Green tea epigallocatechin-3-gallate (EGCG) reduces β-amyloid mediated cognitive impairment and modulates tau pathology in Alzheimer transgenic mice

Correlative Memory Deficits, Aβ Elevation, and Amyloid Plaques in Transgenic Mice

Hsiao, K., Chapman, P., Nilsen, S., Eckman, C., Harigaya, Y., Younkin, S., Yang, F., & Cole, G. (1996) · Science · doi:10.1126/science.274.5284.99 · Cited by 4,210 · see citing works

β-Secretase Cleavage of Alzheimer's Amyloid Precursor Protein by the Transmembrane Aspartic Protease BACE

Vassar, R., Bennett, B. D., Babu-Khan, S., Kahn, S., Mendiaz, E. A., Denis, P., Teplow, D. B., Ross, S., Amarante, P., Loeloff, R., et al. (1999) · Science · doi:10.1126/science.286.5440.735 · Cited by 3,876 · see citing works

Curcumin Inhibits Formation of Amyloid β Oligomers and Fibrils, Binds Plaques, and Reduces Amyloid in Vivo

Yang, F., Lim, G. P., Begum, A. N., Ubeda, O. J., Simmons, M. R., Ambegaokar, S. S., Chen, P. P., Kayed, R., Glabe, C. G., Frautschy, S. A., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m404751200 · Cited by 2,336 · see citing works

Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein

De Strooper, B., Saftig, P., Craessaerts, K., Vanderstichele, H., Guhde, G., Annaert, W., Von Figura, K., & Van Leuven, F. (1998) · Nature · doi:10.1038/34910 · Cited by 1,818 · see citing works

Microtubule-associated protein tau. A component of Alzheimer paired helical filaments.

Grundke, I., Iqbal, K., Quinlan, M., Tung, Y. C., Zaidi, M. S., & Wisniewski, H. M. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38495-8 · Cited by 1,780 · see citing works

Membrane-anchored aspartyl protease with Alzheimer's disease β-secretase activity

Yan, R., Bienkowski, M. J., Shuck, M. E., Miao, H., Tory, M. C., Pauley, A. M., Brashler, J. R., Stratman, N. C., Mathews, W. R., Buhl, A. E., et al. (1999) · Nature · doi:10.1038/990107 · Cited by 1,438 · see citing works

Neurotoxicity induces cleavage of p35 to p25 by calpain

Lee, M.-S., Kwon, Y. T., Li, M., Peng, J., Friedlander, R. M., & Tsai, L. (2000) · Nature · doi:10.1038/35012636 · Cited by 1,057 · see citing works

Hyperphosphorylation induces self-assembly of τ into tangles of paired helical filaments/straight filaments

Alonso, A. D. C., Zaidi, T., Novák, M., Grundke, I., & Iqbal, K. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.121119298 · Cited by 968 · see citing works

Resveratrol Promotes Clearance of Alzheimer's Disease Amyloid-β Peptides

Marambaud, P., Zhao, H., & Davies, P. J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508246200 · Cited by 750 · see citing works

A preparation of Alzheimer paired helical filaments that displays distinct tau proteins by polyacrylamide gel electrophoresis.

Greenberg, S. G., & Davies, P. J. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.15.5827 · Cited by 732 · see citing works

Tau protein and the neurofibrillary pathology of Alzheimer's disease

Goedert, M. (1993) · Trends in Neurosciences · doi:10.1016/0166-2236(93)90078-z · Cited by 718 · see citing works

Green tea Epigallocatechin-3-Gallate (EGCG) Modulates Amyloid Precursor Protein Cleavage and Reduces Cerebral Amyloidosis in Alzheimer Transgenic Mice

Rezai-Zadeh, K., Shytle, D., Sun, N., Mori, T., Hou, H., Jeanniton, D., Ehrhart, J., Townsend, K., Zeng, J., Morgan, D., et al. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.1521-05.2005 · Cited by 713 · see citing works

The high-affinity HSP90–CHIP complex recognizes and selectively degrades phosphorylated tau client proteins

Dickey, C. A., Kamal, A., Lundgren, K., Klosak, N., Bailey, R. M., Dunmore, J., Ash, P., Shoraka, S., Zlatkovic, J., Eckman, C. B., et al. (2007) · Journal of Clinical Investigation · doi:10.1172/jci29715 · Cited by 642 · see citing works

Amyloid precursor protein processing and Aβ 42 deposition in a transgenic mouse model of Alzheimer disease

Johnson‐Wood, K., Lee, M., Motter, R. N., Hu, K., Gordon, G., Barbour, R., Khan, K., Gordon, M. N., Tan, H. T., Games, D., et al. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.4.1550 · Cited by 634 · see citing works

β-Amyloid fibrils induce tau phosphorylation and loss of microtubule binding

Busciglio, J., Lorenzo, A., Yeh, J., & Yankner, B. A. (1995) · Neuron · doi:10.1016/0896-6273(95)90232-5 · Cited by 595 · see citing works

Wide distribution of [3H](-)-epigallocatechin gallate, a cancer preventive tea polyphenol, in mouse tissue

Suganuma, M. (1998) · Carcinogenesis · doi:10.1093/carcin/19.10.1771 · Cited by 527 · see citing works

Neuron loss in APP transgenic mice

Calhoun, M. E., Wiederhold, K.-H., Abramowski, D., Phinney, A. L., Probst, A., Sturchler-Pierrat, C., Staufenbiel, M., Sommer, B., & Jucker, M. (1998) · Nature · doi:10.1038/27351 · Cited by 502 · see citing works

Caffeine protects Alzheimer’s mice against cognitive impairment and reduces brain β-amyloid production

Arendash, G. W., Schleif, W. S., Rezai-Zadeh, K. P., Jackson, E. K., Zacharia, L. C., Cracchiolo, J. R., Shippy, D. C., & Tan, J. (2006) · Neuroscience · doi:10.1016/j.neuroscience.2006.07.021 · Cited by 461 · see citing works

Cellular mechanisms of β-amyloid production and secretion

Sinha, S., & Lieberburg, I. M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.20.11049 · Cited by 438 · see citing works

Increased Activity‐Regulating and Neuroprotective Efficacy of α‐Secretase‐Derived Secreted Amyloid Precursor Protein Conferred by a C‐Terminal Heparin‐Binding Domain

Furukawa, K., Sopher, B. L., Rydel, R. E., Begley, J. G., Pham, D. G., Martin, G. M., Fox, M., & Mattson, M. P. (1996) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1996.67051882.x · Cited by 414 · see citing works

Neuroprotection and neurorescue against Aβ toxicity and PKC‐dependent release of non‐amyloidogenic soluble precursor protein by green tea polyphenol (‐)‐epigallocatechin‐3‐gallate

Levites, Y., Amit, T., Mandel, S. A., & Youdim, M. B. H. (2003) · The FASEB Journal · doi:10.1096/fj.02-0881fje · Cited by 372 · see citing works

Epigallocatechin-3-Gallate Is Absorbed but Extensively Glucuronidated Following Oral Administration to Mice

Lambert, J. D., Lee, M., Lu, H., Meng, X., Hong, J. J. J., Seril, D. N., Yang, C. S., & Sturgill, M. G. (2003) · Journal of Nutrition · doi:10.1093/jn/133.12.4172 · Cited by 318 · see citing works

A Loss of Function Mutation of Presenilin-2 Interferes with Amyloid β-Peptide Production and Notch Signaling

Steiner, H., Duff, K., Capell, A., Romig, H., Grim, M. G., Lincoln, S., Hardy, J., Yu, X., Picciano, M., Fechteler, K., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.40.28669 · Cited by 306 · see citing works

Biochemical detection of Aβ isoforms: implications for pathogenesis, diagnosis, and treatment of Alzheimer’s disease

Golde, T. E., Eckman, C. B., & Younkin, S. G. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(00)00043-0 · Cited by 300 · see citing works

Neutralization of Transthyretin Reverses the Neuroprotective Effects of Secreted Amyloid Precursor Protein (APP) in APPSwMice Resulting in Tau Phosphorylation and Loss of Hippocampal Neurons: Support for the Amyloid Hypothesis

Stein, T. D., Anders, N. J., DeCarli, C. S., Chan, S. L., Mattson, M. P., & Johnson, J. A. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.2211-04.2004 · Cited by 277 · see citing works

Lithium protects cultured neurons against β‐amyloid‐induced neurodegeneration

Alvarez, G., Muñoz-Montaño, J. R., Satrústegui, J., Ávila, J., Bogónez, E., & Díaz‐Nido, J. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00685-7 · Cited by 270 · see citing works

The Role of APP Processing and Trafficking Pathways in the Formation of Amyloid β‐Proteina

Selkoe, D. J., Yamazaki, T., Citron, M., Podlisny, M. B., Koo, E. H., Teplow, D. B., & Haass, C. (1996) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1996.tb34401.x · Cited by 246 · see citing works

Cellular signaling roles of TGFβ, TNFα and βAPP in brain injury responses and Alzheimer's disease

Mattson, M. P., Barger, S. W., Furukawa, K., Bruce‐Keller, A. J., Wyss‐Coray, T., Mark, R. J., & Mucke, L. (1997) · Brain Research Reviews · doi:10.1016/s0165-0173(96)00014-8 · Cited by 243 · see citing works

Behavioral characterization of the Tg2576 transgenic model of Alzheimer's disease through 19 months

King, D. L., & Arendash, G. W. (2002) · Physiology & Behavior · doi:10.1016/s0031-9384(02)00639-x · Cited by 242 · see citing works

Role of CD40 ligand in amyloidosis in transgenic Alzheimer's mice

Tan, J., Town, T., Crawford, F., Mori, T., DelleDonne, A., Crescentini, R., Obregon, D., Flavell, R. A., & Mullan, M. J. (2002) · Nature Neuroscience · doi:10.1038/nn968 · Cited by 217 · see citing works

ADAM10 Activation Is Required for Green Tea (–)-Epigallocatechin-3-gallate-induced α-Secretase Cleavage of Amyloid Precursor Protein

Obregon, D. F., Rezai-Zadeh, K. P., Bai, Y., Sun, N., Hou, H., Ehrhart, J. C., Zeng, J., Mori, T., Arendash, G. W., Shytle, D., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600617200 · Cited by 210 · see citing works

τ is phosphorylated by GSK‐3 at several sites found in Alzheimer disease and its biological activity markedly inhibited only after it is prephosphorylated by A‐kinase

Wang, J.-Z., Wu, Q., Smith, A., Grundke, I., & Iqbal, K. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01090-4 · Cited by 199 · see citing works

Advances in the Cellular and Molecular Biology of the Beta-Amyloid Protein in Alzheimer 's Disease

Sambamurti, K., Greig, N. H., & Lahiri, D. K. (2002) · NeuroMolecular Medicine · doi:10.1385/nmm:1:1:1 · Cited by 184 · see citing works

Epigallocatechin Gallate Inhibits Aryl Hydrocarbon Receptor Gene Transcription through an Indirect Mechanism Involving Binding to a 90 kDa Heat Shock Protein

Palermo, C. M., Westlake, C. A., & Gasiewicz, T. A. (2005) · Biochemistry · doi:10.1021/bi047433p · Cited by 167 · see citing works

Green tea catechins prevent cognitive deficits caused by Aβ1–40 in rats

Haque, A. M., Hashimoto, M., Katakura, M., Hara, Y., & Shido, O. (2008) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2007.08.008 · Cited by 139 · see citing works

Truncated Carboxyl-Terminal Fragments of β-Amyloid Precursor Protein Are Processed to Amyloid β-Proteins 40 and 42

Funamoto, S., Morishima‐Kawashima, M., Tanimura, Y., Hirotani, N., Saido, T. C., & Ihara, Y. (2004) · Biochemistry · doi:10.1021/bi049399k · Cited by 131 · see citing works

Behavioral Assessment of Alzheimer's Transgenic Mice Following Long-Term A β Vaccination: Task Specificity and Correlations between A β Deposition and Spatial Memory

Arendash, G. W., Gordon, M. N., Diamond, D. M., Austin, L. A., Hatcher-Martin, J. M., Jantzen, P. T., DiCarlo, G., Wilcock, D. M., & Morgan, D. (2001) · DNA and Cell Biology · doi:10.1089/10445490152717604 · Cited by 130 · see citing works

The Search for α-Secretase and its Potential as a Therapeutic Approach to Alzheimer's Disease

Hooper, N. M., & Turner, A. J. (2002) · Current Medicinal Chemistry · doi:10.2174/0929867023370121 · Cited by 127 · see citing works

Multi-metric behavioral comparison of APPsw and P301L models for Alzheimer's disease: linkage of poorer cognitive performance to tau pathology in forebrain

Arendash, G. W., Lewis, J., Leighty, R. E., McGowan, E., Cracchiolo, J. R., Hutton, M., & Garcia, M. F. (2004) · Brain Research · doi:10.1016/j.brainres.2004.02.081 · Cited by 127 · see citing works

Phosphorylated tau and the neurodegenerative foldopathies

Kosik, K. S., & Shimura, H. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.10.011 · Cited by 123 · see citing works

Tau Protein and the Neurofibrillary Pathology of Alzheimer's Disease

Goedert, M. (1996) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1996.tb34410.x · Cited by 115 · see citing works

A68 proteins in Alzheimer's disease are composed of several tau isoforms in a phosphorylated state which affects their electrophoretic mobilities

Brion, J., Hanger, D. P., Couck, A. M., & Anderton, B. H. (1991) · Biochemical Journal · doi:10.1042/bj2790831 · Cited by 109 · see citing works

Secreted Form of Amyloid Precursor Protein Enhances Basal Glucose and Glutamate Transport and Protects Against Oxidative Impairment of Glucose and Glutamate Transport in Synaptosomes by a Cyclic GMP‐Mediated Mechanism

Mattson, M. P., Guo, Z. H., & Geiger, J. D. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0730532.x · Cited by 96 · see citing works

Amyloid at the cutting edge: activation of α-secretase prevents amyloidogenesis in an Alzheimer disease mouse model

Lichtenthaler, S. F., & Haass, C. (2004) · Journal of Clinical Investigation · doi:10.1172/jci21746 · Cited by 88 · see citing works

Phosphorylation of Tau, Aβ-Formation, and Apoptosis After In Vivo Inhibition of PP-1 and PP-2A

Arendt, T., Holzer, M., Fruth, R., Brückner, M. K., & Gärtner, U. (1998) · Neurobiology of Aging · doi:10.1016/s0197-4580(98)00003-7 · Cited by 88 · see citing works

Closing in on the Amyloid Cascade

Doms, R. W., & Huse, J. T. (2000) · Molecular Neurobiology · doi:10.1385/mn:22:1-3:081 · Cited by 49 · see citing works

Use of multimetric statistical analysis to characterize and discriminate between the performance of four Alzheimer’s transgenic mouse lines differing in Aβ deposition

Leighty, R. E., Nilsson, L. N. G., Potter, H., Costa, D. A., Low, M. A., Bales, K. R., Paul, S. M., & Arendash, G. W. (2004) · Behavioural Brain Research · doi:10.1016/j.bbr.2003.11.004 · Cited by 47 · see citing works

Alzheimer disease A68 proteins injected into rat brain induce codeposits of beta-amyloid, ubiquitin, and alpha 1-antichymotrypsin.

Shin, R., Bramblett, G. T., Lee, V. M., & Trojanowski, J. Q. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.14.6825 · Cited by 45 · see citing works

Phosphorylation of microtubule-associated protein tau by Ca2+/calmodulin-dependent protein kinase II in its tubulin binding sites

Yamamoto, H., Yamauchi, E., Taniguchi, H., Ono, T., & Miyamoto, E. (2002) · Archives of Biochemistry and Biophysics · doi:10.1016/s0003-9861(02)00556-8 · Cited by 39 · see citing works

Secreted β-APP stimulates MAP kinase and phosphorylation of tau in neurons

Greenberg, S. M., & Kosik, K. S. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(94)00172-w · Cited by 28 · see citing works

Nrf2–ARE pathway: An emerging target against oxidative stress and neuroinflammation in neurodegenerative diseases

Buendía, I., Michalska, P., Navarro, E., Gameiro‐Ros, I., Egea, J., & Leon, R. M. (2015) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2015.11.003 · Cited by 683 · see citing works

Bioinorganic Chemistry of Alzheimer’s Disease

Kepp, K. P. (2012) · Chemical Reviews · doi:10.1021/cr300009x · Cited by 672 · see citing works

Herbal extracts and phytochemicals: Plant secondary metabolites and the enhancement of human brain function

Kennedy, D. O., & Wightman, E. L. (2011) · Advances in Nutrition · doi:10.3945/an.110.000117 · Cited by 684 · see citing works

Development of Multifunctional Molecules as Potential Therapeutic Candidates for Alzheimer's Disease, Parkinson's Disease, and Amyotrophic Lateral Sclerosis in the Last Decade.

Savelieff, M. G., Nam, G., Kang, J., Lee, H. J., Lee, M., & Lim, M.-H. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00138 · Cited by 490 · see citing works

Therapeutic applications of compounds in the Magnolia family

Lee, Y., Lee, Y. M., Lee, C., Jung, J., Han, S., & Hong, J. T. (2011) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2011.01.010 · Cited by 490 · see citing works

Nutraceutical Antioxidants as Novel Neuroprotective Agents

Kelsey, N. A., Wilkins, H., & Linseman, D. A. (2010) · Molecules · doi:10.3390/molecules15117792 · Cited by 481 · see citing works

A Review of the Role of Green Tea (Camellia sinensis) in Antiphotoaging, Stress Resistance, Neuroprotection, and Autophagy

Prasanth, M. I., Sivamaruthi, B. S., Chaiyasut, C., & Tencomnao, T. (2019) · Nutrients · doi:10.3390/nu11020474 · Cited by 457 · see citing works

Flavonoids, cognition, and dementia: Actions, mechanisms, and potential therapeutic utility for Alzheimer disease

Williams, R. J., & Spencer, J. P. E. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.09.010 · Cited by 448 · see citing works

The flavonoid quercetin ameliorates Alzheimer's disease pathology and protects cognitive and emotional function in aged triple transgenic Alzheimer's disease model mice

Sabogal-Guáqueta, A. M., Muñoz‐Manco, J. I., Ramírez‐Pineda, J. R., Lamprea, M. R., Osorio, E., & Cardona‐Gómez, G. P. (2015) · Neuropharmacology · doi:10.1016/j.neuropharm.2015.01.027 · Cited by 453 · see citing works

Dietary Polyphenols as Modulators of Brain Functions: Biological Actions and Molecular Mechanisms Underpinning Their Beneficial Effects

Vauzour, D. (2012) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2012/914273 · Cited by 431 · see citing works

Naturally occurring phytochemicals for the prevention of Alzheimer’s disease

Kim, J., Lee, H. J., & Lee, K. W. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06562.x · Cited by 354 · see citing works

Flavonoids as Prospective Neuroprotectants and Their Therapeutic Propensity in Aging Associated Neurological Disorders

Ayaz, M., Sadiq, A., Junaid, M., Ullah, F., Ovais, M., Ullah, I., Ahmed, J., & Shahid, M. M. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00155 · Cited by 348 · see citing works

Potential neuroprotective properties of epigallocatechin-3-gallate (EGCG)

Singh, N. A., Mandal, A. K. A., & Khan, Z. A. (2015) · Nutrition Journal · doi:10.1186/s12937-016-0179-4 · Cited by 319 · see citing works

Management of oxidative stress and other pathologies in Alzheimer’s disease

Simunkova, M., Alwasel, S. H., Alhazza, I. M., Jomova, K., Kollar, V., Rusko, M., & Valko, M. (2019) · Archives of Toxicology · doi:10.1007/s00204-019-02538-y · Cited by 303 · see citing works

Polyphenols from Food and Natural Products: Neuroprotection and Safety

Silva, R. F. M., & Pogačnik, L. (2020) · Antioxidants · doi:10.3390/antiox9010061 · Cited by 292 · see citing works

Oxidative damage in neurodegeneration: roles in the pathogenesis and progression of Alzheimer disease

Marzia Perluigi, A., Domenico, F. D., & Butterfield, D. A. (2023) · Physiological Reviews · doi:10.1152/physrev.00030.2022 · Cited by 306 · see citing works

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., & Raleigh, D. P. (2010) · Biochemistry · doi:10.1021/bi100939a · Cited by 282 · see citing works

Inhibition and disaggregation of α-synuclein oligomers by natural polyphenolic compounds

Caruana, M., Högen, T., Levin, J., Hillmer, A. S., Giese, A., & Vassallo, N. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.03.046 · Cited by 274 · see citing works

Caloric restriction mimetics: towards a molecular definition

Madeo, F., Pietrocola, F., Eisenberg, T., & Kroemer, G. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4391 · Cited by 264 · see citing works

Beneficial Effects of Green Tea Catechins on Neurodegenerative Diseases

Pervin, M., Unno, K., Ohishi, T., Tanabe, H., Miyoshi, N., & Nakamura, Y. (2018) · Molecules · doi:10.3390/molecules23061297 · Cited by 258 · see citing works

Polyphenol Health Effects on Cardiovascular and Neurodegenerative Disorders: A Review and Meta-Analysis

Potì, F., Santi, D., Spaggiari, G., Zimetti, F., & Zanotti, I. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20020351 · Cited by 256 · see citing works

Neuroprotective molecular mechanisms of (−)-epigallocatechin-3-gallate: a reflective outcome of its antioxidant, iron chelating and neuritogenic properties

Weinreb, O., Amit, T., Mandel, S. A., & Youdim, M. B. H. (2009) · Genes & Nutrition · doi:10.1007/s12263-009-0143-4 · Cited by 244 · see citing works

Polyphenols: Well Beyond The Antioxidant Capacity: Gallic Acid and Related Compounds as Neuroprotective Agents: You are What You Eat!

Daglia, M., Lorenzo, A. D., Nabavi, S. F., Talas, Z., & Nabavi, S. F. (2014) · Current Pharmaceutical Biotechnology · doi:10.2174/138920101504140825120737 · Cited by 244 · see citing works

Phenolic compounds of green tea: Health benefits and technological application in food

Lorenzo, J. M., & Munekata, P. E. S. (2016) · Asian Pacific Journal of Tropical Biomedicine · doi:10.1016/j.apjtb.2016.06.010 · Cited by 239 · see citing works

Current and Emerging Drug Treatment Options for Alzheimerʼs Disease

Herrmann, N., Chau, S. A., Kircanski, I., & Lanctôt, K. L. (2011) · Drugs · doi:10.2165/11595870-000000000-00000 · Cited by 238 · see citing works

Neurotherapeutic applications of nanoparticles in Alzheimer’s disease

Sahni, J. K., Doggui, S., Ali, J., Baboota, S., Dao, L., & Ramassamy, C. (2011) · Journal of Controlled Release · doi:10.1016/j.jconrel.2010.11.033 · Cited by 219 · see citing works

Inhibiting toxic aggregation of amyloidogenic proteins: A therapeutic strategy for protein misfolding diseases

Cheng, B., Gong, H., Xiao, H., Petersen, R. B., Zheng, L., & Huang, K. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.06.029 · Cited by 219 · see citing works

Nutrition and the Risk of Alzheimer's Disease

Hu, N., Yu, J., Tan, L., Wang, Y., Sun, L., & Tan, L. (2013) · BioMed Research International · doi:10.1155/2013/524820 · Cited by 212 · see citing works

Oxidative stress and Alzheimer’s disease: dietary polyphenols as potential therapeutic agents

Darvesh, A. S., Carroll, R. T., Bishayee, A., Geldenhuys, W. J., & der Schyf, C. J. V. (2010) · Expert Review of Neurotherapeutics · doi:10.1586/ern.10.42 · Cited by 203 · see citing works

Natural product-based amyloid inhibitors

Velander, P., Wu, L., Henderson, F. E., Zhang, S., Bevan, D. R., & Xu, B. (2017) · Biochemical Pharmacology · doi:10.1016/j.bcp.2017.04.004 · Cited by 203 · see citing works

Epigallocatechin-3-gallate (EGCG)-Stabilized Selenium Nanoparticles Coated with Tet-1 Peptide To Reduce Amyloid-β Aggregation and Cytotoxicity

Zhang, J., Zhou, X., Yu, Q., Yang, L., Sun, D., Zhou, Y., & Liu, J. (2014) · ACS Applied Materials & Interfaces · doi:10.1021/am501341u · Cited by 199 · see citing works

Epigallocatechin-3-gallate prevents systemic inflammation-induced memory deficiency and amyloidogenesis via its anti-neuroinflammatory properties

Lee, Y., Choi, D., Yun, Y., Han, S., Oh, K., & Hong, J. T. (2012) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2012.06.011 · Cited by 195 · see citing works

l-Theanine, an amino acid in green tea, attenuates β-amyloid-induced cognitive dysfunction and neurotoxicity: Reduction in oxidative damage and inactivation of ERK/p38 kinase and NF-κB pathways

Kim, T. I., Lee, Y. K., Park, S. G., Choi, I. S., Ban, J. O., Park, H. K., Nam, S.-Y., Yun, Y. W., Han, S., Oh, K. W., et al. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.09.008 · Cited by 194 · see citing works

Deferoxamine inhibits iron induced hippocampal tau phosphorylation in the Alzheimer transgenic mouse brain

Guo, C., Wang, P., Zhong, M., Wang, T., Huang, X., Li, J., & Wang, Z. (2012) · Neurochemistry International · doi:10.1016/j.neuint.2012.12.005 · Cited by 190 · see citing works

Ion Mobility Spectrometry–Mass Spectrometry Defines the Oligomeric Intermediates in Amylin Amyloid Formation and the Mode of Action of Inhibitors

Young, L. M., Cao, P., Raleigh, D. P., Ashcroft, A. E., & Radford, S. E. (2013) · Journal of the American Chemical Society · doi:10.1021/ja406831n · Cited by 190 · see citing works

Flavonoids as Therapeutic Compounds Targeting Key Proteins Involved in Alzheimer’s Disease

Baptista, F. I., Henriques, A. G., Silva, A. M. S., Wiltfang, J., & Silva, O. A. B. D. C. E. (2013) · ACS Chemical Neuroscience · doi:10.1021/cn400213r · Cited by 189 · see citing works

Green Tea Epigallocatechin-3-Gallate (EGCG) and Other Flavonoids Reduce Alzheimer's Amyloid-Induced Mitochondrial Dysfunction

Dragicevic, N., Smith, A., Lin, X., Yuan, F., Copes, N., Delic, V., Tan, J., Cao, C., Shytle, R. D., & Bradshaw, P. C. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-101629 · Cited by 189 · see citing works

The Role of Phytochemicals in the Treatment and Prevention of Dementia

Howes, M. R., & Perry, E. K. (2011) · Drugs & Aging · doi:10.2165/11591310-000000000-00000 · Cited by 187 · see citing works

Green Tea Epigallocatechin 3-Gallate Accumulates in Mitochondria and Displays a Selective Antiapoptotic Effect Against Inducers of Mitochondrial Oxidative Stress in Neurons

Schroeder, E. K., Kelsey, N. A., Doyle, J., Breed, E. R., Bouchard, R. J., Loucks, F. A., Harbison, R. A., & Linseman, D. A. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2215 · Cited by 177 · see citing works

Biochemistry of Antioxidants: Mechanisms and Pharmaceutical Applications

Losada‐Barreiro, S., Bayındır, Z. S., Paiva‐Martins, F., & Bravo‐Díaz, C. (2022) · Biomedicines · doi:10.3390/biomedicines10123051 · Cited by 178 · see citing works

Green tea (−)epigallocatechin-3-gallate reverses oxidative stress and reduces acetylcholinesterase activity in a streptozotocin-induced model of dementia

Biasibetti, R., Tramontina, A. C., Costa, A. P., Dutra, M. F., Quincozes‐Santos, A., Nardin, P., Bernardi, C. L., Wartchow, K. M., Lunardi, P. S., & Gonçalves, C. (2012) · Behavioural Brain Research · doi:10.1016/j.bbr.2012.08.039 · Cited by 177 · see citing works

Consumption of Green Tea, but Not Black Tea or Coffee, Is Associated with Reduced Risk of Cognitive Decline

Noguchi-Shinohara, M., Yuki, S., Dohmoto, C., Ikeda, Y., Samuraki, M., Iwasa, K., Yokogawa, M., Asai, K., Komai, K., Nakamura, H., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0096013 · Cited by 174 · see citing works

Protective role of epigallocatechin-3-gallate in health and disease: A perspective

Chowdhury, A., Sarkar, J., Chakraborti, T., Pramanik, P. K., & Chakraborti, S. (2016) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2015.12.013 · Cited by 164 · see citing works

The efficacy of Epigallocatechin-3-gallate (green tea) in the treatment of Alzheimer’s disease: an overview of pre-clinical studies and translational perspectives in clinical practice

Cascella, M., Bimonte, S., Muzio, M. R., Schiavone, V., & Cuomo, A. (2017) · Infectious Agents and Cancer · doi:10.1186/s13027-017-0145-6 · Cited by 167 · see citing works

Structural Properties of EGCG-Induced, Nontoxic Alzheimer's Disease Aβ Oligomers

del Amo, J. M. L., Fink, U., Dasari, M., Grelle, G., Wanker, E. E., Bieschke, J., & Reif, B. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2012.01.013 · Cited by 162 · see citing works

Acute neurocognitive effects of epigallocatechin gallate (EGCG)

Scholey, A. B., Downey, L. A., Ciorciari, J., Pipingas, A., Nolidin, K., Finn, M., Wines, M., Catchlove, S. J., Terrens, A., Barlow, E., et al. (2011) · Appetite · doi:10.1016/j.appet.2011.11.016 · Cited by 150 · see citing works

Oleuropein Aglycone Protects Transgenic C. elegans Strains Expressing Aβ42 by Reducing Plaque Load and Motor Deficit

Diomede, L., Rigacci, S., Romeo, M., Stefani, M., & Salmona, M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0058893 · Cited by 146 · see citing works

Molecular Insight into Conformational Transition of Amyloid β-Peptide 42 Inhibited by (−)-Epigallocatechin-3-gallate Probed by Molecular Simulations

Liu, F., Dong, X., He, L., Middelberg, A. P. J., & Sun, Y. P. (2011) · The Journal of Physical Chemistry B · doi:10.1021/jp202640b · Cited by 142 · see citing works

Natural polyphenols effects on protein aggregates in Alzheimer's and Parkinson's prion-like diseases

Bilan, A. R., Freyssin, A., Page, G., & Fauconneau, B. (2018) · Neural Regeneration Research · doi:10.4103/1673-5374.233432 · Cited by 141 · see citing works

Cognitive function and tea consumption in community dwelling older Chinese in Singapore

Feng, L., Gwee, X., Kua, E. H., & Ng, T. P. (2010) · The journal of nutrition health & aging · doi:10.1007/s12603-010-0095-9 · Cited by 139 · see citing works

Polyphenols and neuroprotection: therapeutic implications for cognitive decline

Caruso, G., Torrisi, S. A., Mogavero, M. P., Currenti, W., Castellano, S., Godos, J., Ferri, R., Galvano, F., Leggio, G. M., Grosso, G., et al. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2021.108013 · Cited by 140 · see citing works

(−)-Epigallocatechin-3-Gallate (EGCG) Maintains κ-Casein in Its Pre-Fibrillar State without Redirecting Its Aggregation Pathway

Hudson, S. A., Ecroyd, H. W., Dehle, F. C., Musgrave, I., & Carver, J. A. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.07.031 · Cited by 138 · see citing works

Ethnopharmacological Approaches for Dementia Therapy and Significance of Natural Products and Herbal Drugs

Tewari, D., Stankiewicz, A. M., Mocan, A., Sah, A. N., Tzvetkov, N. T., Huminiecki, Ł., Horbańczuk, J. O., & Atanasov, A. G. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00003 · Cited by 136 · see citing works

Effect of flavonoids on learning, memory and neurocognitive performance: relevance and potential implications for Alzheimer's disease pathophysiology

Vauzour, D. (2013) · Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.6473 · Cited by 136 · see citing works

Molecular Insight into the Therapeutic Promise of Flavonoids against Alzheimer’s Disease

Uddin, M. S., Kabir, M. T., Niaz, K., Jeandet, P., Clément, C., Mathew, B., Rauf, A., Rengasamy, K. R. R., Sobarzo‐Sánchez, E., Ashraf, G. M., et al. (2020) · Molecules · doi:10.3390/molecules25061267 · Cited by 134 · see citing works

Natural Products as Promising Drug Candidates for the Treatment of Alzheimer’s Disease: Molecular Mechanism Aspect

Ansari, N., & Khodagholi, F. (2013) · Current Neuropharmacology · doi:10.2174/1570159x11311040005 · Cited by 131 · see citing works

Neurotheranostics as Personalized Medicines

Kevadiya, B. D., Ottemann, B. M., Thomas, M. B., Mukadam, I., Nigam, S., McMillan, J., Gorantla, S., Bronich, T. K., Edagwa, B., & Gendelman, H. E. (2019) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2018.10.011 · Cited by 124 · see citing works

Black Tea Theaflavins Inhibit Formation of Toxic Amyloid-β and α-Synuclein Fibrils

Grelle, G., Otto, A., Lorenz, M., Frank, R. F., Wanker, E. E., & Bieschke, J. (2011) · Biochemistry · doi:10.1021/bi2012383 · Cited by 130 · see citing works

Beneficial Effects of Dietary EGCG and Voluntary Exercise on Behavior in an Alzheimer's Disease Mouse Model

Walker, J. M., Klakotskaia, D., Ajit, D., Weisman, G. A., Wood, W. G., Sun, G. Y., Serfözö, P. D., Simonyi, Á., & Schachtman, T. R. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-140981 · Cited by 128 · see citing works

Bioactive Polyphenols and Neuromodulation: Molecular Mechanisms in Neurodegeneration

Meo, F. D., Valentino, A., Petillo, O., Peluso, G., Filosa, S., & Crispi, S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21072564 · Cited by 127 · see citing works

Rifampicin is a candidate preventive medicine against amyloid-β and tau oligomers

Umeda, T., Ono, K., Sakai, A., Yamashita, M., Mizuguchi, M., Klein, W. L., Yamada, M., Mori, H., & Tomiyama, T. (2016) · Brain · doi:10.1093/brain/aww042 · Cited by 125 · see citing works

Multi-Target Mechanisms of Phytochemicals in Alzheimer’s Disease: Effects on Oxidative Stress, Neuroinflammation and Protein Aggregation

Sharifi-Rad, J., Rapposelli, S., Sestito, S., Herrera-Bravo, J., Arancibia-Diaz, A., Salazar, L. A., Yeskaliyeva, B., Beyatli, A., Leyva-Gómez, G., González-Contreras, C., et al. (2022) · Journal of Personalized Medicine · doi:10.3390/jpm12091515 · Cited by 125 · see citing works

The role of polyphenols in the modulation of sirtuins and other pathways involved in Alzheimer's disease

Jayasena, T., Poljak, A., Smythe, G. A., Braidy, N., Münch, G. W., & Sachdev, P. S. (2013) · Ageing Research Reviews · doi:10.1016/j.arr.2013.06.003 · Cited by 120 · see citing works

Effects of Polyphenols on Brain Ageing and Alzheimer’s Disease: Focus on Mitochondria

Schaffer, S., Asseburg, H., Kuntz, S., Muller, W. E., & Eckert, G. P. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8282-9 · Cited by 123 · see citing works

Effect of lycopene and epigallocatechin-3-gallate against 3-nitropropionic acid induced cognitive dysfunction and glutathione depletion in rat: A novel nitric oxide mechanism

Kumar, P., & Kumar, A. (2009) · Food and Chemical Toxicology · doi:10.1016/j.fct.2009.07.011 · Cited by 118 · see citing works

(−)-Epigallocatechin-3-Gallate Ameliorates Learning and Memory Deficits by Adjusting the Balance of TrkA/p75NTR Signaling in APP/PS1 Transgenic Mice

Liu, M., Chen, F., Sha, L., Wang, S., Lin, T., Yao, L., He, M., Yao, Z., Liu, H., Zhu, Z., et al. (2013) · Molecular Neurobiology · doi:10.1007/s12035-013-8608-2 · Cited by 117 · see citing works

Epigallocatechin gallate, cerebral blood flow parameters, cognitive performance and mood in healthy humans: a double‐blind, placebo‐controlled, crossover investigation

Wightman, E. L., Haskell‐Ramsay, C. F., Forster, J. S., Veasey, R. C., & Kennedy, D. O. (2012) · Human Psychopharmacology Clinical and Experimental · doi:10.1002/hup.1263 · Cited by 116 · see citing works

Impact of Flavonoids on Cellular and Molecular Mechanisms Underlying Age-Related Cognitive Decline and Neurodegeneration

Flanagan, E. C., Müller, M. M., Hornberger, M., & Vauzour, D. (2018) · Current Nutrition Reports · doi:10.1007/s13668-018-0226-1 · Cited by 115 · see citing works

Green Tea Epigallocatechin-3-gallate (EGCG) Targeting Protein Misfolding in Drug Discovery for Neurodegenerative Diseases

Gonçalves, P. B., Sodero, A. C. R., & Cordeiro, Y. (2021) · Biomolecules · doi:10.3390/biom11050767 · Cited by 115 · see citing works

The immunology of traumatic brain injury: a prime target for Alzheimer’s disease prevention

Giunta, B., Obregon, D., Velisetty, R., Sanberg, P. R., Borlongan, C. V., & Tan, J. (2012) · Journal of Neuroinflammation · doi:10.1186/1742-2094-9-185 · Cited by 112 · see citing works

Counteracting role of nuclear factor erythroid 2-related factor 2 pathway in Alzheimer's disease

Sharma, V., Kaur, A., & Singh, T. G. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110373 · Cited by 114 · see citing works

Pleiotropic Protective Effects of Phytochemicals in Alzheimer's Disease

Davinelli, S., Sapere, N., Zella, D., Bracale, R., Intrieri, M., & Scapagnini, G. (2012) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2012/386527 · Cited by 111 · see citing works

Green Tea Polyphenol Epigallocatechin-Gallate in Amyloid Aggregation and Neurodegenerative Diseases

Fernandes, L., Cardim-Pires, T. R., Foguel, D., & Palhano, F. L. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.718188 · Cited by 111 · see citing works

(−)-Epigallocatechin gallate inhibits endotoxin-induced expression of inflammatory cytokines in human cerebral microvascular endothelial cells

Li, J., Li, Y., Wang, X., Liu, J., Wang, Y., Zhou, Y., & Ho, W. (2012) · Journal of Neuroinflammation · doi:10.1186/1742-2094-9-161 · Cited by 106 · see citing works

Fibrillar structures in food

Kroes-Nijboer, A., Venema, P., & van der Linden, E. (2011) · Food & Function · doi:10.1039/c1fo10163c · Cited by 105 · see citing works

Green tea epigallocatechin‐3‐gallate ( EGCG ) promotes neural progenitor cell proliferation and sonic hedgehog pathway activation during adult hippocampal neurogenesis

Wang, Y., Li, M., Xu, X., Song, M., Tao, H., & Bai, Y. (2012) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201200035 · Cited by 105 · see citing works

Neuronal and Vascular Oxidative Stress in Alzheimers Disease

Massaad, C. A. (2011) · Current Neuropharmacology · doi:10.2174/157015911798376244 · Cited by 103 · see citing works

Amelioration of cognitive impairment and neurodegeneration by catechin hydrate in rat model of streptozotocin-induced experimental dementia of Alzheimer’s type

Ahmed, M. E., Khan, M. M., Javed, H., Vaibhav, K., Khan, A., Tabassum, R., Ashafaq, M., Islam, F., Safhi, M. M., & Islam, F. (2013) · Neurochemistry International · doi:10.1016/j.neuint.2013.02.006 · Cited by 103 · see citing works

Therapeutic approaches against common structural features of toxic oligomers shared by multiple amyloidogenic proteins

Guerrero‐Munoz, M. J., Castillo‐Carranza, D. L., & Kayed, R. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2013.12.023 · Cited by 103 · see citing works

Green tea compound epigallo-catechin-3-gallate (EGCG) increases neuronal survival in adult hippocampal neurogenesis in vivo and in vitro

Ortiz-López, L. I., Márquez‐Valadez, B., Gómez‐Sánchez, A., Silva‐Lucero, M., Torres-Pérez, M. O., Tellez-Ballesteros, R. I., Ichwan, M., Meraz‐Ríos, M. A., Kempermann, G., & Ramírez-Rodríguez, G. B. (2016) · Neuroscience · doi:10.1016/j.neuroscience.2016.02.040 · Cited by 103 · see citing works

Genistein: A Dual Inhibitor of Both Amyloid β and Human Islet Amylin Peptides

Ren, B., Liu, Y., Zhang, Y., Cai, Y., Gong, X., Chang, Y., Xu, L., & Zheng, J. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00039 · Cited by 102 · see citing works

Polyphenols Modulate Alzheimer’s Amyloid Beta Aggregation in a Structure-Dependent Manner

Phan, H. T. T., Samarat, K., Takamura, Y., Oussou-Azo, A. F., Nakazono, Y., & Vestergaard, M. C. M. (2019) · Nutrients · doi:10.3390/nu11040756 · Cited by 103 · see citing works

Thermodynamic Analysis of the Molecular Interactions between Amyloid β-Peptide 42 and (−)-Epigallocatechin-3-gallate

Wang, S., Liu, F., Dong, X., & Sun, Y. P. (2010) · The Journal of Physical Chemistry B · doi:10.1021/jp1001435 · Cited by 98 · see citing works

Green tea supplementation produces better neuroprotective effects than red and black tea in Alzheimer-like rat model

Schimidt, H. L., Garcia, A., Martins, A., Mello‐Carpes, P. B., & Carpes, F. P. (2017) · Food Research International · doi:10.1016/j.foodres.2017.07.026 · Cited by 97 · see citing works

Green tea polyphenol epigallocatechin-3-gallate (EGCG) induced intermolecular cross-linking of membrane proteins

Chen, R., Wang, J., Zhang, X., Ren, J. M., & Zeng, C. (2011) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2010.12.033 · Cited by 96 · see citing works

Green Tea Extract Ameliorates Learning and Memory Deficits in Ischemic Rats via Its Active Component Polyphenol Epigallocatechin-3-gallate by Modulation of Oxidative Stress and Neuroinflammation

Wu, K., Hsieh, M., Wu, C., Wood, W. G., & Chen, Y.-F. (2012) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2012/163106 · Cited by 96 · see citing works

The Potential of Flavonoids and Flavonoid Metabolites in the Treatment of Neurodegenerative Pathology in Disorders of Cognitive Decline

Melrose, J. (2023) · Antioxidants · doi:10.3390/antiox12030663 · Cited by 95 · see citing works

Nanotechnology for Alzheimer’s disease detection and treatment

Nazem, A., & Mansoori, G. A. (2011) · Insciences Journal · doi:10.5640/insc.0104169 · Cited by 93 · see citing works

Chronic epigallocatechin-3-gallate ameliorates learning and memory deficits in diabetic rats via modulation of nitric oxide and oxidative stress

Baluchnejadmojarad, T., & Roghani, M. (2011) · Behavioural Brain Research · doi:10.1016/j.bbr.2011.06.007 · Cited by 92 · see citing works

The role of lysosomal cathepsins in neurodegeneration: Mechanistic insights, diagnostic potential and therapeutic approaches.

Drobny, A., Huarcaya, S. P., Dobert, J., Kluge, A., Bunk, J., Schlothauer, T., & Zunke, F. (2022) · Biochimica et biophysica acta. Molecular cell research · doi:10.1016/j.bbamcr.2022.119243 · Cited by 86 · see citing works

Cognitive Enhancers (Nootropics). Part 1: Drugs Interacting with Receptors

Froestl, W., Muhs, A., & Pfeifer, A. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-121186 · Cited by 91 · see citing works

The role of dietary antioxidants in type 2 diabetes and neurodegenerative disorders: An assessment of the benefit profile

Fatima, M. T., Bhat, A. A., Nisar, S., Fakhro, K. A., & Akil, A. A. (2022) · Heliyon · doi:10.1016/j.heliyon.2022.e12698 · Cited by 90 · see citing works

Association of Tea Consumption with Risk of Alzheimer’s Disease and Anti-Beta-Amyloid Effects of Tea

Polito, C. A., Cai, Z., Shi, Y., Li, X.-M., Yang, R., Shi, M., Li, Q., Ma, S., Xiang, L., Wang, K., et al. (2018) · Nutrients · doi:10.3390/nu10050655 · Cited by 89 · see citing works

High-dose green tea polyphenols induce nephrotoxicity in dextran sulfate sodium-induced colitis mice by down-regulation of antioxidant enzymes and heat-shock protein expressions

Inoue, H., Akiyama, S., Maeda‐Yamamoto, M., Nesumi, A., Tanaka, T., & Murakami, A. (2011) · Cell Stress and Chaperones · doi:10.1007/s12192-011-0280-8 · Cited by 88 · see citing works

Tau-induced neurodegeneration: mechanisms and targets

Beharry, C., Cohen, L. S., Di, J., Ibrahim, K., Briffa-Mirabella, S., & Alonso, A. D. C. (2014) · Neuroscience Bulletin · doi:10.1007/s12264-013-1414-z · Cited by 88 · see citing works

Dietary (−)-epicatechin as a potent inhibitor of βγ-secretase amyloid precursor protein processing

Cox, C. J., Choudhry, F., Peacey, E., Perkinton, M. S., Richardson, J. C., Howlett, D. R., Lichtenthaler, S. F., Francis, P. T., & Williams, R. J. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.07.032 · Cited by 87 · see citing works

Caffeine increases mitochondrial function and blocks melatonin signaling to mitochondria in Alzheimer's mice and cells

Dragicevic, N., Delic, V., Cao, C., Copes, N., Lin, X., Mamcarz, M., Wang, L., Arendash, G. W., & Bradshaw, P. C. (2012) · Neuropharmacology · doi:10.1016/j.neuropharm.2012.08.018 · Cited by 85 · see citing works

Characterization of catechins, theaflavins, and flavonols by leaf processing step in green and black teas (Camellia sinensis) using UPLC-DAD-QToF/MS

Lee, M., Kim, H., Lee, S.-H., Kim, Y. J., Asamenew, G., Choi, J., Lee, J. W., Jung, H.-A., Yoo, S. M., & Kim, J.-B. (2018) · European Food Research and Technology · doi:10.1007/s00217-018-3201-6 · Cited by 84 · see citing works

Natural Compounds May Open New Routes to Treatment of Amyloid Diseases

Bieschke, J. (2013) · Neurotherapeutics · doi:10.1007/s13311-013-0192-7 · Cited by 84 · see citing works

670 nm Laser Light and EGCG Complementarily Reduce Amyloid-β Aggregates in Human Neuroblastoma Cells: Basis for Treatment of Alzheimer's Disease?

Sommer, A. P., Bieschke, J., Friedrich, R. P., Zhu, D., Wanker, E. E., Fecht, H. ‐., Mereles, D., & HUNSTEIN, W. (2011) · Photomedicine and Laser Surgery · doi:10.1089/pho.2011.3073 · Cited by 83 · see citing works

Green tea Epigallocatechin-3-Gallate (EGCG) Modulates Amyloid Precursor Protein Cleavage and Reduces Cerebral Amyloidosis in Alzheimer Transgenic Mice

Rezai-Zadeh, K., Shytle, D., Sun, N., Mori, T., Hou, H., Jeanniton, D., Ehrhart, J., Townsend, K., Zeng, J., Morgan, D., et al. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.1521-05.2005 · Cited by 713 · see citing works

(−)-Epigallocatechin-3-gallate ameliorates memory impairment and rescues the abnormal synaptic protein levels in the frontal cortex and hippocampus in a mouse model of Alzheimer’s disease

Guo, Y., Zhao, Y., Nan, Y., Wang, X., Chen, Y., & Wang, S. (2017) · Neuroreport · doi:10.1097/wnr.0000000000000803 · Cited by 67 · see citing works

Green Tea (-)-Epigallocatechin-3-Gallate Inhibits β-Amyloid-Induced Cognitive Dysfunction through Modification of Secretase Activity via Inhibition of ERK and NF-κB Pathways in Mice ,

Lee, J. W., Lee, Y. K., Ban, J. O., Ha, T. Y., Yun, Y. P., Han, S., Oh, K. W., & Hong, J. T. (2009) · Journal of Nutrition · doi:10.3945/jn.109.109785 · Cited by 269 · see citing works

Epigallocatechin-3-Gallate Provides Protection Against Alzheimer’s Disease-Induced Learning and Memory Impairments in Rats

Nan, S., Wang, P., Zhang, Y., & Fan, J. (2021) · Drug Design Development and Therapy · doi:10.2147/dddt.s289473 · Cited by 81 · see citing works

Green Tea (−)-Epigallocatechin-3-Gallate and Amyloid Precursor Protein

Giunta, B. N., & Tan, J. (2012) · Tea in Health and Disease Prevention · doi:10.1016/b978-0-12-384937-3.00118-x