Exploring the inhibitory effects of liquiritigenin against tau fibrillation and related neurotoxicity as a model of preventive care in Alzheimer’s disease

The projected effect of risk factor reduction on Alzheimer's disease prevalence

Barnes, D. E., & Yaffe, K. S. (2011) · The Lancet Neurology · doi:10.1016/s1474-4422(11)70072-2 · Cited by 2,668 · see citing works

Unfolding the role of protein misfolding in neurodegenerative diseases

Soto, C. (2003) · Nature Reviews Neuroscience · doi:10.1038/nrn1007 · Cited by 1,506 · see citing works

Molecular Structure of β-Amyloid Fibrils in Alzheimer’s Disease Brain Tissue

Lu, J., Qiang, W., Yau, W., Schwieters, C. D., Meredith, S. C., & Tycko, R. (2013) · Cell · doi:10.1016/j.cell.2013.08.035 · Cited by 1,087 · see citing works

Inhibition of Amyloid Fibril Formation by Polyphenols: Structural Similarity and Aromatic Interactions as a Common Inhibition Mechanism

Porat, Y., Abramowitz, A., & Gazit, E. (2005) · Chemical Biology & Drug Design · doi:10.1111/j.1747-0285.2005.00318.x · Cited by 994 · see citing works

Reconsideration of Amyloid Hypothesis and Tau Hypothesis in Alzheimer's Disease

Kametani, F., & Hasegawa, M. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00025 · Cited by 836 · see citing works

Mechanism of thioflavin T binding to amyloid fibrils

Khurana, R., Coleman, C., Ionescu‐Zanetti, C., Carter, S. A., Krishna, V., Grover, R. K., Roy, R., & Singh, S. S. (2005) · Journal of Structural Biology · doi:10.1016/j.jsb.2005.06.006 · Cited by 833 · see citing works

Bioavailability of bioactive food compounds: a challenging journey to bioefficacy.

Rein, M. J., Renouf, M., Cruz-Hernandez, C., Actis-Goretta, L., Thakkar, S. K., & Pinto, M. I. D. S. (2013) · British Journal of Clinical Pharmacology · doi:10.1111/j.1365-2125.2012.04425.x · Cited by 763 · see citing works

Review on Alzheimer’s Disease: Inhibition of Amyloid Beta and Tau Tangle Formation

Ashrafian, H., Zadeh, E. H., & Khan, R. H. (2021) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.11.192 · Cited by 368 · see citing works

Inhibition of protein aggregation and amyloid formation by small molecules

Doig, A. J., & Derreumaux, P. (2015) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2014.12.004 · Cited by 295 · see citing works

Development of tau aggregation inhibitors for alzheimer's disease

Bulic, B., Pickhardt, M., Schmidt, B., Mandelkow, E., Waldmann, H., & Mandelkow, E. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200802621 · Cited by 286 · see citing works

Bioavailability of Gallic Acid and Catechins from Grape Seed Polyphenol Extract is Improved by Repeated Dosing in Rats: Implications for Treatment in Alzheimer's Disease

Ferruzzi, M. G., Lobo, J., Janle, E. M., Cooper, B. R., Simon, J. E., Wu, Q., Welch, C., Ho, L., Weaver, C. M., & Pasinetti, G. M. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1135 · Cited by 250 · see citing works

Molecular mechanism of neurodegeneration induced by Alzheimer’s β-amyloid protein: channel formation and disruption of calcium homeostasis

Kawahara, M., & Kuroda, Y. (2000) · Brain Research Bulletin · doi:10.1016/s0361-9230(00)00370-1 · Cited by 221 · see citing works

Rutin inhibits β-amyloid aggregation and cytotoxicity, attenuates oxidative stress, and decreases the production of nitric oxide and proinflammatory cytokines

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

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

Amyloid cascade in Alzheimer's disease: Recent advances in medicinal chemistry

Mohamed, T., Shakeri, A., & Rao, P. P. N. (2016) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2016.02.049 · Cited by 181 · see citing works

Vitamin k3 inhibits protein aggregation: Implication in the treatment of amyloid diseases

Alam, P., Chaturvedi, S. K., Siddiqi, M. K., Rajpoot, R. K., Ajmal, M. R., Zaman, M., & Khan, R. H. (2016) · Scientific Reports · doi:10.1038/srep26759 · Cited by 177 · see citing works

Soluble tau aggregates, not large fibrils, are the toxic species that display seeding and cross‐seeding behavior

Ghag, G., Bhatt, N. N., Cantu, D. V., Guerrero‐Munoz, M. J., Ellsworth, A., Sengupta, U., & Kayed, R. (2018) · Protein Science · doi:10.1002/pro.3499 · Cited by 157 · see citing works

Optimised nano-formulation on the bioavailability of hydrophobic polyphenol, curcumin, in freely-moving rats

Tsai, Y.-M., Jan, W.-C., Chien, C.-F., Lee, W.-C., Lin, L.-C., & Tsai, T. (2011) · Food Chemistry · doi:10.1016/j.foodchem.2011.01.059 · Cited by 147 · see citing works

Quantification of Alzheimer pathology in ageing and dementia: age‐related accumulation of amyloid‐β(42) peptide in vascular dementia

Lewis, H. D., Beher, D., Cookson, N., Oakley, A. E., Piggott, M. A., Morris, C. M., Jaros, E., Perry, R., Ince, P. G., Kenny, R. A., et al. (2006) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2006.00696.x · Cited by 143 · see citing works

Amyloid‐beta ( A β1–42)‐induced paralysis in C aenorhabditis elegans is inhibited by the polyphenol quercetin through activation of protein degradation pathways

Regitz, C., Dußling, L. M., & Wenzel, U. (2014) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201400014 · Cited by 142 · see citing works

Beta Amyloid Aggregation Inhibitors: Small Molecules as Candidate Drugs for Therapy of Alzheimers Disease

Re, F., Airoldi, C., Zona, C., Masserini, M., Ferla, B. L., Quattrocchi, N., & Nicotra, F. (2010) · Current Medicinal Chemistry · doi:10.2174/092986710791959729 · Cited by 139 · see citing works

The ubiquitin proteasomal system: a potential target for the management of Alzheimer's disease

Gadhave, K., Bolshette, N. B., Ahire, A., Pardeshi, R., Thakur, K. K., Trandafir, C.-M., Istrate, A., Ahmed, S., Lahkar, M., Muresanu, D. F., et al. (2016) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.12817 · Cited by 119 · see citing works

Protonation favors aggregation of lysozyme with SDS

Khan, J. M., Chaturvedi, S. K., Rahman, S. K., Ishtikhar, M., Qadeer, A., Ahmad, E., & Khan, R. H. (2014) · Soft Matter · doi:10.1039/c3sm52435c · Cited by 115 · see citing works

The Surfactant-Induced Conformational and Activity Alterations in Rhizopus niveus Lipase

Alam, P., Rabbani, G., Badr, G., Badr, B. M., & Khan, R. H. (2014) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-014-0329-2 · Cited by 108 · see citing works

Cognitive Decline, Dementia, Alzheimer’s Disease and Presbycusis: Examination of the Possible Molecular Mechanism

Shen, Y., Ye, B., Chen, P., Wang, Q., Fan, C., Shu, Y., & Xiang, M. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00394 · Cited by 105 · see citing works

Inhibition of amyloid-β aggregation by coumarin analogs can be manipulated by functionalization of the aromatic center

Soto-Ortega, D. D., Murphy, B. P., Gonzalez‐Velasquez, F. J., Wilson, K. A., Xie, F., Wang, Q., & Moss, M. A. (2011) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2011.03.010 · Cited by 104 · see citing works

The Effect of Milk Protein on the Bioavailability of Cocoa Polyphenols

Keogh, J. B., McInerney, J. K., & Clifton, P. M. (2007) · Journal of Food Science · doi:10.1111/j.1750-3841.2007.00314.x · Cited by 104 · see citing works

Thermodynamic and conformational changes of protein toward interaction with nanoparticles: a spectroscopic overview

Zeinabad, H. A., Kachooei, E., Saboury, A. A., Kostova, I. P., Attar, F., Vaezzadeh, M., & Falahati, M. (2016) · RSC Advances · doi:10.1039/c6ra16422f · Cited by 104 · see citing works

Natural polyphenols binding to amyloid: A broad class of compounds to treat different human amyloid diseases

Ndam, V. N., Schluesener, J. K., Moundipa, P. F., & Schluesener, H. J. (2014) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201400290 · Cited by 103 · see citing works

Characterization of a partially folded intermediate of stem bromelain at low pH

Haq, S. K., Rasheedi, S., & Khan, R. H. (2002) · European Journal of Biochemistry · doi:10.1046/j.0014-2956.2002.02620.x · Cited by 98 · see citing works

Structure and Mechanism of Action of Tau Aggregation Inhibitors

Cisek, K. K., Cooper, G., Huseby, C. J., & Kuret, J. (2014) · Current Alzheimer Research · doi:10.2174/1567205011666141107150331 · Cited by 97 · see citing works

Role of aromatic amino acids in amyloid self-assembly

Stanković, I. M., Niu, S., Hall, M. B., & Zarić, S. D. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.03.064 · Cited by 94 · see citing works

Small molecule probes of protein aggregation

Young, L. M., Ashcroft, A. E., & Radford, S. E. (2017) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2017.06.008 · Cited by 93 · see citing works

Liquiritigenin attenuates high glucose-induced mesangial matrix accumulation, oxidative stress, and inflammation by suppression of the NF-κB and NLRP3 inflammasome pathways

Zhu, X., Shi, J., & Li, H. (2018) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.07.045 · Cited by 88 · see citing works

Interactions between Amyloid-β and Tau Fragments Promote Aberrant Aggregates: Implications for Amyloid Toxicity

Do, T. D., Economou, N. J., Chamas, A., Buratto, S. K., Shea, J., & Bowers, M. T. (2014) · The Journal of Physical Chemistry B · doi:10.1021/jp506258g · Cited by 81 · see citing works

Inhibition of the Self-Assembly of Aβ and of Tau by Polyphenols: Mechanistic Studies

Zheng, Q., Kebede, M. T., Kemeh, M. M., Islam, S., Lee, B., Bleck, S. D., Wurfl, L. A., & Lazo, N. D. (2019) · Molecules · doi:10.3390/molecules24122316 · Cited by 81 · see citing works

Myricetin Prevents Fibrillogenesis of Hen Egg White Lysozyme

He, J., Wang, Y., Chang, A. K., Xu, L., Wang, N., Chong, X., Li, H., Zhang, B., Jones, G. W., & Song, Y. (2014) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf5025449 · Cited by 68 · see citing works

Targeting the ensemble of heterogeneous tau oligomers in cells: A novel small molecule screening platform for tauopathies

Lo, C. H., Lim, C. K., Ding, Z., Wickramasinghe, S. P., Braun, A. R., Ashe, K. H., Rhoades, E. R., Thomas, D. D., & Sachs, J. N. (2019) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2019.06.4954 · Cited by 65 · see citing works

Identification of Small Molecule Inhibitors of Tau Aggregation by Targeting Monomeric Tau As a Potential Therapeutic Approach for Tauopathies

Pickhardt, M., Neumann, T., Schwizer, D., Callaway, K., Vendruscolo, M., Schenk, D., George‐Hyslop, P. S., Mandelkow, E., Dobson, C. M., McConlogue, L., et al. (2015) · Current Alzheimer Research · doi:10.2174/156720501209151019104951 · Cited by 63 · see citing works

The ordered assembly of tau is the gain‐of‐toxic function that causes human tauopathies

Goedert, M. (2016) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2016.09.001 · Cited by 62 · see citing works

Cerium oxide NPs mitigate the amyloid formation of α-synuclein and associated cytotoxicity

Zand, Z., Khaki, P. A., Salihi, A. B., Sharifi, M., Nanakali, N. M. Q., Al-Asady, A. A., Aziz, F. M., Shahpasand, K., Hasan, A., & Falahati, M. (2019) · International Journal of Nanomedicine · doi:10.2147/ijn.s220380 · Cited by 62 · see citing works

Mitochondria-derived reactive oxygen species mediate caspase-dependent and -independent neuronal deaths

McManus, M. J., Murphy, M. P., & Franklin, J. L. (2014) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2014.09.002 · Cited by 55 · see citing works

Inhibition of Amyloid Oligomerization into Different Supramolecular Architectures by Small Molecules: Mechanistic Insights and Design Rules

Brahmachari, S., Paul, A., Segal, D., & Gazit, E. (2017) · Future Medicinal Chemistry · doi:10.4155/fmc-2017-0026 · Cited by 52 · see citing works

Modulating disease-relevant tau oligomeric strains by small molecules

Cascio, F. L., García, S., Montalbano, M., Puangmalai, N., McAllen, S., Pace, A., Piccionello, A. P., & Kayed, R. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.014630 · Cited by 51 · see citing works

Liquiritigenin decreases tumorigenesis by inhibiting DNMT activity and increasing BRCA1 transcriptional activity in triple-negative breast cancer

Liang, F., Zhang, H., Gao, H., Cheng, D., Zhang, N., Du, J., Yue, J., Du, P., Zhao, B., & Yin, L. (2020) · Experimental Biology and Medicine · doi:10.1177/1535370220957255 · Cited by 48 · see citing works

Liquiritigenin Decreases Aβ Levels and Ameliorates Cognitive Decline by Regulating Microglia M1/M2 Transformation in AD Mice

Du, Y., Luo, M., Du, Y., Xu, M., Yao, Q., Wang, K., & He, G. (2020) · Neurotoxicity Research · doi:10.1007/s12640-020-00284-z · Cited by 47 · see citing works

Structural Determinants of Tau Aggregation Inhibitor Potency

Schafer, K. N., Cisek, K. K., Huseby, C. J., Chang, E. S., & Kuret, J. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.503474 · Cited by 43 · see citing works

Effective suppression of the modified PHF6 peptide/1N4R Tau amyloid aggregation by intact curcumin, not its degradation products: Another evidence for the pigment as preventive/therapeutic “functional food”

Bijari, N., Balalaie, S., Akbari, V., Golmohammadi, F., Moradi, S., Adibi, H., & Khodarahmi‬, R. (2018) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2018.08.175 · Cited by 43 · see citing works

Insights into the inhibitory mechanism of a resveratrol and clioquinol hybrid against Aβ42 aggregation and protofibril destabilization: A molecular dynamics simulation study

Saini, R. K., Shuaib, S., Goyal, D., & Goyal, B. (2018) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2018.1511475 · Cited by 43 · see citing works

Effects of liquiritigenin treatment on the learning and memory deficits induced by amyloid β-peptide (25–35) in rats

Liu, R. T., Zou, L. B., Fu, J. Y., & Lu, Q. J. (2010) · Behavioural Brain Research · doi:10.1016/j.bbr.2010.01.041 · Cited by 42 · see citing works

Azure C Targets and Modulates Toxic Tau Oligomers

Cascio, F. L., & Kayed, R. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.7b00501 · Cited by 40 · see citing works

α-synuclein interaction with zero-valent iron nanoparticles accelerates structural rearrangement into amyloid-susceptible structure with increased cytotoxic tendency

Gilan, S. S. T., Rayat, D. Y., Mustafa, T. A., Aziz, F. M., Shahpasand, K., Akhtari, K., Salihi, A. B., Abou‐Zied, O. K., & Falahati, M. (2019) · International Journal of Nanomedicine · doi:10.2147/ijn.s212387 · Cited by 36 · see citing works

Liquiritigenin Reduces Blood Glucose Level and Bone Adverse Effects in Hyperglycemic Adult Zebrafish

Carnovali, M., Luzi, L., Terruzzi, I. M., Banfi, G., & Mariotti, M. (2019) · Nutrients · doi:10.3390/nu11051042 · Cited by 31 · see citing works

The antidepressant drug; trazodone inhibits Tau amyloidogenesis: Prospects for prophylaxis and treatment of AD

Akbari, V., Ghobadi, S., Mohammadi, S., & Khodarahmi‬, R. (2019) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2019.108218 · Cited by 31 · see citing works

Decrease of Amyloid-β Levels by Curcumin Derivative via Modulation of Amyloid-β Protein Precursor Trafficking

Kotani, R., Urano, Y., Sugimoto, H., & Noguchi, N. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160794 · Cited by 29 · see citing works

Screening and determination for potential α‐glucosidase inhibitory constituents from Dalbergia odorifera T. Chen using ultrafiltration‐LC/ESI‐MSn

Zhao, C., Liu, Y., Cong, D., Zhang, H., Yu, J., Jiang, Y., Cui, X., & Sun, J. (2013) · Biomedical Chromatography · doi:10.1002/bmc.2970 · Cited by 28 · see citing works

Silybin as a potent inhibitor of a-synuclein aggregation and associated cytotoxicity against neuroblastoma cells induced by zinc oxide nanoparticles

Khodabandeh, A., Yakhchian, R., Hasan, A., Paray, B. A., Shahi, F., Rasti, B., Mirpour, M., Sharifi, M., Derakhshankhah, H., Akhtari, K., et al. (2020) · Journal of Molecular Liquids · doi:10.1016/j.molliq.2020.113198 · Cited by 28 · see citing works

Ortho-methylated 3-hydroxypyridines hinder hen egg-white lysozyme fibrillogenesis

Mariño, L., Pauwels, K., Casasnovas, R., Sanchís, P., Vilanova, B., Muñoz, F., Donoso, J., & Adrover, M. (2015) · Scientific Reports · doi:10.1038/srep12052 · Cited by 27 · see citing works

Binding and neurotoxicity mitigation of toxic tau oligomers by synthetic heparin like oligosaccharides

Wang, P., Cascio, F. L., Gao, J., Kayed, R., & Huang, X. (2018) · Chemical Communications · doi:10.1039/c8cc05072d · Cited by 23 · see citing works

Carbohydrate – Protein aromatic ring interactions beyond CH/π interactions: A Protein Data Bank survey and quantum chemical calculations

Stanković, I. M., Filipović, J. P. B., & Zarić, S. D. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.03.251 · Cited by 19 · see citing works

Cysteine as a potential anti-amyloidogenic agent with protective ability against amyloid induced cytotoxicity

Zaman, M., Zakariya, S. M., Nusrat, S., Chandel, T. I., Meeran, S. M., Ajmal, M. R., Alam, P., Wahiduzzaman, & Khan, R. H. (2017) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2017.07.083 · Cited by 18 · see citing works

Pharmacological characterization of liquiritigenin, a chiral flavonoid in licorice

Sayre, C., Alrushaid, S., Davies, N., & Martinez, S. (2016) · Research in Pharmaceutical Sciences · doi:10.4103/1735-5362.192484 · Cited by 17 · see citing works

Inhibition of tau aggregation and associated cytotoxicity on neuron-like cells by calycosin

Zhang, Z., Min, L., Peikui, Y., Chen, Z., Liu, Y., Junli, W., Fenlian, Y., & Zheng, Y. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.12.030 · Cited by 16 · see citing works

Chiral analytical method development of liquiritigenin with application to a pharmacokinetic study

Sayre, C. L., Hopkins, M. M., Takemoto, J. K., & Davies, N. M. (2012) · Biomedical Chromatography · doi:10.1002/bmc.2787 · Cited by 11 · see citing works

Tau Protein Aggregation in Alzheimer's Disease: Recent Advances in the Development of Novel Therapeutic Agents

Monteiro, K. L. C., Alcântara, M. G. D. S., de Aquino, T. M., & da Silva‐Júnior, E. F. (2020) · Current Pharmaceutical Design · doi:10.2174/1381612826666200414164038 · Cited by 10 · see citing works

Unlocking the Therapeutic Potential of Medicinal Plants for Alzheimer’s Disease: Preclinical to Clinical Trial Insights

Nagori, K., Nakhate, K. T., Yadav, K., Ajazuddin, & Pradhan, M. (2023) · Future Pharmacology · doi:10.3390/futurepharmacol3040053 · Cited by 61 · see citing works

Molecular Mechanisms of Inhibition of Protein Amyloid Fibril Formation: Evidence and Perspectives Based on Kinetic Models

Sedov, I. A., & Khaibrakhmanova, D. R. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232113428 · Cited by 48 · see citing works

Interaction Between Diet and Microbiota in the Pathophysiology of Alzheimer’s Disease: Focus on Polyphenols and Dietary Fibers

Ticinesi, A., Mancabelli, L., Carnevali, L., Nouvenne, A., Meschi, T., Rio, D. D., Ventura, M., Sgoifo, A., & Angelino, D. (2022) · Journal of Alzheimer s Disease · doi:10.3233/jad-215493 · Cited by 40 · see citing works

Research progress of natural products and their derivatives against Alzheimer’s disease

Liu, J., Guo, H., Quan, Z., Shen, Q., Cui, H., & Li, X. (2023) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2023.2171026 · Cited by 36 · see citing works

Liquiritigenin Inhibits Lipid Accumulation in 3T3-L1 Cells via mTOR-Mediated Regulation of the Autophagy Mechanism

Qin, H., Song, Z., Zhao, C., Yang, J., Xia, F., Wang, L., Ali, A., & Zheng, W. (2022) · Nutrients · doi:10.3390/nu14061287 · Cited by 23 · see citing works

The novel anti-fibrillary effects of volatile compounds α-asarone and β-caryophyllene on tau protein: Towards promising therapeutic agents for Alzheimer's disease

Anbaraki, A., Dindar, Z., Mousavi-Jarrahi, Z., Ghasemi, A., Moeini, Z., Evini, M., Saboury, A. A., & Seyedarabi, A. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.132401 · Cited by 13 · see citing works

Isoliquiritigenin attenuated cognitive impairment, cerebral tau phosphorylation and oxidative stress in a streptozotocin-induced mouse model of Alzheimer's disease

Tang, Z., Sha, T., Wang, Y., Xiao, Y. C., Ding, Y., Ni, R., & Qi, X. (2025) · Life Sciences · doi:10.1016/j.lfs.2025.123759 · Cited by 12 · see citing works

Sodium fusidate prevents protein aggregation of silk fibroin and offers new perspectives for human lens material disaggregation

Gasymov, O. K., Mammedzade, A. M., Bakhishova, M. J., Guliyeva, A. J., Ragona, L., & Molinari, H. (2021) · Biophysical Chemistry · doi:10.1016/j.bpc.2021.106680 · Cited by 7 · see citing works

Neuroactive Phytoconstituents of Glycyrrhiza glabra for the Treatment of Alzheimer’s Disease

Verma, M., Usman, M., & Singh, N. K. (2024) · Current Topics in Medicinal Chemistry · doi:10.2174/0115680266357793241223100307 · Cited by 7 · see citing works

Exploring the potential mechanism of Polygonatum sibiricum for Alzheimer’s disease based on network pharmacology and molecular docking: An observational study

Luo, L., Pan, Y., Chen, F., & Zhang, Z. (2024) · Medicine · doi:10.1097/md.0000000000040726 · Cited by 6 · see citing works

Hematoxylin modulates tau-RD protein fibrillization and ameliorates Alzheimer's disease-like symptoms in a yeast model

Yin, H., Han, Y.-L., Yan, X. H., & Guan, Y. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.126140 · Cited by 6 · see citing works

The volatile constituents of rose, saffron and cardamom suppress the fibrillation of tau and not HEWL through the formation of non-toxic tau oligomers

Rasoulian, M., Anbaraki, A., Mousavi-Jarrahi, Z., Ghasemi, A., Absalan, M., Motevaseli, E., Shafizadeh, M., Ahmadian, S., Saboury, A. A., & Seyedarabi, A. (2024) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2024.139177 · Cited by 5 · see citing works

Role of dietary phytopharmaceuticals across the globe to alleviate the Alzheimer’s disease: mechanism-based approach

Mishra, A. K., Mishra, A., Kamal, Y. T., Kumar, A., Singh, H., Verma, S., & Khan, G. (2025) · Phytomedicine Plus · doi:10.1016/j.phyplu.2025.100877 · Cited by 4 · see citing works

Traditional Chinese Medicines for Alzheimer's Disease: Current Knowledge, Clinical Applications, and Future Directions

Deng, Y. L., Chen, C., Li, H., Wang, T., Zhang, X., Wang, X., & Pan, G. (2025) · Current Topics in Medicinal Chemistry · doi:10.2174/0115680266347052250407110353 · Cited by 3 · see citing works

OGT Binding Peptide-Tagged Strategy Increases Protein O-GlcNAcylation Level in E. coli

Li, Y., Yang, Z., Jia, C., Chen, Y., Jiang, C., Zhong, T., Su, Y., Liang, Y., & Sun, H. Z. (2023) · Molecules · doi:10.3390/molecules28052129 · Cited by 3 · see citing works

Osthole's capacity to prevent tau aggregation, a key protein in tauopathy and Alzheimer's disease

Liu, W., Xu, H., Wang, C., Geng, G., Yang, Y., & Chen, G. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.143235 · Cited by 3 · see citing works

Neurobiotech innovative strategies targeting Alzheimer's disease through therapeutic micro and macroalgae potentials

Wagdy, M., Ibrahim, A. A., Yahia, A. M., Maher, R. M., Abo-Elwafa, A. H., Salah, A., & Heikal, Y. M. (2025) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2025.578821 · Cited by 2 · see citing works

Flavonoid-mediated modulation of Tau protein: Implications for targeted therapeutics and clinical relevance in Tau-related disorders

Hedna, R., Relave, E. T., Robin, M., Kovacic, H., & Breuzard, G. (2025) · European Journal of Medicinal Chemistry Reports · doi:10.1016/j.ejmcr.2025.100309 · Cited by 1 · see citing works

Chirality-engineered nanomaterials for biomedical applications

Huang, Z., Zhou, H., Zhang, S., Song, S., Feng, C., Ke, Z., Tang, J., & Dai, Y. (2026) · Journal of Controlled Release · doi:10.1016/j.jconrel.2026.115015 · Cited by 1 · see citing works

Exploring the potential mechanism of Polygonatum sibiricum for Alzheimer's disease based on network pharmacology and molecular dockingPreprint

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Taub, N., Kolb-Lenz, D., Hutter‐Paier, B., & Schweinzer, C. (2015) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2015.06.871

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