Green Tea Extracts EGCG and EGC Display Distinct Mechanisms in Disrupting Aβ42 Protofibril

Comparison of simple potential functions for simulating liquid water

Jorgensen, W. L., Chandrasekhar, J., Madura, J., Impey, R., & Klein, M. (1983) · The Journal of Chemical Physics · doi:10.1063/1.445869 · Cited by 38,335 · see citing works

Particle mesh Ewald: An N⋅log(N) method for Ewald sums in large systems

Darden, T., York, D., & Pedersen, L. (1993) · The Journal of Chemical Physics · doi:10.1063/1.464397 · Cited by 29,588 · see citing works

‘GROMACS: High performance molecular simulations through multi-level parallelism from laptops to supercomputers’

Abraham, M. J., Murtola, T., Schulz, R., Páll, S., Smith, J. C., Hess, B., & Lindahl, E. (2015) · SoftwareX · doi:10.1016/j.softx.2015.06.001 · Cited by 27,190 · see citing works

Polymorphic transitions in single crystals: A new molecular dynamics method

Parrinello, M., & Rahman, A. (1981) · Journal of Applied Physics · doi:10.1063/1.328693 · Cited by 19,668 · see citing works

LINCS: A linear constraint solver for molecular simulations

Hess, B., Bekker, H., Berendsen, H. J. C., & Fraaije, J. G. E. M. (1997) · Journal of Computational Chemistry · doi:10.1002/(sici)1096-987x(199709)18:12 · Cited by 18,369 · see citing works

General atomic and molecular electronic structure system

Schmidt, M., Baldridge, K., Boatz, J., Elbert, S., Gordon, M., Jensen, J., Koseki, S., Matsunaga, N., Nguyen, K., Su, S.-J., et al. (1993) · Journal of Computational Chemistry · doi:10.1002/jcc.540141112 · Cited by 17,380 · see citing works

The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics

Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864 · see citing works

Settle: An analytical version of the SHAKE and RATTLE algorithm for rigid water models

Miyamoto, S., & Kollman, P. A. (1992) · Journal of Computational Chemistry · doi:10.1002/jcc.540130805 · Cited by 7,268 · see citing works

Comparison of multiple Amber force fields and development of improved protein backbone parameters

Horn̆ák, V., Abel, R., Okur, A., Strockbine, B., Roitberg, A. E., & Simmerling, C. L. (2006) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21123 · Cited by 6,903 · see citing works

The amyloid hypothesis of Alzheimer's disease at 25 years

Selkoe, D. J., & Hardy, J. (2016) · EMBO Molecular Medicine · doi:10.15252/emmm.201606210 · Cited by 6,164 · see citing works

PRODRG: a tool for high-throughput crystallography of protein–ligand complexes

Schüttelkopf, A. W., & van Aalten, D. M. F. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904011679 · Cited by 4,815 · see citing works

Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide

Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744 · see citing works

Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003) · Science · doi:10.1126/science.1079469 · Cited by 4,064 · see citing works

The Cation−π Interaction

Jennifer, C., & Dougherty, D. A. (1997) · Chemical Reviews · doi:10.1021/cr9603744 · Cited by 3,487 · see citing works

The antibody aducanumab reduces Aβ plaques in Alzheimer’s disease

Sevigny, J., Chiao, P., Bussière, T., Weinreb, P. H., Williams, L., Maier, M., Dunstan, R., Salloway, S., Chen, T., Ling, Y., et al. (2016) · Nature · doi:10.1038/nature19323 · Cited by 3,059 · see citing works

Advances in methods and algorithms in a modern quantum chemistry program package

Shao, Y., Füsti-Molnár, L., Jung, Y., Kußmann, J., Ochsenfeld, C., Brown, S. T., Gilbert, A. T. B., Slipchenko, L. V., Levchenko, S. V., O'Neill, D. P., et al. (2006) · Physical Chemistry Chemical Physics · doi:10.1039/b517914a · Cited by 2,805 · see citing works

3D structure of Alzheimer's amyloid-β(1–42) fibrils

Lührs, T., Ritter, C., Adrian, M., Riek-Loher, D., Bohrmann, B., Döbeli, H., Schubert, D. A., & Riek, R. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506723102 · Cited by 2,001 · see citing works

Self-Propagating, Molecular-Level Polymorphism in Alzheimer's ß-Amyloid Fibrils

Petkova, A. T., Leapman, R. D., Guo, Z., Yau, W.-M., Mattson, M. P., & Tycko, R. (2005) · Science · doi:10.1126/science.1105850 · Cited by 1,687 · see citing works

Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution

Stefani, M., & Dobson, C. M. (2003) · Journal of Molecular Medicine · doi:10.1007/s00109-003-0464-5 · Cited by 1,643 · see citing works

Translating cell biology into therapeutic advances in Alzheimer's disease

Selkoe, D. J. (1999) · Nature · doi:10.1038/399a023 · Cited by 1,588 · 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

EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers

Ehrnhoefer, D. E., Bieschke, J., Boeddrich, A., Herbst, M., Masino, L., Lurz, R., Engemann, S., Pastore, A., & Wanker, E. (2008) · Nature Structural &Molecular Biology · doi:10.1038/nsmb.1437 · Cited by 1,424 · see citing works

Natural Antioxidants in Foods and Medicinal Plants: Extraction, Assessment and Resources

Xu, D.-P., Li, Y., Meng, X., Zhou, T., Zhou, Y., Zheng, J., Zhang, J., & Li, H. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18010096 · Cited by 1,256 · see citing works

Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils

Paravastu, A. K., Leapman, R. D., Yau, W., & Tycko, R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0806270105 · Cited by 1,165 · see citing works

The Cation−π Interaction

Dougherty, D. A. (2012) · Accounts of Chemical Research · doi:10.1021/ar300265y · Cited by 1,160 · see citing works

Structural conversion of neurotoxic amyloid-β1–42 oligomers to fibrils

Ahmed, M., Davis, J., Aucoin, D., Sato, T., Ahuja, S., Aimoto, S., Elliott, J. I., Van Nostrand, W. E., & Smith, S. O. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1799 · Cited by 1,111 · 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

Fibril structure of amyloid-β(1–42) by cryo–electron microscopy

Gremer, L., Schölzel, D., Schenk, C., Reinartz, E., Labahn, J., Ravelli, R. B. G., Tusche, M., López‐Iglesias, C., Hoyer, W., Heise, H., et al. (2017) · Science · doi:10.1126/science.aao2825 · Cited by 1,031 · see citing works

EGCG remodels mature α-synuclein and amyloid-β fibrils and reduces cellular toxicity

Bieschke, J., Russ, J., Friedrich, R., Ehrnhoefer, D. E., Wobst, H. J., Neugebauer, K., & Wanker, E. (2010) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.0910723107 · Cited by 986 · see citing works

A new era for understanding amyloid structures and disease

Iadanza, M. G., Jackson, M. P., Hewitt, E. W., Ranson, N. A., & Radford, S. E. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0060-8 · Cited by 969 · see citing works

The R.E.D. tools: advances in RESP and ESP charge derivation and force field library building

Dupradeau, F., Pigache, A., Zaffran, T., Savineau, C., Lelong, R., Grivel, N., Lelong, D., Rosanski, W., & Cieplak, P. (2010) · Physical Chemistry Chemical Physics · doi:10.1039/c0cp00111b · Cited by 886 · see citing works

Aβ(1–42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease

Xiao, Y., Ma, B., McElheny, D., Parthasarathy, S., Long, F., Hoshi, M. M., Nussinov, R., & Ishii, Y. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2991 · Cited by 822 · see citing works

Atomic Resolution Structure of Monomorphic Aβ42 Amyloid Fibrils

Colvin, M. T., Silvers, R., Ni, Q. Z., Can, T. V., Sergeyev, I. V., Rosay, M., Donovan, K. J., Michael, B. C., Wall, J. S., Linse, S. S., et al. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b05129 · Cited by 812 · see citing works

Atomic-resolution structure of a disease-relevant Aβ(1–42) amyloid fibril

Wälti, M. A., Ravotti, F., Arai, H., Glabe, C. G., Wall, J. S., Böckmann, A., Güntert, P., Meier, B. H., & Riek, R. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1600749113 · Cited by 810 · see citing works

Structure–neurotoxicity relationships of amyloid β-protein oligomers

Ono, K., Condron, M. M., & Teplow, D. B. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0905127106 · Cited by 774 · see citing works

Folding funnels and binding mechanisms

Ma, B., Kumar, S., Tsai, C.-J., & Nussinov, R. (1999) · Protein Engineering, Design and Selection · doi:10.1093/protein/12.9.713 · Cited by 594 · see citing works

Cryo-EM structure and polymorphism of Aβ amyloid fibrils purified from Alzheimer’s brain tissue

Kollmer, M., Close, W., Funk, L., Rasmussen, J., Bsoul, A., Schierhorn, A., Schmidt, M., Sigurdson, C. J., Jucker, M., & Fändrich, M. (2019) · Nature Communications · doi:10.1038/s41467-019-12683-8 · Cited by 593 · see citing works

Gantenerumab: A Novel Human Anti-Aβ Antibody Demonstrates Sustained Cerebral Amyloid-β Binding and Elicits Cell-Mediated Removal of Human Amyloid-β

Bohrmann, B., Baumann, K., Benz, J., Gerber, F., Huber, W., Knoflach, F., Messer, J., Oroszlan, K., Rauchenberger, R., Richter, W. F., et al. (2012) · Journal of Alzheimer's Disease · doi:10.3233/jad-2011-110977 · Cited by 448 · see citing works

Different soluble aggregates of Aβ42 can give rise to cellular toxicity through different mechanisms

De, S., Wirthensohn, D. C., Flagmeier, P., Hughes, C., Aprile, F. A., Ruggeri, F. S., Whiten, D. R., Emin, D., Xia, Z., Varela, J. A., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-09477-3 · Cited by 448 · see citing works

Polyphenols: Benefits to the Cardiovascular System in Health and in Aging

Khurana, S., Venkataraman, K., Hollingsworth, A., Piché, M., & Tai, T. C. (2013) · Nutrients · doi:10.3390/nu5103779 · Cited by 438 · see citing works

Toward the Molecular Mechanism(s) by Which EGCG Treatment Remodels Mature Amyloid Fibrils

Palhano, F. L., Lee, J., Grimster, N. P., & Kelly, J. W. (2013) · Journal of the American Chemical Society · doi:10.1021/ja3115696 · Cited by 350 · see citing works

Evidence that Aβ42 is the real culprit in alzheimer's disease

Younkin, S. G. (1995) · Annals of Neurology · doi:10.1002/ana.410370303 · Cited by 331 · 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

Screening and classifying small-molecule inhibitors of amyloid formation using ion mobility spectrometry–mass spectrometry

Young, L. M., Saunders, J. C., Mahood, R. A., Revill, C., Foster, R. J., Tu, L., Raleigh, D. P., Radford, S. E., & Ashcroft, A. E. (2014) · Nature Chemistry · doi:10.1038/nchem.2129 · Cited by 281 · see citing works

Peptide and Protein Mimetics Inhibiting Amyloid β-Peptide Aggregation

Takahashi, T., & Mihara, H. (2008) · Accounts of Chemical Research · doi:10.1021/ar8000475 · Cited by 237 · see citing works

Peptide dimer structure in an Aβ(1–42) fibril visualized with cryo-EM

Schmidt, M., Rohou, A. L., Lasker, K., Yadav, J. K., Schiene‐Fischer, C., Fändrich, M., & Grigorieff, N. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1503455112 · Cited by 219 · see citing works

Molecular Mechanism of the Inhibition of EGCG on the Alzheimer Aβ1–42Dimer

Zhang, T., Zhang, J., Derreumaux, P., & Mu, Y. (2013) · The Journal of Physical Chemistry B · doi:10.1021/jp312573y · Cited by 206 · see citing works

Tanshinones Inhibit Amyloid Aggregation by Amyloid-β Peptide, Disaggregate Amyloid Fibrils, and Protect Cultured Cells

Wang, Q., Yu, X., Patal, K., Hu, R., Chuang, S. S. C., Zhang, G., & Zheng, J. (2013) · ACS Chemical Neuroscience · doi:10.1021/cn400051e · Cited by 205 · see citing works

Destabilizing Alzheimer’s Aβ42Protofibrils with Morin: Mechanistic Insights from Molecular Dynamics Simulations

Lemkul, J. A., & Bevan, D. R. (2010) · Biochemistry · doi:10.1021/bi1000855 · Cited by 180 · see citing works

Inhibition of protein misfolding and aggregation by natural phenolic compounds

Dhouafli, Z., Cuanalo-Contreras, K., Hayouni, E. A., Mays, C. E., Soto, C. A., & Moreno‐González, I. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2872-2 · Cited by 174 · see citing works

The Amyloid Phenomenon and Its Significance in Biology and MedicinePreprint

Dobson, C. M., Knowles, T. P. J., & Vendruscolo, M. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a033878 · Cited by 166 · see citing works

Structural Properties of EGCG-Induced, Nontoxic Alzheimer's Disease Aβ Oligomers

del Amo, J. M. L., Fink, U., Dasari, M., Grelle, G., Wanker, E. E., Bieschke, J., & Reif, B. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2012.01.013 · Cited by 162 · see citing works

Molecular Insight into Conformational Transition of Amyloid β-Peptide 42 Inhibited by (−)-Epigallocatechin-3-gallate Probed by Molecular Simulations

Liu, F., Dong, X., He, L., Middelberg, A. P. J., & Sun, Y. P. (2011) · The Journal of Physical Chemistry B · doi:10.1021/jp202640b · Cited by 142 · see citing works

Modeling an In-Register, Parallel “Iowa” Aβ Fibril Structure Using Solid-State NMR Data from Labeled Samples with Rosetta

Sgourakis, N. G., Yau, W., & Qiang, W. (2014) · Structure · doi:10.1016/j.str.2014.10.022 · Cited by 115 · see citing works

Conformational Ensemble of hIAPP Dimer: Insight into the Molecular Mechanism by which a Green Tea Extract inhibits hIAPP Aggregation

Mo, Y., Lei, J., Sun, Y., Zhang, Q., & Wei, G. (2016) · Scientific Reports · doi:10.1038/srep33076 · Cited by 100 · see citing works

Destabilization of Alzheimer’s Aβ42 Protofibrils with a Novel Drug Candidate wgx-50 by Molecular Dynamics Simulations

Fan, H., Gu, R., Wang, Y., Pi, Y.-L., Zhang, Y., Xu, Q., & Wei, D. (2015) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.5b03116 · Cited by 94 · see citing works

An in vivo platform for identifying inhibitors of protein aggregation

Saunders, J. C., Young, L. M., Mahood, R. A., Jackson, M. P., Revill, C., Foster, R. J., Smith, D. A., Ashcroft, A. E., Brockwell, D. J., & Radford, S. E. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1988 · Cited by 85 · see citing works

Hydroxylated Single-Walled Carbon Nanotubes Inhibit Aβ42 Fibrillogenesis, Disaggregate Mature Fibrils, and Protect against Aβ42-Induced Cytotoxicity

Liu, F., Wang, W., Sang, J., Jia, L., & Lu, F. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00441 · Cited by 67 · see citing works

Aggregation of Aβ(17–36) in the Presence of Naturally Occurring Phenolic Inhibitors Using Coarse-Grained Simulations

Wang, Y., Latshaw, D. C., & Hall, C. K. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.10.006 · Cited by 58 · see citing works

Inhibition of β-Amyloid Channels with a Drug Candidate wgx-50 Revealed by Molecular Dynamics Simulations

Hou, S., Gu, R., & Wei, D. (2017) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.7b00452 · Cited by 48 · 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

Caffeine destabilizes preformed Aβ protofilaments: insights from all atom molecular dynamics simulations

Gupta, S., & Dasmahapatra, A. K. (2019) · Physical Chemistry Chemical Physics · doi:10.1039/c9cp04162a · Cited by 42 · see citing works

Critical Nucleus Structure and Aggregation Mechanism of the C-terminal Fragment of Copper–Zinc Superoxide Dismutase Protein

Zou, Y. F., Sun, Y., Zhu, Y., Ma, B., Nussinov, R., & Zhang, Q. (2016) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5b00242 · Cited by 41 · see citing works

Dihydrochalcone molecules destabilize Alzheimer's amyloid-β protofibrils through binding to the protofibril cavity

Jin, Y., Sun, Y., Lei, J., & Wei, G. (2018) · Physical Chemistry Chemical Physics · doi:10.1039/c8cp01631c · Cited by 39 · see citing works

12-Crown-4 Ether Disrupts the Patient Brain-Derived Amyloid-β-Fibril Trimer: Insight from All-Atom Molecular Dynamics Simulations

Agrawal, N., & Skelton, A. A. (2016) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.6b00185 · Cited by 38 · see citing works

Critical nucleus of Greek-key-like core of α-synuclein protofibril and its disruption by dopamine and norepinephrine

Zou, Y. F., Qian, Z., Gong, Y., Tang, Y., Wei, G., & Zhang, Q. (2019) · Physical Chemistry Chemical Physics · doi:10.1039/c9cp04610k · Cited by 38 · see citing works

Distinct Binding Dynamics, Sites and Interactions of Fullerene and Fullerenols with Amyloid-β Peptides Revealed by Molecular Dynamics Simulations

Liu, Z., Zou, Y. F., Zhang, Q., Chen, P., Liu, Y., & Qian, Z. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20082048 · Cited by 36 · see citing works

Interactions of a multifunctional di-triazole derivative with Alzheimer's Aβ 42 monomer and Aβ 42 protofibril: a systematic molecular dynamics study

Kaur, A., Shuaib, S., Goyal, D., & Goyal, B. (2019) · Physical Chemistry Chemical Physics · doi:10.1039/c9cp04775a · Cited by 34 · see citing works

Revealing the Mechanism of EGCG, Genistein, Rutin, Quercetin, and Silibinin Against hIAPP Aggregation via Computational Simulations

Wang, Y., Lv, Y., Jin, L., & Liang, G. (2020) · Interdisciplinary Sciences Computational Life Sciences · doi:10.1007/s12539-019-00352-9 · Cited by 28 · see citing works

Effect of catechins and high-temperature-processed green tea extract on scavenging reactive oxygen species and preventing Aβ1–42fibrils’ formation in brain microvascular endothelium

Lee, S.-B., Choi, E., Jeong, K.-H., Kim, K.-S., Shim, S., & Kim, G.-H. (2018) · Nutritional Neuroscience · doi:10.1080/1028415x.2018.1507618 · Cited by 18 · see citing works

Binding Modes of a Glycopeptidomimetic Molecule on Aβ Protofibrils: Implication for Its Inhibition Mechanism

Tran, L., Kaffy, J., Ongeri, S., & Ha‐Duong, T. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00341 · Cited by 15 · see citing works

Green Tea Polyphenol Epigallocatechin-Gallate in Amyloid Aggregation and Neurodegenerative Diseases

Fernandes, L., Cardim-Pires, T. R., Foguel, D., & Palhano, F. L. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.718188 · Cited by 114 · see citing works

Modulation of Amyloid Protein Fibrillation by Synthetic Polymers: Recent Advances in the Context of Neurodegenerative Diseases

Ghosh, P., & De, P. (2020) · ACS Applied Bio Materials · doi:10.1021/acsabm.0c01021 · Cited by 84 · see citing works

Multifaceted neuroprotective effects of (-)-epigallocatechin-3-gallate (EGCG) in Alzheimer’s disease: an overview of pre-clinical studies focused on β-amyloid peptide

Youn, K., Ho, C., & Jun, M. (2022) · Food Science and Human Wellness · doi:10.1016/j.fshw.2021.12.006 · Cited by 74 · see citing works

Exploring the Therapeutic Potential of Phytochemicals in Alzheimer’s Disease: Focus on Polyphenols and Monoterpenes

Piccialli, I., Tedeschi, V., Caputo, L., D’Errico, S., Ciccone, R., De Feo, V., Secondo, A., & Pannaccione, A. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.876614 · Cited by 73 · see citing works

A Comprehensive Insight into the Mechanisms of Dopamine in Disrupting Aβ Protofibrils and Inhibiting Aβ Aggregation

Chen, Y., Li, X., Zhan, C., Lao, Z., Li, F., Dong, X., & Wei, G. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00306 · Cited by 56 · see citing works

Molecular mechanisms of resveratrol and EGCG in the inhibition of Aβ 42 aggregation and disruption of Aβ 42 protofibril: similarities and differences

Li, F., Zhan, C., Dong, X., & Wei, G. (2021) · Physical Chemistry Chemical Physics · doi:10.1039/d1cp01913a · Cited by 54 · see citing works

Dual modulation of amyloid beta and tau aggregation and dissociation in Alzheimer’s disease: a comprehensive review of the characteristics and therapeutic strategies

Nam, Y., Shin, S. J., Kumar, V., Won, J., Kim, S., & Moon, M. (2025) · Translational Neurodegeneration · doi:10.1186/s40035-025-00479-4 · Cited by 59 · see citing works

Epigallocatechin Gallate Destabilizes α-Synuclein Fibril by Disrupting the E46–K80 Salt-Bridge and Inter-protofibril Interface

Yao, Y., Tang, Y., & Wei, G. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00598 · Cited by 45 · see citing works

Serotonin and Melatonin Show Different Modes of Action on Aβ42 Protofibril Destabilization

Gong, Y., Zhan, C., Zou, Y. F., Qian, Z., Wei, G., & Zhang, Q. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00038 · Cited by 44 · see citing works

From Small Molecules to Synthesized Polymers: Potential Role in Combating Amyloidogenic Disorders

Ghosh, P., Bera, A., Bhadury, P., & De, P. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00104 · Cited by 38 · see citing works

Understanding the Molecular Mechanisms of Polyphenol Inhibition of Amyloid β Aggregation

Han, Y.-L., Yin, H., Chao, X., Bernards, M. T., He, Y., & Guan, Y. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00586 · Cited by 35 · see citing works

Current strategies of detecting Aβ species and inhibiting Aβ aggregation: Status and prospects

Li, J., Liao, W., Huang, D., Ou, M., Chen, T., Wang, X., Zhao, R., Zhang, L., Mei, L., Liu, J., et al. (2023) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2023.215375 · Cited by 36 · see citing works

Green tea extract EGCG plays a dual role in Aβ42 protofibril disruption and membrane protection: A molecular dynamic study

Dong, X., Tang, Y., Zhan, C., & Wei, G. (2020) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2020.105024 · Cited by 34 · see citing works

Inhibition Mechanisms of (−)-Epigallocatechin-3-gallate and Genistein on Amyloid-beta 42 Peptide of Alzheimer’s Disease via Molecular Simulations

Fang, M., Zhang, Q., Wang, X., Su, K., Guan, P., & Hu, X. (2022) · ACS Omega · doi:10.1021/acsomega.2c01412 · Cited by 32 · see citing works

Baicalein exhibits differential effects and mechanisms towards disruption of α-synuclein fibrils with different polymorphs

Yao, Y., Tang, Y., Zhou, Y., Yang, Z., & Wei, G. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.08.088 · Cited by 30 · see citing works

Mechanistic insight into the disruption of Tau R3–R4 protofibrils by curcumin and epinephrine: an all-atom molecular dynamics study

Zou, Y. F., Qi, B., Tan, J., Sun, Y., Gong, Y., & Zhang, Q. (2022) · Physical Chemistry Chemical Physics · doi:10.1039/d2cp02353a · Cited by 30 · see citing works

Green tea improves cognitive function through reducing AD-pathology and improving anti-oxidative stress capacity in Chinese middle-aged and elderly people

Zhang, R., Zhang, L., Zeng, L., Zhang, P., Song, H., Yao, D.-A., Cao, J., & Zhang, J. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.919766 · Cited by 29 · see citing works

Triazole–Peptide Conjugate as a Modulator of Aβ-Aggregation, Metal-Mediated Aβ-Aggregation, and Cytotoxicity

Mann, S., Kaur, A., Kaur, A., Priyadarshi, N., Goyal, B., Singhal, N. K., & Goyal, D. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00041 · Cited by 28 · see citing works

Illustrating the Effect of Small Molecules Derived from Natural Resources on Amyloid Peptides

Roy, R., & Paul, S. (2023) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.2c07607 · Cited by 28 · see citing works

Inhibitory Effects of Six Types of Tea on Aging and High-Fat Diet-Related Amyloid Formation Activities

Wan, J., Feng, M., Pan, W., Zheng, X., Xie, X., Hu, B., Teng, C., Wang, Y., Liu, Z., Wu, J., et al. (2021) · Antioxidants · doi:10.3390/antiox10101513 · Cited by 27 · see citing works

Effect of Terahertz Waves on the Structure of the Aβ42 Monomer, Dimer, and Protofibril: Insights from Molecular Dynamics Simulations

Chen, C., Yan, Z., Ma, Y., & Ding, H. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00485 · Cited by 26 · see citing works

Mechanistic insights into the mitigation of Aβ aggregation and protofibril destabilization by a d -enantiomeric decapeptide rk10

Singh, K., Kaur, A., Goyal, D., & Goyal, B. (2022) · Physical Chemistry Chemical Physics · doi:10.1039/d2cp02601e · Cited by 26 · see citing works

Insights into Molecular Mechanisms of EGCG and Apigenin on Disrupting Amyloid-Beta Protofibrils Based on Molecular Dynamics Simulations

Fang, M., Zhang, Q., Guan, P., Su, K., Wang, X., & Hu, X. (2022) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.2c04230 · Cited by 25 · see citing works

Amyloid Disassembly: What Can We Learn from Chaperones?

Almeida, Z. L., & Brito, R. M. M. (2022) · Biomedicines · doi:10.3390/biomedicines10123276 · Cited by 20 · see citing works

Molecular insights into the inhibition of early stages of Aβ peptide aggregation and destabilization of Alzheimer's Aβ protofibril by dipeptide D-Trp-Aib: A molecular modelling approach

Mohammed, A. A., Barale, S. S., Kamble, S. A., Paymal, S. B., & Sonawane, K. D. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.124880 · Cited by 21 · see citing works

Molecular dynamics simulations reveal the destabilization mechanism of Alzheimer's disease-related tau R3-R4 Protofilament by norepinephrine

Wan, J., Gong, Y., Xu, Z., Dong, X., Wei, G., & Zhang, Q. (2021) · Biophysical Chemistry · doi:10.1016/j.bpc.2021.106541 · Cited by 19 · see citing works

Molecular Insights into the Inhibition and Disaggregation Effects of EGCG on Aβ40 and Aβ42 Cofibrillation

Li, X., Zhang, Y., Wang, Y., Zhang, S., & Zhang, L. (2024) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.3c07232 · Cited by 18 · see citing works

Thiophene‐Based Dual Modulators of Aβ and Tau Aggregation

Ramesh, M., Acharya, A., Murugan, N. A., Ila, H., & Govindaraju, T. (2021) · ChemBioChem · doi:10.1002/cbic.202100383 · Cited by 18 · see citing works

The destructive mechanism of Aβ 1–42 protofibrils by norepinephrine revealed via molecular dynamics simulations

Gao, D., Wan, J., Zou, Y. F., Gong, Y., Dong, X., Xu, Z., Tang, J., Wei, G., & Zhang, Q. (2022) · Physical Chemistry Chemical Physics · doi:10.1039/d2cp01754g · Cited by 17 · see citing works

Plant-Based Inhibitors of Protein Aggregation

Zhytniakivska, O. A., Chaturvedi, T., & Thomsen, M. H. (2025) · Biomolecules · doi:10.3390/biom15040481 · Cited by 18 · see citing works

Structural determinants of the interactions of catechins with Aβ oligomers and lipid membranes

Ahmed, R., Huang, J., Lifshitz, R., Pomier, K. M., & Melacini, G. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101502 · Cited by 16 · see citing works

Inhibition effect of high hydrostatic pressure combined with epigallocatechin gallate treatments on pectin methylesterase in orange juice and model system.

Tian, X.-R., Liu, Y., Zhao, L., Rao, L., Wang, Y.-T., & Liao, X. (2022) · Food Chemistry · doi:10.1016/j.foodchem.2022.133147 · Cited by 14 · see citing works

Dissecting the Inhibitory Mechanism of the αB-Crystallin Domain against Aβ42 Aggregation and Its Effect on Aβ42 Protofibrils: A Molecular Dynamics Simulation Study

Xu, Z., Gong, Y., Zou, Y. F., Wan, J., Tang, J., Zhan, C., Wei, G., & Zhang, Q. (2022) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.2c00224 · Cited by 16 · see citing works

Destabilization of the Alzheimer’s amyloid-β protofibrils by THC: A molecular dynamics simulation study

Kanchi, P. K., & Dasmahapatra, A. K. (2021) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2021.107889 · Cited by 16 · see citing works

Epigallocatechin‐Gallate: Unraveling Its Protective Mechanisms and Therapeutic Potential

Dong, X., Fang, W., Li, Y., & Chai, Y. (2025) · Cell Biochemistry and Function · doi:10.1002/cbf.70056 · Cited by 16 · see citing works

Photooxidative inhibition and decomposition of β-amyloid in Alzheimer's by nano-assemblies of transferrin and indocyanine green

Hou, T., Shao, X., Ding, M., Mei, K., Wang, X., Guan, P., & Hu, X. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.124432 · Cited by 15 · see citing works

Effect of tea polyphenols on the prevention of neurodegenerative diseases through gut microbiota

Xu, L., Wang, R., Liu, Y., Zhan, S., Wu, Z., & Zhang, X. (2023) · Journal of Functional Foods · doi:10.1016/j.jff.2023.105669 · Cited by 15 · see citing works

The Inhibition Effect of Epigallocatechin-3-Gallate on the Co-Aggregation of Amyloid-β and Human Islet Amyloid Polypeptide Revealed by Replica Exchange Molecular Dynamics Simulations

Li, X., Zhang, Y., Yang, Z., Zhang, S., & Zhang, L. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25031636 · Cited by 15 · see citing works

Protection of Green Tea Polyphenols against Neurodegenerative Diseases: Evidence and Possible Mechanisms

Zhao, B., & Zhao, B. (2025) · Journal of Nutrition · doi:10.1016/j.tjnut.2025.02.010 · Cited by 15 · see citing works

Tea intake or consumption and the risk of dementia: a meta-analysis of prospective cohort studies

Jiang, N., Ma, J., Wang, Q., Xu, Y., & Wei, B. (2023) · PeerJ · doi:10.7717/peerj.15688 · Cited by 14 · see citing works

Neuroprotective potential of epigallocatechin gallate in Neurodegenerative Diseases: Insights into molecular mechanisms and clinical Relevance

Al-Amin, M., Zehravi, M., Sweilam, S. H., Shatu, M. M., Durgawale, T. P., Qureshi, M. S., Durgapal, S., Haque, M. A., Vodeti, R., Panigrahy, U. P., et al. (2025) · Brain Research · doi:10.1016/j.brainres.2025.149693 · Cited by 15 · see citing works

Molecular Mechanism in the Disruption of Chronic Traumatic Encephalopathy-Related R3–R4 Tau Protofibril by Quercetin and Gallic Acid: Similarities and Differences

Tang, J., Zou, Y. F., Gong, Y., Xu, Z., Wan, J., Wei, G., & Zhang, Q. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.2c00688 · Cited by 14 · see citing works

Nutraceuticals and their Derived Nano-Formulations for the Prevention and Treatment of Alzheimer's Disease

Haque, S. E., Iqubal, A., Iqubal, M. K., Fazal, S. A., & Pottoo, F. H. (2021) · Current Molecular Pharmacology · doi:10.2174/1874467214666210309115605 · Cited by 14 · see citing works

Oolonghomobisflavans exert neuroprotective activities in cultured neuronal cells and anti-aging effects in Caenorhabditis elegans

Zhang, S., Duangjan, C., Tencomnao, T., Wu, L., Wink, M., & Lin, J. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.967316 · Cited by 13 · see citing works

EGCG Suppresses Adipogenesis and Promotes Browning of 3T3-L1 Cells by Inhibiting Notch1 Expression

Wang, Y., Li, C., Peng, W., Sheng, J., Zi, C., & Wu, X. (2024) · Molecules · doi:10.3390/molecules29112555 · Cited by 13 · see citing works

Profiling of In Vitro Bioaccessibility and Intestinal Uptake of Flavonoids after Consumption of Commonly Available Green Tea Types

Oh, J.-H., Lee, C.-Y., Lee, Y., Yoo, S., Chung, J., Rha, C., Park, M., Hong, Y., & Shim, S. (2021) · Molecules · doi:10.3390/molecules26061518 · Cited by 13 · see citing works

Green tea hydroxycinnamoylated catechins extend lifespan and attenuate Aβ-induced paralysis of Caenorhabditis elegans via anti-oxidation and peptides dis-aggregation

Yang, Y., Ke, J., Yang, Z. M., Chen, C., Li, J.-Y., Yu, J.-Y., Zhang, Y., & Bao, G. (2024) · Industrial Crops and Products · doi:10.1016/j.indcrop.2024.118390 · Cited by 12 · see citing works

Lipids and EGCG Affect α-Synuclein Association and Disruption of Nanodiscs

Sanders, H. M., Kostelic, M. M., Zak, C. K., & Marty, M. T. (2022) · Biochemistry · doi:10.1021/acs.biochem.2c00160 · Cited by 12 · see citing works

Five similar anthocyanidin molecules display distinct disruptive effects and mechanisms of action on Aβ1–42 protofibril: A molecular dynamic simulation study

Chen, Y., Zhan, C., Li, X., Pan, T., Yao, Y., Tan, Y., & Wei, G. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.128467 · Cited by 11 · see citing works

Effect of the Number of Gallate Groups of Polyphenols on the Structure, Gel Properties, and Biological Activity of Soy Protein Fibrils

Xu, T., Su, R.-H., Yang, B.-W., Dai, S., Wang, J., Zhu, W., Fang, Q., Wang, H., & Jiang, L.-Z. (2025) · Foods · doi:10.3390/foods14060974 · Cited by 12 · see citing works

Identification of new pentapeptides as potential inhibitors of amyloid–β42 aggregation using virtual screening and molecular dynamics simulations

Kaur, A., & Goyal, B. (2023) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2023.108558 · Cited by 11 · see citing works

How oxidized EGCG remodels α-synuclein fibrils into non-toxic aggregates: insights from computational simulations

Gonçalves, P. B., Palhano, F. L., Cordeiro, Y., & Sodero, A. C. R. (2023) · Physical Chemistry Chemical Physics · doi:10.1039/d3cp02261g · Cited by 11 · see citing works

Strategies for Inhibition and Disaggregation of Amyloid‐β Fibrillation

Geng, H., Gao, D. M., Wang, Z., Liu, X., Cao, Z., & Xing, C. (2021) · Chinese Journal of Chemistry · doi:10.1002/cjoc.202100646 · Cited by 10 · see citing works

Inhibitive and Destructive Mechanisms of Chronic Traumatic Encephalopathy-Related R3-R4 Tau Peptide Chains and Protofibril by Epigallocatechin Gallate: Evidence from Molecular Dynamics Simulation

Tang, J., Sun, R., Wan, J., Xu, Z., Gong, Y., Zou, Y. F., & Zhang, Q. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00103 · Cited by 10 · see citing works

Interactions of Curcumin’s Degradation Products with the Aβ 42 Dimer: A Computational Study

Dehabadi, M. H., Caflisch, A., Ilie, I. M., & Firouzi, R. (2022) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.2c05846 · Cited by 10 · see citing works

Natural Compounds as Inhibitors of Aβ Peptide and Tau Aggregation

Monteiro, K. L. C., de Aquino, T. M., & da Silva‐Júnior, E. F. (2023) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/0118715273273539231114095300 · Cited by 9 · see citing works

Real-time monitoring of the amyloid β1–42 monomer-to-oligomer channel transition using a lipid bilayer system

Numaguchi, Y., Tsukakoshi, K., Takeuchi, N., Suzuki, Y., Ikebukuro, K., & Kawano, R. (2023) · PNAS Nexus · doi:10.1093/pnasnexus/pgad437 · Cited by 9 · see citing works

Constructing conformational library for amyloid-β42 dimers as the smallest toxic oligomers using two CHARMM force fields

Dehabadi, M. H., & Firouzi, R. (2022) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2022.108207 · Cited by 9 · see citing works

Molecular insights into the very early steps of Aβ1-42 pentameric protofibril disassembly by PGG: A molecular dynamics simulation study

Nie, R., Cai, S., Yu, B., Fan, W., Li, H., Tang, S., & Huo, Y. (2022) · Journal of Molecular Liquids · doi:10.1016/j.molliq.2022.119638 · Cited by 9 · see citing works

Molecular insights into the structure destabilization effects of ECG and EC on the Aβ protofilament: An all-atom molecular dynamics simulation study

Nie, R., Zhang, S.-S., Yan, X.-K., Feng, K., Lao, Y.-J., & Bao, Y.-R. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.127002 · Cited by 9 · see citing works

β‐sheet breakers with consecutive phenylalanines: Insights into mechanism of dissolution of β‐amyloid fibrils

Jarmuła, A., Ludwiczak, J., & Stępkowski, D. (2021) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26057 · Cited by 9 · see citing works

Unveiling the inhibitory mechanism of peptidomimetic inhibitor against Aβ42 aggregation and protofibril disaggregation by molecular dynamics

Kaur, R., Saini, R. K., Singh, P., & Goyal, B. (2021) · Journal of Molecular Liquids · doi:10.1016/j.molliq.2021.116474 · Cited by 9 · see citing works

Molecular Dynamics Simulations Reveal the Modulated Mechanism of STING Conformation

Chen, L., Zhao, S., Zhu, Y., Liu, Y., Li, H., & Zhao, Q. (2021) · Interdisciplinary Sciences Computational Life Sciences · doi:10.1007/s12539-021-00446-3 · Cited by 9 · see citing works

Atomistic Insights into A315E Mutation-Enhanced Pathogenicity of TDP-43 Core Fibrils

Li, F., Chen, Y., Liu, X., Tang, Y., Dong, X., & Wei, G. (2022) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.2c00416 · Cited by 9 · see citing works

Identification of Catechins’ Binding Sites in Monomeric Aβ42 through Ensemble Docking and MD Simulations

Firouzi, R., Sowlati‐Hashjin, S., Chávez-García, C., Ashouri, M., Karimi‐Jafari, M. H., & Karttunen, M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24098161 · Cited by 9 · see citing works

Atomic insights into the inhibition of R3 domain of tau protein by epigallocatechin gallate, quercetin and gallic acid

Tang, J., Sun, R., Wan, J., Xu, Z., Zou, Y. F., & Zhang, Q. (2023) · Biophysical Chemistry · doi:10.1016/j.bpc.2023.107142 · Cited by 8 · see citing works

Polyphenol-Peptide Interactions in Mitigation of Alzheimer’s Disease: Role of Biosurface-Induced Aggregation

Gaudreault, R., Hervé, V., van de Ven, T. G. M., Mousseau, N., & Ramassamy, C. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-201549 · Cited by 8 · see citing works

The Synergistic Potential of Rationally Designed Phenol-Triazole Derivatives to Attenuate Aβ/Cu2+–Aβ Aggregation and Reactive Oxygen Species

Kaur, G., Mankoo, O. K., Kaur, A., Mann, S., Priyadarshi, N., Singh, P. P., Goyal, B., Singhal, N. K., & Goyal, D. (2025) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5c00386 · Cited by 7 · see citing works

Origin of stronger binding of ionic pair (IP) inhibitor to Aβ42 than the equimolar neutral counterparts: synergy mechanism of IP in disrupting Aβ42 protofibril and inhibiting Aβ42 aggregation under two pH conditions

Xu, W. W., Mei, J., Wang, C., Yang, H., Ma, X., Gao, W., Ahmad, S., & Ai, H. (2023) · Physical Chemistry Chemical Physics · doi:10.1039/d3cp01683h · Cited by 7 · see citing works

Atomistic Insights into the Stabilization of TDP-43 Protofibrils by ATP

Xu, Z., Tang, J., Gong, Y., Zhang, J., & Zou, Y. F. (2024) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.4c01140 · Cited by 7 · see citing works

From Self-Assembly to Drug Delivery: Understanding and Exploring Protein Fibrils

Jain, A., Lopus, M., & Kishore, N. (2025) · Langmuir · doi:10.1021/acs.langmuir.4c03745 · Cited by 7 · see citing works

Functionalized carbon dots with guanidine salt ionic liquid regulate oxidative damage and amyloid aggregation

Wang, C., Hou, T., Shao, X., Wang, C., Wang, X., Guan, P., Wu, Y., & Hu, X. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.141531 · Cited by 7 · see citing works

Study on molecular mechanisms of destabilizing Aβ(1–42) protofibrils by licochalcone A and licochalcone B using molecular dynamics simulations

Fang, M., Su, K., Wang, X., Guan, P., & Hu, X. (2023) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2023.108500 · Cited by 7 · see citing works

EGCG-Mediated Protection of Transthyretin Amyloidosis by Stabilizing Transthyretin Tetramers and Disrupting Transthyretin Aggregates

Zou, H., & Zhou, S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241814146 · Cited by 6 · see citing works

Insights into the baicalein-induced destabilization of LS-shaped Aβ 42 protofibrils using computer simulations

Kaur, G., Mankoo, O. K., Kaur, A., Goyal, D., & Goyal, B. (2024) · Physical Chemistry Chemical Physics · doi:10.1039/d3cp06006c · Cited by 6 · see citing works

Understanding the mechanisms of green tea EGCG against amyloid β oligomer neurotoxicity through computational studies

Gonçalves, P. B., Cordeiro, Y., & Sodero, A. C. R. (2024) · RSC Advances · doi:10.1039/d4ra03343d · Cited by 7 · see citing works

Destabilisation of Alzheimer’s amyloid-β protofibrils by Baicalein: mechanistic insights from all-atom molecular dynamics simulations

Choudhury, S., & Dasmahapatra, A. K. (2024) · Molecular Diversity · doi:10.1007/s11030-024-11001-9 · Cited by 6 · see citing works

Small-Molecule Inhibitors of Amyloid Beta: Insights from Molecular Dynamics—Part B: Natural Compounds

Atanasova, M. (2025) · Pharmaceuticals · doi:10.3390/ph18101457 · Cited by 5 · see citing works

Molecular mechanisms involved in the destabilization of two types of R3–R4 tau fibrils associated with chronic traumatic encephalopathy by Fisetin

Tang, J., Sun, R., Wan, J., Zou, Y. F., & Zhang, Q. (2023) · Physical Chemistry Chemical Physics · doi:10.1039/d3cp05427f · Cited by 5 · see citing works

Structure of cytotoxic amyloid oligomers generated during disaggregation

Kaku, T., Ikebukuro, K., & Tsukakoshi, K. (2024) · The Journal of Biochemistry · doi:10.1093/jb/mvae023 · Cited by 5 · see citing works

Molecular Deformation Is a Key Factor in Screening Aggregation Inhibitor for Intrinsically Disordered Protein Tau

Chai, K., Yang, J., Tu, Y., Wu, J., Fang, K., Shi, S., & Yao, T. (2024) · ACS Central Science · doi:10.1021/acscentsci.3c01196 · Cited by 5 · see citing works

Structural Reorganization Mechanism of the Aβ42 Fibril Mediated by N-Substituted Oligopyrrolamide ADH-353

Dabas, A., & Goyal, B. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.4c00253 · Cited by 5 · see citing works

Interdisciplinary Approaches to Deal with Alzheimer’s Disease—From Bench to Bedside: What Feasible Options Do Already Exist Today?

Ablinger, I., Dressel, K., Rott, T., Lauer, A. A., Tiemann, M., Batista, J. P., Taddey, T., Grimm, H. S., & Grimm, M. O. W. (2022) · Biomedicines · doi:10.3390/biomedicines10112922 · Cited by 5 · see citing works

In Silico Screening of Small Molecule Inhibitors for Amyloid-β Aggregation

Han, Y.-L., Li, C., Yin, H., He, Y., & Guan, Y. (2025) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.5c00831 · Cited by 4 · see citing works

Cytotoxic Aβ Protofilaments Are Generated in the Process of Aβ Fibril Disaggregation

Kaku, T., Tsukakoshi, K., & Ikebukuro, K. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222312780 · Cited by 4 · see citing works

EGCG Promotes FUS Condensate Formation in a Methylation-Dependent Manner

Lenard, A. J., Zhou, Q., Madreiter‐Sokolowski, C. T., Bourgeois, B. M. R., Habacher, H., Khanna, Y., & Madl, T. (2022) · Cells · doi:10.3390/cells11040592 · Cited by 4 · see citing works

Dissecting the effect of ALS mutation S375G on the conformational properties and aggregation dynamics of TDP-43370-375 fragment

Xu, Z., Zhang, J., Tang, J., Gong, Y., Zou, Y. F., & Zhang, Q. (2024) · Biophysical Chemistry · doi:10.1016/j.bpc.2024.107230 · Cited by 4 · see citing works

Exploring the Impact of C‐Terminal Based Pentapeptides on the Disassembly of Aβ42 Fibrils

Kaur, A., Mankoo, O. K., Rani, D., Priyadarshi, N., Goyal, D., Singhal, N. K., & Goyal, B. (2024) · ChemMedChem · doi:10.1002/cmdc.202400486 · Cited by 4 · see citing works

Theoretical Insights into the Inhibitory Mechanism of EGCG-Functionalized Gold Nanoparticles on hIAPP Protofibrils

Singh, A. K., & Jha, A. N. (2024) · BioNanoScience · doi:10.1007/s12668-024-01733-1 · Cited by 4 · see citing works

Interactive Mechanism of Potential Inhibitors with Glycosyl for SARS-CoV-2 by Molecular Dynamics Simulation

Zhang, Y., Chen, L., Wang, X., Zhu, Y., Liu, Y., Li, H., & Zhao, Q. (2021) · Processes · doi:10.3390/pr9101749 · Cited by 3 · see citing works

Destabilization mechanism of R3–R4 tau protofilament by purpurin: a molecular dynamics study

Wan, J., Zou, Y. F., Sun, R., Xu, Z., Tang, J., Gong, Y., Wei, G., & Zhang, Q. (2023) · Physical Chemistry Chemical Physics · doi:10.1039/d3cp01039b · Cited by 4 · see citing works

Delineating the tryptophan–galactosylamine conjugate mediated structural distortions in Aβ 42 protofibrils

Dabas, A., & Goyal, B. (2025) · Physical Chemistry Chemical Physics · doi:10.1039/d4cp03330b · Cited by 2 · see citing works

Epigallocatechin-3-gallate (EGCG) as a molecular chaperone and network rebalancer in neurodegenerative diseases

Farah, H. S., Ahmed, M. H., Al-Hasnaawei, S., Malathi, H., Mishra, S., Nanda, A., Arora, V., & Chauhan, A. S. (2026) · Inflammopharmacology · doi:10.1007/s10787-026-02291-6 · Cited by 2 · see citing works

Self-assembled silk fibroin nanofibrils enhance the storage stability and bioaccessibility of anthocyanins: the role of β-sheet architecture

Ma, Z., & Jing, P. (2026) · Food Chemistry · doi:10.1016/j.foodchem.2026.150567 · Cited by 2 · see citing works

Catechol‐Amyloid Interactions

Le, N. T. K., Kang, E. J., Park, J. H., & Kang, K. (2023) · ChemBioChem · doi:10.1002/cbic.202300628 · Cited by 2 · see citing works

Distinct disruption mechanisms of green tea extracts EGC and EGCG on ATTR fibrils: a molecular simulation study

Yan, X., Cao, Y., Xu, Z., Zhu, Y., Zhao, Q., Li, H., & Chen, Y. (2025) · Physical Chemistry Chemical Physics · doi:10.1039/d5cp03218k · Cited by 1 · see citing works

Aloe Vera Inhibits Protein Fibrillation: Mechanistic Biophysical Evaluation

Jain, A., & Kishore, N. (2025) · Langmuir · doi:10.1021/acs.langmuir.5c03925 · Cited by 1 · see citing works

Epigallocatechin-3-Gallate: A potential amyloid Fibril Disaggregator of Serum amyloid A1

Horgan, N. G., Djurovic-Topalovic, A., Ademoye, T. A., Reyes-Charles, H. I., Kobayashi, N., Plascencia‐Villa, G., Perry, G. L., Murakami, T., & Fortin, J. S. (2025) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2025.102365 · Cited by 1 · see citing works

The inhibitory mechanisms of PGG, a natural polyphenol enriched with gallate moieties, against Aβ42 amyloid aggregation: A unified experimental and molecular dynamics simulation study

Nie, R., Luo, H.-M., Wang, H., Yang, Y.-R., Wang, Y.-Z., Zhang, S.-Z., Feng, K., Li, Y.-L., Chen, F., Duan, C.-X., et al. (2026) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2026.118584 · Cited by 1 · see citing works

Epigallocatechin Gallate as a State-Dependent Modulator of Amyloid-β: Molecular Simulation-Guided Mechanistic Synthesis for Structure-Based Inhibitor Design

Ilić, B. S. (2026) · Biomolecules · doi:10.3390/biom16050734 · Cited by 1 · see citing works

Green tea extract EGCG plays a dual role in Aβ42 protofibril disruption and membrane protection: A molecular dynamic study

Dong, X., Tang, Y., Zhan, C., & Wei, G. (2020) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2020.105024 · Cited by 34 · see citing works

Insights into Molecular Mechanisms of EGCG and Apigenin on Disrupting Amyloid-Beta Protofibrils Based on Molecular Dynamics Simulations

Fang, M., Zhang, Q., Guan, P., Su, K., Wang, X., & Hu, X. (2022) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.2c04230 · Cited by 25 · see citing works

Structural Remodeling Mechanism of the Toxic Amyloid Fibrillary Mediated by Epigallocatechin-3-gallate

Zhang, N., Yan, C., Yin, C., Hu, X., Guan, P., & Cheng, Y. (2022) · ACS Omega · doi:10.1021/acsomega.2c05995 · Cited by 13 · see citing works

Molecular insights into the structure destabilization effects of ECG and EC on the Aβ protofilament: An all-atom molecular dynamics simulation study

Nie, R., Zhang, S.-S., Yan, X.-K., Feng, K., Lao, Y.-J., & Bao, Y.-R. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.127002 · Cited by 9 · see citing works

CryoEM reveals how the small molecule EGCG binds to Alzheimer’s brain-derived tau fibrils and initiates fibril disaggregationPreprint

Seidler, P. M., Boyer, D. R., Sawaya, M. R., Ge, P., Shin, W., DeTure, M., Dickson, D. W., Jiang, L., & Eisenberg, D. S. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.05.29.124537 · Cited by 18 · see citing works