Secondary Metabolites from Plants Possessing Inhibitory Properties against Beta-Amyloid Aggregation as Revealed by Thioflavin-T Assay and Correlations with Investigations on Transgenic Mouse Models of Alzheimer's Disease
Open accessAbstract
Alzheimer's disease is a neurodegenerative disorder for which there is a continuous search of drugs able to reduce or stop the cognitive decline. Beta-amyloid peptides are composed of 40 and 42 amino acids and are considered a major cause of neuronal toxicity. They are prone to aggregation, yielding oligomers and fibrils through the inter-molecular binding between the amino acid sequences (17-42) of multiple amyloid-beta molecules. Additionally, amyloid deposition causes cerebral amyloid angiopathy. The present study aims to identify, in the existing literature, natural plant derived products possessing inhibitory properties against aggregation. The studies searched proved the anti-aggregating effects by the thioflavin T assay and through behavioral, biochemical, and histological analysis carried out upon administration of natural chemical compounds to transgenic mouse models of Alzheimer's disease. According to our present study results, fifteen secondary metabolites from plants were identified which presented both evidence coming from the thioflavin T assay and transgenic mouse models developing Alzheimer's disease and six additional metabolites were mentioned due to their inhibitory effects against fibrillogenesis. Among them, epigallocatechin-3-gallate, luteolin, myricetin, and silibinin were proven to lower the aggregation to less than 40%.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
Phenolic compounds interfere with Aβ peptide aggregation by targeting one or multiple steps.
“A huge number of phenolic compounds have displayed the capability to interfere with the aggregation of the Aβ peptide by targeting one or multiple steps (Ma et al., 2020; Stefanescu et al., 2020)”
From Exploring the Therapeutic Potential of Phytochemicals in Alzheimer’s Disease: Focus on Polyphenols and Monoterpenes (2022) · cites this paper as Stefanescu et al., 2020
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
1 retracted
Wang, P., Su, C., Li, R., Wang, H., Ren, Y., Sun, H., Yang, J., Sun, J., Shi, J., Tian, J., et al. (2014) · Journal of Neuroscience Research · doi:10.1002/jnr.23322 · Cited by 65 · see citing works
RetractedCorrelative 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
Triple-Transgenic Model of Alzheimer’s Disease with Plaques and Tangles
Oddo, S., Caccamo, A., Shepherd, J. D., Murphy, M. P., Golde, T. E., Kayed, R., Metherate, R., Mattson, M. P., Akbari, Y., & LaFerla, F. M. (2003) · Neuron · doi:10.1016/s0896-6273(03)00434-3 · Cited by 4,126 · see citing works
Oakley, H., Cole, S. L., Logan, S., Maus, E., Shao, P., Craft, J., Guillozet-Bongaarts, A., Ohno, M., Disterhoft, J., Van Eldik, L., et al. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.1202-06.2006 · Cited by 3,530 · cited 1× · see citing works
“Figure 2 presents the pathological changes and the neurological deficits of the most common mouse transgenic models of AD used in research: Aβ models: PDAPP [19], APP23 [20,21], Tg2576 [22,23], PS2APP [24], APPlon [25], APPswe/PSEN1dE9 [26]; tau models: hTau [27], Thy-Tau22 [28], hTau-AT [29] and multiple transgenic m…”
MethodThe neuropathological diagnosis of Alzheimer's disease
DeTure, M. A., & Dickson, D. W. (2019) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0333-5 · Cited by 3,329 · see citing works
Hopkins, A. L., & Groom, C. R. (2002) · Nature Reviews Drug Discovery · doi:10.1038/nrd892 · Cited by 3,305 · see citing works
Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein
Games, D., Adams, D., Alessandrini, R., Barbour, R., Borthelette, P., Blackwell, C., Carr, T., Clemens, J., Donaldson, T., Gillespie, F., et al. (1995) · Nature · doi:10.1038/373523a0 · Cited by 2,516 · see citing works
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
LeVine, H. (1993) · Protein Science · doi:10.1002/pro.5560020312 · Cited by 2,268 · see citing works
Molecular mechanism of Thioflavin-T binding to amyloid fibrils
Biancalana, M., & Koide, S. (2010) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2010.04.001 · Cited by 2,203 · see citing works
3D structure of Alzheimer's amyloid-β(1–42) fibrils
Lührs, T., Ritter, C., Adrian, M., Riek-Loher, D., Bohrmann, B., Döbeli, H., Schubert, D. A., & Riek, R. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506723102 · Cited by 2,001 · see citing works
Lim, G. P., Chu, T., Yang, F., Beech, W., Frautschy, S. A., & Cole, G. M. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-21-08370.2001 · Cited by 1,530 · see citing works
Two amyloid precursor protein transgenic mouse models with Alzheimer disease-like pathology
Sturchler-Pierrat, C., Abramowski, D., Duke, M., Wiederhold, K.-H., Mistl, C., Rothacher, S., Ledermann, B., Bürki, K., Frey, P., Paganetti, P. A., et al. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.24.13287 · Cited by 1,507 · see citing works
Holcomb, L., Gordon, M. N., McGowan, E., Yu, X., Benkovic, S., Jantzen, P., Wright, K., Saad, I., Mueller, R., Morgan, D., et al. (1998) · Nature Medicine · doi:10.1038/nm0198-097 · Cited by 1,386 · see citing works
EGCG remodels mature α-synuclein and amyloid-β fibrils and reduces cellular toxicity
Bieschke, J., Russ, J., Friedrich, R., Ehrnhoefer, D. E., Wobst, H. J., Neugebauer, K., & Wanker, E. (2010) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.0910723107 · Cited by 986 · see citing works
Voluntary Exercise Decreases Amyloid Load in a Transgenic Model of Alzheimer's Disease
Adlard, P. A., Perreau, V. M., Pop, V., & Cotman, C. W. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.0496-05.2005 · Cited by 806 · see citing works
History and progress of hypotheses and clinical trials for Alzheimer’s disease
Liu, P.-P., Xie, Y., Meng, X.-Y., & Kang, J.-S. (2019) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-019-0063-8 · Cited by 723 · see citing works
Hyperphosphorylation and aggregation of tau in mice expressing normal human tau isoforms
Andorfer, C., Kress, Y., Espinoza, M., De Silva, R., Tucker, K. L., Barde, Y., Duff, K., & Davies, P. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01879.x · Cited by 722 · see citing works
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
Moechars, D., Dewachter, I., Lorent, K., Reversé, D., Baekelandt, V., Naidu, A., Tesseur, I., Spittaels, K., Haute, C. V. D., Checler, F., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.10.6483 · Cited by 668 · see citing works
Garcı́a-Alloza, M., Borrelli, L. A., Rozkalne, A., Hyman, B. T., & Bacskai, B. J. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04613.x · Cited by 663 · see citing works
Groenning, M. (2009) · Journal of Chemical Biology · doi:10.1007/s12154-009-0027-5 · Cited by 643 · see citing works
Hudson, S. A., Ecroyd, H. W., Kee, T. W., & Carver, J. A. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07307.x · Cited by 614 · see citing works
Baum, L., Lam, C. W. K., Cheung, S. K. K., Kwok, T. C. Y., Lui, V. W.-C., Tsoh, J., LAM, L. C. W., Leung, V., Hui, E., Ng, C., et al. (2008) · Journal of Clinical Psychopharmacology · doi:10.1097/jcp.0b013e318160862c · Cited by 594 · see citing works
Ringman, J. M., Frautschy, S. A., Teng, E., Begum, A. N., Bardens, J., Beigi, M., Gylys, K. H., Badmaev, V., Heath, D. D., Apostolova, L. G., et al. (2012) · Alzheimer s Research & Therapy · doi:10.1186/alzrt146 · Cited by 546 · see citing works
Neuroprotective Effects of Quercetin in Alzheimer’s Disease
Khan, H. Z., Ullah, H., Aschner, M., Cheang, W. S., & Akkol, E. K. (2019) · Biomolecules · doi:10.3390/biom10010059 · Cited by 541 · see citing works
Cellular and molecular mechanisms of curcumin in prevention and treatment of disease
Patel, S. S., Acharya, A., Ray, R. S., Agrawal, R. K., Raghuwanshi, R., & Jain, P. (2019) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2018.1552244 · Cited by 518 · 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
Rezai-Zadeh, K., Arendash, G. W., Hou, H., Fernandez, F., Jensen, M., Runfeldt, M., Shytle, R. D., & Tan, J. (2008) · Brain Research · doi:10.1016/j.brainres.2008.02.107 · Cited by 459 · see citing works
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
Hamaguchi, T., Ono, K., Murase, A., & Yamada, M. (2009) · American Journal Of Pathology · doi:10.2353/ajpath.2009.090417 · Cited by 396 · see citing works
Schindowski, K., Bretteville, A., Leroy, K., Bégard, S., Brion, J., Hamdane, M., & Buée, L. (2006) · American Journal Of Pathology · doi:10.2353/ajpath.2006.060002 · Cited by 396 · see citing works
Alzheimer’s Disease Pharmacotherapy in Relation to Cholinergic System Involvement
Stanciu, G. D., Luca, A., Rusu, R.-N., Bild, V., Chiriac, S. I. B., Solcan, C., Bild, W., & Ababei, D. C. (2019) · Biomolecules · doi:10.3390/biom10010040 · Cited by 307 · see citing works
Self-citationMandel, S. A., Amit, T., Reznichenko, L., Weinreb, O., & Youdim, M. B. H. (2006) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200500156 · Cited by 293 · see citing works
Xu, P., Wang, S.-W., Yu, X., Su, Y., Wang, T., Zhou, W., Zhang, H., Wang, Y., & Liu, R. (2014) · Behavioural Brain Research · doi:10.1016/j.bbr.2014.02.002 · Cited by 245 · see citing works
New Insights on How Metals Disrupt Amyloid β-Aggregation and Their Effects on Amyloid-β Cytotoxicity
Yoshiike, Y., Tanemura, K., Murayama, O., Akagi, T., Murayama, M., Sato, S., Sun, X., Tanaka, N., & Takashima, A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010706200 · Cited by 244 · cited 1× · see citing works
“Sandwich ELISA and UV spectroscopy were also described for quantifying the degree of aggregation, although these methods do not distinguish between the form of the aggregated peptide, namely oligomers or fibrils [11,12].”
BackgroundNie, Q., Du, X., & Geng, M. (2011) · Acta Pharmacologica Sinica · doi:10.1038/aps.2011.14 · Cited by 239 · see citing works
The Polyphenol Oleuropein Aglycone Protects TgCRND8 Mice against Aß Plaque Pathology
Grossi, C., Rigacci, S., Ambrosini, S., Dami, T. E., Luccarini, I., Traini, C., Failli, P., Berti, A., Casamenti, F., & Stefani, M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0071702 · Cited by 228 · see citing works
Congo red and thioflavin‐T analogs detect Aβ oligomers
Maezawa, I., Hong, H., Liu, R., Wu, C., Cheng, R. H., Kung, M., Kung, H. F., Lam, K. S., Oddo, S., LaFerla, F. M., et al. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04972.x · Cited by 226 · see citing works
Wang, S., Wang, Y., Su, Y., Zhou, W., Yang, S., Zhang, R., Zhao, M., Li, Y., Zhang, Z., Zhan, D., et al. (2012) · NeuroToxicology · doi:10.1016/j.neuro.2012.03.003 · Cited by 221 · see citing works
Currais, A. J. M., Prior, M., Dargusch, R., Armando, A. M., Ehren, J. L., Schubert, D. A., Quehenberger, O., & Maher, P. A. (2013) · Aging Cell · doi:10.1111/acel.12185 · Cited by 206 · 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
Richards, J., Higgins, G., Ouagazzal, A., Ozmen, L., Kew, J., Bohrmann, B., Malherbe, P., Brockhaus, M., Loetscher, H., Czech, C., et al. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-26-08989.2003 · Cited by 197 · see citing works
APP processing and amyloid deposition in mice haplo-insufficient for presenilin 1
Jankowsky, J. L., Slunt, H. H., Gonzales, V., Jenkins, N. A., Copeland, N. G., & Borchelt, D. (2004) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2003.09.008 · Cited by 189 · see citing works
Inhibition of protein misfolding and aggregation by natural phenolic compounds
Dhouafli, Z., Cuanalo-Contreras, K., Hayouni, E. A., Mays, C. E., Soto, C. A., & Moreno‐González, I. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2872-2 · Cited by 174 · see citing works
Epigallocatechin gallate and mitochondria—A story of life and death
de Oliveira, M. R., Nabavi, S. F., Daglia, M., Rastrelli, L., & Nabavi, S. M. (2015) · Pharmacological Research · doi:10.1016/j.phrs.2015.12.027 · Cited by 171 · see citing works
Luteolin Reduces Alzheimer’s Disease Pathologies Induced by Traumatic Brain Injury
Sawmiller, D. R., Li, S., Shahaduzzaman, M., de Smith, A. J., Obregon, D. F., Giunta, B. N., Borlongan, C. V., Sanberg, P. R., & Tan, J. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms15010895 · Cited by 170 · see citing works
Ethnopharmacology, phytochemistry, and pharmacology of Chinese Salvia species: A review
Xu, J., Wei, K., Zhang, G., et al. (2018) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2018.06.029 · Cited by 163 · see citing works
Hase, T., Shishido, S., Yamamoto, S., Yamashita, R., Nukima, H., Taira, S., Toyoda, T., Abe, K., Hamaguchi, T., Ono, K., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-45168-1 · Cited by 162 · see citing works
Akaishi, T., Morimoto, T., Shibao, M., Watanabe, S., Sakai‐Kato, K., Utsunomiya‐Tate, N., & Abe, K. (2008) · Neuroscience Letters · doi:10.1016/j.neulet.2008.08.052 · Cited by 155 · see citing works
Hu, B., Dai, F., Fan, Z., Ma, G., Tang, Q., & Zhang, X. (2015) · Advanced Materials · doi:10.1002/adma.201502227 · Cited by 155 · see citing works
Flavonoid‐mediated presenilin‐1 phosphorylation reduces Alzheimer's disease β‐amyloid production
Rezai-Zadeh, K. P., Shytle, R. D., Bai, Y., Tian, J., Hou, H., Mori, T., Zeng, J., Obregon, D. F., Town, T., & Tan, J. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00344.x · Cited by 153 · see citing works
Durairajan, S. S. K., Yuan, Q., Xie, L., Chan, W. S., Kum, W.-F., Koo, I., Liu, C., Song, Y., Huang, J., Klein, W. L., et al. (2007) · Neurochemistry International · doi:10.1016/j.neuint.2007.09.006 · Cited by 149 · see citing works
Aβ aggregation and possible implications in Alzheimer's disease pathogenesis
Bharadwaj, P. R., Dubey, A. K., Masters, C. L., Martins, R. N., & Macreadie, I. G. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2009.00609.x · Cited by 147 · see citing works
Overview of Transgenic Mouse Models for Alzheimer's Disease
Myers, A., & McGonigle, P. (2019) · Current Protocols in Neuroscience · doi:10.1002/cpns.81 · Cited by 140 · see citing works
Silibinin: A novel inhibitor of Aβ aggregation
Yin, F., Liu, J., Ji, X., Wang, Y., Zidichouski, J. A., & Zhang, J. (2010) · Neurochemistry International · doi:10.1016/j.neuint.2010.12.017 · Cited by 135 · see citing works
Adler, B. L., Yarchoan, M. M., Hwang, H. M., Louneva, N., Blair, J. A., Palm, R. F., Smith, M. A., Lee, H., Arnold, S. E., & Casadesús, G. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.10.076 · Cited by 131 · see citing works
Shimmyo, Y., Kihara, T., Akaike, A., Niidome, T., & Sugimoto, H. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21476 · Cited by 126 · see citing works
Preclinical Models of Alzheimer's Disease: Relevance and Translational Validity
Mullane, K., & Williams, M. J. (2019) · Current Protocols in Pharmacology · doi:10.1002/cpph.57 · Cited by 126 · see citing works
The Early Events That Initiate β-Amyloid Aggregation in Alzheimer’s Disease
Zhang, X., Fu, Z., Meng, L., He, M., & Zhang, Z. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00359 · Cited by 122 · see citing works
Duan, S., Guan, X., Lin, R., Liu, X., Yan, Y., Lin, R., Zhang, T., Chen, X., Huang, J., Sun, X., et al. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.02.002 · Cited by 121 · see citing works
Gallic acid is the major component of grape seed extract that inhibits amyloid fibril formation.
Liu, Y.-Q., Pukala, T., Musgrave, I., Williams, D. M., Dehle, F., & Carver, J. (2013) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2013.09.071 · Cited by 121 · see citing works
Polyphenols in dementia: From molecular basis to clinical trials
Molino, S., Dossena, M., Buonocore, D., Ferrari, F., Venturini, L., Ricevuti, G., & Verri, M. (2016) · Life Sciences · doi:10.1016/j.lfs.2016.07.021 · Cited by 119 · see citing works
Decker, J., Krüger, L., Sydow, A., Dennissen, F. J., Šišková, Z., Mandelkow, E., & Mandelkow, E. (2016) · EMBO Reports · doi:10.15252/embr.201541439 · Cited by 115 · see citing works
Yu, M., Chen, X., Liu, J., Ma, Q., Zhuo, Z., Chen, H., Zhou, L., Yang, S., Zheng, L., Ning, C., et al. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.11.009 · Cited by 114 · see citing works
Preventive Effect of Quercetin in a Triple Transgenic Alzheimer’s Disease Mice Model
Perez-Corredor, P. A., Sabogal-Guáqueta, A. M., Luis, C.-H., & Cardona‐Gómez, G. P. (2019) · Molecules · doi:10.3390/molecules24122287 · Cited by 107 · see citing works
Batarseh, Y. S., Bharate, S. S., Kumar, V., Kumar, A., Vishwakarma, R. A., Bharate, S. B., & Kaddoumi, A. (2017) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.7b00101 · Cited by 99 · see citing works
Ryan, P., Patel, B., Makwana, V., Jadhav, H. R., Kiefel, M. J., Davey, A. K., Reekie, T. A., Rudrawar, S., & Kassiou, M. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00185 · Cited by 99 · see citing works
Targeting Voltage-Gated Calcium Channels for Neuropathic Pain Management
Perret, D. M., & Luo, Z. D. (2009) · Neurotherapeutics · doi:10.1016/j.nurt.2009.07.006 · Cited by 95 · see citing works
Meng, F., Marek, P., Potter, K. J., Verchere, C. B., & Raleigh, D. P. (2008) · Biochemistry · doi:10.1021/bi702518m · Cited by 93 · see citing works
Bazoti, F. N., Bergquist, J., Markides, K. E., & Tsarbopoulos, A. (2006) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2005.11.016 · Cited by 88 · see citing works
Naturally occurring polyphenolic inhibitors of amyloid beta aggregation
Churches, Q. I., Caine, J. M., Cavanagh, K., Epa, V. C., Waddington, L. J., Tranberg, C. E., Meyer, A. G., Varghese, J. N., Streltsov, V. A., & Duggan, P. J. (2014) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2014.05.008 · Cited by 85 · see citing works
Qin, L., Nie, Xiaoguang, et al. (2011) · 中国药理学报:英文版 · Cited by 85 · see citing works
Quercetin stabilizes apolipoprotein E and reduces brain Aβ levels in amyloid model mice
Zhang, X., Hu, J., Zhong, L., Wang, N., Yang, L., Liu, C., Li, H., Wang, X., Zhou, Y., Zhang, Y., et al. (2016) · Neuropharmacology · doi:10.1016/j.neuropharm.2016.04.032 · Cited by 84 · see citing works
Mei, Z., Zhang, F., Tao, L., Zheng, W., Cao, Y., Wang, Z., Tang, S., Le, K., Chen, S., Pi, R., et al. (2009) · Neuroscience Letters · doi:10.1016/j.neulet.2009.01.013 · Cited by 82 · see citing works
The protective effect of crocin on the amyloid fibril formation of aβ42 peptide in vitro
Ghahghaei, A., Bathaie, S. Z., Kheirkhah, H., & Bahraminejad, E. (2013) · Cellular & Molecular Biology Letters · doi:10.2478/s11658-013-0092-1 · Cited by 79 · see citing works
Lee, J., Moon, J.-H., Kim, S.-W., Jeong, J., Nazim, U. M., Lee, Y.-J., Seol, J., & Park, S. (2015) · Oncotarget · doi:10.18632/oncotarget.3832 · Cited by 76 · see citing works
Pogačnik, L., Pirc, K., Palmela, I., Skrt, M., Kim, K. S., Brites, D. M. T. O., Brito, M. A., Ulrih, N. P., & Silva, R. F. M. (2016) · Brain Research · doi:10.1016/j.brainres.2016.09.020 · Cited by 76 · see citing works
Olive Biophenols Reduces Alzheimer’s Pathology in SH-SY5Y Cells and APPswe Mice
Omar, S. H., Scott, C., Hamlin, A. S., & Obied, H. K. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms20010125 · Cited by 70 · see citing works
Liang, J., Lindemeyer, A. K., Shen, Y., López-Valdés, H. E., Martínez‐Coria, H., Shao, X. M., & Olsen, R. W. (2014) · Neurochemical Research · doi:10.1007/s11064-014-1304-4 · Cited by 66 · see citing works
Non-polyphenolic natural inhibitors of amyloid aggregation
Ma, L., Yang, C., Zheng, J., Chen, Y., Xiao, Y., & Huang, K. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112197 · Cited by 66 · see citing works
Tabersonine Inhibits Amyloid Fibril Formation and Cytotoxicity of Aβ(1–42)
Kai, T., Zhang, L., Wang, X., Jing, A., Zhao, B., Yu, X., Zheng, J., & Zhou, F. (2015) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5b00015 · Cited by 65 · see citing works
Zhang, X., Wu, M., Lu, F., Luo, N., He, Z., & Yang, H. (2013) · Molecular Neurobiology · doi:10.1007/s12035-013-8491-x · Cited by 62 · see citing works
Inhibitory effect of curcumin on the Al(III)-induced Aβ42 aggregation and neurotoxicity in vitro
Jiang, T., Zhi, X., Zhang, Y., Pan, L., & Zhou, P. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2012.04.015 · Cited by 61 · see citing works
Jia, L., Zhao, W., Sang, J., et al. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00480 · Cited by 59 · see citing works
Cryptotanshinione Inhibits β-Amyloid Aggregation and Protects Damage from β-Amyloid in SH-SY5Y Cells
Mei, Z., Yan, P., Situ, B., Mou, Y., & Liu, P. (2011) · Neurochemical Research · doi:10.1007/s11064-011-0652-6 · Cited by 57 · see citing works
Can mouse models mimic sporadic Alzheimer’s disease?
Humpel, C., & Foidl, B. (2020) · Neural Regeneration Research · doi:10.4103/1673-5374.266046 · Cited by 56 · see citing works
Wong, D. Y. S., Musgrave, I., Harvey, B. S., & Smid, S. D. (2013) · Neuroscience Letters · doi:10.1016/j.neulet.2013.10.027 · Cited by 54 · see citing works
Jia, N., Han, K. S., Kong, J., Zhang, X., Sha, S., Ren, G.-R., & Cao, Y. (2013) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-013-1675-x · Cited by 50 · see citing works
Anti-Amyloidogenic Properties of Some Phenolic Compounds
Porzoor, A., Alford, B. L., Hügel, H., Grando, D., Caine, J. M., & Macreadie, I. G. (2015) · Biomolecules · doi:10.3390/biom5020505 · Cited by 45 · see citing works
Bazoti, F. N., Bergquist, J., Markides, K. E., & Tsarbopoulos, A. (2008) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2008.03.011 · Cited by 43 · see citing works
Druggability predictions: methods, limitations, and applications
Barril, X. (2012) · Wiley Interdisciplinary Reviews Computational Molecular Science · doi:10.1002/wcms.1134 · Cited by 42 · see citing works
Ma, Q., Cai, S., Jia, Y., Sun, X., Yi, J., & Du, J. (2020) · Foods · doi:10.3390/foods9030373 · Cited by 40 · see citing works
Lippi, S. L. P., Smith, M. L., & Flinn, J. M. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00382 · Cited by 36 · see citing works
Challenges in neurodegeneration research
Noble, W. J. (2010) · Frontiers in Psychiatry · doi:10.3389/fpsyt.2010.00007 · Cited by 33 · see citing works
Ghahghaei, A., Bathaie, S. Z., & Bahraminejad, E. (2012) · International Journal of Peptide Research and Therapeutics · doi:10.1007/s10989-012-9308-x · Cited by 32 · see citing works
Chemistry and biology of the genusVoacanga
Hussain, H., Hussain, J., Al-Harrasi, A., et al. (2012) · Pharmaceutical Biology · doi:10.3109/13880209.2012.658478 · Cited by 26 · see citing works
Huang, Q., Zhao, Q., Peng, J., Yu, Y., Wang, C., Zou, Y., Su, Y., Zhu, L., Wang, C., & Yang, Y. (2019) · ACS Omega · doi:10.1021/acsomega.8b02797 · Cited by 25 · see citing works
Ştefănescu, R., Stanciu, G. D., Luca, A., Caba, I.-C., Tamba, B.-I., & Mihai, C. T. (2019) · Molecules · doi:10.3390/molecules24061167 · Cited by 25 · see citing works
Self-citationThioflavin T fluorescence assay for beta-lactoglobulin fibrils hindered by DAPH.
Kroes-Nijboer, A., Lubbersen, Y. S., Venema, P., & van der Linden, E. (2009) · Journal of Structural Biology · doi:10.1016/j.jsb.2008.11.003 · Cited by 23 · see citing works
Li, Q., Gordon, M. N., Tan, J., & Morgan, D. (2006) · Experimental Neurology · doi:10.1016/j.expneurol.2006.02.062 · Cited by 21 · see citing works
Sun, J., Jiang, G., & Shigemori, H. (2019) · Natural Product Communications · doi:10.1177/1934578x19843039 · Cited by 20 · see citing works
Shen, L., Han, B., Geng, Y., Wang, J., Wang, Z., & Wang, M. (2017) · PLoS ONE · doi:10.1371/journal.pone.0174763 · Cited by 19 · see citing works
Ştefănescu, R., Lupu, L., Manea, M., Iacob, R. E., & Przybylski, M. (2018) · Journal of Peptide Science · doi:10.1002/psc.3047 · Cited by 12 · see citing works
Șerban, D. N., Anton, E., Chiriță, R., Bild, V., Ciobica, A. S., Alexinschi, O., Arcan, O., Popescu, R., Păduraru, L., & Timofte, D. V. (2015) · Archives of Biological Sciences · doi:10.2298/abs140228051s · Cited by 7 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Piccialli, I., Tedeschi, V., Caputo, L., D’Errico, S., Ciccone, R., De Feo, V., Secondo, A., & Pannaccione, A. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.876614 · Cited by 73 · see citing works
Lobine, D., Sadeer, N., Jugreet, S., Suroowan, S., Keenoo, B. S., Imran, M., Venugopala, K. N., Ibrahim, F. M., Zengin, G., & Mahomoodally, M. F. (2021) · Current Neuropharmacology · doi:10.2174/1570159x19666210412095251 · Cited by 32 · see citing works
- Authors
- Stefanescu, R., Stanciu, G. D., Luca, A., Paduraru, L., & Tamba, B.-I.
- Affiliations
- Center for Advanced Research and Development in Experimental Medicine (CEMEX), “Grigore T. Popa” University of Medicine and Pharmacy, 700115 Iasi, Romania
- Grigore T. Popa University of Medicine and Pharmacy (RO)
- Division Neonatology, Department Mother & Child Care, “Grigore T. Popa” University of Medicine and Pharmacy, 700115 Iasi, Romania
- Venue
- Biomolecules
- Publisher
- MDPI AG
- Published
- 2020-06-06
- Volume
- 10
- Issue
- 6
- Pages
- 870
- ISSN
- 2218-273X (ISSN-L)
- PMC
- PMC7355648
- OpenAlex
- W3033682886
- Cited by
- 35
- References
- 105
- Citations by year
- 2026: 3 · 2025: 6 · 2024: 4 · 2023: 5 · 2022: 7 · 2021: 6 · 2020: 4
- FWCI
- 0.70
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Biomolecules (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Universitatea de Medicina și Farmacie Grigore T. Popa - Iasi (27498/20.12.2018)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Complementary and alternative medicine › Medicinal Plants and Neuroprotection
- Health Sciences › Medicine › Pharmacology › Cholinesterase and Neurodegenerative Diseases
- Keywords
- Alzheimer's disease, amyloid-beta aggregation, plant secondary metabolites, Thioflavin T assay, transgenic mouse model, fibrillogenesis inhibition, epigallocatechin gallate, luteolin, myricetin, silibinin, natural products
- MeSH terms
- Silybin, Alzheimer Disease, Animals, Biological Products, Catechin, Flavonoids, Fluorescent Dyes, Mice, Transgenic, Amyloid beta-Peptides, Luteolin, Mice, Benzothiazoles, Protein Aggregates
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