The culprit behind amyloid beta peptide related neurotoxicity in Alzheimer's disease: oligomer size or conformation?

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Amyloid-β protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory

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Diffusible, nonfibrillar ligands derived from Aβ _1–42 are potent central nervous system neurotoxins

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Amyloid β-peptide is produced by cultured cells during normal metabolism

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Natural oligomers of the amyloid-β protein specifically disrupt cognitive function

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The role of apolipoprotein E in Alzheimer's disease

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Non–cell autonomous toxicity in neurodegenerative disorders: ALS and beyond

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Protofibrillar Intermediates of Amyloid β-Protein Induce Acute Electrophysiological Changes and Progressive Neurotoxicity in Cortical Neurons

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Yun, H., Jin, P., Han, J., Lee, M.-S., Han, S., Oh, K., Hong, S.-H., Jung, E.-Y., & Hong, J. T. (2013) · Molecular Neurobiology · doi:10.1007/s12035-013-8479-6 · Cited by 51 · see citing works

Self-Assembly Pathways of β-Sheet-Rich Amyloid-β(1–40) Dimers: Markov State Model Analysis on Millisecond Hybrid-Resolution Simulations

Cao, Y., Jiang, X., & Han, W. (2017) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.7b00803 · Cited by 51 · see citing works

The role of amyloidogenic protein oligomerization in neurodegenerative disease

Lotz, G. P., & Legleiter, J. A. (2013) · Journal of Molecular Medicine · doi:10.1007/s00109-013-1025-1 · Cited by 49 · see citing works

The Triggering Receptor Expressed on Myeloid Cells 2: “TREM-ming” the Inflammatory Component Associated with Alzheimer's Disease

Rohn, T. T. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/860959 · Cited by 48 · see citing works

Polyphenolic Biflavonoids Inhibit Amyloid-Beta Fibrillation and Disaggregate Preformed Amyloid-Beta Fibrils

Choi, E. Y., Kang, S. S., Lee, S. K., & Han, B. H. (2019) · Biomolecules & Therapeutics · doi:10.4062/biomolther.2019.113 · Cited by 45 · see citing works

Enhancing the Therapeutic Effect in Alzheimer's Disease Drugs: The role of Polypharmacology and Cholinesterase inhibitors

Martins, M. M., Branco, P. S., & Ferreira, L. M. (2023) · ChemistrySelect · doi:10.1002/slct.202300461 · Cited by 45 · see citing works

Activated Scavenger Receptor A Promotes Glial Internalization of Aβ

Zhang, H., Su, Y., Zhou, W.-W., Wang, S.-W., Xu, P., Yu, X., & Liu, R. (2014) · PLoS ONE · doi:10.1371/journal.pone.0094197 · Cited by 43 · see citing works

Native metastable prefibrillar oligomers are the most neurotoxic species among amyloid aggregates

Diociaiuti, M., Macchia, G., Paradisi, S., Frank, C., Camerini, S., Chistolini, P., Gaudiano, M. C., Petrucci, T. C., & Malchiodi‐Albedi, F. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.06.006 · Cited by 42 · see citing works

Antioxidant role of amyloid β protein in cell-free and biological systems: implication for the pathogenesis of Alzheimer disease.

Sinha, M., Bhowmick, P., Banerjee, A., & Chakrabarti, S. (2013) · Free Radical Biology & Medicine · doi:10.1016/j.freeradbiomed.2012.09.036 · Cited by 40 · see citing works

A Structure-Toxicity Study of Aß42 Reveals a New Anti-Parallel Aggregation Pathway

Vignaud, H., Bobo, C., Lascu, I., Sörgjerd, K. M., Zako, T., Maeda, M., Salin, B., Lecomte, S., & Cullin, C. (2013) · PLoS ONE · doi:10.1371/journal.pone.0080262 · Cited by 41 · see citing works

Naphthoquinone-tyrptophan reduces neurotoxic Aβ*56 levels and improves cognition in Alzheimer's disease animal model

Scherzer‐Attali, R., Farfara, D., Cooper, I., Levin, A., Benromano, T., Trudler, D., Vientrov, M., Shaltiel‐Karyo, R., Shalev, D. E., Segev‐Amzaleg, N., et al. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2012.03.005 · Cited by 38 · see citing works

Amyloid Prefibrillar Oligomers: The Surprising Commonalities in Their Structure and Activity

Diociaiuti, M., Bonanni, R., Cariati, I., Frank, C., & D’Arcangelo, G. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22126435 · Cited by 38 · see citing works

Scrutiny of the mechanism of small molecule inhibitor preventing conformational transition of amyloid-β 42 monomer: insights from molecular dynamics simulations

Shuaib, S., & Goyal, B. (2017) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2017.1291363 · Cited by 35 · see citing works

Age-Specific Retinal and Cerebral Immunodetection of Amyloid-β Plaques and Oligomers in a Rodent Model of Alzheimer’s Disease

Habiba, U., Merlin, S., Lim, J. K. H., Wong, V. H. Y., Nguyen, C. T. O., Morley, J. W., Bui, B. V., & Tayebi, M. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-191346 · Cited by 33 · see citing works

Two distinct β-sheet structures in Italian-mutant amyloid-beta fibrils: a potential link to different clinical phenotypes

Hubin, E., Deroo, S., Schierle, G. S. K., Kaminski, C. F., Serpell, L. C., Subramaniam, V., van Nuland, N. A. J., Broersen, K., Raussens, V., & Sarroukh, R. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-1983-2 · Cited by 34 · see citing works

A2T and A2V Aβ peptides exhibit different aggregation kinetics, primary nucleation, morphology, structure, and LTP inhibition

Murray, B., Sorci, M., Rosenthal, J., Lippens, J. L., Isaacson, D., Das, P., Fabris, D., Li, S., & Belfort, G. (2016) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24995 · Cited by 33 · see citing works

Dynamic Imaging by Fluorescence Correlation Spectroscopy Identifies Diverse Populations of Polyglutamine Oligomers Formed in Vivo

Beam, M., Silva, M. C., & Morimoto, R. I. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.362764 · Cited by 31 · see citing works

Effects of Single Doses of Avagacestat (BMS-708163) on Cerebrospinal Fluid Aβ Levels in Healthy Young Men

Tong, G., Castaneda, L., Wang, J.-S., Sverdlov, O., Huang, S., Slemmon, R., Gu, H., Wong, O. T., Li, H., Berman, R., et al. (2012) · Clinical Drug Investigation · doi:10.1007/s40261-012-0006-4 · Cited by 33 · see citing works

Interaction of the amyloid β peptide with sodium dodecyl sulfate as a membrane-mimicking detergent

Shabestari, M., Meeuwenoord, N., Filippov, D., & Huber, M. (2016) · Journal of biological physics (Print) · doi:10.1007/s10867-016-9408-5 · Cited by 28 · see citing works

Alzheimer’s Disease: Lessons Learned from Amyloidocentric Clinical Trials

Soejitno, A., Tjan, A., & Purwata, T. E. (2015) · CNS Drugs · doi:10.1007/s40263-015-0257-8 · Cited by 31 · see citing works

Assembly of Alzheimer's Aβ peptide into nanostructured amyloid fibrils

Morgado, I., & Fändrich, M. (2011) · Current Opinion in Colloid & Interface Science · doi:10.1016/j.cocis.2011.06.016 · Cited by 29 · see citing works

The role of Alzheimer’s and cerebrovascular pathology in mediating the effects of age, race, and apolipoprotein E genotype on dementia severity in pathologically confirmed Alzheimer’s disease

Gavett, B., John, S., Gurnani, A., Bussell, C., & Saurman, J. (2015) · Journal of Alzheimer's Disease · doi:10.3233/jad-150252 · Cited by 31 · see citing works

From a Microscopic to a Macroscopic Model for Alzheimer Disease: Two-Scale Homogenization of the Smoluchowski Equation in Perforated Domains

Franchi, B., & Lorenzani, S. (2016) · Journal of Nonlinear Science · doi:10.1007/s00332-016-9288-7 · Cited by 30 · see citing works

HSA targets multiple Aβ42 species and inhibits the seeding-mediated aggregation and cytotoxicity of Aβ42 aggregates

Wang, C., Cheng, F., Xu, L., & Jia, L. (2016) · RSC Advances · doi:10.1039/c6ra14590f · Cited by 30 · see citing works

Molecular insights into Aβ42 protofibril destabilization with a fluorinated compound D744: A molecular dynamics simulation study

Saini, R. K., Shuaib, S., & Goyal, B. (2017) · Journal of Molecular Recognition · doi:10.1002/jmr.2656 · Cited by 30 · see citing works

The elusive nature and diagnostics of misfolded Aβ oligomers

Cerasoli, E., Ryadnov, M. G., & Austen, B. (2015) · Frontiers in Chemistry · doi:10.3389/fchem.2015.00017 · Cited by 28 · see citing works

Current status of PET-imaging probes of β-amyloid plaques

Koo, J., & Byun, Y. (2013) · Archives of Pharmacal Research · doi:10.1007/s12272-013-0193-4 · Cited by 28 · see citing works

Solid-state NMR reveals a comprehensive view of the dynamics of the flexible, disordered N-terminal domain of amyloid-β fibrils

Au, D. F., Ostrovsky, D., Fu, R., & Vugmeyster, L. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.006559 · Cited by 28 · see citing works

Role of Species-Specific Primary Structure Differences in Aβ42 Assembly and Neurotoxicity

Roychaudhuri, R., Zheng, X., Lomakin, A., Maiti, P., Condron, M. M., Benedek, G. B., Bitan, G., Bowers, M. T., & Teplow, D. B. (2015) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5b00180 · Cited by 26 · see citing works

Elucidating Molecular Mass and Shape of a Neurotoxic Aβ Oligomer

Sebollela, A. S., Mustata, G.-M., Luo, K., Velasco, P. T., Viola, K. L., Cline, E. N., Shekhawat, G. S., Wilcox, K. C., Dravid, V. P., & Klein, W. L. (2014) · ACS Chemical Neuroscience · doi:10.1021/cn500156r · Cited by 25 · see citing works

Mitochondria-Targeted Molecules as Potential Drugs to Treat Patients With Alzheimer's Disease

Reddy, A. P., & Reddy, P. H. (2017) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2016.12.010 · Cited by 25 · see citing works

Collagen hydrogel confinement of Amyloid-β (Aβ) accelerates aggregation and reduces cytotoxic effects

Simpson, L. W., Szeto, G. L., Boukari, H., Good, T. A., & Leach, J. B. (2019) · Acta Biomaterialia · doi:10.1016/j.actbio.2020.05.030 · Cited by 24 · see citing works

Microfluidic Platforms to Unravel Mysteries of Alzheimer’s Disease: How Far Have We Come?

Prasanna, P., Rathee, S., Rahul, V., Mandal, D., Goud, M. S. C., Yadav, P., Hawthorne, S. J., Sharma, A., Gupta, P. K., Ojha, S. K., et al. (2021) · Life · doi:10.3390/life11101022 · Cited by 24 · see citing works

The proof-of-concept of ASS234: Peripherally administered ASS234 enters the central nervous system and reduces pathology in a male mouse model of Alzheimer disease

Serrano‐Regal, M. P., Herrero-Labrador, R., Futch, H. S., Serrano, J., Romero, A., Fernández, A. P., Samadi, A., Unzeta, M., Marco‐Contelles, J., & Martínez‐Murillo, R. (2016) · Journal of Psychiatry and Neuroscience · doi:10.1503/jpn.150209 · Cited by 25 · see citing works

Conformational Dynamics of Specific Aβ Oligomers Govern Their Ability To Replicate and Induce Neuronal Apoptosis

Dean, D. N., Pate, K. M., Moss, M. A., & Rangachari, V. (2016) · Biochemistry · doi:10.1021/acs.biochem.6b00161 · Cited by 23 · see citing works

Restoring long-term potentiation impaired by amyloid-beta oligomers: Comparison of an acetylcholinesterase inhibitior and selective neuronal nicotinic receptor agonists

Kroker, K. S., Moreth, J., Kußmaul, L., Rast, G. F., & Rosenbrock, H. (2013) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2013.04.006 · Cited by 24 · see citing works

Sodium dodecyl sulphate modulates the fibrillation of human serum albumin in a dose-dependent manner and impacts the PC12 cells retraction

Movaghati, S., Moosavi‐Movahedi, A. A., Khodagholi, F., Digaleh, H., Kachooei, E., & Sheibani, N. (2014) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2014.07.002 · Cited by 24 · see citing works

Amyloid beta peptides (Aβ) from Alzheimer's disease neuronal secretome induce endothelial activation in a human cerebral microvessel model

Shin, Y. J., Evitts, K. M., Jin, S., Howard, C. C., Sharp-Milgrom, M., Schwarze‐Taufiq, T. A., Kinoshita, C., Young, J. E., & Zheng, Y. Y. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106125 · Cited by 22 · see citing works

Globular and Protofibrillar Aβ Aggregates Impair Neurotransmission by Different Mechanisms

Moreth, J., Kroker, K. S., Schwanzar, D., Schnack, C., Arnim, C. A. F. V., Hengerer, B., Rosenbrock, H., & Kußmaul, L. (2013) · Biochemistry · doi:10.1021/bi3016444 · Cited by 22 · see citing works

A phlorotannin isolated from Ecklonia radiata, Dibenzodioxin-fucodiphloroethol, inhibits neurotoxicity and aggregation of β-amyloid

Shrestha, S., Johnston, M. R., Zhang, W. Y., & Smid, S. D. (2021) · Phytomedicine Plus · doi:10.1016/j.phyplu.2021.100125 · Cited by 22 · see citing works

Possible Role of Fibrinaloid Microclots in Postural Orthostatic Tachycardia Syndrome (POTS): Focus on Long COVID

Kell, D. B., Khan, A., Kane, B., Lip, G. Y. H., & Pretorius, E. (2024) · Journal of Personalized Medicine · doi:10.3390/jpm14020170 · Cited by 23 · see citing works

Mechanism of the Chaperone-like and Antichaperone Activities of Amyloid Fibrils of Peptides from αA-Crystallin

Fukuhara, S., Nishigaki, T., Miyata, K., Tsuchiya, N., Waku, T., & Tanaka, N. (2012) · Biochemistry · doi:10.1021/bi3004236 · Cited by 20 · see citing works

Fibril Nucleation Kinetics of a Pharmaceutical Peptide: The Role of Conformation Stability, Formulation Factors, and Temperature Effect

Zhang, J., Mao, X., & Xu, W. (2018) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.8b00769 · Cited by 20 · see citing works

Therapeutic Effects of Curcumin on Alzheimer’s Disease

Yao, E. C., & Xue, L. (2014) · Advances in Alzheimer s Disease · doi:10.4236/aad.2014.34014 · Cited by 19 · see citing works

Modulation of gut microbiota with probiotics as a strategy to counteract endogenous and exogenous neurotoxicity

Skalny, A. V., Aschner, M., Гриценко, В. А., Martins, A. C., Tizabi, Y., Korobeinikova, T. V., Paoliello, M. M. B., & Tinkov, A. A. (2024) · Advances in neurotoxicology · doi:10.1016/bs.ant.2024.02.002 · Cited by 17 · see citing works

Therapeutic Potential of Vaccines for Alzheimer‘s Disease

Shah, S., & Federoff, H. J. (2011) · Immunotherapy · doi:10.2217/imt.10.94 · Cited by 15 · see citing works

Mesenchymal Stem Cells Can Prevent Alterations in Behavior and Neurogenesis Induced by Aß25–35 Administration

Hamisha, K. N., Tfilin, M., Yanai, J., & Turgeman, G. (2014) · Journal of Molecular Neuroscience · doi:10.1007/s12031-014-0457-6 · Cited by 15 · see citing works

Is abeta a sufficient biomarker for monitoring anti-abeta clinical studies? A critical review

Moreth, J., Mavoungou, C., & Schindowski, K. (2013) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2013.00025 · Cited by 18 · see citing works

Discrete Pools of Oligomeric Amyloid-β Track with Spatial Learning Deficits in a Mouse Model of Alzheimer Amyloidosis

Chiang, A. C. A., Fowler, S., Reddy, R., Pletniková, O., Troncoso, J. C., Sherman, M. A., Lesné, S., & Jankowsky, J. L. (2017) · American Journal Of Pathology · doi:10.1016/j.ajpath.2017.11.011 · Cited by 15 · see citing works

Colorimetric Detection of Mutant β-Amyloid(1–40) Membrane-Active Aggregation with Biosensing Vesicles

Dorsey, M. P., Nguelifack, B. M., & Yates, E. A. (2019) · ACS Applied Bio Materials · doi:10.1021/acsabm.9b00694 · Cited by 14 · see citing works

A Systematic Bioinformatics Workflow With Meta-Analytics Identified Potential Pathogenic Factors of Alzheimer’s Disease

Yuen, S. C., Zhu, H., & Leung, S.-W. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00209 · Cited by 15 · see citing works

Hereditary and sporadic beta-amyloidoses

Fede, G. D. (2013) · Frontiers in bioscience · doi:10.2741/4173 · Cited by 13 · see citing works

The A2V mutation as a new tool for hindering Aβ aggregation: A neutron and x-ray diffraction study

Cantú, L., Colombo, L., Stoilova, T., Demé, B., Inouye, H., Booth, R., Rondelli, V., Fede, G. D., Tagliavini, F., Favero, E. D., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-05582-9 · Cited by 13 · see citing works

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 12 · see citing works

A Highly Specific Genome-Wide Association Study Integrated with Transcriptome Data Reveals the Contribution of Copy Number Variations to Specialized Metabolites in Arabidopsis thaliana Accessions

Shirai, K., Matsuda, F., Nakabayashi, R., Okamoto, M., Tanaka, M., Fujimoto, A., Shimizu, M., Shinozaki, K., Seki, M., Saito, K., et al. (2017) · Molecular Biology and Evolution · doi:10.1093/molbev/msx234 · Cited by 12 · see citing works

Insight into Amyloid Formation Using Congo Red as the Electrochemical Probe

Veloso, A. J., Chan, T., Hung, V. W. S., Lam, L., & Kerman, K. (2011) · Electroanalysis · doi:10.1002/elan.201100329 · Cited by 11 · see citing works

Temporal Cortex Microarray Analysis Revealed Impaired Ribosomal Biogenesis and Hyperactivity of the Glutamatergic System: An Early Signature of Asymptomatic Alzheimer's Disease

Kumari, A., Rahaman, A., Zeng, X., Farooq, M. A., Huang, Y., Yao, R., Ali, M., Ishrat, R., & Ali, R. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.966877 · Cited by 11 · see citing works

Fluorescence imaging of the interaction of amyloid beta 40 peptides with live cells and model membrane

Jamasbi, E., Hossain, M. A., Tan, M., Separovic, F., & Ciccotosto, G. D. (2018) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2018.01.024 · Cited by 11 · see citing works

An evaluation of the self-assembly enhancing properties of cell-derived hexameric amyloid-β

Vadukul, D. M., Vrancx, C., Burguet, P., Contino, S., Suelves, N., Serpell, L. C., Quinton, L., & Kienlen‐Campard, P. (2021) · Scientific Reports · doi:10.1038/s41598-021-90680-y · Cited by 11 · see citing works

The self-assembly mechanism of ovotransferrin fibrils induced by subtilisin A and Ca2+ ions and their application in nutrient delivery and texture optimization for liquid food

Zhang, J., Zhang, X., & Zhu, C. (2024) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2024.110582 · Cited by 10 · see citing works

Beta-amyloid oligomers: recent developments

Borutaite, V., Morkuniene, R., & Valincius, G. (2011) · bmc · doi:10.1515/bmc.2011.019 · Cited by 9 · see citing works

Probing the anti-Aβ42 aggregation and protective effects of prenylated xanthone against Aβ42-induced toxicity in transgenic Caenorhabditis elegans model

Thew, H. Y., Khor, B., Tan, Y. C., Ong, Y. S., Parat, M., Murugaiyah, V., Goh, B. H., & Khaw, K. Y. (2024) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2024.110978 · Cited by 9 · see citing works

Opportunities for Conformation-Selective Antibodies in Amyloid-Related Diseases

Westwood, M., & Lawson, A. D. G. (2015) · Antibodies · doi:10.3390/antib4030170 · Cited by 9 · see citing works

A Human Embryonic Stem Cell Model of Aβ-Dependent Chronic Progressive Neurodegeneration

Ubina, T., Magallanes, M., Srivastava, S., Warden, C., Yee, J., & Salvaterra, P. M. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.01007 · Cited by 9 · see citing works

Transnasal delivery of human A-beta peptides elicits impaired learning and memory performance in wild type mice

Endres, K., Reinhardt, S., Geladaris, A., Knies, J., Grimm, M. O. W., Hartmann, T., & Schmitt, U. (2016) · BMC Neuroscience · doi:10.1186/s12868-016-0280-9 · Cited by 8 · see citing works

Insights into the bioactive compounds of endophytic fungi in mangroves

Hamzah, T. N. T., Öztürk, M., Altay, V., & Hakeem, K. R. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-819541-3.00015-3 · Cited by 8 · see citing works

REVIEW

(2013)

Investigation of neurotoxic effects of various aggregate forms of beta amyloid

Morkūnienė, R., Čižas, P., Budvytytė, R., Valinčius, G., & Borutaitė, V. (2012) · Lithuanian University of Health Sciences

Can size alone explain some of the differences in toxicity between β‐amyloid oligomers and fibrils?

Keshet, B., Yang, I. H., & Good, T. A. (2010) · Biotechnology and Bioengineering · doi:10.1002/bit.22691 · Cited by 16 · see citing works

Size-dependent neurotoxicity of β-amyloid oligomers

Čižas, P., Budvytytė, R., Morkūnienė, R., Moldovan, R., Broccio, M., Lösche, M., Niaura, G., Valinčius, G., & Borutaitė, V. (2010) · Lithuanian University of Health Sciences

Internalisation and toxicity of amyloid‐β 1‐42 are influenced by its conformation and assembly state rather than size

Vadukul, D. M., Maina, M. B., Franklin, H., Nardecchia, A., Serpell, L. C., & Marshall, K. E. (2020) · FEBS Letters · doi:10.1002/1873-3468.13919 · Cited by 52 · see citing works