Iridoids and other monoterpenes in the Alzheimer’s brain: Recent development and future prospects
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Iridoids are a class of monoterpenoid compounds constructed from 10-carbon skeleton of isoprene building units. These compounds in their aglycones and glycosylated forms exist in nature to contribute to mechanisms related to plant defenses and diverse plant-animal interactions. Recent studies have also shown that iridoids and other structurally related monoterpenes display a vast array of pharmacological effects that make them potential modulators of the Alzheimer's disease (AD). This review critically evaluates the therapeutic potential of these natural products by assessing key in vitro and in vivo data published in the scientific literature. Mechanistic approach of scrutiny addressing their effects in the Alzheimer's brain including the τ-protein phosphorylation signaling, amyloid beta (Aβ) formation, aggregation, toxicity and clearance along with various effects from antioxidant to antiinflammatory mechanisms are discussed. The drug likeness of these compounds and future prospects to consider in their development as potential leads are addressed.
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A previous review has discussed the role of monoterpenes in mechanisms related to Aβ formation, aggregation, and clearance, τ-protein phosphorylation, and aggregation.
“A previous review on monoterpenes has already discussed the role of monoterpenes in mechanisms related to Aβ formation, aggregation, and clearance, τ-protein phosphorylation, and aggregation (Habtemariam, 2018).”
From Alpha-terpinyl acetate: A natural monoterpenoid from Elettaria cardamomum as multi-target directed ligand in Alzheimer’s disease (2020) · cites this paper as Habtemariam, 2018
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Immune attack: the role of inflammation in Alzheimer disease
Heppner, F. L., Ransohoff, R. M., & Becher, B. (2015) · Nature Reviews Neuroscience · doi:10.1038/nrn3880 · Cited by 2,134 · see citing works
p38 MAP-Kinases pathway regulation, function and role in human diseases
Cuenda, A., & Rousseau, S. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2007.03.010 · Cited by 1,397 · see citing works
Iron accumulation in Alzheimer disease is a source of redox-generated free radicals
Smith, M. A., Harris, P. L. R., Sayre, L. M., & Perry, G. L. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.18.9866 · Cited by 1,357 · see citing works
Compromised MAPK signaling in human diseases: an update
Kim, E., & Choi, E. (2015) · Archives of Toxicology · doi:10.1007/s00204-015-1472-2 · Cited by 1,017 · see citing works
Biosynthesis and Biological Functions of Terpenoids in Plants
Tholl, D. (2015) · Advances in biochemical engineering, biotechnology · doi:10.1007/10_2014_295 · Cited by 949 · see citing works
Metabolic Regulation of Brain Aβ by Neprilysin
Iwata, N., Tsubuki, S., Takaki, Y., Shirotani, K., Lu, B., Gerard, N., Gerard, C., Hama, E., Lee, H., & Saido, T. (2001) · Science · doi:10.1126/science.1059946 · Cited by 894 · see citing works
(2016) · London School of Economics and Political Science Research Online (London School of Economics and Political Science) · Cited by 874 · see citing works
McGeer, P. L., Itagaki, S., Tago, H., & McGeer, E. G. (1987) · Neuroscience Letters · doi:10.1016/0304-3940(87)90696-3 · Cited by 836 · see citing works
Insulin-degrading Enzyme Regulates Extracellular Levels of Amyloid β-Protein by Degradation
Qiu, W. Q., Walsh, D. M., Ye, Z., Vekrellis, K., Zhang, J., Podlisny, M. B., Rosner, M. R., Safavi, A., Hersh, L. B., & Selkoe, D. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.49.32730 · Cited by 812 · see citing works
Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease.
Alonso, A. C., Zaidi, T., Grundke-Iqbal, I., & Iqbal, K. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.12.5562 · Cited by 738 · see citing works
Why do plants produce so many terpenoid compounds?
Pichersky, E., & Raguso, R. A. (2016) · New Phytologist · doi:10.1111/nph.14178 · Cited by 706 · see citing works
Plant terpenes: defense responses, phylogenetic analysis, regulation and clinical applications
Singh, B., & Sharma, R. A. (2015) · 3 Biotech · doi:10.1007/s13205-014-0220-2 · Cited by 562 · see citing works
Mechanisms of Aβ Clearance and Degradation by Glial Cells
Ries, M., & Sastre, M. (2016) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2016.00160 · Cited by 527 · see citing works
The application of in silico drug-likeness predictions in pharmaceutical research
Tian, S., Wang, J., Li, Y., Li, D., Xu, L., & Hou, T. (2015) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2015.01.009 · Cited by 509 · see citing works
Vekrellis, K., Ye, Z., Qiu, W. Q., Walsh, D. M., Hartley, D. M., Chesneau, V., Rosner, M. R., & Selkoe, D. J. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-05-01657.2000 · Cited by 495 · see citing works
Leon, R. M., Garcı́a, A. G., & Marco, J. L. (2011) · Medicinal Research Reviews · doi:10.1002/med.20248 · Cited by 442 · see citing works
Association of Plasma Leptin Levels With Incident Alzheimer Disease and MRI Measures of Brain Aging
Lieb, W. (2009) · JAMA · doi:10.1001/jama.2009.1836 · Cited by 428 · see citing works
Brennan, A. M., & Mantzoros, C. S. (2006) · Nature Clinical Practice Endocrinology & Metabolism · doi:10.1038/ncpendmet0196 · Cited by 374 · see citing works
Targeting Tumor Necrosis Factor Alpha for Alzheimer’s Disease
Decourt, B., Lahiri, D. K., & Sabbagh, M. N. (2016) · Current Alzheimer Research · doi:10.2174/1567205013666160930110551 · Cited by 373 · see citing works
Targeting p38 MAPK pathway for the treatment of Alzheimer's disease
Munoz, L., & Ammit, A. J. (2009) · Neuropharmacology · doi:10.1016/j.neuropharm.2009.11.010 · Cited by 370 · see citing works
The biosynthesis of C5–C25 terpenoid compounds
Dewick, P. M. (2002) · Natural Product Reports · doi:10.1039/b002685i · Cited by 357 · see citing works
Leptin signaling in astrocytes regulates hypothalamic neuronal circuits and feeding
Kim, J. G., Suyama, S., Koch, M., Jin, S., Argente-Arizon, P., Argente, J., Liu, Z.-W., Zimmer, M. R., Jeong, J. K., Szigeti-Buck, K., et al. (2014) · Nature Neuroscience · doi:10.1038/nn.3725 · Cited by 336 · see citing works
Cook, D. G., Leverenz, J. B., McMillan, P. J., Kulstad, J. J., Ericksen, S., Roth, R. A., Schellenberg, G. D., Jin, L., Kovacina, K. S., & Craft, S. (2003) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63822-9 · Cited by 329 · see citing works
Regulation of Neuronal and Glial Proteins by Leptin: Implications for Brain Development
Ahima, R. S., Bjørbæk, C., Osei, S. Y., & Flier, J. S. (1999) · Endocrinology · doi:10.1210/endo.140.6.6774 · Cited by 327 · see citing works
Crystal structure of human aquaporin 4 at 1.8 Å and its mechanism of conductance
Ho, J. D., Yeh, R., Sandstrom, A., Chorny, I., Harries, W. E. C., Robbins, R. A., Miercke, L. J. W., & Stroud, R. M. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0902725106 · Cited by 324 · see citing works
Salomone, S., Caraci, F., Leggio, G. M., Fedotova, J., & Drago, F. (2011) · British Journal of Clinical Pharmacology · doi:10.1111/j.1365-2125.2011.04134.x · Cited by 322 · see citing works
Age- and region-dependent alterations in Aβ-degrading enzymes: implications for Aβ-induced disorders
Caccamo, A., Oddo, S., Sugarman, M. C., Akbari, Y., & LaFerla, F. M. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.06.013 · Cited by 299 · see citing works
Astrocytes: Implications for Neuroinflammatory Pathogenesis of Alzheimers Disease
Li, C., Zhao, R., Gao, K., Wei, Z. Z., Yin, M. Y., Lau, L. T., Chui, D., & Yu, A. C. (2011) · Current Alzheimer Research · doi:10.2174/156720511794604543 · Cited by 291 · see citing works
Cho, J., & Johnson, G. V. W. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02155.x · Cited by 282 · see citing works
Clearance of cerebral Aβ in Alzheimer’s disease: reassessing the role of microglia and monocytes
Zuroff, L. R., Daley, D. A., Black, K. L., & Koronyo‐Hamaoui, M. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2463-7 · Cited by 275 · see citing works
Aquaporin 4: a player in cerebral edema and neuroinflammation
Fukuda, A. M., & Badaut, J. (2012) · Journal of Neuroinflammation · doi:10.1186/1742-2094-9-279 · Cited by 265 · see citing works
Wagner, U., Utton, M. A., Gallo, J., & Miller, C. C. J. (1996) · Journal of Cell Science · doi:10.1242/jcs.109.6.1537 · Cited by 255 · see citing works
Rojo, A. I., de Sagarra, M. R., & Cuadrado, A. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.05124.x · Cited by 241 · see citing works
Leptin Increases Adult Hippocampal Neurogenesis in Vivo and in Vitro
Garza, J. C., Guo, M., Zhang, W., & Lu, X. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800053200 · Cited by 236 · see citing works
Enzymic Studies on the Animal and Intestinal Bacterial Metabolism of Geniposide.
Akao, T., Kobashi, K., & Aburada, M. (1994) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.17.1573 · Cited by 235 · see citing works
Inflammatory Aspects of Alzheimer Disease and Other Neurodegenerative Disorders
Schwab, C., & McGeer, P. L. (2008) · Journal of Alzheimer s Disease · doi:10.3233/jad-2008-13402 · Cited by 234 · see citing works
Garwood, C. J., Ratcliffe, L. E., Simpson, J. E., Heath, P. R., Ince, P. G., & Wharton, S. B. (2017) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12338 · Cited by 233 · see citing works
Serum leptin level and cognition in the elderly: Findings from the Health ABC Study
Holden, K. F., Lindquist, K. J., Tylavsky, F. A., Rosano, C., Harris, T. B., & Yaffe, K. S. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.11.024 · Cited by 227 · see citing works
Apigenin as neuroprotective agent: Of mice and men
Nabavi, S. F., Khan, H. Z., D’Onofrio, G., Šamec, D., Shirooie, S., Dehpour, A. R., Argüelles, S., Habtemariam, S., & Sobarzo‐Sánchez, E. (2017) · Pharmacological Research · doi:10.1016/j.phrs.2017.10.008 · Cited by 221 · see citing works
Badaut, J., Fukuda, A. M., Jullienne, A., & Petry, K. G. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.10.032 · Cited by 212 · see citing works
Neuroprotective effects of chrysin: From chemistry to medicine
Nabavi, S. F., Braidy, N., Habtemariam, S., Orhan, İ., Daglia, M., Manayi, A., Gortzi, O., & Nabavi, S. M. (2015) · Neurochemistry International · doi:10.1016/j.neuint.2015.09.006 · Cited by 203 · see citing works
Iron(II) Binding to Amyloid-β, the Alzheimer’s Peptide
Garah, F. E., Bijani, C., Coppel, Y., Faller, P., & Hureau, C. (2011) · Inorganic Chemistry · doi:10.1021/ic201233b · Cited by 199 · see citing works
The Therapeutic Potential of Rosemary (Rosmarinus officinalis) Diterpenes for Alzheimer’s Disease
Habtemariam, S. (2016) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2016/2680409 · Cited by 195 · see citing works
Neprilysin: An Enzyme Candidate to Slow the Progression of Alzheimer's Disease
El‐Amouri, S. S., Zhu, H., Yu, J., Marr, R. A., Verma, I. M., & Kindy, M. S. (2008) · American Journal Of Pathology · doi:10.2353/ajpath.2008.070620 · Cited by 188 · see citing works
The aquaporin-4 water channel as a potential drug target in neurological disorders
Verkman, A. S., Smith, A. J., Phuan, P., Tradtrantip, L., & Anderson, M. O. (2017) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2017.1398236 · Cited by 185 · see citing works
Are amyloid‐degrading enzymes viable therapeutic targets in Alzheimer’s disease?
Nalivaeva, N., Beckett, C. S., Belyaev, N. D., & Turner, A. J. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07510.x · Cited by 178 · see citing works
Leptin promotes rapid dynamic changes in hippocampal dendritic morphology
O’Malley, D., MacDonald, N., Mizielinska, S., Connolly, C. N., Irving, A. J., & Harvey, J. (2007) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2007.05.001 · Cited by 178 · see citing works
Systemic Availability and Pharmacokinetics of Thymol in Humans
Kohlert, C., Schindler, G., März, R., Abel, G., Brinkhaus, B., Derendorf, H., Gräfe, E., & Veit, M. (2002) · The Journal of Clinical Pharmacology · doi:10.1177/009127002401102678 · Cited by 175 · see citing works
Glycogen synthase kinase 3β and Alzheimer’s disease: pathophysiological and therapeutic significance
Balaraman, Y., Limaye, A. R., Levey, A. I., & Srinivasan, S. (2006) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5597-y · Cited by 167 · see citing works
The Role of Tau Phosphorylation in the Pathogenesis of Alzheimers Disease
Mi, K., & Johnson, G. V. W. (2006) · Current Alzheimer Research · doi:10.2174/156720506779025279 · Cited by 166 · see citing works
Habtemariam, S. (1997) · Journal of Natural Products · doi:10.1021/np960581z · Cited by 163 · see citing works
Plant chemical defense against herbivores and pathogens: generalized defense or trade-offs?
Biere, A., Marak, H. B., & DAMME, J. M. M. V. (2004) · Oecologia · doi:10.1007/s00442-004-1603-6 · Cited by 160 · see citing works
Wahlberg, N. (2001) · Evolution · doi:10.1554/0014-3820(2001)055[0522:tpaboh]2.0.co;2 · Cited by 160 · see citing works
Braidy, N., Behzad, S., Habtemariam, S., Ahmed, T., Daglia, M., Nabavi, S. M., Sobarzo‐Sánchez, E., & Nabavi, S. F. (2017) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527316666170328113309 · Cited by 158 · see citing works
Sabogal-Guáqueta, A. M., Osorio, E., & Cardona-Gómez, G. P. (2016) · Neuropharmacology · doi:10.1016/j.neuropharm.2015.11.002 · Cited by 148 · see citing works
Dysregulation of leptin signaling in Alzheimer disease: evidence for neuronal leptin resistance
Bonda, D., Stone, J. G., Torres, S. L., Siedlak, S. L., Perry, G. L., Kryscio, R. J., Jicha, G. A., Casadesús, G., Smith, M. A., Zhu, X., et al. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12380 · Cited by 145 · see citing works
Liu, J., Yin, F., Zheng, X., Jing, J., & Hu, Y. (2007) · Neurochemistry International · doi:10.1016/j.neuint.2007.04.021 · Cited by 145 · see citing works
The central role of aquaporins in the pathophysiology of ischemic stroke
Vella, J. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00108 · Cited by 143 · see citing works
Gao, C., Liu, Y., Jiang, Y., Ding, J., & Li, L. (2013) · Brain Pathology · doi:10.1111/bpa.12116 · Cited by 141 · see citing works
Liu, J., Yin, F., Guo, L., Deng, X., & Hu, Y. (2009) · Acta Pharmacologica Sinica · doi:10.1038/aps.2008.25 · Cited by 140 · see citing works
Zawisza, I. A., Rózga, M., & Bal, W. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.03.012 · Cited by 138 · see citing works
Human Breast Tissue Disposition and Bioactivity of Limonene in Women with Early-Stage Breast Cancer
Miller, J. A., Lang, J. E., Ley, M., Nagle, R. B., Hsu, C., Thompson, P. A., Cordova, C. A., Waer, A. L., & Chow, H. ‐. S. (2013) · Cancer Prevention Research · doi:10.1158/1940-6207.capr-12-0452 · Cited by 135 · see citing works
Rutin as a Natural Therapy for Alzheimer’s Disease: Insights into its Mechanisms of Action
Habtemariam, S. (2016) · Current Medicinal Chemistry · doi:10.2174/0929867323666160217124333 · Cited by 130 · see citing works
Son, S. M., Cha, M.-Y., Choi, H., Kang, S., Choi, H., Lee, M., Park, S. A., & Mook‐Jung, I. (2016) · Autophagy · doi:10.1080/15548627.2016.1159375 · Cited by 129 · see citing works
Upstream regulators and downstream effectors of NF-κB in Alzheimer’s disease
Shi, Z.-M., Han, Y.-W., Han, X.-H., Zhang, K., Chang, Y.-N., Hu, Z.-M., Qi, H.-X., Ting, C., Zhen, Z., & Hong, W. (2016) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2016.05.022 · Cited by 125 · see citing works
Modulation of GSK-3 as a Therapeutic Strategy on Tau Pathologies
Medina, M., Garrido, J. J., & Wandosell, F. G. (2011) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2011.00024 · Cited by 124 · see citing works
The Natural History of Alzheimer's Disease: A Brain Bank Study
Jost, B. C., & Grossberg, G. T. (1995) · Journal of the American Geriatrics Society · doi:10.1111/j.1532-5415.1995.tb07401.x · Cited by 123 · see citing works
Genipin inhibits the inflammatory response of rat brain microglial cells
Nam, K. N., Choi, Y.-S., Jung, H.-J., Park, G. H., Park, J., Moon, S., Cho, K., Kang, C., Kang, I., Oh, M. S., et al. (2010) · International Immunopharmacology · doi:10.1016/j.intimp.2010.01.011 · Cited by 121 · see citing works
Free Superoxide is an Intermediate in the Production of H 2 O 2 by Copper(I)‐Aβ Peptide and O 2
Reybier, K., Ayala, S., Aliès, B., Rodrigues, J. V., Rodriguez, S. B., Penna, G. L., Collin, F., Gomes, C. M., Hureau, C., & Faller, P. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201508597 · Cited by 120 · see citing works
Loganin improves learning and memory impairments induced by scopolamine in mice
Kwon, S., Kim, H., Lee, S., & Jang, C. (2009) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2009.06.062 · Cited by 118 · see citing works
Porres-Martínez, M., González‐Burgos, E., Carretero, M. E., & Gómez-Serranillos, M. P. (2016) · Zeitschrift für Naturforschung C · doi:10.1515/znc-2014-4135 · Cited by 118 · see citing works
Migliorini, C., Porciatti, E., Łuczkowski, M., & Valensin, D. (2011) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2011.07.004 · Cited by 116 · see citing works
Liu, Z. Q., Jiang, Z., Liu, L., & Hu, M. (2006) · Pharmaceutical Research · doi:10.1007/s11095-006-9100-8 · Cited by 112 · see citing works
Khan, A., Vaibhav, K., Javed, H., Tabassum, R., Ahmed, M. E., Khan, M. M., Khan, M. B., Shrivastava, P., Islam, F., Siddiqui, M. S., et al. (2013) · Neurochemical Research · doi:10.1007/s11064-013-1231-9 · Cited by 110 · see citing works
Zhong, S., Ge, Q.-H., Li, Q., Qu, R., & Ma, S. (2009) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2009.01.027 · Cited by 108 · see citing works
Plants-derived neuroprotective agents: cutting the cycle of cell death through multiple mechanisms
Elufioye, T. O., Berida, T. I., & Habtemariam, S. (2017) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2017/3574012 · Cited by 107 · see citing works
New isoforms of rat Aquaporin-4
Moe, S. E., Sorbo, J. G., Sogaard, R., Zeuthen, T., Ottersen, O. P., & Holen, T. (2008) · Genomics · doi:10.1016/j.ygeno.2007.12.003 · Cited by 103 · see citing works
Altered Serum Levels of Adipokines and Insulin in Probable Alzheimer's Disease
Khemka, V. K., Bagchi, D., Bandyopadhyay, K., Bir, A., Chattopadhyay, M., Biswas, A., Basu, D., & Chakrabarti, S. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-140006 · Cited by 101 · see citing works
Antidiabetic Potential of Monoterpenes: A Case of Small Molecules Punching above Their Weight
Habtemariam, S. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms19010004 · Cited by 100 · see citing works
Wang, K., Zhu, L., Zhu, X., Zhang, K., Huang, B., Zhang, J., Zhang, Y., Zhu, L., Zhou, B., & Zhou, F. (2013) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-013-0006-9 · Cited by 96 · see citing works
Protective effects of catalpol against H2O2-induced oxidative stress in astrocytes primary cultures
Bi, J., Jiang, B., Liu, J. H., Chen, L., Zhang, X. L., & An, L. (2008) · Neuroscience Letters · doi:10.1016/j.neulet.2008.07.029 · Cited by 94 · see citing works
Lv, C., Wang, L., Liu, X., Yan, S., Yan, S. S., Wang, Y., & Zhang, W. (2014) · Neuropharmacology · doi:10.1016/j.neuropharm.2014.09.019 · Cited by 93 · see citing works
Dong, H., Li, R., Yu, C., Xu, T., Zhang, X., & Dong, M. (2014) · Neuroscience · doi:10.1016/j.neuroscience.2014.11.008 · Cited by 92 · see citing works
Metabolism in Rats ofp‐Cymene Derivatives: Carvacrol and Thymol
Austgulen, L.-T., Solheim, E., & Scheline, R. R. (1987) · Pharmacology & Toxicology · doi:10.1111/j.1600-0773.1987.tb01783.x · Cited by 91 · see citing works
Capsaicin reduces Alzheimer-associated tau changes in the hippocampus of type 2 diabetes rats
Xu, W., Liu, J., Ma, D., Yuan, G., Lü, Y., & Yang, Y. (2017) · PLoS ONE · doi:10.1371/journal.pone.0172477 · Cited by 89 · see citing works
Neuroprotective effects of leptin in vivo and in vitro
Dicou, E., Attoub, S., & Gressèns, P. (2001) · Neuroreport · doi:10.1097/00001756-200112210-00019 · Cited by 87 · see citing works
Hoeijmakers, L., Heinen, Y., van Dam, A.-M., Lucassen, P. J., & Korosi, A. (2016) · Frontiers in Human Neuroscience · doi:10.3389/fnhum.2016.00398 · Cited by 85 · see citing works
Varghese, G. K., Bose, L. V., & Habtemariam, S. (2012) · Pharmaceutical Biology · doi:10.3109/13880209.2012.729066 · Cited by 83 · see citing works
Gu, X., CAI, Z., Cai, M., Liu, K., Liu, D., ZHANG, Q., Tan, J. H., & Ma, Q. (2016) · Molecular Medicine Reports · doi:10.3892/mmr.2016.4805 · Cited by 81 · see citing works
Myrtenal inhibits acetylcholinesterase, a known Alzheimer target
Kaufmann, D., Dogra, A. K., & Wink, M. (2011) · Journal of Pharmacy and Pharmacology · doi:10.1111/j.2042-7158.2011.01344.x · Cited by 80 · see citing works
The Therapeutic Potential of Rutin for Diabetes: An Update
Habtemariam, S., & Lentini, G. (2015) · Mini-Reviews in Medicinal Chemistry · doi:10.2174/138955751507150424103721 · Cited by 80 · see citing works
Leptin protects hippocampal CA1 neurons against ischemic injury
Zhang, F., & Chen, J. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05645.x · Cited by 79 · see citing works
Further pharmacological evidence of the neuroprotective effect of catalpol from Rehmannia glutinosa
Zhang, X., Zhang, A., Jiang, B., Bao, Y., Wang, J., & An, L. (2008) · Phytomedicine · doi:10.1016/j.phymed.2008.01.001 · Cited by 79 · see citing works
Nabavi, S. F., Braidy, N., Habtemariam, S., Sureda, A., Manayi, A., & Nabavi, S. M. (2016) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026616666160204121725 · Cited by 79 · see citing works
Protective Effects of Caffeic Acid and the Alzheimer's Brain: An Update
Habtemariam, S. (2016) · Mini-Reviews in Medicinal Chemistry · doi:10.2174/1389557516666161130100947 · Cited by 78 · see citing works
Protective effects of linalool against amyloid beta-induced cognitive deficits and damages in mice
Xu, P., Wang, K., Lü, C., Dong, L., Gao, L., Yan, M., Aibai, S., Yang, Y., & Liu, X. (2017) · Life Sciences · doi:10.1016/j.lfs.2017.02.010 · Cited by 77 · see citing works
The Antidiabetic Therapeutic Potential of Dietary Polyphenols
Habtemariam, S., & Varghese, G. I. (2014) · Current Pharmaceutical Biotechnology · doi:10.2174/1389201015666140617104643 · Cited by 76 · see citing works
Natural Therapies of the Inflammatory Bowel Disease: The Case of Rutin and its Aglycone, Quercetin
Habtemariam, S., & Belai, A. (2017) · Mini-Reviews in Medicinal Chemistry · doi:10.2174/1389557517666170120152417 · Cited by 76 · see citing works
Zhang, X., Jin, C., Li, Y., Guan, S., Han, F., & Zhang, S. (2013) · Food and Chemical Toxicology · doi:10.1016/j.fct.2013.04.006 · Cited by 75 · see citing works
Pourkhodadad, S., Alirezaei, M., Moghaddasi, M., Ahmadvand, H., Karami, M., Delfan, B., & khayat, Z. K. (2016) · The Journal of Physiological Sciences · doi:10.1007/s12576-016-0437-4 · Cited by 75 · see citing works
Leal, M. C., Dorfman, V. B., Fernández-Gamba, A. C., Frangione, B., Wısnıewskı, T., Castaño, E. M., Sigurdsson, E. M., & Morelli, L. (2006) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/01.jnen.0000235853.70092.ba · Cited by 74 · see citing works
Zhang, X., An, L., Bao, Y., Wang, J., & Jiang, B. (2008) · Food and Chemical Toxicology · doi:10.1016/j.fct.2008.05.032 · Cited by 73 · see citing works
Extractability of Rutin in Herbal Tea Preparations of Moringa stenopetala Leaves
Habtemariam, S., & Varghese, G. K. (2015) · Beverages · doi:10.3390/beverages1030169 · Cited by 73 · see citing works
Tahmasebinia, F., & Emadi, S. (2017) · BioMetals · doi:10.1007/s10534-017-0005-2 · Cited by 73 · see citing works
α-Glucosidase Inhibitory Activity of Kaempferol-3- O -rutinoside
Habtemariam, S. (2011) · Natural Product Communications · doi:10.1177/1934578x1100600211 · Cited by 72 · see citing works
New Insights into the Roles of Metalloproteinases in Neurodegeneration and Neuroprotection
Turner, A. J., & Nalivaeva, N. N. (2007) · International review of neurobiology · doi:10.1016/s0074-7742(07)82006-x · Cited by 70 · see citing works
Regulation of AQP4 surface expression via vesicle mobility in astrocytes
Potokar, M., Stenovec, M., Jorgačevski, J., Holen, T., Kreft, M., Ottersen, O. P., & Zorec, R. (2013) · Glia · doi:10.1002/glia.22485 · Cited by 68 · see citing works
Protein Phosphorylation is a Key Mechanism in Alzheimer’s Disease
Oliveira, J., Costa, M., de Almeida, M. S. C., Silva, O. A. B. D. C. E., & Henriques, A. G. (2017) · Journal of Alzheimer's Disease · doi:10.3233/jad-170176 · Cited by 68 · see citing works
Antioxidant compounds from a South Asian beverage and medicinal plant, Cassia auriculata
Juan-Badaturuge, M., Habtemariam, S., & Thomas, M. J. K. (2010) · Food Chemistry · doi:10.1016/j.foodchem.2010.08.065 · Cited by 67 · see citing works
Jhang, K. A., Park, J., Kim, H.-S., & Chong, Y. H. (2017) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.7b03252 · Cited by 67 · see citing works
Kurt, B. Z., Gazioğlu, I., Dağ, A., Salmas, R. E., Kayık, G., Durdağı, S., & Sönmez, F. (2016) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2016.12.037 · Cited by 66 · see citing works
Zhang, H., Peng, J., Cheng, X.-B., Shi, B., Zhang, M., & Xu, R. (2015) · Neurochemical Research · doi:10.1007/s11064-015-1632-z · Cited by 62 · see citing works
Prevention of the Neurotoxicity of the Amyloid Beta Protein by Genipin
YAMAZAKI, M., SAKURA, N., CHIBA, K., & MOHRI, T. (2001) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.24.1454 · Cited by 62 · see citing works
Tau Oligomers as Potential Targets for Alzheimer’s Diagnosis and Novel Drugs
Guzmán‐Martínez, L., Farias, G. A., & Maccioni, R. B. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00167 · Cited by 62 · see citing works
Strategies, Development, and Pitfalls of Therapeutic Options for Alzheimer's Disease
Haas, C. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-110986 · Cited by 61 · see citing works
Habtemariam, S. (2012) · Phytotherapy Research · doi:10.1002/ptr.4711 · Cited by 60 · see citing works
Costs and benefits of plant allelochemicals in herbivore diet in a multi enemy world
Reudler, J. H., Lindstedt, C., Pakkanen, H. K., Lehtinen, I., & Mappes, J. (2015) · Oecologia · doi:10.1007/s00442-015-3425-0 · Cited by 59 · see citing works
Huang, W., Chen, P., Yu, K., Han, Y., Song, M., & Li, Y. (2017) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2017.09.114 · Cited by 59 · see citing works
Han, H., Yang, L., Xu, Y., Ding, Y., Bligh, S. W. A., Zhang, T., & Wang, Z. (2011) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.5216 · Cited by 58 · see citing works
Phytochemical, Antioxidant and Anti‐α‐glucosidase Activity Evaluations of Bergenia cordifolia
Roselli, M., Lentini, G., & Habtemariam, S. (2011) · Phytotherapy Research · doi:10.1002/ptr.3655 · Cited by 57 · see citing works
Zhong, Z., Wang, B., Dai, M.-C., Sun, Y., Sun, Q., Yang, G., & Bian, L. (2013) · Neuroscience Letters · doi:10.1016/j.neulet.2013.09.023 · Cited by 57 · see citing works
Shamim, D., & Laskowski, M. C. (2017) · Journal of Central Nervous System Disease · doi:10.1177/1179573517722512 · Cited by 56 · see citing works
Cheng, C., Lin, J.-Z., Li, L., Yang, J., Jia, W., Huang, Y., Du, F., Wang, F.-Q., Li, M., Li, Y., et al. (2016) · Acta Pharmacologica Sinica · doi:10.1038/aps.2015.103 · Cited by 55 · see citing works
Sun, J., Zhang, X., Wang, C., Teng, Z., & Li, Y. (2017) · The American Journal of Chinese Medicine · doi:10.1142/s0192415x17500902 · Cited by 54 · see citing works
Yu, B., Ruan, M., Cui, X., Guo, J., Xu, L., & Dong, X. (2013) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/j.jpba.2013.01.017 · Cited by 53 · see citing works
Amyloid Fibrils and Prefibrillar Aggregates
Lorenzen, N., Wanker, E. E., & Otzen, D. E. (2013) · Wiley eBooks · doi:10.1002/9783527654185 · Cited by 52 · see citing works
Leptin inhibits 1-methyl-4-phenylpyridinium-induced cell death in SH-SY5Y cells
Lu, J., Park, C., Lee, S., Shin, D. W., & Kang, J. (2006) · Neuroscience Letters · doi:10.1016/j.neulet.2006.08.053 · Cited by 51 · see citing works
Borneol alleviates oxidative stress via upregulation of Nrf2 and Bcl-2 in SH-SY5Y cells
Hur, J., Pak, S. C., Koo, B., & Jeon, S. (2012) · Pharmaceutical Biology · doi:10.3109/13880209.2012.700718 · Cited by 50 · see citing works
Kim, H., Youn, K., Ahn, M.-R., Kim, O. Y., Jeong, W., Ho, C., & Jun, M. (2015) · Food & Function · doi:10.1039/c5fo00055f · Cited by 49 · see citing works
Geniposide Attenuates Mitochondrial Dysfunction and Memory Deficits in APP/PS1 Transgenic Mice
Lv, C., Liu, X., Liu, H., Chen, T., & Zhang, W. (2014) · Current Alzheimer Research · doi:10.2174/1567205011666140618095925 · Cited by 49 · see citing works
Laurentz, M., Reudler, J. H., Mappes, J., Friman, V., Ikonen, S., & Lindstedt, C. (2012) · Journal of Chemical Ecology · doi:10.1007/s10886-012-0066-1 · Cited by 48 · see citing works
Comparative Antioxidant, Prooxidant and Cytotoxic Activity of Sigmoidin A and Eriodictyol
Habtemariam, S., & Dagne, E. (2009) · Planta Medica · doi:10.1055/s-0029-1240604 · Cited by 46 · see citing works
Hwang, E., Kim, H.-B., Lee, S., Kim, M., Lee, S.-O., Han, S., Maeng, S., & Park, J. H. (2017) · Physiology & Behavior · doi:10.1016/j.physbeh.2016.12.043 · Cited by 46 · see citing works
Zhang, Y., Yin, F., Liu, J., Liu, Z., Guo, L., Xia, Z., & Zidichouski, J. (2015) · Neurochemistry International · doi:10.1016/j.neuint.2015.04.002 · Cited by 45 · see citing works
Noël, S., Rodriguez, S. B., Sayen, S., Guillon, E., Faller, P., & Hureau, C. (2014) · Metallomics · doi:10.1039/c4mt00016a · Cited by 44 · see citing works
Sun, R., Wang, K., Wu, D., Li, X., & Ou, Y. (2012) · Folia Neuropathologica · doi:10.5114/fn.2012.30527 · Cited by 44 · see citing works
Therapeutic options in Alzheimer’s disease
Moreira, P. I., Zhu, X., Nunomura, A., Smith, M. A., & Perry, G. L. (2006) · Expert Review of Neurotherapeutics · doi:10.1586/14737175.6.6.897 · Cited by 43 · see citing works
Investigation of UDP‐glucuronosyltransferases ( UGTs ) Inhibitory Properties of Carvacrol
Dong, R., Fang, Z., Zhu, L., Liang, S., Ge, G., Yang, L., & Ze-yuan, L. (2011) · Phytotherapy Research · doi:10.1002/ptr.3525 · Cited by 43 · see citing works
Antioxidant Principles of Tanacetum vulgare L. Aerial Parts
Juan-Badaturuge, M., Habtemariam, S., Jackson, C., & Thomas, M. J. K. (2009) · Natural Product Communications · doi:10.1177/1934578x0900401121 · Cited by 41 · see citing works
Maggio, A., Rosselli, S., & Bruno, M. (2016) · Current Pharmaceutical Design · doi:10.2174/1381612822666160607065917 · Cited by 41 · see citing works
Miller, J. A., Hakim, I. A., Chew, W. M., Thompson, P. A., Thomson, C. A., & Chow, H. ‐. S. (2010) · Nutrition and Cancer · doi:10.1080/01635581003693066 · Cited by 40 · see citing works
The protective effect of geniposide on human neuroblastoma cells in the presence of formaldehyde
Sun, P., Chen, J., Li, J., Sun, M., Mo, W., Liu, K.-L., Meng, Y., Liu, Y. M., Wang, F., He, R., et al. (2013) · BMC Complementary and Alternative Medicine · doi:10.1186/1472-6882-13-152 · Cited by 39 · see citing works
Genipin Suppresses A23187-Induced Cytotoxicity in Neuro2a Cells
Yamazaki, M., Chiba, K., & Yoshikawa, C. (2009) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.32.1043 · Cited by 39 · see citing works
Zhao, C., Lv, C., Li, H., Du, S., Liu, X., Li, Z., Xin, W., & Zhang, W. (2016) · PLoS ONE · doi:10.1371/journal.pone.0152551 · Cited by 39 · see citing works
Catalpol preserves neural function and attenuates the pathology of Alzheimer's disease in mice
Huang, J., WU, J., Xiang, S., Sheng, S., Jiang, Y., Yang, Z., & Hua, F. (2015) · Molecular Medicine Reports · doi:10.3892/mmr.2015.4496 · Cited by 37 · see citing works
Habtemariam, S. (2015) · Natural Product Communications · doi:10.1177/1934578x1501000324 · Cited by 35 · see citing works
Bhakta, H. K., Park, C. H., Yokozawa, T., Min, B.-S., Jung, H. A., & Choi, J. S. (2016) · Archives of Pharmacal Research · doi:10.1007/s12272-016-0745-5 · Cited by 35 · see citing works
Roles of Aquaporin-4 Isoforms and Amino Acids in Square Array Assembly
Strand, L., Moe, S. E., Solbu, T. T., Vaadal, M., & Holen, T. (2009) · Biochemistry · doi:10.1021/bi802231q · Cited by 34 · see citing works
Zhang, Y., Yin, F., Liu, J., & Liu, Z. (2016) · Chemical Biology & Drug Design · doi:10.1111/cbdd.12673 · Cited by 34 · see citing works
Habtemariam, S., & Varghese, G. K. (2014) · Phytotherapy Research · doi:10.1002/ptr.5229 · Cited by 33 · see citing works
Cheng, S., Lin, L.-C., Lin, C.-H., & Tsai, T. (2013) · Journal of Pharmacy and Pharmacology · doi:10.1111/jphp.12185 · Cited by 32 · see citing works
Habtemariam, S. (2011) · Journal of Medicinal Food · doi:10.1089/jmf.2010.0257 · Cited by 32 · see citing works
Geniposide decreases the level of Aβ1−42 in the hippocampus of streptozotocin-induced diabetic rats
Liu, J., Zhang, Y., Deng, X., & Yin, F. (2013) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmt069 · Cited by 32 · see citing works
Stavrakov, G., Philipova, I., Zheleva‐Dimitrova, D., Valkova, I., Salamanova, E., Konstantinov, S., & Doytchinova, I. A. (2017) · Chemical Biology & Drug Design · doi:10.1111/cbdd.12991 · Cited by 32 · see citing works
Antioxidant and cytoprotective activity of leaves of Peltiphyllum peltatum (Torr.) Engl.
Habtemariam, S., & JACKSON, C. (2007) · Food Chemistry · doi:10.1016/j.foodchem.2007.03.073 · Cited by 31 · see citing works
Li, J., Ji, X., Zhang, J., Shi, G., Xue, Z., & Wang, K. (2014) · Folia Neuropathologica · doi:10.5114/fn.2014.45569 · Cited by 31 · see citing works
Li, J., Ji, X., Zhang, J., Shi, G., Zhu, X., & Wang, K. (2014) · PubMed · Cited by 28 · see citing works
β-Secretase (BACE1) inhibitory property of loganin isolated fromCorni fructus
Youn, K., Jeong, W., & Jun, M. (2012) · Natural Product Research · doi:10.1080/14786419.2012.718774 · Cited by 26 · see citing works
Antioxidant and Anti‐α‐glucosidase Compounds from the Rhizome of Peltiphyllum peltatum (Torr.) Engl
Habtemariam, S., & Cowley, R. A. (2012) · Phytotherapy Research · doi:10.1002/ptr.4626 · Cited by 25 · see citing works
Catechols and quercetin reduce MTT through iron ions: A possible artefact in cell viability assays
Habtemariam, S. (1995) · Phytotherapy Research · doi:10.1002/ptr.2650090816 · Cited by 23 · see citing works
Liu, Z., Zhang, Y., Liu, J., & Yin, F. (2017) · Archives of Pharmacal Research · doi:10.1007/s12272-016-0875-9 · Cited by 21 · see citing works
Sun, P., Ding, H., Liang, M., Li, X., Mo, W., Wang, X., Liu, Y. M., He, R., & Hua, Q. (2014) · BioMed Research International · doi:10.1155/2014/284314 · Cited by 20 · see citing works
Rahimi, N., Delfan, B., Motamed-Gorji, N., & Dehpour, A. R. (2017) · Journal of Natural Medicines · doi:10.1007/s11418-017-1071-z · Cited by 20 · see citing works
Li, H.-L., He, J., Bai, M., Song, Q.-Y., Feng, E.-F., Rao, G.-X., & Xu, G. (2012) · Arzneimittelforschung · doi:10.1055/s-0031-1298021 · Cited by 17 · see citing works
Zhang, Y., Xia, Z., Liu, J., & Yin, F. (2015) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527314666141229110156 · Cited by 17 · see citing works
Wang, J., Li, W.-T., Yu, S.-T., Xie, H., & Han, H.-R. (2014) · Die Pharmazie · doi:10.31083/ph.2014.4503 · Cited by 17 · see citing works
Chen, C., Han, F., Zhang, Y., Lu, J., & Shi, Y. (2008) · Biomedical Chromatography · doi:10.1002/bmc.993 · Cited by 14 · see citing works
Padma, P. R., Chansouria, J. P. N., & Khosa, R. L. (1997) · Phytotherapy Research · doi:10.1002/(sici)1099-1573(199706)11:4 · Cited by 12 · see citing works
Terpenoids and Plant Communication
Llusià, J., Peñuelas, J., & Garrofé, M. E. I. (1997) · Estudis Romànics (Institut d'Estudis Catalans) · doi:10.2436/bichn.vi.8913 · Cited by 11 · see citing works
Leptin Signaling Plays a Critical Role in the Geniposide-Induced Decrease of Tau Phosphorylation
Liu, J., Liu, Z., Zhang, Y., & Yin, F. (2015) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmv106 · Cited by 11 · see citing works
Wang, J.-H., Xie, H., Zhao, T.-K., & Bai, K. (2014) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2014.12.014 · Cited by 10 · see citing works
Zhong, S., Ma, S., & Hong, Z. (2013) · PubMed · Cited by 10 · see citing works
Inhibition of β-Secretase Activity by Monoterpenes, Sesquiterpenes, and C13 Norisoprenoids
Marumoto, S., Okuno, Y., & Miyazawa, M. (2017) · Journal of Oleo Science · doi:10.5650/jos.ess16188 · Cited by 9 · see citing works
Martey, O., Shi, X., & He, X. (2013) · Pharmacology & Pharmacy · doi:10.4236/pp.2013.47a1002 · Cited by 7 · see citing works
Study on active constituents against Alzheimer's disease from Valeriana amurensis
Wan, Y.-Y., Wang, C., Wang, Q., Xiao, Y., Wang, Z., & Kuang, H. (2014) · China Journal of Chinese Materia Medica · doi:10.4268/cjcmm20160914 · Cited by 6 · see citing works
Localization of Defensive Chemicals in Two Congeneric Butterflies (Euphydryas, Nymphalidae)
Mason, P. A., & Bowers, M. D. (2017) · Journal of Chemical Ecology · doi:10.1007/s10886-017-0841-0 · Cited by 5 · see citing works
The Role of Aβ in Alzheimer's Disease
Ryan, T. M., Roberts, B. R., Streltsov, V. A., Nuttall, S. D., & Masters, C. L. (2013) · doi:10.1002/9783527654185.ch13 · Cited by 4 · see citing works
Hu, Y. (2006) · Zhongguo yaolixue tongbao · Cited by 4 · see citing works
[Role of PI3K/Akt pathway in effect of paeoniflorin against Aβ25-35-induced PC12 cell injury].
Liu, L., Wang, S., & Wang, J. (2014) · PubMed · Cited by 3 · see citing works
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Iridoids: Research Advances in Their Phytochemistry, Biological Activities, and Pharmacokinetics
Wang, C., Gong, X., Bo, A., Zhang, L., Zhang, M., Zang, E., Zhang, C., & Li, M. (2020) · Molecules · doi:10.3390/molecules25020287 · Cited by 222 · see citing works
Habtemariam, S. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/4724920 · Cited by 148 · see citing works
Habtemariam, S. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/8512048 · Cited by 140 · see citing works
Habtemariam, S. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19020458 · Cited by 110 · see citing works
Habtemariam, S. (2019) · Molecules · doi:10.3390/molecules24081519 · Cited by 107 · see citing works
Habtemariam, S., & Lentini, G. (2018) · Biomedicines · doi:10.3390/biomedicines6020039 · Cited by 104 · see citing works
Therapeutic Potential of Ursolic Acid in Cancer and Diabetic Neuropathy Diseases
Alam, M., Ali, S., Ahmed, S., Elasbali, A. M., Adnan, M., Islam, A., Hassan, M. I., & Yadav, D. K. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222212162 · Cited by 91 · see citing works
Habtemariam, S. (2019) · Biomedicines · doi:10.3390/biomedicines7040098 · Cited by 71 · see citing works
Chowdhury, S., & Kumar, S. (2020) · Journal of Functional Foods · doi:10.1016/j.jff.2020.103892 · Cited by 69 · see citing works
A Review of Biologically Active Natural Products from a Desert Plant Cistanche tubulosa
Morikawa, T., Xie, H., Pan, Y., Ninomiya, K., Yuan, D., Jia, X., Yoshikawa, M., Nakamura, S., Matsuda, H., & Muraoka, O. (2019) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.c19-00008 · Cited by 65 · see citing works
Habtemariam, S. (2018) · Neural Regeneration Research · doi:10.4103/1673-5374.233438 · Cited by 61 · see citing works
Pugliese, R., Maleki, M., Zuckermann, R. N., & Gelain, F. (2018) · Biomaterials Science · doi:10.1039/c8bm00825f · Cited by 60 · see citing works
Modulation of Reactive Oxygen Species in Health and Disease
Habtemariam, S. (2019) · Antioxidants · doi:10.3390/antiox8110513 · Cited by 57 · see citing works
Wojtunik‐Kulesza, K. A., Rudkowska, M., Kasprzak‐Drozd, K., Oniszczuk, A., & Borowicz, K. K. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22147366 · Cited by 50 · see citing works
Therapeutic potential of plant iridoids in depression: a review
Kou, Y., Li, Z.-H., Yang, T.-G., Shen, X., Wang, X., Li, H.-P., Zhou, K., Li, L., Xia, Z., Zheng, X.-O., et al. (2022) · Pharmaceutical Biology · doi:10.1080/13880209.2022.2136206 · Cited by 34 · see citing works
Sánchez-Martínez, J. D., Álvarez‐Rivera, G., Gallego, R., Fagundes, M. B., Valdés, A., Mendiola, J. A., Ibáñez, E., & Cifuentes, A. (2022) · Food Chemistry X · doi:10.1016/j.fochx.2022.100242 · Cited by 36 · see citing works
Iridoid Derivatives as Anticancer Agents: An Updated Review from 1970–2022
Ndongwe, T., Witika, B. A., Mncwangi, N. P., Poka, M., Skosana, P., Demana, P. H., Summers, B., & Siwe‐Noundou, X. (2023) · Cancers · doi:10.3390/cancers15030770 · Cited by 32 · see citing works
Central nervous system and analgesic profiles of Lippia genus
Siqueira-Lima, P. S., Passos, F. R. S., Angélica, M., de Menezes, I. R. A., Coutinho, H. D. M., de Lima, Á. A. N., Zengin, G., Quintans, J. D. S. S., & Quintans‐Júnior, L. J. (2018) · Revista Brasileira de Farmacognosia · doi:10.1016/j.bjp.2018.11.006 · Cited by 31 · see citing works
Paul, K., Ganguly, U., Chakrabarti, S., & Bhattacharjee, P. (2019) · NeuroMolecular Medicine · doi:10.1007/s12017-019-08574-2 · Cited by 29 · see citing works
Azizi, Z., Salimi, M., Amanzadeh, A., Majelssi, N., & Naghdi, N. (2020) · Iranian Biomedical Journal · doi:10.29252/ibj.24.4.243 · Cited by 28 · see citing works
Panizzutti, B., Bortolasci, C. C., Spolding, B., Kidnapillai, S., Connor, T., Richardson, M. F., Truong, T. T. T., Liu, Z. S.-J., Morris, G., Gray, L. J., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22137164 · Cited by 25 · see citing works
Hriţcu, L., Boiangiu, R. Ş., de Morais, M. C., & de Sousa, D. P. (2020) · BioMed Research International · doi:10.1155/2020/8082560 · Cited by 25 · see citing works
Saidi, I., Nimbarte, V. D., Schwalbe, H., Waffo‐Téguo, P., Harrath, A. H., Mansour, L. A., Alwasel, S. H., & Jannet, H. B. (2020) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2020.104093 · Cited by 22 · see citing works
Monoterpenes as a perspective for the treatment of seizures: A Systematic Review
Pina, L. T. S., Guimarães, A. G., Santos, W. B. D. R., Oliveira, M. A., Rabelo, T. K., & Serafini, M. R. (2020) · Phytomedicine · doi:10.1016/j.phymed.2020.153422 · Cited by 21 · see citing works
Michalea, R., Stathopoulou, K., Polychronopoulos, P., Benaki, D. C., Mikros, E., & Aligiannis, N. (2018) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2018.10.008 · Cited by 19 · see citing works
Hamedi, A., Zengin, G., Aktümsek, A., Selamoğlu, Z., & Pasdaran, A. (2020) · Biointerface Research in Applied Chemistry · doi:10.33263/briac103.429454 · Cited by 19 · see citing works
Saidi, I., Baccari, W., Marchal, A., Waffo‐Téguo, P., Harrath, A. H., Mansour, L. A., & Jannet, H. B. (2020) · Industrial Crops and Products · doi:10.1016/j.indcrop.2020.112440 · Cited by 18 · see citing works
Tan, M. A., Gonzalez, S. J. B., Alejandro, G. J. D., & An, S. S. A. (2020) · 3 Biotech · doi:10.1007/s13205-020-02421-z · Cited by 17 · see citing works
Nahavandi, B. S., Yaghmaei, P., Ahmadian, S., Ghobeh, M., & Ebrahim‐Habibi, A. (2020) · Journal of Diabetes & Metabolic Disorders · doi:10.1007/s40200-020-00658-2 · Cited by 17 · see citing works
The Role of Supplementation with Natural Compounds in Post-Stroke Patients
Cichoń, N., Saluk, J., Miller, E. D., Gorniak, L., Redlicka, J., Niwald, M., & Bijak, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22157893 · Cited by 16 · see citing works
Waszkiewicz, M., Sokół‐Łętowska, A., Pałczyńska, A., & Kucharska, A. Z. (2023) · Foods · doi:10.3390/foods12193667 · Cited by 14 · see citing works
Bai, G., Chen, B., Xiao, X., Li, Y., Liu, X., Zhao, D., Zhang, L., & Zhao, D. (2022) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2022.11642 · Cited by 13 · see citing works
Chandel, P., Thapa, K., Kanojia, N., Rani, L., Singh, T. G., & Rohilla, P. (2024) · Neuroscience · doi:10.1016/j.neuroscience.2024.05.002 · Cited by 12 · see citing works
Michalska-Ciechanowska, A., Brzezowska, J., Nowicka, P., Tkacz, K., Turkiewicz, I. P., Hendrysiak, A., Oszmiański, J., & Andlauer, W. (2024) · Molecules · doi:10.3390/molecules29153586 · Cited by 12 · see citing works
Effect of Abiotic Stress on Terpene Biosynthesis in Plants
Sinha, D., Abid, R., Chakraborty, W., Rashid, M., Gupta, L. K., Khan, B., Datta, P. N., Noor, S., Pomila, Ghazanfar, S., et al. (2024) · doi:10.1002/9781394186457.ch16 · Cited by 10 · see citing works
Hadipour, E., Shahangian, S. S., & Mashayekhi, F. (2024) · Caspian Journal of Neurological Sciences · doi:10.32598/cjns.10.36.460.1 · Cited by 9 · see citing works
Antiangiogenic Activity of Compounds Isolated from Anarrhinum pedatum
Beladjila, K. A., Berrehal, D., Kabouche, Z., Germanò, M. P., D’Angelo, V., Tommasi, N. D., D’Andrea, F., Braca, A., & Leo, M. D. (2019) · Journal of Natural Products · doi:10.1021/acs.jnatprod.8b00893 · Cited by 9 · see citing works
Terzo, S., Amato, A., Calvi, P., Giardina, M., Nuzzo, D., Picone, P., Piccionello, A. P., Amata, S., Giardina, I. C., Massaro, A. S., et al. (2024) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-23-02039 · Cited by 8 · see citing works
Modification of iridoids in focus: Bridging structural complexity with biological innovation
Bai, M., Xiang, H., Ding, K., Wei, S., Wang, X., Pan, X.-G., Yin, W., Zhang, W., He, J., & Xu, J. (2025) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2025.108519 · Cited by 6 · see citing works
Barman, M., & Mishra, P. (2025) · Journal of Food Science and Technology · doi:10.1007/s13197-025-06351-7 · Cited by 3 · see citing works
Mitochondria as a target for monoterpenes
Luiz, R. C., & Cecchini, A. L. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-821562-3.00051-4 · Cited by 3 · see citing works
Chromosome-level genome assembly of Cornus officinalis reveals the evolution of loganin biosynthesis
Zhang, X., Xie, J., Wu, J., Zhang, H., Jin, Z., Liu, Q., & Zhang, D. (2025) · Horticulture Research · doi:10.1093/hr/uhaf259 · Cited by 2 · see citing works
Yang, G., Li, J., Guo, J., Liu, Y., Yan, J., Huang, H., Liu, J., Peng, C., Gan, M., & Shu, J. (2025) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2025.109098 · Cited by 2 · see citing works
Stem Cells and Natural Agents in the Management of Neurodegenerative Diseases: A New Approach
Brockmueller, A., Mahmoudi, N., Moaveni, A. K., Mueller, A., Kajbafzadeh, A. M., Shakibaei, M., & Zolbin, M. M. (2022) · Neurochemical Research · doi:10.1007/s11064-022-03746-2 · Cited by 2 · see citing works
Singh, B., Singh, L., Belwal, T., BHATT, I. D., & Kandpal, N. D. (2026) · Process Safety and Environmental Protection · doi:10.1016/j.psep.2026.109336 · Cited by 1 · see citing works
Borges, J. M. P., de Jesus, L. B., Souza, C. D. S., da Silva, V. D. A., Costa, S. L., Costa, M. D. F. D., & El-Bachá, R. D. S. (2022) · Neurotoxicity Research · doi:10.1007/s12640-022-00528-0 · Cited by 1 · see citing works
Iridoids Analysis by Different Analytical Techniques and its Role as Pharmacologic Agents: A Review
Taleuzzaman, M., Verma, R., Arshad, M. F., Grover, P., Kaur, J., Gandhi, N., & Das, V. (2021) · Current Bioactive Compounds · doi:10.2174/1573407218666211231122928
Structural Diversity and Sources of Drugs: From Nature to Synthetic and Recombinant DNA Technology
(2023) · Royal Society of Chemistry eBooks · doi:10.1039/9781839168086-00397
Composition and Functional Properties of Cardamom Seeds
Tan, C. X., Tan, S. S., & Tan, S. T. (2023) · Springer eBooks · doi:10.1007/978-3-031-35426-7_7
Neuroprotection induced by salvianolic acids
Habtemariam, S. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-23763-8.00052-x
Mandave, P. C., Bhawe, K. M., Deshpande, M., Das, J. K., & Ranjekar, P. K. (2026) · Phytomedicine Plus · doi:10.1016/j.phyplu.2026.101015
Shakir, S. A., Tan, J. K., & Chin, K. (2026) · Pharmaceuticals · doi:10.3390/ph19091407
Moreira, L. D. C., Crispim, G. S., de Souza, F. G., da Silva, D. R., Vieira, G. J. D. S. G., Lucena, S. R. B., Navarro, D. M. D. A. F., & Núñez, C. V. (2026) · Frontiers in Natural Products · doi:10.3389/fntpr.2026.1913240
- Authors
- Habtemariam, S.
- Affiliations
- University of Greenwich (GB)
- Corresponding author
- Habtemariam, Solomon
- ORCID
- Habtemariam, Solomon
- Venue
- Molecules
- Publisher
- MDPI AG
- Published
- 2018-01-07
- Volume
- 23
- Issue
- 1
- Pages
- 117
- ISSN
- 1420-3049 (ISSN-L)
- PMC
- PMC6017424
- OpenAlex
- W2782983616
- Cited by
- 55
- References
- 180
- Citations by year
- 2026: 4 · 2025: 4 · 2024: 6 · 2023: 4 · 2022: 6 · 2021: 6 · 2020: 10 · 2019: 9 · 2018: 6
- FWCI
- 1.02
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Molecules (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Greenwich Academic Literature Archive (University of Greenwich) (acceptedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Complementary and alternative medicine › Medicinal Plants and Neuroprotection
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Phytochemistry and Biological Activities
- Keywords
- iridoids, monoterpenes, Alzheimer's disease, natural products, tau phosphorylation, amyloid-beta aggregation, amyloid-beta clearance, antioxidant activity, anti-inflammatory activity, drug-likeness, Alzheimer's disease therapeutics
- MeSH terms
- Alzheimer Disease, Animals, Brain, Humans, Amyloid beta-Peptides, Neuroprotective Agents, Monoterpenes, Iridoids
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