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

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

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

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

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

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

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

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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

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

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

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Stability of Aβ (1-42) peptide fibrils as consequence of environmental modifications

Gregori, M., Cassina, V., Brogioli, D., Salerno, D., Kimpe, L. D., Scheper, W., Masserini, M., & Mantegazza, F. (2010) · European Biophysics Journal · doi:10.1007/s00249-010-0619-6 · Cited by 20

Inhibition of Aβ42 oligomerization in yeast by a PICALM ortholog and certain FDA approved drugs

Park, S.-K., Ratia, K. M., Ba, M. A., Valencik, M. L., & Liebman, S. W. (2016) · Microbial Cell · doi:10.15698/mic2016.02.476 · Cited by 21

Norovirus P particle-based active Aβ immunotherapy elicits sufficient immunogenicity and improves cognitive capacity in a mouse model of Alzheimer’s disease

Fu, L., Li, Y., Hu, Y., Zheng, Y., Yu, B., Zhang, H., Wu, J., Wu, H., Yu, X., & Kong, W. (2017) · Scientific Reports · doi:10.1038/srep41041 · Cited by 20

Protective Roles of Monsonia angustifolia and Its Active Compounds in Experimental Models of Alzheimer’s Disease

Chun, Y. S., Kim, J., Chung, S., Khorombi, E., Naidoo, D., Nthambeleni, R., Harding, N., Maharaj, V. J., Fouché, G., & Yang, H. O. (2017) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.6b04451 · Cited by 20

Immunoglobulin G transport increases in an in vitro blood–brain barrier model with amyloid‐β and with neuroinflammatory cytokines

Mantle, J. L., & Lee, K. H. (2019) · Biotechnology and Bioengineering · doi:10.1002/bit.26967 · Cited by 20

Kinetic Transition in Amyloid Assembly as a Screening Assay for Oligomer-Selective Dyes

Barton, J., Arias, D. S., Niyangoda, C., Borjas, G. J., Le, N., Mohamed, S., & Muschol, M. (2019) · Biomolecules · doi:10.3390/biom9100539 · Cited by 20

Haptoglobin Modulates Beta-Amyloid Uptake by U-87 MG Astrocyte Cell Line

Maresca, B., Spagnuolo, M. S., & Cigliano, L. (2015) · Journal of Molecular Neuroscience · doi:10.1007/s12031-014-0465-6 · Cited by 20

Granular Non-Fibrillar Aggregates and Toxicity in Alzheimer’s Disease

Benseny‐Cases, N., Klementieva, O. L., Malý, J., & Cladera, J. (2012) · Current Alzheimer Research · doi:10.2174/156720512803251129 · Cited by 19

Systematic analysis of cellular cross-talk reveals a role for SEMA6D-TREM2 regulating microglial function in Alzheimer’s disease

D’Oliveira Albanus, R., Finan, G. M., Brase, L., Sweeney, N., Kim, T. Y., Chen, S., Ryoo, Y., Park, J., Guo, Q., Iyer, A. K., et al. (2025) · Science Translational Medicine · doi:10.1126/scitranslmed.adx0027 · Cited by 19

Amyloid Beta Oligomers Activate Death Receptors and Mitochondria-Mediated Apoptotic Pathways in Cerebral Vascular Smooth Muscle Cells; Protective Effects of Carbonic Anhydrase Inhibitors

Anzovino, A., Canepa, E., Alves, M., Lemon, N. L., Carare, R. O., & Fossati, S. (2023) · Cells · doi:10.3390/cells12242840 · Cited by 19

Protein folding, misfolding and aggregation: The importance of two-electron stabilizing interactions

Cieplak, A. S. (2017) · PLoS ONE · doi:10.1371/journal.pone.0180905 · Cited by 21

Probing the role of aromatic residues in the self-assembly of Aβ(16–22) in fluorinated alcohols and their aqueous mixtures

Pachahara, S. K., & Nagaraj, R. (2015) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2015.04.005 · Cited by 19

Amyloid-β(1−42) Fibrillar Precursors Are Optimal for Inducing Tumor Necrosis Factor-α Production in the THP-1 Human Monocytic Cell Line

Ajit, D., Udan, M. L. D., Paranjape, G. S., & Nichols, M. R. (2009) · Biochemistry · doi:10.1021/bi9003777 · Cited by 18

Aβ1-42 peptides blunt the adenosine A2A receptor-mediated control of the interplay between P2X7 and P2Y1 receptors mediated calcium responses in astrocytes

Dias, L., Madeira, D., Dias, R., Tomé, Â. R., Cunha, R. A., & Agostinho, P. M. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04492-y · Cited by 19

Protein aggregation and neurodegenerative disease: Structural outlook for the novel therapeutics

Arar, S. H., Haque, M. A., & Kayed, R. (2023) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26561 · Cited by 20

Simple model for the simulation of peptide folding and aggregation with different sequences

Enciso, M., & Rey, A. (2012) · The Journal of Chemical Physics · doi:10.1063/1.4725883 · Cited by 18

Conformational Diseases: Structural Studies of Aggregation of Polyglutamine Proteins

Papaleo, E., & Invernizzi, G. (2010) · Current Computer - Aided Drug Design · doi:10.2174/157340911793743574 · Cited by 18

The Multimerization State of the Amyloid-β42 Peptide (Aβ42) Governs its Interaction Network with the Extracellular Matrix

Salza, R., Lethias, C., & Ricard‐Blum, S. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-160751 · Cited by 18

Reactive oxygen species released from astrocytes treated with amyloid beta oligomers elicit neuronal calcium signals that decrease phospho-Ser727-STAT3 nuclear content

Muñoz, Y., Paula-Lima, A. C., & Núñez, M. T. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.01.006 · Cited by 21

Cell surface proteoglycan-mediated uptake and accumulation of the Alzheimer's disease peptide Aβ(1–42)

Wesén, E. V., Gallud, A., Paul, A., Lindberg, D. J., Malmberg, P., & Esbjörner, E. K. (2018) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2018.08.010 · Cited by 20

NMDAR-dependent somatic potentiation of synaptic inputs is correlated with β amyloid-mediated neuronal hyperactivity

Bao, Y., Yang, X., Fu, Y., Zhengyan, L., Gong, R., & Lü, W. (2021) · Translational Neurodegeneration · doi:10.1186/s40035-021-00260-3 · Cited by 18

Role of phosphatidylserine in amyloid-beta oligomerization at asymmetric phospholipid bilayers

Robinson, J., Sarangi, N. K., & Keyes, T. E. (2022) · Physical Chemistry Chemical Physics · doi:10.1039/d2cp03344e · Cited by 18

Nucleic Acid Aptamers as Novel Class of Therapeutics to Mitigate Alzheimer’s Disease Pathology

Tannenberg, R. K., Shamaileh, H. A., Lauridsen, L. H., Kanwar, J. R., Dodd, P. R., & Veedu, R. N. (2013) · Current Alzheimer Research · doi:10.2174/1567205011310040009 · Cited by 17

Interaction of a β‐sheet breaker peptide with lipid membranes

Vitiello, G., Grimaldi, M., Ramunno, A., Ortona, O., Martino, G., D’Ursi, A. M., & D’Errico, G. (2010) · Journal of Peptide Science · doi:10.1002/psc.1207 · Cited by 18

Novel analogues of chlormethiazole are neuroprotective in four cellular models of neurodegeneration by a mechanism with variable dependence on GABAA receptor potentiation

VandeVrede, L. A., Tavassoli, E., Luo, J., Qin, Z., Lan, Y., Pepperberg, D. R., & Thatcher, G. R. J. (2013) · British Journal of Pharmacology · doi:10.1111/bph.12454 · Cited by 19

Multiple effects of β-amyloid on single excitatory synaptic connections in the PFC

Wang, Y., Zhou, T. H., Zhi, Z., Barakat, A., Hlatky, L., & Querfurth, H. W. (2013) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2013.00129 · Cited by 20

A new procedure for amyloid β oligomers preparation enables the unambiguous testing of their effects on cytosolic and mitochondrial Ca 2+ entry and cell death in primary neurons

Caballero, E., Calvo-Rodríguez, M., Gonzalo‐Ruiz, A., Villalobos, C., & Núñez, L. (2015) · Neuroscience Letters · doi:10.1016/j.neulet.2015.11.041 · Cited by 20

Development of peptide aptamers as alternatives for antibody in the detection of amyloid-beta 42 aggregates

Kim, S., Lee, E.-H., Lee, S., Kim, A.-R., Park, H., Son, J., Koh, S., & Yoon, M. (2020) · Analytical Biochemistry · doi:10.1016/j.ab.2020.113921 · Cited by 18

Hierarchy and the mechanism of fibril formation in ADan peptides

Surolia, I., Reddy, G. B., & Sinha, S. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04072.x · Cited by 18

Rapid Detection of Protein Aggregation and Inhibition by Dual Functions of Gold Nanoplasmonic Particles: Catalytic Activator and Optical Reporter

Choi, I., Lee, E., Song, M., & Lee, L. P. (2014) · Biophysical Journal · doi:10.1016/j.bpj.2013.11.2344 · Cited by 17

Probing Interfacial Charge Transfer between Amyloid-β and Graphene during Amyloid Fibrillization Using Raman Spectroscopy

Cha, W., Heo, C., Lee, S., Yun, S. J., Cho, B. W., Ha, T., & Lee, Y. H. (2023) · ACS Nano · doi:10.1021/acsnano.2c11428 · Cited by 17

Probing differences among Aβ oligomers with two triangular trimers derived from Aβ

Kreutzer, A. G., Guaglianone, G., Yoo, S., Parrocha, C. M. T., Ruttenberg, S. M., Malonis, R. J., Tong, K., Lin, Y.-F., Nguyen, J. T., Howitz, W. J., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2219216120 · Cited by 18

Neuroprotective Effect of NO-Delivery Dinitrosyl Iron Complexes (DNICs) on Amyloid Pathology in the Alzheimer’s Disease Cell Model

Chuang, W.-H., Chou, Y.-T., Chen, Y.-H., Kuo, T.-H., Liaw, W., Lu, T., Kao, C.-F., & Wang, Y. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00348 · Cited by 17

Uric Acid Mitigates Cognitive Deficits via TFEB-Mediated Microglial Autophagy in Mice Models of Alzheimer’s Disease

Xiao, Q., Wang, J., Tian, Q., Tian, N., Tian, Q., He, X., Wang, Y., & Dong, Z. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03818-6 · Cited by 18

Anti-Aβ Oligomer IgG and Surface Sialic Acid in Intravenous Immunoglobulin: Measurement and Correlation with Clinical Outcomes in Alzheimer’s Disease Treatment

Kwon, H., Crisostomo, A. C., Smalls, H. M., & Finke, J. M. (2015) · PLoS ONE · doi:10.1371/journal.pone.0120420 · Cited by 17

Convergence of Synapses, Endosomes, and Prions in the Biology of Neurodegenerative Diseases

Gouras, G. K. (2013) · International Journal of Cell Biology · doi:10.1155/2013/141083 · Cited by 17

Linking Alzheimer’s Disease and Type 2 Diabetes: Characterization and Inhibition of Cytotoxic Aβ and IAPP Hetero-Aggregates

Adem, K. A., Shanti, A., Srivastava, A., Homouz, D., Thomas, S. A., Khair, M., Stefanini, C., Chan, V., Kim, T., & Lee, S. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.842582 · Cited by 17

Non-competitive AMPA glutamate receptors antagonism by perampanel as a strategy to counteract hippocampal hyper-excitability and cognitive deficits in cerebral amyloidosis

Bellingacci, L., Tallarico, M., Mancini, A., Megaro, A., Caro, C. D., Citraro, R., Sarro, G. D., Tozzi, A., Filippo, M. D., Sciaccaluga, M., et al. (2022) · Neuropharmacology · doi:10.1016/j.neuropharm.2022.109373 · Cited by 17

The study of Alzheimer’s disease biomarkers

Vestergaard, M. C. M., Kerman, K., & Tamiya, E. (2006) · Nanobiotechnology · doi:10.1007/s12030-006-0002-y · Cited by 17

Detection and reduction of microaggregates in insulin preparations

Heldt, C. L., Sorci, M., Posada, D., Hirsa, A. H., & Belfort, G. (2010) · Biotechnology and Bioengineering · doi:10.1002/bit.22902 · Cited by 17

Nuclear magnetic resonance evidence for the dimer formation of beta amyloid peptide 1–42 in 1,1,1,3,3,3-hexafluoro-2-propanol

Shigemitsu, Y., Iwaya, N., Goda, N., Matsuzaki, M., Tenno, T., Narita, A., Hoshi, M. M., & Hiroaki, H. (2016) · Analytical Biochemistry · doi:10.1016/j.ab.2015.12.021 · Cited by 17

Aβ40 has a subtle effect on Aβ42 protofibril formation, but to a lesser degree than Aβ42 concentration, in Aβ42/Aβ40 mixtures

Terrill, S. E., Colvin, B. A., Davenport, R. E., & Nichols, M. R. (2016) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2016.03.017 · Cited by 18

Enlargement of Aβ aggregates through chemokine-dependent microglial clustering

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Genuine selective caspase-2 inhibition with new irreversible small peptidomimetics

Bosc, E., Anastasie, J., Soualmia, F., Coric, P., Kim, J. Y., Wang, L. Q., Lacin, G., Zhao, K., Patel, R., Duplus, E., et al. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-05396-2 · Cited by 16

Evaluating the Role of N-Acetyl-L-Tryptophan in the Aβ 1-42-Induced Neuroinflammation and Cognitive Decline in Alzheimer’s Disease

Satarker, S., Gurram, P. C., Nassar, A., Manandhar, S., Vibhavari, R. J. A., Yarlagadda, D. L., Mudgal, J., Lewis, S. A., Arora, D. S., & Nampoothiri, M. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03844-4 · Cited by 16

Effects of Amyloid Beta (Aβ) Oligomers on Blood–Brain Barrier Using a 3D Microfluidic Vasculature-on-a-Chip Model

Uzoechi, S. C., Collins, B., Badeaux, C. J., Li, Y., Kwak, S. S., Kim, D. Y., Laskowitz, D. T., Lee, J., & Yun, Y. (2024) · Applied Sciences · doi:10.3390/app14093917 · Cited by 16

Pathophysiological amyloid concentrations induce sustained upregulation of readthrough acetylcholinesterase mediating anti-apoptotic effects

Li, G., Klein, J., & Zimmermann, M. (2013) · Neuroscience · doi:10.1016/j.neuroscience.2013.02.040 · Cited by 16

Morphology‐Specific Inhibition of β‐Amyloid Aggregates by 17β‐Hydroxysteroid Dehydrogenase Type 10

Aitken, L., Quinn, S. D., Pérez‐González, C., Samuel, I. D. W., Penedo, J. C., & Gunn‐Moore, F. J. (2016) · ChemBioChem · doi:10.1002/cbic.201600081 · Cited by 16

Arabidopsis thaliana extracts optimized for polyphenols production as potential therapeutics for the APOE-modulated neuroinflammation characteristic of Alzheimer’s disease in vitro

Ghura, S., Tai, L. M., Zhao, M., Collins, N., Che, C., Warpeha, K. M., & LaDu, M. J. (2016) · Scientific Reports · doi:10.1038/srep29364 · Cited by 17

Phloroglucinol attenuates oligomeric amyloid beta peptide1-42-induced astrocytic activation by reducing oxidative stress

Yang, E.-J., Kim, H.-J., Kim, H.-S., & Chang, M. (2021) · Journal of Pharmacological Sciences · doi:10.1016/j.jphs.2021.01.008 · Cited by 16

Amyloid-β25-35 Induces Apolipoprotein D Synthesis and Growth Arrest in HT22 Hippocampal Cells

Martínez‐Pinilla, E., Navarro, A., Ordóñez, C., del Valle, E., & Tolivia, J. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-112102 · Cited by 16

Histamine induces the production of matrix metalloproteinase-9 in human astrocytic cultures via H1-receptor subtype

Patel, A., Vasanthan, V., Fu, W., Fahlman, R. P., MacTavish, D., & Jhamandas, J. H. (2015) · Brain Structure and Function · doi:10.1007/s00429-015-1007-x · Cited by 19

Up-regulation of calsyntenin-3 by β-amyloid increases vulnerability of cortical neurons

Uchida, Y., Nakano, S.-I., Gomi, F., & Takahashi, H. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.01.025 · Cited by 16

Interactions of Alzheimer amyloid peptides with cultured cells and brain tissue, and their biological consequences

Bateman, D. A., & Chakrabartty, A. (2004) · Biopolymers · doi:10.1002/bip.10561 · Cited by 16

Photothermal and Photodynamic Strategies for Diagnosis and Therapy of Alzheimer’s Disease by Modulating Amyloid-β Aggregation

Gao, F., Hou, Y., Wang, Y., Liu, L., Yi, X., & Xia, N. (2025) · Biosensors · doi:10.3390/bios15080480 · Cited by 15

Engineering chimeric antigen receptor CD4 T cells for Alzheimer’s disease

Boskovic, P., Shalita, R., Gao, W., Vernon, H., Deng, Y. L., Colonna, M., Majzner, R. G., Amit, I., & Kipnis, J. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2530977123 · Cited by 16

Critical aggregation concentration and reversibility of amyloid-β (1–40) oligomers

Illodo, S., Al‐Soufi, W., & Novo, M. (2024) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2024.110179 · Cited by 16

Carbon Nanotubes Electrochemistry Allows the In Situ Evaluation of the Effect of β‐Sheet Breakers on the Aggregation Process of β‐Amyloid

de la Fuente, E., Adura, C., Kogan, M. J., & Bollo, S. (2012) · Electroanalysis · doi:10.1002/elan.201100607 · Cited by 15

Structural Diversity and Initial Oligomerization of PrP106–126 Studied by Replica-Exchange and Conventional Molecular Dynamics Simulations

Ning, L., Guo, J., Bai, Q., Jin, N., Liu, H., & Yao, X. (2014) · PLoS ONE · doi:10.1371/journal.pone.0087266 · Cited by 15

The Nuclear Inclusion a (NIa) Protease of Turnip Mosaic Virus (TuMV) Cleaves Amyloid-β

Han, H.-E., Sellamuthu, S., Shin, B. H., Lee, Y., Song, S., Seo, J.-S., Baek, I., Bae, J., Kim, H., Yoo, Y. J., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015645 · Cited by 15

A Cyclic Undecamer Peptide Mimics a Turn in Folded Alzheimer Amyloid β and Elicits Antibodies against Oligomeric and Fibrillar Amyloid and Plaques

Hoogerhout, P., Kamphuis, W., Brugghe, H. F., Sluijs, J. A., Timmermans, H., Westdijk, J., Zomer, G., Boog, C. J. P., Hol, E. M., & van den Dobbelsteen, G. P. J. M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0019110 · Cited by 15

Studying the Progression of Amyloid Pathology and Its Therapy Using Translational Longitudinal Model of Accumulation and Distribution of Amyloid Beta

Karelina, T., Demin, O. O., Demin, O. O., Duvvuri, S., & Nicholas, T. (2017) · CPT Pharmacometrics & Systems Pharmacology · doi:10.1002/psp4.12249 · Cited by 15

Optical Spike Detection and Connectivity Analysis With a Far-Red Voltage-Sensitive Fluorophore Reveals Changes to Network Connectivity in Development and Disease

Walker, A., Raliski, B. K., Karbasi, K., Zhang, P., Sanders, K., & Miller, E. W. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.643859 · Cited by 16

Neurotransmitter-stimulated neuron-derived sEVs have opposite effects on amyloid β-induced neuronal damage

Dou, Y., Xie, J., Tan, Y., Zhang, M., Zhao, Y., & Liu, X. (2021) · Journal of Nanobiotechnology · doi:10.1186/s12951-021-01070-5 · Cited by 15

Pathology of Neurodegenerative Diseases

Kim, Y. S., Kim, Y.-K., Hwang, O., & Dong, J. (2012) · InTech eBooks · doi:10.5772/38028 · Cited by 16

Fine Mapping of the Amyloid β-Protein Binding Site on Myelin Basic Protein

Kotarba, A. E., Aucoin, D., Hoos, M. D., Smith, S. O., & Nostrand, W. E. V. (2013) · Biochemistry · doi:10.1021/bi4001936 · Cited by 15

A new methodology for simultaneous quantification of total-Aβ, Aβx-38, Aβx-40, and Aβx-42 by column-switching LC/MS/MS

Watanabe, K., Ishikawa, C., Kuwahara, H., Sato, K., Komuro, S., Nakagawa, T., Nomura, N., Watanabe, S., & Yabuki, M. (2011) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-011-5648-1 · Cited by 15

Facile Methodology for Monitoring Amyloid-β Fibrillization

Cook, N. P., & Martí, A. A. (2012) · ACS Chemical Neuroscience · doi:10.1021/cn300135n · Cited by 17

A gold nanoparticle-mediated rapid in vitro assay of anti-aggregation reagents for amyloid β and its validation

Kim, H. Y., Lee, D., Ryu, K., & Choi, I. (2017) · Chemical Communications · doi:10.1039/c7cc00358g · Cited by 15

Mitochondrial dysfunction induced by a post-translationally modified amyloid linked to a familial mutation in an alternative model of neurodegeneration

Todd, K. L., Fossati, S., Ghiso, J. A., & Rostagno, A. A. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.09.010 · Cited by 15

Oligomeric amyloid-β(1–42) induces THP-1 human monocyte adhesion and maturation

Crouse, N. R., Ajit, D., Udan, M. L. D., & Nichols, M. R. (2008) · Brain Research · doi:10.1016/j.brainres.2008.11.093 · Cited by 17

The gain-of-function TREM2-T96K mutation increases risk for Alzheimer’s disease by impairing microglial function

Pilat, D. J., Le, H., Prokopenko, D., Lin, C.-C. J., Eimer, W. A., Quinti, L., Gavrilles, E. P., Garcia, S. N., Heitman, S. N., McGinty, D., et al. (2026) · Neuron · doi:10.1016/j.neuron.2025.09.032 · Cited by 14

Near-infrared II theranostic agents for the diagnosis and treatment of Alzheimer’s disease

Zhou, C., Zeng, F., Yang, H., Liang, Z., Xu, G., Li, X., Liu, X., & Yang, J. (2024) · European Journal of Nuclear Medicine and Molecular Imaging · doi:10.1007/s00259-024-06690-1 · Cited by 14

The Anemonia Sulcata Toxin BDS-I Protects Astrocytes Exposed to Aβ1-42 Oligomers by Restoring [Ca2+]i Transients and ER Ca2+ Signaling

Piccialli, I., Tedeschi, V., Boscia, F., Ciccone, R., Casamassa, A., de Rosa, V., Grieco, P., Secondo, A., & Pannaccione, A. (2020) · Toxins · doi:10.3390/toxins13010020 · Cited by 14

A Solvatochromic Near Infrared Fluorophore Sensitive to the Full Amyloid Beta Aggregation Pathway

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Anchored FRET sensors detect local caspase activation prior to neuronal degeneration

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