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

The Clustering of mApoE Anti-Amyloidogenic Peptide on Nanoparticle Surface Does Not Alter Its Performance in Controlling Beta-Amyloid Aggregation

Corti, R., Cox, A., Cassina, V., Nardo, L., Salerno, D., Marrano, C. A., Missana, N., Andreozzi, P., Silva, P. J., Stellacci, F., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21031066 · Cited by 13

1MeTIQ Provides Protection Against Aβ-Induced Reduction of Surface Expression of Synaptic Proteins and Inhibits H2O2-Induced Oxidative Stress in Primary Hippocampal Neurons

Kuszczyk, M. A., Sadowski, M. J., Antkiewicz‐Michaluk, L., & Łazarewicz, J. W. (2013) · Neurotoxicity Research · doi:10.1007/s12640-013-9440-1 · Cited by 13

Effects of amyloid peptides on A-type K+ currents ofDrosophila larval cholinergic neurons

Kidd, J. F., Brown, L. A., & Sattelle, D. B. (2006) · Journal of Neurobiology · doi:10.1002/neu.20227 · Cited by 13

1,25‐Dihydroxy Vitamin D3 Facilitates the M2 Polarization and β‐Amyloid Uptake by Human Microglia in a TREM2‐Dependent Manner

Thu, V. T. A., Hoang, T. X., & Kim, J. Y. (2023) · BioMed Research International · doi:10.1155/2023/3483411 · Cited by 12

Current progress in aptamer-based sensors for the detection of protein biomarkers in neurodegenerative diseases

Cheng, T., Afshan, N., Jiao, J., & Jiao, J. (2024) · Biosensors and Bioelectronics X · doi:10.1016/j.biosx.2024.100528 · Cited by 12

Ultrafast colorimetric determination of predominant protein structure evolution with gold nanoplasmonic particles

Kim, H. Y., & Choi, I. (2015) · Nanoscale · doi:10.1039/c5nr06517h · Cited by 12

A Weakly Clustered N terminus Inhibits Aβ(1–40) Amyloidogenesis

Lim, K. H. (2006) · ChemBioChem · doi:10.1002/cbic.200600270 · Cited by 12

Modeling Amyloid-Beta as Homogeneous Dodecamers and in Complex with Cellular Prion Protein

Gallion, S. L. (2012) · PLoS ONE · doi:10.1371/journal.pone.0049375 · Cited by 14

Autophagy-ERK1/2-Involved Disinhibition of Hippocampal Neurons Contributes to the Pre-Synaptic Toxicity Induced by Aβ 42 Exposure

Yin, Y., Zhao, Y., Han, S., Zhang, N., Chen, H., & Wang, X. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170246 · Cited by 12

Acetylation of Aβ 40 Alters Aggregation in the Presence and Absence of Lipid Membranes

Pilkington, A. W., Schupp, J. E., Nyman, M., Valentine, S. J., Smith, D. M., & Legleiter, J. A. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00483 · Cited by 12

A conformation-specific antibody against oligomeric β-amyloid restores neuronal integrity in a mouse model of Alzheimer's disease

He, P., Schulz, P., & Sierks, M. R. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.015327 · Cited by 11

An adjustable amyloid-β oligomers aptasensor based on the synergistic effect of self-enhanced metal-organic gel luminophore and triple-helix DNA system

Wang, X., Chen, R., Hu, J., & Yuan, W. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.09.182 · Cited by 13

Alzheimer amyloid-β peptides block the activation of C/EBPβ and C/EBPδ in glial cells

Samuelsson, M., Ramberg, V., & Iverfeldt, K. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.03.150 · Cited by 12

Reciprocal modulation of Aβ42 aggregation by copper and homocysteine

Keskitalo, S., Farkas, M., Hanenberg, M., Szodorai, A., Kulic, L., Semmler, A., Weller, M., Nitsch, R. M., & Linnebank, M. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00237 · Cited by 13

82-kDa choline acetyltransferase and SATB1 localize to β-amyloid induced matrix attachment regions

Winick‐Ng, W., Caetano, F. A., Winick‐Ng, J., Morey, T. M., Heit, B., & Rylett, R. J. (2016) · Scientific Reports · doi:10.1038/srep23914 · Cited by 13

Evaluation of a DNA Aβ 42 Vaccine in Aged NZW Rabbits: Antibody Kinetics and Immune Profile after Intradermal Immunization with Full-Length DNA Aβ 42 Trimer

Lambracht‐Washington, D., Fu, M., Wight‐Carter, M., Riegel, M. S., & Rosenberg, R. N. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-160947 · Cited by 12

Rapid, Refined, and Robust Method for Expression, Purification, and Characterization of Recombinant Human Amyloid beta 1-42

Prakash, P., Lantz, T. C., Jethava, K. P., & Chopra, G. (2019) · Methods and Protocols · doi:10.3390/mps2020048 · Cited by 12

Effects of Physical Damage in the Intermediate Phase on the Progression of Amyloid β Fibrillization

Tashiro, R., Taguchi, H., Hidaka, K., Endo, M., & Sugiyama, H. (2019) · Chemistry - An Asian Journal · doi:10.1002/asia.201901193 · Cited by 12

Amyloid Metabolism and Amyloid-Targeting Blood-Based Biomarkers of Alzheimer’s Disease

Pyun, J., Kang, M. J., Ryoo, N., Suh, J., Youn, Y. C., Park, Y. H., & Kim, S. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-200104 · Cited by 11

Propolis Promotes Memantine-Dependent Rescue of Cognitive Deficits in APP-KI Mice

Moriguchi, S., Inagaki, R., Saito, T., Saido, T. C., & Fukunaga, K. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-02876-6 · Cited by 14

Luminometric Nanoparticle-Based Assay for High Sensitivity Detection of β-Amyloid Aggregation

Pihlasalo, S., Deguchi, T., Virtamo, M., Jacobino, J., Chary, K., Lopez‐Picon, F. R., Brunhofer, G., Huttunen, R. J., Fallarero, A., Vuorela, P. M., et al. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.6b04266 · Cited by 12

Shifting the balance: soluble ADAM10 as a potential treatment for Alzheimer's disease

Hershkovits, A. S., Gelley, S., Hanna, R., Kleifeld, O., Shulman, A., & Fishman, A. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1171123 · Cited by 12

Dynamic properties of pH-dependent structural organization of the amyloidogenic β-protein (1-40)

Rubinstein, A. I., Lyubchenko, Y. L., & Sherman, S. (2009) · Prion · doi:10.4161/pri.3.1.8388 · Cited by 11

A label-free high-throughput protein solubility assay and its application to Aβ40

Lindberg, M., Axell, E., Sparr, E., & Linse, S. S. (2024) · Biophysical Chemistry · doi:10.1016/j.bpc.2023.107165 · Cited by 13

Nonfibrillar Abeta1–42 Inhibits Glutamate Uptake and Phosphorylates p38 in Human Fibroblasts

Zoia, C., Riva, C., Isella, V., Proserpio, P., Terruzzi, A., Arban, S., Salerno, D., Cassina, V., Mantegazza, F., Tremolizzo, L., et al. (2010) · Alzheimer Disease & Associated Disorders · doi:10.1097/wad.0b013e3181f9860f · Cited by 11

The role of calsyntenin‐3 in dystrophic neurite formation in A lzheimer's disease brain

Uchida, Y., & Gomi, F. (2016) · Geriatrics and gerontology international/Geriatrics & gerontology international · doi:10.1111/ggi.12737 · Cited by 11

Identification of an acute functional cross-talk between amyloid-β and glucocorticoid receptors at hippocampal excitatory synapses

Kootar, S., Frandemiche, M., Dhib, G., Mouska, X., Lorivel, T., Poupon, G., Hunt, H., Tronche, F., Bethus, I., Barik, J., et al. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.07.001 · Cited by 11

Impaired hippocampal and thalamic acetylcholine release in P301L tau-transgenic mice

Stein, C., Koch, K. A., Hopfeld, J., Lobentanzer, S., Lau, H., & Klein, J. (2019) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2019.07.014 · Cited by 11

Scutellaria barbata Leaf Extract Mediated Gold Nanoparticles for Alzheimer’s Disease Treatment by Metal-Induced Amyloid β Aggregation Inhibition

Wang, G., Dai, J., & Lu, X. (2019) · Journal of Cluster Science · doi:10.1007/s10876-019-01735-0 · Cited by 11

Effect of Zhenxin Xingshui Yizhi Fang on Aβ25-35 induced expression of related transporters in HBMEC cell model

Wu, L., Zheng, Q., Guo, Y., Zhang, K., Luo, J., Xiao, S., Li, W., & Yang, M. (2020) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2020.112783 · Cited by 11

Inhibition of aggregation of amyloid-β through covalent modification with benzylpenicillin; potential relevance to Alzheimer's disease

Alsalahat, I., Al‐Majdoub, Z. M., Taha, M. O., Barber, J., Aojula, H. S., Hodson, N. W., & Freeman, S. (2021) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2021.100943 · Cited by 11

Cytotoxic Intermediates in the Fibrillation Pathway: Aβ Oligomers in Alzheimer’s Disease as a Case Study

Klein, W. L. (2007) · Springer eBooks · doi:10.1007/0-387-25919-8_4 · Cited by 11

Nanoparticles for Diagnosis and/or Treatment of Alzheimer's Disease

Antimisiaris, S. G., Mourtas, S., Markoutsa, E., Σκούρας, Α., & Παπαδιά, Κ. (2014) · Advanced Healthcare Materials · doi:10.1002/9781118774205.ch4 · Cited by 11

Role of Alginate Composition on Copper Ion Uptake in the Presence of Histidine or Beta-Amyloid

Mahl, C. R. A., Bataglioli, R. A., Calais, G. B., Taketa, T. B., & Beppu, M. M. (2022) · Molecules · doi:10.3390/molecules27238334 · Cited by 10

Inducers and modulators of protein aggregation in Alzheimer's disease - Critical tools for understanding the foundations of aggregate structures

Sun, K. T., & Mok, S. (2025) · Neurotherapeutics · doi:10.1016/j.neurot.2024.e00512 · Cited by 12

Noninvasive label-free nanoplasmonic optical imaging for real-time monitoring of in vitro amyloid fibrogenesis

Lee, S. S., & Lee, L. P. (2014) · Nanoscale · doi:10.1039/c3nr06269d · Cited by 10

A New Caged‐Glutamine Derivative as a Tool To Control the Assembly of Glutamine‐Containing Amyloidogenic Peptides

Awad, L., Jejelava, N., Burai, R., & Lashuel, H. A. (2016) · ChemBioChem · doi:10.1002/cbic.201600474 · Cited by 10

Pretreatment of PC12 Cells with 17β-estradiol Prevents Aβ-Induced Down-Regulation of CREB Phosphorylation and Prolongs Inhibition of GSK-3β

Chen, Y., Su, Y., Run, X., Sun, Z., Wang, T., Sun, S., & Liang, Z. (2012) · Journal of Molecular Neuroscience · doi:10.1007/s12031-012-9938-7 · Cited by 10

Human eukaryotic elongation factor 1A forms oligomers through specific cysteine residues

Liu, T., Yu, Y., Wang, D., Xiao, Y., Du, G., Wu, L., Ding, M., Li, L., & Wu, C. (2015) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmv113 · Cited by 10

The Amyloid Aggregation Accelerator Diacetyl Prevents Cognitive Decline in Alzheimer’s Mouse Models

Xie, W., Kim, K., Vince, R., & More, S. S. (2021) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.1c00089 · Cited by 11

Concurrence of Danish Dementia and Cataract: Insights from the Interactions of Dementia Associated Peptides with Eye Lens α-Crystallin

Surolia, I., Sinha, S., Sarkar, D. P., Reddy, P. Y., Reddy, G. B., & Surolia, A. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002927 · Cited by 10

Conformational Behavior and Aggregation of Ataxin-3 in SDS

Saunders, H., Hughes, V. A., Cappai, R., & Bottomley, S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0069416 · Cited by 9

Flow of essential elements in subcellular fractions during oxidative stress

Lago, L., Nunes, E. A., Vigato, A. A., Souza, V. C. O., Barbosa, F., Sato, J. R., Batista, B. L., & Cerchiaro, G. (2017) · BioMetals · doi:10.1007/s10534-016-9988-3 · Cited by 10

Probing the putative α7 nAChR/NMDAR complex in human and murine cortex and hippocampus: Different degrees of complex formation in healthy and Alzheimer brain tissue

Elnagar, M. R., Walls, A. B., Helal, G. K., Hamada, F. M. A., Thomsen, M. S., & Jensen, A. A. (2017) · PLoS ONE · doi:10.1371/journal.pone.0189513 · Cited by 11

Role of Membrane Tension Sensitive Endocytosis and Rho GTPases in the Uptake of the Alzheimer’s Disease Peptide Aβ(1-42)

Wesén, E. V., Lundmark, R., & Esbjörner, E. K. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00053 · Cited by 9

Protein Folding

Szilágyi, A., Kardos, J., Osváth, S., Barna, L., & Závodszky, P. (2007) · Springer eBooks · doi:10.1007/978-0-387-30379-6_10 · Cited by 10

Alzheimer's disease protein Aβ1–42 does not disrupt isolated synaptic vesicles

Allen, P. B., & Chiu, D. T. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2008.02.002 · Cited by 10

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

Compound (E)-2-(3,4-dihydroxystyryl)-3-hydroxy-4H-pyran-4-one downregulation of Galectin-3 ameliorates Aβ pathogenesis-induced neuroinflammation in 5 × FAD mice

Liu, X., Chen, P., Wu, W., Zhong, M., Dong, S., Lin, H., Dai, C., Zhang, Z., Lin, S., Che, C., et al. (2024) · Life Sciences · doi:10.1016/j.lfs.2024.123085 · Cited by 9

Distinct effects of SDC3 and FGFRL1 on selective neurodegeneration in AD and PD

Wang, J., Chen, P., Hu, B., Cai, F., Xu, Q., Pan, S., Wu, Y., & Song, W. (2023) · The FASEB Journal · doi:10.1096/fj.202201359r · Cited by 10

EPR Studies of Aβ42 Oligomers Indicate a Parallel In-Register β-Sheet Structure

Jang, C., Barron, D. P., Duo, L., Ma, C., Seabaugh, H., & Guo, Z. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00364 · Cited by 9

Adverse Effects of Aβ1-42 Oligomers: Impaired Contextual Memory and Altered Intrinsic Properties of CA1 Pyramidal Neurons

Min-Kaung-Wint-Mon, Kida, H., Kanehisa, I., Kurose, M., Ishikawa, J., Sakimoto, Y., Paw-Min-Thein-Oo, Kimura, R., & Mitsushima, D. (2024) · Biomolecules · doi:10.3390/biom14111425 · Cited by 8

PrP106-126 and Aβ1-42 Peptides Induce BV-2 Microglia Chemotaxis and Proliferation

Tu, J., Yang, L., Zhou, X., Qi, K., Wang, J., Kouadir, M., Xu, L., Yin, X., & Zhao, D. (2013) · Journal of Molecular Neuroscience · doi:10.1007/s12031-013-0140-3 · Cited by 9

Oligomerization Alters Binding Affinity between Amyloid Beta and a Modulator of Peptide Aggregation

Hilt, S., Rojalin, T., Viitala, T., Koivuniemi, A., Bunker, A., Wachsmann‐Hogiu, S., Kálai, T., Hideg, K., Yliperttula, M. L., & Voss, J. C. (2017) · The Journal of Physical Chemistry C · doi:10.1021/acs.jpcc.7b06164 · Cited by 9

Mutual structural effects of unmodified and pyroglutamylated amyloid β peptides during aggregation

Abedin, F., & Tatulian, S. A. (2021) · Journal of Peptide Science · doi:10.1002/psc.3312 · Cited by 9

Kinetic and thermodynamic insights into the interaction of Aβ1–42 with astaxanthin and aggregation behavior of Aβ1–42: Surface plasmon resonance, microscopic, and molecular docking studies

Dehghani, M., Jalal, R., & Rashidi, M. (2021) · Biophysical Chemistry · doi:10.1016/j.bpc.2021.106612 · Cited by 9

Slingshot homolog-1 amplifies mitochondrial abnormalities by distinctly impairing health and clearance of mitochondria

Cazzaro, S., Zhao, X., Zhao, V. K., Kim, Y. K., & Woo, J. A. (2023) · Human Molecular Genetics · doi:10.1093/hmg/ddad006 · Cited by 9

SorCS1 inhibits amyloid-β binding to neurexin and rescues amyloid-β–induced synaptic pathology

Lee, A. K., Yi, N., Khaled, H., Feller, B., Chofflet, N., & Takahashi, H. (2023) · Life Science Alliance · doi:10.26508/lsa.202201681 · Cited by 11

Effect on memory of acute administration of naturally secreted fibrils and synthetic amyloid-beta peptides in an invertebrate model

Feld, M., Galli, C., Piccini, A., & Romano, A. G. (2007) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2007.08.011 · Cited by 9

Microtubule modification influences cellular response to amyloid-β exposure

Shamitko-Klingensmith, N. M., Boyd, J. W., & Legleiter, J. A. (2016) · AIMS Biophysics · doi:10.3934/biophy.2016.2.261 · Cited by 9

How Salt and Temperature Drive Reentrant Condensation of Aβ40

Sarkar, S., & Mondal, J. (2024) · Biochemistry · doi:10.1021/acs.biochem.4c00412 · Cited by 8

Novel Copper Chelators Enhance Spatial Memory and Biochemical Outcomes in Alzheimer’s Disease Model

Camargo, M. L. M., Farias, A. B., Bertazzo, G. B., Gomes, R. N., Gomes, K. S., Bosquetti, L. M., Takada, S. H., Braga, F. C., Augusto, C. C., Batista, B. L., et al. (2025) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5c00291 · Cited by 8

The effect of neuroprotector isatin on binding of some model proteins with beta-amyloid peptide: a biosensor study

Бунеева, О. А., Gnedenko, O. V., Medvedeva, M. V., Ivanov, A. S., & Medvedev, A. E. (2016) · Biomeditsinskaya Khimiya · doi:10.18097/pbmc20166206720 · Cited by 8

Preparation and Characterization of Zn(II)-Stabilized Aβ42 Oligomers

Díaz, A. G., Cataldi, R., Mannini, B., & Vendruscolo, M. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.4c00084 · Cited by 10

Penetratin and Mannose-Functionalized Cannabidiol Lipid Nanoparticles Encapsulating the BDNF Gene Reduce Amyloid-Induced Inflammation

Chaulagain, B., & Singh, J. (2024) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.4c00811 · Cited by 10

Amyloid-β oligomers drive amyloid deposit and cascaded tau pathology of Alzheimer's disease in aged brains of non-human primates

He, Z., Zhang, W., Chen, P., Li, S., Tao, M., Yue, F., Hong, W., Feng, S., & Jing, N. (2025) · Journal of genetics and genomics/Journal of Genetics and Genomics · doi:10.1016/j.jgg.2025.02.007 · Cited by 9

Amyloid β Instigates Cardiac Neurotrophic Signaling Impairment, Driving Alzheimer's Associated Heart Disease

Elia, A., Parodi‐Rullán, R. M., Vázquez‐Torres, R., Carey, A. M., Zhao, H., Javadov, S. A., & Fossati, S. (2026) · Advanced Science · doi:10.1002/advs.202511924 · Cited by 9

Nanomechanics of Amyloid Materials Studied by Atomic Force Microscopy

Zeng, G., Duan, Y., Besenbacher, F., & Dong, M. (2012) · InTech eBooks · doi:10.5772/36342 · Cited by 8

Effect of the Surface Chemistry of Insulin Fibrils on the Aggregation Rate

Hsieh, S., Hsieh, C., Chou, H., Chang, C., & Chu, L. (2013) · ChemPhysChem · doi:10.1002/cphc.201300838 · Cited by 8

Intracellular Cleavage of Amyloid β by a Viral Protease NIa Prevents Amyloid β-Mediated Cytotoxicity

Shin, B., Oh, H., Park, S. M., Han, H.-E., Ye, M., Song, W. K., & Park, W. J. (2014) · PLoS ONE · doi:10.1371/journal.pone.0098650 · Cited by 8

Regulation of IL-1β-Induced Cyclooxygenase-2 Expression by Interactions of Aβ Peptide, Apolipoprotein E and Nitric Oxide in Human Neuroglioma

Samy, A. S., & Igwe, O. J. (2011) · Journal of Molecular Neuroscience · doi:10.1007/s12031-011-9670-8 · Cited by 8

Rapid size-exclusion high performance liquid chromatography method for the quality control of amyloid-β oligomers

Fontana, I. C., Ferreira, P. C. L., Miron, D., Santos, L. E., Ferreira, S. T., Souza, D. O., Gosmann, G., Zimmer, E. R., & Zimmer, A. R. (2021) · Journal of Chromatography A · doi:10.1016/j.chroma.2021.462024 · Cited by 8

Probing Amyloid Nanostructures Using Photoluminescent Metal Complexes

Jiang, B., & Martı́, A. A. (2021) · European Journal of Inorganic Chemistry · doi:10.1002/ejic.202100422 · Cited by 8

TSPO Modulates Oligomeric Amyloid-β-Induced Monocyte Chemotaxis: Relevance for Neuroinflammation in Alzheimer’s Disease

Conti, E., ImmunAD-Brianza Network, Grana, D., Angiulli, F., Karantzoulis, A., Villa, C., Combi, R., Appollonio, I. M., Ferrarese, C., & Tremolizzo, L. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-230239 · Cited by 8

Proteasome Inhibition Augments New Protein Accumulation Early in Long-Term Synaptic Plasticity and Rescues Adverse Aβ Effects on Protein Synthesis

Haynes, K. A., Smith, T. K., Preston, C. J., & Hegde, A. N. (2015) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5b00068 · Cited by 8

Assessing Aβ Aggregation State by Atomic Force Microscopy

Legleiter, J. A. (2010) · Methods in molecular biology · doi:10.1007/978-1-60761-744-0_5 · Cited by 8

Evidence from ITIR-FCS Diffusion Studies that the Amyloid-Beta (Aβ) Peptide Does Not Perturb Plasma Membrane Fluidity in Neuronal Cells

Ng, J. T. Y., Kamm, R. D., Wohland, T., & Kraut, R. S. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.04.030 · Cited by 8

Occurrence of Biased Conformations as Precursors of Assembly States in Fibril Elongation of Amyloid-β Fibril Variants: An In Silico Study

Frigori, R. B., da Silva, F. L. B., Carvalho, P. P. D., & Alves, N. A. (2020) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.0c01360 · Cited by 8

The Amyloid-β-SDR5C1(ABAD) Interaction Does Not Mediate a Specific Inhibition of Mitochondrial RNase P

Vilardo, E., & Rossmanith, W. (2013) · PLoS ONE · doi:10.1371/journal.pone.0065609 · Cited by 8

Thiosemicarbazonate Complexes with Affinity for amyloid-β Fibers: Synthesis, Characterization and Biological Studies

Pino‐Cuevas, A., Raposinho, P., Fernandes, C., Paulo, A., Abram, U., Carballo, R., & Vázquez-López, E. M. (2019) · Future Medicinal Chemistry · doi:10.4155/fmc-2019-0013 · Cited by 8

Investigation of the self-assembly of hydrophobic self-complementary ionic tetrapeptides

Desii, A., Duce, C., Ghezzi, L., Monti, S., Solaro, R., & Tinè, M. R. (2009) · Journal of Thermal Analysis and Calorimetry · doi:10.1007/s10973-009-0277-z · Cited by 8

Soluble CSF1R promotes microglial activation and amyloid clearance in Alzheimer’s disease

Zhang, L., Chen, K., Zeng, R., Bu, G., & Chen, X.-F. (2025) · Journal of Neuroinflammation · doi:10.1186/s12974-025-03558-5 · Cited by 7

Light on Alzheimer’s disease: from basic insights to preclinical studies

Mi, J., Liu, C., Chen, H., Qian, Y., Zhu, J., Zhang, Y., Liang, Y., Wang, L., & Ta, D. (2024) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2024.1363458 · Cited by 8

Elevated Levels of Naturally-Occurring Autoantibodies Against the Extracellular Domain of p75NTR Aggravate the Pathology of Alzheimer’s Disease

He, C.-Y., Tian, D., Chen, S.-H., Jin, W., Cheng, Y., Xin, J., Li, W., Zeng, G., Tan, C., Jian, J.-M., et al. (2022) · Neuroscience Bulletin · doi:10.1007/s12264-022-00936-4 · Cited by 8

Locally Synthetized 17-β-Estradiol Reverses Amyloid-β-42-Induced Hippocampal Long-Term Potentiation Deficits

Bellingacci, L., Canonichesi, J., Sciaccaluga, M., Megaro, A., Mazzocchetti, P., Mauro, M. D., Costa, C., Filippo, M. D., Pettorossi, V. E., & Tozzi, A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25031377 · Cited by 7

PHPB ameliorates memory deficits and reduces oxidative injury in Alzheimer’s disease mouse model by activating Nrf2 signaling pathway

Shang, N.-Y., Huang, L., Lan, J., Kang, Y.-Y., Tang, J., Wang, H., Li, X., Sun, Z., Chen, Q.-Y., Liu, M., et al. (2024) · Acta Pharmacologica Sinica · doi:10.1038/s41401-024-01240-9 · Cited by 7

Cell invasive amyloid assemblies from SARS-CoV-2 peptides can form multiple polymorphs with varying neurotoxicity

Sanislav, O., Tetaj, R., Metali, Ratcliffe, J., Phillips, W., Klein, A. R., Sethi, A., Zhou, J., Mezzenga, R., Saxer, S., et al. (2024) · Nanoscale · doi:10.1039/d4nr03030c · Cited by 7

Amyloid capture and aggregation inhibition by human serum albumin

Cora, D., Al‐Soufi, W., & Novo, M. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.140367 · Cited by 7

Challenges in understanding the structure/activity relationship of Aβ oligomers

Pilkington, A. W., & Legleiter, J. A. (2019) · AIMS Biophysics · doi:10.3934/biophy.2019.1.1 · Cited by 7

Electrochemical assessment of dielectric damage to phospholipid bilayers by amyloid β-Oligomers

Budvytytė, R., Ambrulevičius, F., Jankaitytė, E., & Valinčius, G. (2022) · Bioelectrochemistry · doi:10.1016/j.bioelechem.2022.108091 · Cited by 7

Discovery of Y-Shaped Supramolecular Polymers in a Self-Assembling Peptide Amphiphile System

Wang, Y., Su, H., Wang, Y., & Cui, H. (2022) · ACS Macro Letters · doi:10.1021/acsmacrolett.2c00630 · Cited by 8

Curcumin tautomerization in the mechanism of pentameric amyloid- β42 oligomers disassembly

Matsui, A., Bellier, J., Hayashi, D., Ishibe, T., Nakamura, Y., Taguchi, H., Naruse, N., & Mera, Y. (2023) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2023.04.076 · Cited by 7

A novel peptide derived from vascular endothelial growth factor prevents amyloid beta aggregation and toxicity

Bouvet, P., Gea, P. D., Aimard, M., Chounlamountri, N., Honnorat, J., Delcros, J., Salin, P. A., & Meissirel, C. (2023) · Aging Cell · doi:10.1111/acel.13907 · Cited by 9

Immunotherapy for Alzheimer‘s Disease

Steinitz, M. O. (2009) · Immunotherapy · doi:10.2217/imt.09.3 · Cited by 7

Chronochemistry in neurodegeneration

Pastore, A., & Adinolfi, S. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00020 · Cited by 7

Why Alzheimer’s is a Disease of Memory: Synaptic Targeting by Pathogenic Aβ Oligomers (ADDLs)

Klein, W. L., Felice, F. G. D., Lacor, P. N., Lambert, M. P., & Zhao, W.-Q. (2008) · Research and perspectives in Alzheimer's disease · doi:10.1007/978-3-540-76330-7_9 · Cited by 7

Covalent modifications of the amyloid beta peptide by hydroxynonenal: Effects on metal ion binding by monomers and insights into the fibril topology

Grasso, G., Komatsu, H., & Axelsen, P. H. (2017) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2017.06.007 · Cited by 8

The shape effect of reconstituted high-density lipoprotein nanocarriers on brain delivery and Aβ clearance

Song, H., Ma, X., Xu, J., Song, Q., Meng, H., Gu, X. Q., Zhang, Q., Hou, L., Chen, L., Huang, Y., et al. (2018) · Nano Research · doi:10.1007/s12274-018-2107-8 · Cited by 7

Reduced Expression of the PP2A Methylesterase, PME-1, or the PP2A Methyltransferase, LCMT-1, Alters Sensitivity to Beta-Amyloid-Induced Cognitive and Electrophysiological Impairments in Mice

Staniszewski, A., Zhang, H., Asam, K. R., Pitstick, R., Kavanaugh, M. P., Arancio, O., & Nicholls, R. E. (2020) · Journal of Neuroscience · doi:10.1523/jneurosci.2983-19.2020 · Cited by 7

Immunization with Small Amyloid-β-derived Cyclopeptide Conjugates Diminishes Amyloid-β-Induced Neurodegeneration in Mice

Mulder, C. K., Dong, Y., Brugghe, H. F., Timmermans, H., Tilstra, W., Westdijk, J., van Riet, E., STEEG, H. V., Hoogerhout, P., & Eisel, U. L. M. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-151136 · Cited by 7

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