In Vitro Characterization of Conditions for Amyloid-β Peptide Oligomerization and Fibrillogenesis

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

Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease

Goate, A., Chartier-Harlin, M.-C., Mullan, M., Brown, J., Crawford, F., Fidani, L., Giuffra, L., Haynes, A., Irving, N., James, L., et al. (1991) · Nature · doi:10.1038/349704a0 · Cited by 4,659

Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo

Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291

Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins

Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6448 · Cited by 3,506

Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse

Schenk, D., Barbour, R., Dunn, W., Gordon, G., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., Khan, K., et al. (1999) · Nature · doi:10.1038/22124 · Cited by 3,160

Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

Bucciantini, M., Giannoni, E., Chiti, F., Baroni, F., Formigli, L., Zurdo, J., Taddei, N., Ramponi, G., Dobson, C. M., & Stefani, M. (2002) · Nature · doi:10.1038/416507a · Cited by 2,434

Mutation of the β-amyloid precursor protein in familial Alzheimer's disease increases β-protein production

Citron, M., Oltersdorf, T., Haass, C., McConlogue, L., Hung, A. Y., Seubert, P., Vigo-Pelfrey, C., Lieberburg, I., & Selkoe, D. J. (1992) · Nature · doi:10.1038/360672a0 · Cited by 1,757

Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy

Conway, K. A., Lee, S., Rochet, J., Ding, T. T., Williamson, R. E., & Lansbury, P. T. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.2.571 · Cited by 1,559

Soluble Amyloid β Peptide Concentration as a Predictor of Synaptic Change in Alzheimer's Disease

Lue, L.-F., Kuo, Y.-M., Roher, A. E., Brachova, L., Shen, Y., Sue, L., Beach, T., Kurth, J. H., Rydel, R. E., & Rogers, J. (1999) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)65184-x · Cited by 1,530

Formation of Neurofibrillary Tangles in P301L Tau Transgenic Mice Induced by Aβ42 Fibrils

Götz, J., Chen, F., van Dorpe, J., & Nitsch, R. M. (2001) · Science · doi:10.1126/science.1062097 · Cited by 1,526

Amyloid Beta sharply increases HMG-CoA reductase protein levels in astrocytes isolated from C57BL/6 mice

Cheraghzadeh, M., Nazeri, Z., Mohammadi, A., Azizidoost, S., Aberomand, M., & Kheirollah, A. (2021) · Gene Reports · doi:10.1016/j.genrep.2021.101070 · Cited by 7

β-Amyloid Peptide Binds Equivalently to Binary and Ternary α2-Macroglobulin–protease Complexes

Mettenburg, J., & Gonias, S. L. (2005) · The Protein Journal · doi:10.1007/s10930-004-1515-7 · Cited by 7

Tapping, pulling, probing: atomic force microscopy in drug discovery

Legleiter, J. A., & Kowalewski, T. (2004) · Drug Discovery Today Technologies · doi:10.1016/j.ddtec.2004.09.008 · Cited by 7

Enhanced G‐protein activation by a mixture of Aβ(25–35), Aβ(1–40/42) and zinc

Molnár, Z., Kovacs, P., Laczkó, I., Soós, K., Fülöp, L., Penke, B., & Lengyel, I. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02427.x · Cited by 7

Pathways to Amyloid Fibril Formation: Partially Folded Intermediates in the Fibrillation of Natively Unfolded Proteins

Uversky, V. N., & Fink, A. L. (2005) · Wiley eBooks · doi:10.1002/9783527619344.ch11 · Cited by 7

Human astrocytes from healthy individuals and Alzheimer’s patients respond differently to Aβ1–42 oligomers, triggering distinct paths of reactivity and senescence

Ristori, S., Bertoni, G., Bigi, A., Cecchi, C., Sollazzo, M., Iommarini, L., Monti, D., & Bientinesi, E. (2025) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2025.112116 · Cited by 6

Dissecting the behaviour of β‐amyloid peptide variants during oligomerization and fibrillation

Shi, J., Zhang, L., & Liu, E. (2017) · Journal of Peptide Science · doi:10.1002/psc.3028 · Cited by 6

Human Amyloid-β40 Kinetics after Intravenous and Intracerebroventricular Injections and Calcitriol Treatment in Rats In Vivo

Peng, H., Noh, K., Pan, S. R., Saldivia, V., Serson, S., Toscan, A., de Lannoy, I. A. M., & Pang, K. S. (2020) · Drug Metabolism and Disposition · doi:10.1124/dmd.120.090886 · Cited by 8

The Effect of Ethanol on Disassembly of Amyloid-β1-42 Pentamer Revealed by Atomic Force Microscopy and Gel Electrophoresis

Matsui, A., Bellier, J., Kanai, T., Satooka, H., Nakanishi, A., TERADA, T., Ishibe, T., Nakamura, Y., Taguchi, H., Naruse, N., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23020889 · Cited by 6

A Cationic Zn-Phthalocyanine Turns Alzheimer’s Amyloid β Aggregates into Non-Toxic Oligomers and Inhibits Neurotoxicity in Culture

Sheikh, A. M., Tabassum, S., Yano, S., Abdullah, F. B., Wang, R., Ikeue, T., & Nagai, A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25168931 · Cited by 6

Substituted Organosiloxanes as Potential Therapeutics for Treatment and Prevention of Neurodegenerative Diseases

Friedman, O. M., Matsudaira, P. T., Reis, A. H., Simister, N. E., Correia, I., Kew, D., Wei, J. Y., & Pochapsky, T. C. (2007) · Journal of Alzheimer s Disease · doi:10.3233/jad-2007-11304 · Cited by 6

Study of the Specific Lipid Binding Properties of Aβ 11−22 Fragment at Endosomal pH

Ravault, S., Flore, C., Saurel, O., Milon, A., Brasseur, R., & Lins, L. (2009) · Langmuir · doi:10.1021/la901544g · Cited by 6

Insights into the mechanism of Alzheimer’s β-amyloid aggregation as a function of concentration by using atomic force microscopy

Mustata, G.-M., Shekhawat, G. S., Lambert, M. P., Viola, K. L., Velasco, P. T., Klein, W. L., & Dravid, V. P. (2012) · Applied Physics Letters · doi:10.1063/1.3697682 · Cited by 6

Modified Roller Tube Method for Precisely Localized and Repetitive Intermittent Imaging During Long-term Culture of Brain Slices in an Enclosed System

Fixman, B. B., Babcock, I. W., Minamide, L. S., Shaw, A. E., da Silva, M. I. O., Runyan, A. M., Maloney, M. T., Field, J. J., & Bamburg, J. R. (2017) · Journal of Visualized Experiments · doi:10.3791/56436 · Cited by 6

Molecular Insight into Cu2+-Induced Conformational Transitions of Amyloid β-Protein from Fast Kinetic Analysis and Molecular Dynamics Simulations

Xu, S., Wang, W., Dong, X., & Sun, Y. P. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00502 · Cited by 6

Cellular prion protein offers neuroprotection in astrocytes submitted to amyloid β oligomer toxicity

Marques, C. M. S., Gomes, R. N., Pedron, T., Batista, B. L., & Cerchiaro, G. (2022) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-022-04631-w · Cited by 6

Links Between Amyloid and Tau Biology in Alzheimer’s Disease and Their Cholinergic Aspects

Siegel, G. J., Chauhan, N. B., & Karczma, A. G. (2007) · Springer eBooks · doi:10.1007/978-0-387-46526-5_10 · Cited by 6

Oligomerization and toxicity of Aβ fusion proteins

Caine, J. M., Bharadwaj, P. R., Sankovich, S. E., Ciccotosto, G. D., Streltsov, V. A., & Varghese, J. N. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.05.029 · Cited by 6

Cu2+ Effects on Beta‐Amyloid Oligomerisation Monitored by the Fluorescence of Intrinsic Tyrosine

Alghamdi, A., Wellbrock, T., Birch, D. J. S., Vyshemirsky, V., & Rolinski, O. J. (2019) · ChemPhysChem · doi:10.1002/cphc.201900565 · Cited by 6

Association of clusterin with the BRI2-derived amyloid molecules ABri and ADan

Rostagno, A. A., Calero, M., Holton, J. L., Révész, T., Lashley, T., & Ghiso, J. A. (2021) · Neurobiology of Disease · doi:10.1016/j.nbd.2021.105452 · Cited by 6

The Contribution of Microscopy to the Study of Alzheimer’s Disease, Amyloid Plaques and Aβ Fibrillogenesis

Harris, J. R. (2006) · Springer eBooks · doi:10.1007/0-387-23226-5_1 · Cited by 6

Interactions between gold nanoparticles and amyloid β 25–35 peptide

Peng, J., Weng, J., Ren, L., & Sun, L. (2014) · IET Nanobiotechnology · doi:10.1049/iet-nbt.2013.0071 · Cited by 6

Generation of hiPSC-derived brain microvascular endothelial cells using a combination of directed differentiation and transcriptional reprogramming strategiesPreprint

Cui, A.-M., Patel, R., Bosco, P., Akcan, U., Richters, E., Delgado, P., Agalliu, D., & Sproul, A. A. (2024) · bioRxiv · doi:10.1101/2024.04.03.588012 · Cited by 6

Validation of a functional human AD model with four AD therapeutics utilizing patterned ipsc-derived cortical neurons integrated with microelectrode arrays

Caneus, J., Autar, K., Akanda, N., Grillo, M., Long, C. J., Jackson, M., Lindquist, S., Guo, X., Morgan, D., & Hickman, J. J. (2024) · Scientific Reports · doi:10.1038/s41598-024-73869-9 · Cited by 6

Electrolyte-Gated Organic Field-Effect Transistor for Monitoring Amyloid Aggregation

Ruiz‐Molina, S., Martínez‐Domingo, C., Ricci, S., Casalini, S., & Mas‐Torrent, M. (2024) · ACS Applied Electronic Materials · doi:10.1021/acsaelm.4c01673 · Cited by 5

Microparticle immunocapture assay for quantitation of protein multimer amount and size

Gutknecht, M. F., Kaku, H., & Rothstein, T. L. (2022) · Cell Reports Methods · doi:10.1016/j.crmeth.2022.100214 · Cited by 5

Crystal Violet Selectively Detects Aβ Oligomers but Not Fibrils In Vitro and in Alzheimer’s Disease Brain Tissue

Karunarathne, K., Kee, T. R., Jeon, H., Cazzaro, S., Gamage, Y. I., Pan, J., Woo, J. A., Kang, D. E., & Muschol, M. (2024) · Biomolecules · doi:10.3390/biom14060615 · Cited by 5

The dynamic nature of incubation solution after cooling to room temperature in amyloid formation of hen egg white lysozyme: An FTIR assessment

Ma, G., Li, Y., Dong, J., Zou, Y., Zhang, Z., & Sun, Y. (2012) · Vibrational Spectroscopy · doi:10.1016/j.vibspec.2012.10.004 · Cited by 5

Rapid and high-throughput colorimetric screening for anti-aggregation reagents of protein conformational diseases by using gold nanoplasmonic particles

Kim, H. Y., Kwon, J. A., Kang, T., & Choi, I. (2017) · Nanomedicine Nanotechnology Biology and Medicine · doi:10.1016/j.nano.2017.01.004 · Cited by 5

Review: Investigating the aggregation of amyloid beta with surface plasmon resonance: Do different approaches yield different results?

Young, K. A., & Mancera, R. L. (2022) · Analytical Biochemistry · doi:10.1016/j.ab.2022.114828 · Cited by 5

Early Aggregation of Amyloid-β(1–42) Studied by Fluorescence Correlation Spectroscopy

Novo, M., Pérez‐González, C., Freire, S., & Al‐Soufi, W. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2597-2_1 · Cited by 5

The Effects of Amyloid-β on Metabolomic Profiles of Cardiomyocytes and Coronary Endothelial Cells

Jang, S., Chorna, N., Rodríguez‐Graciani, K. M., Inyushin, M. Y., Fossati, S., & Javadov, S. A. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-221199 · Cited by 5

Oligomers imaging of amyloid- β 1-42 by scanning tunneling microscopy

Naruse, N., Satooka, H., Todo, K., Nakanishi, A., Taguchi, H., & Mera, Y. (2019) · Japanese Journal of Applied Physics · doi:10.7567/1347-4065/ab203b · Cited by 5

What Can Atomic Force Microscopy Say About Amyloid Aggregates?

Relini, A., Cavalleri, O., Canale, C., Svaldo-Lanero, T., Rolandi, R., & Gliozzi, A. (2007) · Springer eBooks · doi:10.1007/978-3-540-74083-4_8 · Cited by 5

Modeling Amyloid Fibril Formation

Wolf, M. G., van Gestel, J., & de Leeuw, S. W. (2008) · Methods in molecular biology · doi:10.1007/978-1-59745-480-3_10 · Cited by 5

GSK-3beta inhibitory effects of 6-gingerol and 6-shogaol help to the recovery of SHSY-5Y cells after amyloid beta1–42 oligomer or aggregate toxicity

Yerer, M. B., Tiryaki, M., & Demirpolat, E. (2017) · Journal of Cellular Biotechnology · doi:10.3233/jcb-15035 · Cited by 5

Differential binding and activation of caspase‐3 in cultured hippocampal neurons by assembly forms of Aβ1–42

John, P. A. S. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21251 · Cited by 5

Structural and Functional Analysis of TREM2 Interactions with Amyloid Beta Reveal Molecular Mechanisms That Mediate Phagocytosis of Oligomeric Amyloid BetaPreprint

Greven, J. A., Osario, O., Nix, J. C., Alexander‐Brett, J. M., & Brett, T. J. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.05.23.595586 · Cited by 4

Neuroprotection against beta-amyloid toxicity by the novel estrogen receptor modulator STX requires convergent signaling pathways

Lee, H., Bostick, Z., Doherty, J., Swanson, T. L., Kelly, M. J., Quinn, J. F., Gray, N. E., & Copenhaver, P. F. (2025) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2025.1670646 · Cited by 8

Synthesis of fluorinated curcumin derivatives for detecting amyloid plaques by 19 F-MRI

Micocci, S., Stefanìa, R., Garello, F., Fasoglio, U., Hawala, I., Tei, L., Crich, S. G., & Digilio, G. (2024) · Organic & Biomolecular Chemistry · doi:10.1039/d4ob00730a · Cited by 4

Slow Release of Hydrogen Sulfide in CA1 Hippocampal Neurons Rescues Long-Term Synaptic Plasticity and Associativity in an Amyloid-β Induced Model of Alzheimer’s Disease

Manakkadan, A., Krishnan, D., Ang, S. R. X., & Sajikumar, S. (2024) · Journal of Alzheimer s Disease · doi:10.3233/jad-240456 · Cited by 4

Generation of hiPSC-Derived Brain Microvascular Endothelial Cells Using Directed Differentiation and Transcriptional Reprogramming

Cui, A., Patel, R., Bosco, P., Akcan, U., Richters, E., Delgado, P. B., Agalliu, D., & Sproul, A. A. (2025) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.125.323397 · Cited by 12

MicroRNA-29a-5p contributes to neuroinflammation through TLR7

McGurran, H., Graceffo, E., Kumbol, V. W.-A., Jendrach, M., Hinkelmann, L., Brehm, M., Ravatt, L. M., Krüger, C., Wallach, T., Haake, A., et al. (2026) · Journal of Neuroinflammation · doi:10.1186/s12974-025-03680-4 · Cited by 4

Nano C60 Promotes Synaptic Distribution of Phosphorylated CaMKIIα and Improves Cognitive Function in APP/PS1 Transgenic Mice

Dai, W., Zhao, M., Chen, C., Zhou, C., Wang, P., Yang, Z., Gao, S., Lu, Y., Zhang, J., & Liu, X. (2022) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.2c00569 · Cited by 4

Self-Assembly of Amyloid Fibrils into 3D Gel Clusters versus 2D Sheets

Karunarathne, K., Bushra, N., Williams, O., Raza, I., Tirado, L., Fakhre, D., Fakhre, F., & Muschol, M. (2023) · Biomolecules · doi:10.3390/biom13020230 · Cited by 4

Amyloid peptide hydrogels via formation of coordination polymers with Ag + by its core peptide equipped with a C-cysteine

Wang, Q., Zhou, F.-P., Tao, D.-D., Wei, J.-H., Cai, R., & Jiang, Y. (2023) · Chemical Communications · doi:10.1039/d3cc02076b · Cited by 4

Effects of Tanshinone IIA on Cognitive Impairment in Alzheimer’s Disease Rats Via Oxidative Stress, Inflammatory Responses and Apoptosis

Ren, W.-J., Li, X., Wang, T., Liu, Y., Dai, X., Huo, Q., Wang, S., Zheng, Q., & Sun, Y. (2024) · Pharmacognosy Magazine · doi:10.1177/09731296241246632 · Cited by 4

Reduced SH3RF3 May Protect Against Alzheimer's Disease by Lowering Microglial Pro‐Inflammatory Responses via Modulation of JNK and NFkB Signaling

Patel, R., Cheng, R., Cardona, C. L., Angeles, E., Singh, G., Miller, S., Ashok, A., Teich, A. F., Piriz, A. L., Maldonado, A., et al. (2026) · Glia · doi:10.1002/glia.70165 · Cited by 5

Co‐activation of Selective Nicotinic Acetylcholine Receptor Subtypes Is Required for Neuroprotection against Alzheimer's Disease

Lee, R., Kim, G., Black, E. R., & Kim, S. (2026) · Advanced Science · doi:10.1002/advs.77858 · Cited by 4

Non-pretreated O-acyl isopeptide of amyloid β peptide 1–42 is monomeric with a random coil structure but starts to aggregate in a concentration-dependent manner

Yoshiya, T., Maruno, T., Uemura, T., Kubo, S., Kiso, Y., Sohma, Y., Yoshizawa‐Kumagaye, K., Kobayashi, Y., & Nishiuchi, Y. (2014) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2014.06.052 · Cited by 4

p75NTR is mainly responsible for Aβ toxicity but not for its internalization: a primary study

Yu, H., Yang, M., Wang, Y., Xiao, R., & Zhou, X. (2011) · Neurological Sciences · doi:10.1007/s10072-011-0892-x · Cited by 4

Methods for Studying and Structure–Function Relationships of Non-Fibrillar Protein Assemblies in Alzheimer's Disease and Related Disorders

Bitan, F. R. A. G. (2014) · BENTHAM SCIENCE PUBLISHERS eBooks · doi:10.2174/9781608058525114020014 · Cited by 4

Induction of neuronal activation by femtosecond‐pulsed laser irradiation and its potential application for amyloid‐β–induced toxicity assessment

Lee, S., Yoon, J. W., Choi, M., & Choi, C. (2016) · Journal of Biophotonics · doi:10.1002/jbio.201600004 · Cited by 4

Stability and Inter-domain Interactions Modulate Amyloid Binding Activity of a General Amyloid Interaction Motif

Asp, E., Proschitsky, M., Lulu, M., Rockwell‐Postel, C., Tsubery, H., & Krishnan, R. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.03.022 · Cited by 4

The Interaction between Amyloid Prefibrillar Oligomers of Salmon Calcitonin and a Lipid-Raft Model: Molecular Mechanisms Leading to Membrane Damage, Ca2+-Influx and Neurotoxicity

Diociaiuti, M., Bombelli, C., Polzi, L. Z., Belfiore, M., Fioravanti, R., Macchia, G., & Giordani, C. (2019) · Biomolecules · doi:10.3390/biom10010058 · Cited by 4

Discovery of a dual pathway aggregation mechanism for a therapeutic constrained peptide

Chen, T., Tang, S., Hecht, E. S., Yen, C., Andersen, N., Chin, S., Cadang, L., Roper, B., Estevez, A., Rohou, A. L., et al. (2021) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2020.12.041 · Cited by 4

An enzyme-linked immunosorbent assay to compare the affinity of chemical compounds for β-amyloid peptide as a monomer

Jiang, C., Feng, Y., Huang, X., Xu, Y., Zhang, Y., Zhou, N., Shen, X., Chen, K., Jiang, H., & Liu, D. (2010) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-009-3420-6 · Cited by 4

Amyloid‐β concentration and structure influences the transport and immunomodulatory effects of IVIG

Wuest, D., & Lee, K. H. (2014) · Journal of Neurochemistry · doi:10.1111/jnc.12678 · Cited by 4

A chemically engineered, stable oligomer mimic of amyloid β42 containing an oxime switch for fibril formation

Yamamoto, M., Shinoda, K., Ni, J., Sasaki, D., Kanai, M., & Sohma, Y. (2018) · Organic & Biomolecular Chemistry · doi:10.1039/c8ob01875h · Cited by 4

Click Peptides: Design and Applications

Kiso, Y., Taniguchi, A., & Sohma, Y. (2008) · Wiley eBooks · doi:10.1002/9780470048672.wecb632 · Cited by 4

The insulin-degrading enzyme: from molecular evolution and subcellular localization to new roles in microglial physiology

Corraliza-Gómez, M. (2021) · UVaDOC UVaDOC University of Valladolid Documentary Repository (University of Valladolid) · doi:10.35376/10324/51889 · Cited by 4

In Vivo Seeding of Amyloid-β Protein and Implications in Modeling Alzheimer’s Disease Pathology

Liu, Q., Song, S., Liu, L., & Hong, W. (2025) · Biomolecules · doi:10.3390/biom15040571 · Cited by 5

GPR40 agonist ameliorates neurodegeneration by regulating mitochondria dysfunction and NLRP3 inflammasome in Alzheimer’s disease animal models

Ha, T.-Y., Kim, Y., Lim, S. M., Hong, Y., & Chang, K. (2025) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2025.118678 · Cited by 3

Protein Amyloid and Synthetic Polymer Self-Assemblies: Similar Challenges for Their Preparation Associated with Shared Properties

Lonetti, B., Bourgault, S., Chamieh, J., Cottet, H., Couderc, F., Mingotaud, C., Vicendo, P., Mingotaud, A., & Collin, F. (2026) · Biomacromolecules · doi:10.1021/acs.biomac.5c01931 · Cited by 3

Electron Transfer Mechanism–Mediated Host–Guest Nanoswitch Powered Amplification-Free CRISPR/Cas12a–Electrochemiluminescence Bioassay for Alzheimer’s Disease Diagnosis

Li, J., Chen, X., Yang, Y., Xu, Y., Lai, M., Shi, L., Lin, X., Chen, W., & Peng, H. (2026) · Analytical Chemistry · doi:10.1021/acs.analchem.5c06614 · Cited by 3

Elevated concentrations of amyloid‐β oligomers and their proapoptotic effects on age‐related cataract

Lin, P., Xu, J., Yang, F., Li, D., Zhang, R., Jiang, Y., & Zheng, T. (2024) · The FASEB Journal · doi:10.1096/fj.202301281rr · Cited by 3

Effect of Different Aβ Aggregates as Antigen on the Measure of Naturally Occurring Autoantibodies against Amyloid-β40/42 in IVIG

Cao, H., Du, X., Zeng, R., Lv, Z., Ye, S., Jiang, P., Wang, Z., Ma, L., Huang, Y., Li, C., et al. (2020) · Current Alzheimer Research · doi:10.2174/1567205017666200102151731 · Cited by 3

Amplifying Intermolecular Events by Streptavidin-Induced Proximity

Li, H., Liu, T., & Yang, H. (2022) · Journal of the American Chemical Society · doi:10.1021/jacs.2c03666 · Cited by 3

Application of 3D Printing Technology to Produce Hippocampal Customized Guide Cannulas

Tropea, M. R., Torrisi, A., Vacanti, V., Pizzone, D., Puzzo, D., & Gulisano, W. (2022) · eNeuro · doi:10.1523/eneuro.0099-22.2022 · Cited by 3

Extremophilic behavior of catalytic amyloids sustained by backbone structuring

Beasley, M. A., Dunkelberger, A. D., Thum, M. D., Ryland, E. S., Fears, K. P., Grafton, A. B., Owrutsky, J. C., Lundin, J. G., & So, C. R. (2022) · Journal of Materials Chemistry B · doi:10.1039/d2tb01605b · Cited by 3

Cyclic β-hairpin peptide loaded PLGA nanoparticles: A potential anti-amyloid therapeutic

Khairnar, B. D., Padhye, A., Madiwal, V., Jha, A., Jadhav, S. H., & Rajwade, J. M. (2023) · Materials Today Communications · doi:10.1016/j.mtcomm.2023.106322 · Cited by 3

The 3-(3-oxoisoindolin-1-yl)pentane-2,4-dione (ISOAC1) as a new molecule able to inhibit Amyloid β aggregation and neurotoxicity

Piccialli, I., Greco, F., Roviello, G. N., Sisalli, M. J., Tedeschi, V., Mola, A. D., Borbone, N., Oliviero, G., Feo, V. D., Secondo, A., et al. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115745 · Cited by 3

Challenges in Peptide Solubilization – Amyloids Case Study

Polańska, O., Szulc, N., Stottko, R., Olek, M., Nadwodna, J., Gąsior‐Głogowska, M., & Szefczyk, M. (2024) · The Chemical Record · doi:10.1002/tcr.202400053 · Cited by 3

Effects of Surface Coating on Nanoparticle-Protein Adsorption Selectivity

Khoury, L. R., Kost, J., & Enden, G. (2018) · Regenerative Engineering and Translational Medicine · doi:10.1007/s40883-018-0049-z · Cited by 3

Disaggregation of Aβ42 for Structural and Biochemical Studies

Chung, H., Crooks, E. J., Ziliox, M., & Smith, S. O. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-7811-3_20 · Cited by 3

Atomic Force Microscopy

Legleiter, J. A., & Kowalewski, T. (2007) · Springer eBooks · doi:10.1007/0-387-25919-8_16 · Cited by 3

Apolipoproteins in Different Amyloidoses

Sadowski, M., & Wısnıewskı, T. (2007) · Springer eBooks · doi:10.1007/0-387-25919-8_6 · Cited by 3

Cholesterol seco‐Sterol‐Induced Aggregation of Methylated Amyloid‐β Peptides—Insights into Aldehyde‐Initiated Fibrillization of Amyloid‐β

Scheinost, J. C., Wang, H., Boldt, G. E., Offer, J., & Wentworth, P. (2008) · Angewandte Chemie · doi:10.1002/ange.200705922 · Cited by 3

miR-449a mediated repression of the cell cycle machinery prevents neuronal apoptosis

Chauhan, M., Singh, K., Chongtham, C., Aneeshkumar, A. G., & Sharma, P. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107698 · Cited by 3

Modulation of CREB3L2-ATF4 heterodimerization via proteasome inhibition and HRI activation in Alzheimer’s disease pathology

Herline, K., Pauers, M. M., Lipponen, J. E., Zrzavy, M. A., Roque, C. G., McCurdy, E. P., Chung, K. M., & Hengst, U. (2025) · Cell Death and Disease · doi:10.1038/s41419-025-07586-0 · Cited by 2

Amyloidogenic SARS-CoV-2 Spike Protein-Derived Peptides Form Oligomers and Selectively Damage Lipid Membranes

Adewoye, A., Ezeigbo, E., Vo, Q., & Legleiter, J. A. (2025) · Biochemistry · doi:10.1021/acs.biochem.5c00290 · Cited by 2

Multiomics analysis reveals early administration of the Medhya rasayana formulation of Bacopa monnieri (L.) Wettst. and Centella asiatica (L.) Urb. prevents neuroinflammation and cognitive deficits in an AβO-injected AD mouse model

Maruthiyodan, S., Munegowda, G., Thomas, M., Gangadharan, G., Joshi, M. B., Mumbrekar, K. D., Goyal, A., Mahadevan, A., Anandan, E. M., Sankaran, M. T., et al. (2025) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2025.120633 · Cited by 5

Rosavin and salidroside attenuate microglia injury via nuclear factor κ -B signaling pathway

Liu, H., Ma, Y., Chen, Q., Dai, Y., Wang, Y., Huang, H., Yao, Z., Yan, C., & Shi, J. (2025) · Journal of Pharmacy and Pharmacology · doi:10.1093/jpp/rgaf094 · Cited by 2

The uptake of β-amyloid by various brain cells exhibits heterogeneity and correlates with the CD14 expression

Shi, J., Ma, Y., Gao, L., Dai, Y., Chen, Q., Li, X., Liu, H., Li, R., Zhang, J., & Yan, C. (2025) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2025.111699 · Cited by 2

Pterostilbene targets microglia-mediated neuroinflammation for Alzheimer’s therapy

Chen, F., Lv, X., Xiang, K., Lin, X., Dai, C., Wei, C., Zhang, Y., Liu, J., & Li, J. (2026) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2026.110382 · Cited by 2

PYGL-driven glycogenolysis impairs microglial autophagic flux via SNAP29 O-GlcNAcylation in Alzheimer's disease

Ding, Y., Li, S.-Y., Zhang, W.-F., Chu, M.-M., Wang, X.-J., Zhang, Y., Zhang, H., Zhang, Y., Xu, L., Liu, X., et al. (2026) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2026.04.017 · Cited by 2

Targeting the microglial phosphatidylethanolamine synthesis pathway promotes GABARAP-associated phagocytosis and Aβ clearance in Alzheimer’s disease

Hyeon, S. J., Kim, S. C., Chu, J., Kim, Y., Kim, C., Park, U., Tufail, Z., Nguyen, P. T., Eom, A., Kim, S., et al. (2026) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-026-02789-z · Cited by 2

A Signal-Enhanced Regenerative Electrochemical Aptasensor for Amyloid-β Oligomers Based on Triple-Helix Aptamer Probe

Hu, J., Chen, X., Xu, J., & Wang, X. (2023) · Journal of The Electrochemical Society · doi:10.1149/1945-7111/acb5c5 · Cited by 2

The Amyloid Beta Aggregation Inhibition Properties of New Pt (II) Complexes and Their Potential in Alzheimer's Treatment

Günnaz, S., Şahın, O., & İrişli, S. (2025) · Applied Organometallic Chemistry · doi:10.1002/aoc.70159 · Cited by 2

Structure–Function Studies of Amyloid Pores in Alzheimer’s Disease as a Case Example of Neurodegenerative Diseases

Arce, F. T., Jang, H., Connelly, L. S., Ramachandran, S., Kagan, B. L., Nussinov, R., & Lal, R. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-394431-3.00036-5 · Cited by 3

Insights into amyloid disease from fly models

Chen, K., & Crowther, D. C. (2014) · Essays in Biochemistry · doi:10.1042/bse0560069 · Cited by 2

Effect of Ionic Strength on the Aggregation Propensity of Aβ1-42 Peptide: An In-silico Study

Borah, P., & Mattaparthi, V. S. K. (2020) · Current Chemical Biology · doi:10.2174/2212796814999200818103157 · Cited by 2

Generation and study of antibodies against two triangular trimers derived from Aβ

Kreutzer, A. G., Malonis, R. J., Parrocha, C. M. T., Tong, K., Guaglianone, G., Nguyen, J. T., Diab, M. N., Lai, J. R., & Nowick, J. S. (2023) · Peptide Science · doi:10.1002/pep2.24333 · Cited by 2

Systematic study of amyloid beta peptide conformations: Implications for alzheimer's disease

Jimenez, J. P. (2005) · Digital Commons - University of South Florida (University of South Florida) · Cited by 2

Pyk2 Overexpression in Postsynaptic Neurons Blocks Aβ 1-42 -induced Synaptotoxicity in a Microfluidic Co-Culture ModelPreprint

Kilinc, D., Vreulx, A.-C., Mendes, T., Flaig, A., Coelho, D. M., Verschoore, M., Demiautte, F., Amouyel, P., Bank, N.-C. B., Eysert, F., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2019.12.20.884205 · Cited by 2

SSRI antidepressants and SIADH.

Ayonrinde, O. T., & Sanfilippo, F. M. (1997) · PubMed · Cited by 2

Microenvironment Drives Reentrant Condensation of Aβ40Preprint

Sarkar, S., & Mondal, J. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.04.27.591429 · Cited by 2

Hemoglobin as a peroxidase and drug target for oxidative stress-related diseasesPreprint

Won, W., Lee, E. H., Gotina, L., Chun, H., Lee, J.-H., Park, U., Kim, D., Kim, T. Y., Choi, J. W., Kim, Y., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.05.21.594979 · Cited by 2

β-Amyloid impairs Proteasome structure and function. Proteasome activation mitigates amyloid induced toxicity and cognitive deficitsPreprint

Davidson, K., Bano, M., Parker, D. J., Rodriguez, K., Osmulski, P. A., Gaczynska, M. E., & Pickering, A. M. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.23.619877 · Cited by 2

Amyloid beta is released by lysosomal exocytosis from hiPSC-derived neuronsPreprint

Tsang, A. R., Medapati, M. R., Seah, C., Krupa, J. M., & Pasternak, S. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.03.01.640950 · Cited by 2

Oligomeric and fibrillar species of amyloid-β peptides differentially affect neuronal viability

Dahlgren, K. N., Manelli, A. M., Stine, W. B., Baker, L. K., Krafft, G. A., & LaDu, M. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201750200 · Cited by 1,452

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

P1‐167: Effects of beta‐amyloid oligomers on neuronal viability and microglial activation

Ferrera, D., Canale, C., Benfenati, F., & Gasparini, L. (2009) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2009.04.173

The Alzheimer's Amyloid-β(1–42) Peptide Forms Off-Pathway Oligomers and Fibrils That Are Distinguished Structurally by Intermolecular Organization

Tay, W. M., Huang, D., Rosenberry, T. L., & Paravastu, A. K. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.04.003 · Cited by 111

Conformational Differences between Two Amyloid β Oligomers of Similar Size and Dissimilar Toxicity

Ladiwala, A. R. A., Litt, J., Kane, R. S., Aucoin, D., Smith, S. O., Ranjan, S., Davis, J., Nostrand, W. E. V., & Tessier, P. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.329763 · Cited by 228