrzad, S.1    Aoyagi, K.2    Winter, A.3    Koyama, A.4    Bitsch, I.5
  • 71
    • 33644660982 scopus 로고    scopus 로고
    • Green tea catechins as brain-permeable, natural iron chelators- antioxidants for the treatment of neurodegenerative disorders
    • DOI 10.1002/mnfr.200500156
    • Mandel, S., Amit, T., Reznichenko, L., Weinreb, O., and Youdim, M. B. (2006) Green tea catechins as brain-permeable, natural iron chelators- antioxidants for the treatment of neurodegenerative disorders. Mol. Nutr. Food Res. 50, 229-234 (Pubitemid 43325663)
    • (2006) Molecular Nutrition and Food Research , vol.50 , Issue.2 , pp. 229-234
    • Mandel, S.1    Amit, T.2    Reznichenko, L.3    Weinreb, O.4    Youdim, M.B.H.5
  • 72
    • 70349106346 scopus 로고    scopus 로고
    • Bioavailability of gallic acid and catechins from grape seed polyphenol extract is improved by repeated dosing in rats: Implications for treatment in Alzheimer's disease
    • Ferruzzi, M. G., Lobo, J. K., Janle, E. M., Cooper, B., Simon, J. E., Wu, Q. L., Welch, C., Ho, L., Weaver, C., and Pasinetti, G. M. (2009) Bioavailability of gallic acid and catechins from grape seed polyphenol extract is improved by repeated dosing in rats: implications for treatment in Alzheimer's disease. J. Alzheimers's Dis. 18, 113-124
    • (2009) J. Alzheimers's Dis. , vol.18 , pp. 113-124
    • Ferruzzi, M.G.1    Lobo, J.K.2    Janle, E.M.3    Cooper, B.4    Simon, J.E.5    Wu, Q.L.6    Welch, C.7    Ho, L.8    Weaver, C.9    Pasinetti, G.M.10
  • 73
    • 16544373574 scopus 로고    scopus 로고
    • Amyloid precursor protein compartmentalization restricts β-amyloid production: Therapeutic targets based on BACE compartmentalization
    • DOI 10.1385/JMN:24:1:137
    • Gandhi, S., Refolo, L. M., and Sambamurti, K. (2004) Amyloid precursor protein compartmentalization restricts β-amyloid production: therapeutic targets based on BACE compartmentalization. J. Mol. Neurosci. 24, 137-143 (Pubitemid 41359179)
    • (2004) Journal of Molecular Neuroscience , vol.24 , Issue.1 , pp. 137-143
    • Gandhi, S.1    Refolo, L.M.2    Sambamurti, K.3
  • 76
    • 0026740957 scopus 로고
    • Hydrolyzable tannins: Potent inhibitors of hydroperoxide production and tumor promotion in mouse skin treated with 12-O-tetradecanoylphorbol-13-acetate in vivo
    • Gali, H. U., Perchellet, E. M., Klish, D. S., Johnson, J. M., and Perchellet, J. P. (1992) Hydrolyzable tannins: potent inhibitors of hydroperoxide production and tumor promotion in mouse skin treated with 12-O-tetradecanoylphorbol-13-acetate in vivo. Int. J. Cancer 51, 425-432
    • (1992) Int. J. Cancer , vol.51 , pp. 425-432
    • Gali, H.U.1    Perchellet, E.M.2    Klish, D.S.3    Johnson, J.M.4    Perchellet, J.P.5
  • 77
    • 33746351505 scopus 로고    scopus 로고
    • Preventive effect of tannic acid on 2-acetylaminofluorene induced antioxidant level, tumor promotion and hepatotoxicity: A chemopreventive study
    • DOI 10.1179/135100006X101066
    • Sehrawat, A., Sharma, S., and Sultana, S. (2006) Preventive effect of tannic acid on 2-acetylaminofluorene induced antioxidant level, tumor promotion and hepatotoxicity: a chemopreventive study. Redox Rep. 11, 85-95 (Pubitemid 44111116)
    • (2006) Redox Report , vol.11 , Issue.2 , pp. 85-95
    • Sehrawat, A.1    Sharma, S.2    Sultana, S.3
  • 78
    • 0023633015 scopus 로고
    • Reactive microglia in patients with senile dementia of the Alzheimer type are positive for the histocompatibility glycoprotein HLA-DR
    • McGeer, P. L., Itagaki, S., Tago, H., and McGeer, E. G. (1987) Reactive microglia in patients with senile dementia of the Alzheimer type are positive for the histocompatibility glycoprotein HLA-DR. Neurosci. Lett. 79, 195-200 (Pubitemid 17144469)
    • (1987) Neuroscience Letters , vol.79 , Issue.1-2 , pp. 195-200
    • McGeer, P.L.1    Itagaki, S.2    Tago, H.3    McGeer, E.G.4


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