Cited by 460Alzheimer's disease research and treatmentsTea Polyphenols and EffectsMedicinal Plants and Neuroprotection

The DOI matches its Crossref record; 50 of the 50 references it cites were found in a registry or an index.

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

Rezai-Zadeh, Kavon, Arendash, Gary W., Hou, Huayan, Fernandez, Frank, Jensen, Maren, Runfeldt, Melissa, Shytle, R. Douglas, Tan, Jun·2008·Brain Research

DOI 10.1016/j.brainres.2008.02.107

Open this paper in CoChat — free account

Abstract

We previously reported that intraperitoneal (i.p.) injection (20 mg/kg) of (-)-epigallocatechin-3-gallate (EGCG), the main polyphenolic constituent of green tea, decreased beta-amyloid (Abeta) levels and plaques via promotion of the non-amyloidogenic alpha-secretase proteolytic pathway in "Swedish" mutant amyloid precursor protein overexpressing (APPsw, Tg) mice. Here, we find that EGCG administered orally in drinking water (50 mg/kg) similarly reduces Abeta deposition in these mice. Following a six month treatment of an 8 month old cohort, immunohistochemical analysis of coronal sections reveals that plaque burdens were reduced in the cingulate cortex, hippocampus, and entorhinal cortex by 54%, 43%, and 51%, respectively. Congo red plaque burdens were decreased in the cingulate cortex, hippocampus, and entorhinal cortex by 53%, 53%, and 58%, respectively as well. ELISA of brain homogenates of the treatment Tg mice revealed consistent reductions in both Abeta1-40 and 1-42 soluble and insoluble forms. In the present study we also investigated the effect EGCG administration had on tau pathology and cognition in Tg mice. Both i.p. and orally-treated Tg animals were found to have modulated tau profiles, with markedly suppressed sarkosyl-soluble phosphorylated tau isoforms. Radial arm water maze (RAWM) testing for working memory indicated that EGCG provided cognitive benefit to Tg mice with both i.p. and oral administration, although i.p.-treated animals showed a more pronounced benefit because of the greater impairment of their Tg controls at the time of testing. Taken together, these data further the notion of EGCG dietary supplementation as a potentially safe and effective prophylaxis for Alzheimer's disease.

Integrity signals

Registry

Crossref · 10.1016/j.brainres.2008.02.107

Cites

50 of 50 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

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
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
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
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
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
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
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
Hyperphosphorylation induces self-assembly of τ into tangles of paired helical filaments/straight filaments
Alonso, A. D. C., Zaidi, T., Novak, M., Grundke-Iqbal, I., & Iqbal, K. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.121119298 · Cited by 827
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 766
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 735

Show all 50 references

Sorted by citations

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 696
Bioinorganic Chemistry of Alzheimer’s Disease
Kepp, K. P. (2012) · Chemical Reviews · doi:10.1021/cr300009x · Cited by 683
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
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 612
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 491
Nutraceutical Antioxidants as Novel Neuroprotective Agents
Kelsey, N. A., Wilkins, H., & Linseman, D. A. (2010) · Molecules · doi:10.3390/molecules15117792 · Cited by 488
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
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
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
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 449
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 361
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. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00155 · Cited by 320
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 324
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
Polyphenols from Food and Natural Products: Neuroprotection and Safety
Silva, R. F. M., & Pogačnik, L. (2020) · Antioxidants · doi:10.3390/antiox9010061 · Cited by 292
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 322
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 285
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
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 245
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 268
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
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
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 249
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
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 245
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
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
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
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
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 205
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
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 196
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
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 192
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
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 195
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
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
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 178
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 209
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
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
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
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 168
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 160
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
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 151
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 144
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 143
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
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
(−)-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 141
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 142
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 139
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 135
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 132
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
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 133
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 131
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 131
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 124
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
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 122
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 124
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
(−)-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
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
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 119
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
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
Self-citation
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 116
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 114
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 114
(−)-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 107
Fibrillar structures in food
Kroes-Nijboer, A., Venema, P., & van der Linden, E. (2011) · Food & Function · doi:10.1039/c1fo10163c · Cited by 109
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
Neuronal and Vascular Oxidative Stress in Alzheimers Disease
Massaad, C. A. (2011) · Current Neuropharmacology · doi:10.2174/157015911798376244 · Cited by 102
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
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 105
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
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
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 105
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 99
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
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
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
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 97
Nanotechnology for Alzheimer’s disease detection and treatment
Nazem, A., & Mansoori, G. A. (2011) · Insciences Journal · doi:10.5640/insc.0104169 · Cited by 96
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
The role of lysosomal cathepsins in neurodegeneration: Mechanistic insights, diagnostic potential and therapeutic approaches
Drobny, A., Huarcaya, S. P., Dobert, J. P., Kluge, A., Bunk, J., Schlothauer, T., & Zunke, F. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2022.119243 · Cited by 94
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 94
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 112
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
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
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 92
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 89
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
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
Natural Compounds May Open New Routes to Treatment of Amyloid Diseases
Bieschke, J. (2013) · Neurotherapeutics · doi:10.1007/s13311-013-0192-7 · Cited by 85
Potential Role of Natural Polyphenols against Protein Aggregation Toxicity: In Vitro, In Vivo, and Clinical Studies
Henríquez, G., Gomez, A., Guerrero, E., & Narayan, M. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00381 · Cited by 83

Authors: Rezai-Zadeh, K., Arendash, G. W., Hou, H., Fernandez, F., Jensen, M., Runfeldt, M., Shytle, R. D., & Tan, J.
Affiliations: University of South Florida (US)
USF Health Byrd Alzheimer's Institute (US)
Corresponding author: Tan, Jun
ORCID: Rezai-Zadeh, Kavon
Arendash, Gary W.
Shytle, R. Douglas
Tan, Jun
Venue: Brain Research
Publisher: Elsevier BV
Published: 2008-06
Volume: 1214
Pages: 177-187
ISSN: 0006-8993 (ISSN-L)
DOI: 10.1016/j.brainres.2008.02.107
OpenAlex: W2052380265
Cited by: 459
References: 50
Citations by year: 2026: 14 · 2025: 28 · 2024: 17 · 2023: 26 · 2022: 27 · 2021: 30 · 2020: 37 · 2019: 20 · 2018: 28 · 2017: 31 · 2016: 20 · 2015: 27 · 2014: 27 · 2013: 33 · 2012: 32
FWCI: 13.81
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Brain Research (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Institute on Aging (AG04418, P01AG004418, R21AG031037, P50AG025711, AG025711, AG031037)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Agricultural and Biological Sciences › Food Science › Tea Polyphenols and Effects
Health Sciences › Medicine › Complementary and alternative medicine › Medicinal Plants and Neuroprotection
Keywords: epigallocatechin gallate, green tea polyphenols, Alzheimer's disease, amyloid plaques, tau phosphorylation, oral administration, working memory, cognitive impairment, dietary supplementation, neuroprotection
MeSH terms: Alzheimer Disease, Analysis of Variance, Animals, Catechin, Cognition Disorders, Disease Models, Animal, Enzyme-Linked Immunosorbent Assay, Mice, Transgenic, Mutation, Phosphorylation, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, tau Proteins, Neuroprotective Agents, Maze Learning, Mice

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

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

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks