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Journal articles on the topic 'Antiamyloidogenic'

Author: Grafiati

Published: 9 March 2023

Last updated: 31 July 2025

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1

Benseny-Cases, Núria, Oxana Klementieva, and Josep Cladera. "Dendrimers antiamyloidogenic potential in neurodegenerative diseases." New J. Chem. 36, no. 2 (2012): 211–16. http://dx.doi.org/10.1039/c1nj20469f.

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2

Chauhan, Ved, Lina Ji, and Abha Chauhan. "P1-442: Antiamyloidogenic properties of gelsolin." Alzheimer's & Dementia 4 (July 2008): T349. http://dx.doi.org/10.1016/j.jalz.2008.05.1024.

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3

Bermejo-Bescós, Paloma, Sagrario Martín-Aragón, Karim L. Jiménez-Aliaga, et al. "In vitro antiamyloidogenic properties of 1,4-naphthoquinones." Biochemical and Biophysical Research Communications 400, no. 1 (2010): 169–74. http://dx.doi.org/10.1016/j.bbrc.2010.08.038.

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4

Yu, Kun-Hua, and Cheng-I. Lee. "Quercetin Disaggregates Prion Fibrils and Decreases Fibril-Induced Cytotoxicity and Oxidative Stress." Pharmaceutics 12, no. 11 (2020): 1081. http://dx.doi.org/10.3390/pharmaceutics12111081.

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Transmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative diseases caused by misfolding and aggregation of prion protein (PrP). Previous studies have demonstrated that quercetin can disaggregate some amyloid fibrils, such as amyloid β peptide (Aβ) and α-synuclein. However, the disaggregating ability is unclear in PrP fibrils. In this study, we examined the amyloid fibril-disaggregating activity of quercetin on mouse prion protein (moPrP) and characterized quercetin-bound moPrP fibrils by imaging, proteinase resistance, hemolysis assay, cell viability, and cellular oxidative

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5

Khaengkhan, Parinda, Yuki Nishikaze, Tetsuhiro Niidome, et al. "Identification of an antiamyloidogenic substance from mulberry leaves." NeuroReport 20, no. 13 (2009): 1214–18. http://dx.doi.org/10.1097/wnr.0b013e32832fa645.

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6

Benseny-Cases, Nuria, Oxana Klementieva, and Josep Cladera. "ChemInform Abstract: Dendrimers Antiamyloidogenic Potential in Neurodegenerative Diseases." ChemInform 43, no. 22 (2012): no. http://dx.doi.org/10.1002/chin.201222233.

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7

Pandini, Giuseppe, Vincenza Pace, Agata Copani, Sebastiano Squatrito, Danilo Milardi, and Riccardo Vigneri. "Insulin Has Multiple Antiamyloidogenic Effects on Human Neuronal Cells." Endocrinology 154, no. 1 (2013): 375–87. http://dx.doi.org/10.1210/en.2012-1661.

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Alzheimer’s disease is increased in diabetic patients. A defective insulin activity on the brain has been hypothesized to contribute to the neuronal cell dysregulation leading to AD, but the mechanism is not clear. We analyzed the effect of insulin on several molecular steps of amyloid precursor protein (APP) processing and β-amyloid (Aβ) intracellular accumulation in a panel of human neuronal cells and in human embryonic kidney 293 cells overexpressing APP-695. The data indicate that insulin, via its own receptor and the phosphatidylinositol-3-kinase/AKT pathway, influences APP phosphorylatio

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8

Fortin, Jessica S., and Marie-Odile Benoit-Biancamano. "Inhibition of islet amyloid polypeptide aggregation and associated cytotoxicity by nonsteroidal anti-inflammatory drugs." Canadian Journal of Physiology and Pharmacology 94, no. 1 (2016): 35–48. http://dx.doi.org/10.1139/cjpp-2015-0117.

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Nonsteroidal anti-inflammatory drugs (NSAIDs) constitute an important pharmacotherapeutic class that, over the past decade, have expanded in application to a panoply of medical conditions. They have been tested for neurodegenerative diseases such as Alzheimer’s to reduce inflammation and also in the attempt to abrogate amyloid deposition. However, the use of NSAIDs as aggregation inhibitors has not been extensively studied in pancreatic amyloid deposition. Pancreatic amyloidosis involves the misfolding of islet amyloid polypeptide (IAPP) and contributes to the progression of type-2 diabetes in

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9

Chemerovski-Glikman, Marina, Michal Richman та Shai Rahimipour. "Structure-based study of antiamyloidogenic cyclic d,l-α-peptides". Tetrahedron 70, № 42 (2014): 7639–44. http://dx.doi.org/10.1016/j.tet.2014.07.097.

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10

Zhao, Zijian, Ling Zhu, Haiyun Li та ін. "Antiamyloidogenic Activity of Aβ42-Binding Peptoid in Modulating Amyloid Oligomerization". Small 13, № 1 (2016): 1602857. http://dx.doi.org/10.1002/smll.201602857.

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11

Mueller-Steiner, Sarah, Yungui Zhou, Hideaki Arai, et al. "Antiamyloidogenic and Neuroprotective Functions of Cathepsin B: Implications for Alzheimer's Disease." Neuron 51, no. 6 (2006): 703–14. http://dx.doi.org/10.1016/j.neuron.2006.07.027.

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12

ONO, K., Y. YOSHIIKE, A. TAKASHIMA, K. HASEGAWA, H. NAIKI, and M. YAMADA. "Vitamin A exhibits potent antiamyloidogenic and fibril-destabilizing effects in vitro." Experimental Neurology 189, no. 2 (2004): 380–92. http://dx.doi.org/10.1016/j.expneurol.2004.05.035.

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13

NAIKI, Hironobu, Kazuhiro HASEGAWA, Kenjiro ONO, and Masahito YAMADA. "A Search for Antiamyloidogenic Compounds Based on a Nucleation-Dependent Polymerization Model." YAKUGAKU ZASSHI 130, no. 4 (2010): 503–9. http://dx.doi.org/10.1248/yakushi.130.503.

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14

Colas, Julien, Natacha Chessel, Allaeddine Ouared та ін. "Neuroprotection against Amyloid-β-Induced DNA Double-Strand Breaks Is Mediated by Multiple Retinoic Acid-Dependent Pathways". Neural Plasticity 2020 (20 березня 2020): 1–14. http://dx.doi.org/10.1155/2020/9369815.

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In this study, we have investigated the role of all-trans-retinoic acid (RA) as a neuroprotective agent against Aβ1-42-induced DNA double-strand breaks (DSBs) in neuronal SH-SY5Y and astrocytic DI TNC1 cell lines and in murine brain tissues, by single-cell gel electrophoresis. We showed that RA does not only repair Aβ1-42-induced DSBs, as already known, but also prevents their occurrence. This effect is independent of that of other antioxidants studied, such as vitamin C, and appears to be mediated, at least in part, by changes in expression, not of the RARα, but of the PPARβ/δ and of antiamyl

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15

Kim, Ju Eun, and Jae Yoon Leem. "Acetylcholinesterase Inhibitory Activity and Antiamyloidogenic Effect of Cercis chinensis Bunge Seed Ethanolic Extract." Korean Journal of Medicinal Crop Science 29, no. 5 (2021): 337–44. http://dx.doi.org/10.7783/kjmcs.2021.29.5.337.

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16

Siposova, Katarina, Veronika Huntosova, Yulia Shlapa, et al. "Advances in the Study of Cerium Oxide Nanoparticles: New Insights into Antiamyloidogenic Activity." ACS Applied Bio Materials 2, no. 5 (2019): 1884–96. http://dx.doi.org/10.1021/acsabm.8b00816.

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17

Gupta, Veer Bala, S. S. Indi, and K. S. J. Rao. "Garlic extract exhibits antiamyloidogenic activity on amyloid-beta fibrillogenesis: relevance to Alzheimer's disease." Phytotherapy Research 23, no. 1 (2009): 111–15. http://dx.doi.org/10.1002/ptr.2574.

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18

Pérez-Hernández, Jesús, Víctor Javier Zaldívar-Machorro, David Villanueva-Porras, Elisa Vega-Ávila, and Anahí Chavarría. "A Potential Alternative against Neurodegenerative Diseases: Phytodrugs." Oxidative Medicine and Cellular Longevity 2016 (2016): 1–19. http://dx.doi.org/10.1155/2016/8378613.

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Neurodegenerative diseases (ND) primarily affect the neurons in the human brain secondary to oxidative stress and neuroinflammation. ND are more common and have a disproportionate impact on countries with longer life expectancies and represent the fourth highest source of overall disease burden in the high-income countries. A large majority of the medicinal plant compounds, such as polyphenols, alkaloids, and terpenes, have therapeutic properties. Polyphenols are the most common active compounds in herbs and vegetables consumed by man. The biological bioactivity of polyphenols against neurodeg

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19

Ozawa, Daisaku, Ryo Nomura, P. Patrizia Mangione, et al. "Antiamyloidogenic and proamyloidogenic chaperone effects of C-reactive protein and serum amyloid P component." Amyloid 24, sup1 (2017): 28–29. http://dx.doi.org/10.1080/13506129.2017.1295943.

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20

Bhatia, Nidhi K., Priya Modi, Shilpa Sharma, and Shashank Deep. "Quercetin and Baicalein Act as Potent Antiamyloidogenic and Fibril Destabilizing Agents for SOD1 Fibrils." ACS Chemical Neuroscience 11, no. 8 (2020): 1129–38. http://dx.doi.org/10.1021/acschemneuro.9b00677.

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21

Zga, N., Y. Papastamoulis, A. Toribio, et al. "Preparative purification of antiamyloidogenic stilbenoids from Vitis vinifera (Chardonnay) stems by centrifugal partition chromatography." Journal of Chromatography B 877, no. 10 (2009): 1000–1004. http://dx.doi.org/10.1016/j.jchromb.2009.02.026.

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22

Das, Sucharita, Suchismita Datta, Agamani Ghosal, Nibedita Ray Chaudhuri, Geetanjali Sundaram, and Soumalee Basu. "Screening of BACE1 inhibitors with antiamyloidogenic activity: A study of flavonoids and flavonoid derivatives." Neuroscience Letters 792 (January 2023): 136965. http://dx.doi.org/10.1016/j.neulet.2022.136965.

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23

Lee, Young-Jung, Dong-Young Choi, Yeo-Pyo Yun, et al. "Ethanol Extract ofMagnolia officinalisPrevents Lipopolysaccharide-Induced Memory Deficiency via Its Antineuroinflammatory and Antiamyloidogenic Effects." Phytotherapy Research 27, no. 3 (2012): 438–47. http://dx.doi.org/10.1002/ptr.4740.

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24

Naiki, Hironobu, Kazuhiro Hasegawa, Kenjiro Ono, and Masahito Yamada. "ChemInform Abstract: A Search for Antiamyloidogenic Compounds Based on a Nucleation-Dependent Polymerization Model." ChemInform 41, no. 32 (2010): no. http://dx.doi.org/10.1002/chin.201032277.

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25

Kouakou, Hilaire Tanoh, Laurent Kouakou Kouakou, Alain Decendit, et al. "Preparative Purification of Delphinidin 3-0-sambubioside from Roselle (Hibiscus sabdariffa L.) Petals by fast Centrifugation Partition Chromatography." JOURNAL OF ADVANCES IN CHEMISTRY 6, no. 2 (2010): 999–1004. http://dx.doi.org/10.24297/jac.v6i2.2628.

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Delphinidin 3-0-sambubioside, a Hibiscus anthocyanin, was isolated from MeOH/TFA dried flower of H. sabdariffa. Its purification on preparative scale was obtained by centrifugal partition chromatography (CPC) using the ternary biphasic solvent systems composed of ethyl acetate/1-butanol/water, acidified by 0.1% of TFA. Stationary phase was ethyl acetate/1-butanol/water (5:5:90; v/v). We tested 4 mobile phases and found that the system acetate/1-butanol/water (40:46:14; v/v) was the best to separate anthocyanin mentioned above. This support-free liquid-liquid chromatographic procedure made it p

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26

Pradhan, Nibedita, Koushik Debnath, Suman Mandal, Nihar R. Jana, and Nikhil R. Jana. "Antiamyloidogenic Chemical/Biochemical-Based Designed Nanoparticle as Artificial Chaperone for Efficient Inhibition of Protein Aggregation." Biomacromolecules 19, no. 6 (2018): 1721–31. http://dx.doi.org/10.1021/acs.biomac.8b00671.

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27

Pappolla, M. A., Y. J. Chyan, B. Poeggeler, et al. "An assessment of the antioxidant and the antiamyloidogenic properties of melatonin: implications for Alzheimer's disease." Journal of Neural Transmission 107, no. 2 (2000): 203–31. http://dx.doi.org/10.1007/s007020050018.

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28

Bustos, Victor, Maria V. Pulina, Ashley Bispo та ін. "Phosphorylated Presenilin 1 decreases β-amyloid by facilitating autophagosome–lysosome fusion". Proceedings of the National Academy of Sciences 114, № 27 (2017): 7148–53. http://dx.doi.org/10.1073/pnas.1705240114.

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Presenilin 1 (PS1), the catalytic subunit of the γ-secretase complex, cleaves βCTF to produce Aβ. We have shown that PS1 regulates Aβ levels by a unique bifunctional mechanism. In addition to its known role as the catalytic subunit of the γ-secretase complex, selective phosphorylation of PS1 on Ser367 decreases Aβ levels by increasing βCTF degradation through autophagy. Here, we report the molecular mechanism by which PS1 modulates βCTF degradation. We show that PS1 phosphorylated at Ser367, but not nonphosphorylated PS1, interacts with Annexin A2, which, in turn, interacts with the lysosomal

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29

Davinelli, Sergio, Nadia Sapere, Davide Zella, Renata Bracale, Mariano Intrieri, and Giovanni Scapagnini. "Pleiotropic Protective Effects of Phytochemicals in Alzheimer's Disease." Oxidative Medicine and Cellular Longevity 2012 (2012): 1–11. http://dx.doi.org/10.1155/2012/386527.

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Alzheimer’s disease (AD) is a severe chronic neurodegenerative disorder of the brain characterised by progressive impairment in memory and cognition. In the past years an intense research has aimed at dissecting the molecular events of AD. However, there is not an exhaustive knowledge about AD pathogenesis and a limited number of therapeutic options are available to treat this neurodegenerative disease. Consequently, considering the heterogeneity of AD, therapeutic agents acting on multiple levels of the pathology are needed. Recent findings suggest that phytochemicals compounds with neuroprot

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30

Pasinetti, Giulio Maria. "Cyclooxygenase as a Target for the Antiamyloidogenic Activities of Nonsteroidal Anti-Inflammatory Drugs in Alzheimer’s Disease." Neurosignals 11, no. 5 (2002): 293–97. http://dx.doi.org/10.1159/000067428.

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31

Richman, Michal, Sarah Wilk, Marina Chemerovski та ін. "In Vitro and Mechanistic Studies of an Antiamyloidogenic Self-Assembled Cyclic d,l-α-Peptide Architecture". Journal of the American Chemical Society 135, № 9 (2013): 3474–84. http://dx.doi.org/10.1021/ja310064v.

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32

Purgatorio, Rosa, Nicola Gambacorta, Marco Catto, et al. "Pharmacophore Modeling and 3D-QSAR Study of Indole and Isatin Derivatives as Antiamyloidogenic Agents Targeting Alzheimer’s Disease." Molecules 25, no. 23 (2020): 5773. http://dx.doi.org/10.3390/molecules25235773.

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Thirty-six novel indole-containing compounds, mainly 3-(2-phenylhydrazono) isatins and structurally related 1H-indole-3-carbaldehyde derivatives, were synthesized and assayed as inhibitors of beta amyloid (Aβ) aggregation, a hallmark of pathophysiology of Alzheimer’s disease. The newly synthesized molecules spanned their IC50 values from sub- to two-digit micromolar range, bearing further information into structure-activity relationships. Some of the new compounds showed interesting multitarget activity, by inhibiting monoamine oxidases A and B. A cell-based assay in tau overexpressing bacteri

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33

Hyung, S. J., A. S. DeToma, J. R. Brender, et al. "Insights into antiamyloidogenic properties of the green tea extract (-)-epigallocatechin-3-gallate toward metal-associated amyloid- species." Proceedings of the National Academy of Sciences 110, no. 10 (2013): 3743–48. http://dx.doi.org/10.1073/pnas.1220326110.

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34

Zhang, Qian, Jing Liu, Xiaoyu Hu, Wei Wang та Zhi Yuan. "In Vitro Studies on Accelerating the Degradation and Clearance of Amyloid-β Fibrils by an Antiamyloidogenic Peptide". ACS Macro Letters 4, № 4 (2015): 339–42. http://dx.doi.org/10.1021/acsmacrolett.5b00033.

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35

Taghavi, F., M. Habibi-Rezaei, M. Bohlooli, et al. "Antiamyloidogenic Effects of Ellagic Acid on Human Serum Albumin Fibril Formation Induced by Potassium Sorbate and Glucose." Journal of Molecular Recognition 29, no. 12 (2016): 611–18. http://dx.doi.org/10.1002/jmr.2560.

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36

Torricelli, C., E. Capurro, A. Santucci, et al. "Multiple plasma proteins control atrial natriuretic peptide (ANP) aggregation." Journal of Molecular Endocrinology 33, no. 2 (2004): 335–41. http://dx.doi.org/10.1677/jme.1.01530.

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We have recently demonstrated that human α-atrial natriuretic peptide (α-hANP), an amyloidogenic peptide responsible for isolated atrial amyloidosis, binds to a dimeric form of apo A-I belonging to small high-density lipoproteins (HDL). This binding phenomenon is considered a protective mechanism since it inhibits or strongly reduces the ANP aggregation process. The observation that plasma exhibits at least four times greater amyloid inhibitory activity than HDL prompted us to determine whether small HDL are the only ANP plasma-binding factors. After incubation of whole plasma with labelled AN

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37

Caillon, Lucie, Anais R. F. Hoffmann, Alexandra Botz, and Lucie Khemtemourian. "Molecular Structure, Membrane Interactions, and Toxicity of the Islet Amyloid Polypeptide in Type 2 Diabetes Mellitus." Journal of Diabetes Research 2016 (2016): 1–13. http://dx.doi.org/10.1155/2016/5639875.

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Human islet amyloid polypeptide (hIAPP) is the major component of the amyloid deposits found in the pancreatic islets of patients with type 2 diabetes mellitus (T2DM). Mature hIAPP, a 37-aa peptide, is natively unfolded in its monomeric state but forms islet amyloid in T2DM. In common with other misfolded and aggregated proteins, amyloid formation involves aggregation of monomers of hIAPP into oligomers, fibrils, and ultimately mature amyloid deposits. hIAPP is coproduced and stored with insulin by the pancreatic isletβ-cells and is released in response to the stimuli that lead to insulin secr

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38

Young, Sherri. "A Systematic Review of Antiamyloidogenic and Metal-Chelating Peptoids: Two Structural Motifs for the Treatment of Alzheimer’s Disease." Molecules 23, no. 2 (2018): 296. http://dx.doi.org/10.3390/molecules23020296.

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39

Koshti, Bharti, Vivekshinh Kshtriya, Corinne Nardin, and Nidhi Gour. "Chemical Perspective of the Mechanism of Action of Antiamyloidogenic Compounds Using a Minimalistic Peptide as a Reductionist Model." ACS Chemical Neuroscience 12, no. 15 (2021): 2851–64. http://dx.doi.org/10.1021/acschemneuro.1c00221.

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40

Jiménez-Aliaga, Karim, Paloma Bermejo-Bescós, Juana Benedí, and Sagrario Martín-Aragón. "Quercetin and rutin exhibit antiamyloidogenic and fibril-disaggregating effects in vitro and potent antioxidant activity in APPswe cells." Life Sciences 89, no. 25-26 (2011): 939–45. http://dx.doi.org/10.1016/j.lfs.2011.09.023.

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41

Pichla, Monika, Grzegorz Bartosz, and Izabela Sadowska-Bartosz. "The Antiaggregative and Antiamyloidogenic Properties of Nanoparticles: A Promising Tool for the Treatment and Diagnostics of Neurodegenerative Diseases." Oxidative Medicine and Cellular Longevity 2020 (October 13, 2020): 1–11. http://dx.doi.org/10.1155/2020/3534570.

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Due to the progressive aging of the society, the prevalence and socioeconomic burden of neurodegenerative diseases are predicted to rise. The most common neurodegenerative disorders nowadays, such as Parkinson’s disease, Alzheimer’s disease, and amyotrophic lateral sclerosis, can be classified as proteinopathies. They can be either synucleinopathies, amyloidopathies, tauopathies, or TDP-43-related proteinopathies; thus, nanoparticles with a potential ability to inhibit pathological protein aggregation and/or degrade already existing aggregates can be a promising approach in the treatment of ne

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42

Kim, Jungsu, Adam E. M. Eltorai, Hong Jiang та ін. "Anti-apoE immunotherapy inhibits amyloid accumulation in a transgenic mouse model of Aβ amyloidosis". Journal of Experimental Medicine 209, № 12 (2012): 2149–56. http://dx.doi.org/10.1084/jem.20121274.

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The apolipoprotein E (APOE) ε4 allele is the strongest genetic risk factor for Alzheimer’s disease (AD). The influence of apoE on amyloid β (Aβ) accumulation may be the major mechanism by which apoE affects AD. ApoE interacts with Aβ and facilitates Aβ fibrillogenesis in vitro. In addition, apoE is one of the protein components in plaques. We hypothesized that certain anti-apoE antibodies, similar to certain anti-Aβ antibodies, may have antiamyloidogenic effects by binding to apoE in the plaques and activating microglia-mediated amyloid clearance. To test this hypothesis, we developed several

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43

Azmi, Nur Hanisah, Maznah Ismail, Norsharina Ismail, Mustapha Umar Imam, Noorjahan Banu Mohammed Alitheen та Maizaton Atmadini Abdullah. "Germinated Brown Rice Alters Aβ(1-42) Aggregation and Modulates Alzheimer’s Disease-Related Genes in Differentiated Human SH-SY5Y Cells". Evidence-Based Complementary and Alternative Medicine 2015 (2015): 1–12. http://dx.doi.org/10.1155/2015/153684.

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The pathogenesis of Alzheimer’s disease involves complex etiological factors, of which the deposition of beta-amyloid (Aβ) protein and oxidative stress have been strongly implicated. We explored the effects of H2O2, which is a precursor for highly reactive hydroxyl radicals, on neurotoxicity and genes related to AD on neuronal cells. Candidate bioactive compounds responsible for the effects were quantified using HPLC-DAD. Additionally, the effects of germinated brown rice (GBR) on the morphology of Aβ(1-42) were assessed by Transmission Electron Microscopy and its regulatory effects on gene ex

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44

Venkatesan, Ramu, Eunhee Ji, and Sun Yeou Kim. "Phytochemicals That Regulate Neurodegenerative Disease by Targeting Neurotrophins: A Comprehensive Review." BioMed Research International 2015 (2015): 1–22. http://dx.doi.org/10.1155/2015/814068.

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Alzheimer’s disease (AD), characterized by progressive dementia and deterioration of cognitive function, is an unsolved social and medical problem. Age, nutrition, and toxins are the most common causes of AD. However, currently no credible treatment is available for AD. Traditional herbs and phytochemicals may delay its onset and slow its progression and also allow recovery by targeting multiple pathological causes by antioxidative, anti-inflammatory, and antiamyloidogenic properties. They also regulate mitochondrial stress, apoptotic factors, free radical scavenging system, and neurotrophic f

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45

Uddin, Md Sahab, Abdullah Al Mamun, Md Motiar Rahman, et al. "Natural Products for Neurodegeneration: Regulating Neurotrophic Signals." Oxidative Medicine and Cellular Longevity 2021 (June 21, 2021): 1–17. http://dx.doi.org/10.1155/2021/8820406.

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Neurodegenerative disorders (NDs) are heterogeneous groups of ailments typically characterized by progressive damage of the nervous system. Several drugs are used to treat NDs but they have only symptomatic benefits with various side effects. Numerous researches have been performed to prove the advantages of phytochemicals for the treatment of NDs. Furthermore, phytochemicals such as polyphenols might play a pivotal role in rescue from neurodegeneration due to their various effects as anti-inflammatory, antioxidative, and antiamyloidogenic agents by controlling apoptotic factors, neurotrophic

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46

Naoi, Makoto, Masayo Shamoto-Nagai, and Wakako Maruyama. "Neuroprotection of multifunctional phytochemicals as novel therapeutic strategy for neurodegenerative disorders: antiapoptotic and antiamyloidogenic activities by modulation of cellular signal pathways." Future Neurology 14, no. 1 (2019): FNL9. http://dx.doi.org/10.2217/fnl-2018-0028.

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47

Kashyap, Priya, Heera Ram, Sunil Dutt Shukla, and Suresh Kumar. "Scopoletin: Antiamyloidogenic, Anticholinesterase, and Neuroprotective Potential of a Natural Compound Present in Argyreia speciosa Roots by In Vitro and In Silico Study." Neuroscience Insights 15 (January 2020): 263310552093769. http://dx.doi.org/10.1177/2633105520937693.

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Alzheimer’s disease (AD) is characterized by depositions of amyloid β (Aβ) peptides aggregates resulting in plaques formation in the central nervous system (CNS). This study evaluates the disease-modifying potential of scopoletin against multiple factors associated with AD such as cholinesterase enzymes, Aβ peptides, and neuroprotective properties against Aβ- and H2O2-induced cytotoxicity under in vitro conditions. Scopoletin was identified and quantified using UPLC-QTOF (ultra-high performance liquid chromatography-quadrupole time-of-flight) and high-performance liquid chromatography (HPLC),

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48

Chakraborty, Biswajit, Nobendu Mukerjee, Swastika Maitra, et al. "Therapeutic Potential of Different Natural Products for the Treatment of Alzheimer’s Disease." Oxidative Medicine and Cellular Longevity 2022 (July 22, 2022): 1–18. http://dx.doi.org/10.1155/2022/6873874.

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A high incidence of dementia (60–80%) and a high rate of memory loss are two of the most common symptoms of Alzheimer’s disease (AD), which affects the elderly. Researchers have recommended that traditional Chinese medicine (TCM) and Indian medicines can be used to prevent and cure AD. Several studies have linked neuroinflammation linked to amyloid-β (Aβ) deposition in the brain to the pathophysiology of neurodegenerative disorders. As a result, more research is needed to determine the role of inflammation in neurodegeneration. Increased microglial activation, cytokine production, reactive oxy

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49

Suganthy, Natarajan, Vijayan Sri Ramkumar, Arivalagan Pugazhendhi, Giovanni Benelli, and Govindaraju Archunan. "Biogenic synthesis of gold nanoparticles from Terminalia arjuna bark extract: assessment of safety aspects and neuroprotective potential via antioxidant, anticholinesterase, and antiamyloidogenic effects." Environmental Science and Pollution Research 25, no. 11 (2017): 10418–33. http://dx.doi.org/10.1007/s11356-017-9789-4.

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Forloni, Gianluigi. "Alzheimer’s disease: from basic science to precision medicine approach." BMJ Neurology Open 2, no. 2 (2020): e000079. http://dx.doi.org/10.1136/bmjno-2020-000079.

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Abstract:

Alzheimer’s disease (AD) is the most common form of dementia in the elderly. Together with cerebral amyloid accumulation, several factors contribute to AD pathology including vascular alterations, systemic inflammation, genetic/epigenetic status and mitochondrial dysfunction. Much is now being devoted to neuroinflammation. However, anti-inflammatory drugs as numerous other therapies, mainly targeted on β-amyloid, have failed to show efficacious effects in AD. Timing, proper selection of patients, and the need for a multitarget approach appear to be the main weak points of current therapeutic e

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