Cited by 119Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

The DOI matches its Crossref record; 178 of the 181 references it cites were found in a registry or an index.

The keystone of Alzheimer pathogenesis might be sought in Aβ physiology

Open access

Puzzo, D., Gulisano, W., Arancio, O., Palmeri, A.·2015·Neuroscience

DOI 10.1016/j.neuroscience.2015.08.039PMC PMC4591241

Open this paper in CoChat — free account

Abstract

For several years Amyloid-beta peptide (Aβ) has been considered the main pathogenetic factor of Alzheimer's disease (AD). According to the so called Amyloid Cascade Hypothesis the increase of Aβ triggers a series of events leading to synaptic dysfunction and memory loss as well as to the structural brain damage in the later stage of the disease. However, several evidences suggest that this hypothesis is not sufficient to explain AD pathogenesis, especially considering that most of the clinical trials aimed to decrease Aβ levels have been unsuccessful. Moreover, Aβ is physiologically produced in the healthy brain during neuronal activity and it is needed for synaptic plasticity and memory. Here we propose a model interpreting AD pathogenesis as an alteration of the negative feedback loop between Aβ and its physiological receptors, focusing on alpha7 nicotinic acetylcholine receptors (α7-nAchRs). According to this vision, when Aβ cannot exert its physiological function a negative feedback mechanism would induce a compensatory increase of its production leading to an abnormal accumulation that reduces α7-nAchR function, leading to synaptic dysfunction and memory loss. In this perspective, the indiscriminate Aβ removal might worsen neuronal homeostasis, causing a further impoverishment of learning and memory. Even if further studies are needed to better understand and validate these mechanisms, we believe that to deepen the role of Aβ in physiological conditions might represent the keystone to elucidate important aspects of AD pathogenesis.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1016/j.neuroscience.2015.08.039

Cites

178 of 178 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

1 retracted

RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
Lesné, S., Koh, M. T., Kotilinek, L., Kayed, R., Glabe, C. G., Yang, A., Gallagher, M., & Ashe, K. H. (2006) · Nature · doi:10.1038/nature04533 · Cited by 2,769 · cited 2×
“, 1999) have been found in soluble fractions and in extracts of plaques in AD brains and CSF (Podlisny et al., 1995; Roher et al., 1996; Funato et al., 1998; Enya et al., 1999; McLean et al., 1999; Kawarabayashi et al., 2004; Lesne et al., 2006); (ii) administration of Ab oligomers (synthetic, derived from AD brains o…”
Retracted
Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359
Gene Dose of Apolipoprotein E Type 4 Allele and the Risk of Alzheimer's Disease in Late Onset Families
Corder, E. H., Saunders, A. M., Strittmatter, W. J., Schmechel, D. E., Gaskell, P. C., Small, G. W., Roses, A. D., Haines, J. L., & Pericak-Vance, M. A. (1993) · Science · doi:10.1126/science.8346443 · Cited by 9,429
Alzheimer's Disease Is a Synaptic Failure
Selkoe, D. J. (2002) · Science · doi:10.1126/science.1074069 · Cited by 4,420
Physical basis of cognitive alterations in alzheimer's disease: Synapse loss is the major correlate of cognitive impairment
Terry, R. D., Masliah, E., Salmon, D. P., Butters, N., DeTeresa, R., Hill, R., Hansen, L. A., & Katzman, R. (1991) · Annals of Neurology · doi:10.1002/ana.410300410 · Cited by 4,397
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
Amyloid-β protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory
Shankar, G. M., Li, S., Mehta, T. H., Garcia-Munoz, A., Shepardson, N. E., Smith, I., Brett, F. M., Farrell, M. A., Rowan, M. J., Lemere, C. A., et al. (2008) · Nature Medicine · doi:10.1038/nm1782 · Cited by 3,685
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
Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease
Arriagada, P. V., Growdon, J. H., Hedley-Whyte, E. T., & Hyman, B. T. (1992) · Neurology · doi:10.1212/wnl.42.3.631 · Cited by 2,668
Amyloid deposition as the central event in the aetiology of Alzheimer’s disease
Hardy, J., & Allsop, D. (1991) · Trends in Pharmacological Sciences · doi:10.1016/0165-6147(91)90609-v · Cited by 2,538

Show all 181 references

Sorted by citations

Amyloid Beta: Structure, Biology and Structure-Based Therapeutic Development
Chen, G.-F., Xu, T.-H., Yan, Y., Zhou, Y.-R., Jiang, Y., Melcher, K., & Xu, H. E. (2017) · Acta Pharmacologica Sinica · doi:10.1038/aps.2017.28 · Cited by 1,965
A critical appraisal of amyloid-β-targeting therapies for Alzheimer disease
Panza, F., Lozupone, M., Logroscino, G., & Imbimbo, B. P. (2019) · Nature Reviews Neurology · doi:10.1038/s41582-018-0116-6 · Cited by 965
Clinical trials of new drugs for Alzheimer disease
Huang, L.-K., Chao, S.-P., & Hu, C.-J. (2020) · Journal of Biomedical Science · doi:10.1186/s12929-019-0609-7 · Cited by 702
“Soluble Aβ exerts a physiological function, modulating synaptic function and facilitating neuronal growth; furthermore, Aβ protects the brain from infections, repairs leaks in the blood–brain barrier, and promotes recovery from injury [57, 58].”
Background
The Physiological Roles of Amyloid-β Peptide Hint at New Ways to Treat Alzheimer's Disease
Brothers, H. M., Gosztyla, M. L., & Robinson, S. R. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00118 · Cited by 314
Role of Amyloid-β and Tau Proteins in Alzheimer’s Disease: Confuting the Amyloid Cascade
Gulisano, W., Maugeri, D., Baltrons, M. A., Fà, M., Amato, A., Palmeri, A., D’Adamio, L., Grassi, C., Devanand, D. P., Honig, L. S., et al. (2018) · Journal of Alzheimer's Disease · doi:10.3233/jad-179935 · Cited by 313
Self-citation
Therapies for Prevention and Treatment of Alzheimer’s Disease
Mendiola-Precoma, J., Berumen, L. C., Padilla, K., & García‐Alcocer, G. (2016) · BioMed Research International · doi:10.1155/2016/2589276 · Cited by 262
Questions concerning the role of amyloid-β in the definition, aetiology and diagnosis of Alzheimer’s disease
Morris, G. P., Clark, I. A., & Vissel, B. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1918-8 · Cited by 212
The duality of amyloid-β: its role in normal and Alzheimer’s disease states
Azargoonjahromi, A. (2024) · Molecular Brain · doi:10.1186/s13041-024-01118-1 · Cited by 214
Amyloid‐β immunotherapy for alzheimer disease: Is it now a long shot?
Panza, F., Lozupone, M., Seripa, D., & Imbimbo, B. P. (2019) · Annals of Neurology · doi:10.1002/ana.25410 · Cited by 178
Innovative Therapy for Alzheimer’s Disease-With Focus on Biodelivery of NGF
Mitra, S., Behbahani, H., & Eriksdotter, M. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00038 · Cited by 164
Alzheimer’s Disease as a Membrane Disorder: Spatial Cross-Talk Among Beta-Amyloid Peptides, Nicotinic Acetylcholine Receptors and Lipid Rafts
Fabiani, C., & Antollini, S. S. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00309 · Cited by 158
Alpha 7 nicotinic acetylcholine receptor and its effects on Alzheimer's disease
Ma, K., & Qian, Y. (2018) · Neuropeptides · doi:10.1016/j.npep.2018.12.003 · Cited by 147
Microglial activation states and their implications for Alzheimer's Disease
Valiukas, Z., Tangalakis, K., Apostolopoulos, V., & Feehan, J. (2025) · The Journal of Prevention of Alzheimer s Disease · doi:10.1016/j.tjpad.2024.100013 · Cited by 167
Investigational BACE inhibitors for the treatment of Alzheimer’s disease
Imbimbo, B. P., & Watling, M. (2019) · Expert Opinion on Investigational Drugs · doi:10.1080/13543784.2019.1683160 · Cited by 132
How serotonin receptors regulate morphogenic signalling in neurons
Wirth, A., Holst, K., & Ponimaskin, E. G. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2016.03.007 · Cited by 125
Minocycline reduces inflammatory parameters in the brain structures and serum and reverses memory impairment caused by the administration of amyloid β (1-42) in mice
Garcez, M. L., Mina, F., Bellettini-Santos, T., Carneiro, F. G., Luz, A. P., Schiavo, G. L., Andrighetti, M. S., Scheid, M. G., Bolfe, R. P., & Budni, J. (2017) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2017.03.010 · Cited by 102
Neuromodulatory Action of Picomolar Extracellular Aβ42 Oligomers on Presynaptic and Postsynaptic Mechanisms Underlying Synaptic Function and Memory
Gulisano, W., Melone, M., Ripoli, C., Tropea, M. R., Li Puma, D. D., Giunta, S., Cocco, S., Marcotulli, D., Origlia, N., Palmeri, A., et al. (2019) · The Journal of Neuroscience · doi:10.1523/jneurosci.0163-19.2019 · Cited by 100
Self-citation
Alzheimer’s disease (AD) therapeutics – 1: Repeated clinical failures continue to question the amyloid hypothesis of AD and the current understanding of AD causality
Mullane, K., & Williams, M. (2018) · Biochemical Pharmacology · doi:10.1016/j.bcp.2018.09.026 · Cited by 98
Role of Chemokines in the Development and Progression of Alzheimer’s Disease
Wojcieszak, J., Kuczyńska, K., & Zawilska, J. B. (2022) · Journal of Molecular Neuroscience · doi:10.1007/s12031-022-02047-1 · Cited by 97
Tissue Engineering and Regenerative Medicine 2015: A Year in Review
Wobma, H., & Vunjak‐Novakovic, G. (2015) · Tissue Engineering Part B Reviews · doi:10.1089/ten.teb.2015.0535 · Cited by 92
Ascorbic acid ameliorates behavioural deficits and neuropathological alterations in rat model of Alzheimer’s disease
Olajide, O. J., Yawson, E. O., Gbadamosi, I. T., Arogundade, T. T., Lambe, E., Obasi, K., Lawal, I. T., Ibrahim, A., & Ogunrinola, K. Y. (2017) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2017.02.010 · Cited by 79
Amyloid-β Peptide Is Needed for cGMP-Induced Long-Term Potentiation and Memory
Palmeri, A., Ricciarelli, R., Gulisano, W., Rivera, D., Rebosio, C., Calcagno, E., Tropea, M. R., Conti, S., Das, U., Roy, S., et al. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.3607-16.2017 · Cited by 79
Self-citation
Membrane Interactions and Toxicity by Misfolded Protein Oligomers
Gonzalez-Garcia, M., Fusco, G., & Simone, A. D. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.642623 · Cited by 73
Role of monomeric amyloid-β in cognitive performance in Alzheimer's disease: Insights from clinical trials with secretase inhibitors and monoclonal antibodies
Imbimbo, B. P., Ippati, S., Watling, M., & Imbimbo, C. (2022) · Pharmacological Research · doi:10.1016/j.phrs.2022.106631 · Cited by 69
Time-dependent reversal of synaptic plasticity induced by physiological concentrations of oligomeric Aβ42: an early index of Alzheimer’s disease
Koppensteiner, P., Trinchese, F., Fà, M., Puzzo, D., Gulisano, W., Yan, S., Poussin, A., Liu, S., Orozco, I. J., Dale, E., et al. (2016) · Scientific Reports · doi:10.1038/srep32553 · Cited by 67
Self-citation
Potentials of Neuropeptides as Therapeutic Agents for Neurological Diseases
Yeo, X. Y., Cunliffe, G., Ho, R., Lee, S. S., & Jung, S. (2022) · Biomedicines · doi:10.3390/biomedicines10020343 · Cited by 66
Molecular Modulation of Human α7 Nicotinic Receptor by Amyloid-β Peptides
Lasala, M., Fabiani, C., Corradi, J., Antollini, S. S., & Bouzat, C. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00037 · Cited by 59
Diminished α7 nicotinic acetylcholine receptor (α7nAChR) rescues amyloid-β induced atrial remodeling by oxi-CaMKII/MAPK/AP-1 axis-mediated mitochondrial oxidative stress
Zhao, J.-K., Yu, L.-M., Xue, X., Xu, Y., Huang, T., Xu, D., Wang, Z.-S., Luo, L., & Wang, H.-S. (2023) · Redox Biology · doi:10.1016/j.redox.2022.102594 · Cited by 50
Nitric oxide/cGMP/CREB pathway and amyloid-beta crosstalk: From physiology to Alzheimer’s disease
Tropea, M. R., Gulisano, W., Vacanti, V., Arancio, O., Puzzo, D., & Palmeri, A. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.11.022 · Cited by 55
Self-citation
Evaluation and targeting of amyloid precursor protein (APP)/amyloid beta (Aβ) axis in amyloidogenic and non-amyloidogenic pathways: A time outside the tunnel
Al-Kuraishy, H. M., Jabir, M. S., Al-Gareeb, A. I., Albuhadily, A. K., Albukhaty, S., Sulaiman, G. M., & Batiha, G. E. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.102119 · Cited by 58
Neonicotinoid Insecticides Alter the Gene Expression Profile of Neuron-Enriched Cultures from Neonatal Rat Cerebellum
Kimura‐Kuroda, J., Nishito, Y., Yanagisawa, H., Kuroda, Y., Komuta, Y., Kawano, H., & Hayashi, M. (2016) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph13100987 · Cited by 52
Dementias
Sacuiu, S. F. (2016) · Handbook of clinical neurology · doi:10.1016/b978-0-12-802973-2.00008-2 · Cited by 57
Intracellular metalloprotease activity controls intraneuronal Aβ aggregation and limits secretion of Aβ via exosomes
Pacheco‐Quinto, J., Clausen, D. M., Pérez‐González, R., Peng, H., Meszaros, A., Eckman, C. B., Levy, E., & Eckman, E. A. (2018) · The FASEB Journal · doi:10.1096/fj.201801319r · Cited by 46
Early Alterations of Hippocampal Neuronal Firing Induced by Abeta42
Gavello, D., Calorio, C., Franchino, C., Cesano, F., Carabelli, V., Carbone, E., & Marcantoni, A. (2016) · Cerebral Cortex · doi:10.1093/cercor/bhw377 · Cited by 45
Toward a Unified Framework in Molecular Neurobiology of Alzheimer’s Disease: Revisiting the Pathophysiological Hypotheses
Hein, Z. M., Karikalan, B., Gopalakrishna, P. K., Dhevi, K., Alkatiri, A., Hussan, F., Mohd Moklas, M. A., Jagadeesan, S., Che Ramli, M. D., Che Mohd Nassir, C. M. N., et al. (2026) · Molecular Neurobiology · doi:10.1007/s12035-025-05602-0 · Cited by 43
Major amyloid-β degrading enzymes endothelin-converting enzyme-2 and neprilysin are expressed by distinct populations of GABAergic interneurons in hippocampus and neocortex
Pacheco-Quinto, J., Eckman, C., & Eckman, E. (2016) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2016.08.011 · Cited by 33
Unified theory of Alzheimer’s disease (UTAD): implications for prevention and curative therapy
Nehls, M. (2016) · Journal of Molecular Psychiatry · doi:10.1186/s40303-016-0018-8 · Cited by 41
Do BACE inhibitor failures in Alzheimer patients challenge the amyloid hypothesis of the disease?
Panza, F., Lozupone, M., Watling, M. I. L., & Imbimbo, B. P. (2019) · Expert Review of Neurotherapeutics · doi:10.1080/14737175.2019.1621751 · Cited by 42
Alzheimer's disease: The use of contrast agents for magnetic resonance imaging to detect amyloid beta peptide inside the brain
Salerno, M., & Porqueras, D. S. D. (2016) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2016.04.018 · Cited by 41
Genetic deletion of α7 nicotinic acetylcholine receptors induces an age-dependent Alzheimer’s disease-like pathology
Tropea, M. R., Puma, D. D. L., Melone, M., Gulisano, W., Arancio, O., Grassi, C., Conti, F., & Puzzo, D. (2021) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2021.102154 · Cited by 42
Self-citation
When, where and how? Focus on neuronal calcium dysfunctions in Alzheimer’s Disease
Agostini, M., & Fasolato, C. (2016) · Cell Calcium · doi:10.1016/j.ceca.2016.06.008 · Cited by 40
Alpha7 nicotinic acetylcholine receptor is required for amyloid pathology in brain endothelial cells induced by Glycoprotein 120, methamphetamine and nicotine
Liu, L., Yu, J., Li, L., Zhang, B., Liu, L., Wu, C., Jong, A., Mao, D.-A., & Huang, S. (2017) · Scientific Reports · doi:10.1038/srep40467 · Cited by 36
Elucidating Important Sites and the Mechanism for Amyloid Fibril Formation by Coarse-Grained Molecular Dynamics
Rojas, A. V., Maisuradze, N., Kachlishvili, K., Scheraga, H. A., & Maisuradze, G. G. (2016) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.6b00331 · Cited by 36
Discovery of Conformationally Restricted Human Glutaminyl Cyclase Inhibitors as Potent Anti-Alzheimer’s Agents by Structure-Based Design
Hoang, V.-H., Ngo, V. T. H., Cui, M., Mạnh, N. V., Tran, P., Ann, J., Ha, H.-J., Kim, H., Choi, K., Kim, Y.-H., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b00751 · Cited by 35
Intracerebroventricular administration of okadaic acid induces hippocampal glucose uptake dysfunction and tau phosphorylation
Cunha, N. B., Hansen, F., Brolese, G., Batassini, C., Pedroso, F. L., Galland, F., dos Santos, J. P. A., Dutra, M. F., & Gonçalves, C. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.04.014 · Cited by 33
Active Vaccines for Alzheimer Disease Treatment
Sterner, R. M., Takahashi, P. Y., & Ballard, A. Y. (2016) · Journal of the American Medical Directors Association · doi:10.1016/j.jamda.2016.06.009 · Cited by 33
Free-floating adult human brain-derived slice cultures as a model to study the neuronal impact of Alzheimer’s disease-associated Aβ oligomers
Mendes, N. D., Fernandes, A., de Almeida, G. M., Santos, L. E., Sellés, M. C., Silva, N. M. L. E., Machado, C. D. M., Horta‐Júnior, J. D. A. C., Louzada, P. R., Felice, F. G. D., et al. (2018) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2018.05.021 · Cited by 35
Depichering the Effects of Astragaloside IV on AD‐Like Phenotypes: A Systematic and Experimental Investigation
Wang, X., Gao, F., Xu, W., Cao, Y., Wang, J., & Zhu, G. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/1020614 · Cited by 32
Based on molecular structures: Amyloid-β generation, clearance, toxicity and therapeutic strategies
Yang, H., Li, J., Li, X., Ma, L., Hou, M., Zhou, H., & Zhou, R. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.927530 · Cited by 33
Small molecule LX2343 ameliorates cognitive deficits in AD model mice by targeting both amyloid β production and clearance
Guo, X., Sun, G., Zhou, T., Xu, X., Zhu, Z., Rukachaisirikul, V., Hu, L., & Shen, X. (2016) · Acta Pharmacologica Sinica · doi:10.1038/aps.2016.80 · Cited by 25
Spatially resolved mass spectrometry analysis of amyloid plaque‐associated lipids
Blank, M., & Hopf, C. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15216 · Cited by 24
Benzimidazole and Benzoxazole Derivatives Against Alzheimer's Disease
Faydalı, N., & Temiz‐Arpacı, Ö. (2024) · Chemistry & Biodiversity · doi:10.1002/cbdv.202400123 · Cited by 22
Association between ABCB1 polymorphisms and haplotypes and Alzheimer’s disease: a meta-analysis
Zhong, X., Liu, M.-Y., Sun, X., & Wei, M. (2016) · Scientific Reports · doi:10.1038/srep32708 · Cited by 22
Multitarget Drug Design Strategy in Alzheimer'S Disease: Focus on Cholinergic Transmission and Amyloid-β Aggregation
Simoni, E., Bartolini, M., Abu, I. F., Blockley, A., Gotti, C., Bottegoni, G., Caporaso, R., Bergamini, C., Andrisano, V., Cavalli, A., et al. (2017) · Future Medicinal Chemistry · doi:10.4155/fmc-2017-0039 · Cited by 22
The p38 mitogen activated protein kinase regulates β-amyloid protein internalization through the α7 nicotinic acetylcholine receptor in mouse brain
Ma, K., Lv, J., Yang, W., Chang, K.-W., Hu, X., Shi, L., Zhai, W.-Y., Zong, H.-F., & Qian, Y. (2017) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2017.11.006 · Cited by 21
Steady, Symmetric, and Reversible Growth and Dissolution of Individual Amyloid-β Fibrils
Xu, Y., Safari, M. S., Ma, W., Schafer, N. P., Wolynes, P. G., & Vekilov, P. G. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00179 · Cited by 20
Protein kinases A and C regulate amyloid-β degradation by modulating protein levels of neprilysin and insulin-degrading enzyme in astrocytes
Yamamoto, N., Nakazawa, M., Nunono, N., Yoshida, N., Obuchi, A., Tanida, M., Suzuki, K., Ikeda‐Matsuo, Y., & Sobue, K. (2020) · Neuroscience Research · doi:10.1016/j.neures.2020.05.008 · Cited by 20
Structural polymorphism and cytotoxicity of brain‐derived β‐amyloid extracts
Adem, K. A., & Lee, S.-M. (2023) · Protein Science · doi:10.1002/pro.4639 · Cited by 14
Mitogen-activated protein kinase phosphatase 1 protects PC12 cells from amyloid beta-induced neurotoxicity
Li, X., Gu, Y., Ma, L., Bai, X., Jie, J., Zhang, X.-F., & Chen, D. (2018) · Neural Regeneration Research · doi:10.4103/1673-5374.238621 · Cited by 19
Protective Role of Electroacupuncture Against Cognitive Impairment in Neurological Diseases
Xin, Y., Zhou, S., Chu, T., Zhou, Y., & Xu, A. (2024) · Current Neuropharmacology · doi:10.2174/1570159x22999240209102116 · Cited by 18
Interaction of Isoflurane, Tumor Necrosis Factor-α and β-Amyloid on Long-term Potentiation in Rat Hippocampal Slices
Zhou, R., & Bickler, P. E. (2016) · Anesthesia & Analgesia · doi:10.1213/ane.0000000000001698 · Cited by 16
Discovery of highly potent human glutaminyl cyclase (QC) inhibitors as anti-Alzheimer's agents by the combination of pharmacophore-based and structure-based design
Mạnh, N. V., Hoang, V.-H., Ngo, V. T. H., Ann, J., Jang, T., Ha, J.-H., Song, J. Y., Ha, H.-J., Kim, H., Kim, Y.-H., et al. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113819 · Cited by 17
Modified Snake α-Neurotoxin Averts β-Amyloid Binding to α7 Nicotinic Acetylcholine Receptor and Reverses Cognitive Deficits in Alzheimer’s Disease Mice
Fonar, G., Polis, B., Sams, D. S., Levi, A., Malka, A., Bal, N. V., Maltsev, A. V., Elliott, E., & Samson, A. O. (2021) · Molecular Neurobiology · doi:10.1007/s12035-020-02270-0 · Cited by 16
Hearing loss and impaired short-term memory in an Alzheimer's disease mouse model of amyloid-beta pathology
Jafari, Z., Afrashteh, N., Kolb, B. E., & Mohajerani, M. H. (2023) · Experimental Neurology · doi:10.1016/j.expneurol.2023.114413 · Cited by 17
In Vivo Sub-chronic Treatment with Dichlorvos in Young Rats Promotes Synaptic Plasticity and Learning by a Mechanism that Involves Acylpeptide Hydrolase Instead of Acetylcholinesterase Inhibition. Correlation with Endogenous β-Amyloid Levels
García‐Rojo, G., Gámiz, F., Ampuero, E., Rojas-Espina, D., Sandoval, R., Rozas, C., Morales, B., Wyneken, Ú., & Pancetti, F. C. (2017) · Frontiers in Pharmacology · doi:10.3389/fphar.2017.00483 · Cited by 16
Effects of novel acylhydrazones derived from 4-quinolone on the acetylcholinesterase activity and Aβ42 peptide fibrils formation
da Silva, G. S., Figueiró, M., Tormena, C. F., Coelho, F., & Almeida, W. P. (2016) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.3109/14756366.2016.1144597 · Cited by 16
Multifunctional imaging of amyloid-beta peptides with a new gadolinium-based contrast agent in Alzheimer’s disease
Choi, G., Kim, H.-K., Baek, A., Kim, S., Kim, M. J., Kim, M., Cho, A. E., Lee, G. H., Jung, H., Yang, J.-U., et al. (2019) · Journal of Industrial and Engineering Chemistry · doi:10.1016/j.jiec.2019.11.031 · Cited by 16
Multitarget Anti-Alzheimer Hybrid Compounds
Muñoz‐Torrero, D. (2017) · Elsevier eBooks · doi:10.1016/b978-0-08-101011-2.00006-4 · Cited by 15
Structural Isomerism and Enhanced Lipophilicity of Pyrithione Ligands of Organoruthenium(II) Complexes Increase Inhibition on AChE and BuChE
Kladnik, J., Ristovski, S., Kljun, J., Defant, A., Mancini, I., Sepčić, K., & Turel, I. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21165628 · Cited by 14
Synthesis and biological evaluation of ranitidine analogs as multiple-target-directed cognitive enhancers for the treatment of Alzheimer’s disease
Gao, J., Midde, N. M., Zhu, J., Terry, A. V., McInnes, C., & Chapman, J. M. (2016) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2016.09.072 · Cited by 13
Mechanism of Progesterone Action in the Brain
Camacho‐Arroyo, I., Hansberg-Pastor, V., Vázquez-Martínez, E. R., & Cerbón, M. A. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-803592-4.00053-5 · Cited by 14
D‐Ser2‐oxyntomodulin ameliorated Aβ31‐35‐induced circadian rhythm disorder in mice
Wang, L., Zhao, J., Wang, C., Hou, X., Ning, N., Sun, C., Guo, S., Yuan, Y., Lin, L., Hölscher, C., et al. (2019) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.13211 · Cited by 12
RETRACTED ARTICLE: nAChRs gene expression and neuroinflammation in APPswe/PS1dE9 transgenic mouse
D'Angelo, C., Costantini, E., Salvador, N., Marchioni, M., Nicola, M. D., Greig, N., & Reale, M. (2021) · Scientific Reports · doi:10.1038/s41598-021-89139-x · Cited by 14
Retracted
β-amyloid expression in age-related cataract lens epithelia and the effect of β-amyloid on oxidative damage in human lens epithelial cells.
Xu, J., Li, D., Zheng, T., & Lu, Y. (2017) · PubMed Central · Cited by 11
A method for the efficient evaluation of substrate-based cholinesterase imaging probes for Alzheimer’s disease
Darvesh, S., Banfield, S. C., Dufour, M., Forrestall, K. L., Maillet, H., Reid, G. A., Sands, D. C., & Pottie, I. R. (2023) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2023.2225797 · Cited by 10
α7-Nicotinic Acetylcholine Receptors: New Therapeutic Avenues in Alzheimer’s Disease
Öz, M., Petroianu, G. A., & Lorke, D. E. (2016) · Neuromethods · doi:10.1007/978-1-4939-3768-4_9 · Cited by 10
Memory Loss and the Onset of Alzheimer’s Disease Could Be Under the Control of Extracellular Heat Shock Proteins
Arispe, N. J., & Maio, A. D. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-180161 · Cited by 11
Electrochemical studies of human nAChR a7 subunit phosphorylation by kinases PKA, PKC and Src
Ahmad, S., She, Z., & Kraatz, H. (2019) · Analytical Biochemistry · doi:10.1016/j.ab.2019.03.012 · Cited by 9
β‐sheet breakers with consecutive phenylalanines: Insights into mechanism of dissolution of β‐amyloid fibrils
Jarmuła, A., Ludwiczak, J., & Stępkowski, D. (2021) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26057 · Cited by 9
Aβ oligomers: role at the synapse
Puzzo, D. (2019) · Aging · doi:10.18632/aging.101818 · Cited by 9
Self-citation
Vanadyl acetylacetonate attenuates Aβ pathogenesis in APP/PS1 transgenic mice depending on the intervention stage
Tan, C., Dong, Y., Wang, J., & Yang, X. (2019) · New Journal of Chemistry · doi:10.1039/c9nj00820a · Cited by 8
Age‐related synaptic dysfunction in Tg2576 mice starts as a failure in early long‐term potentiation which develops into a full abolishment of late long‐term potentiation
Fernández‐Fernández, D., Dorner‐Ciossek, C., Kroker, K. S., & Rosenbrock, H. (2015) · Journal of Neuroscience Research · doi:10.1002/jnr.23701 · Cited by 7
Cognition-enhancing drugs and applications to aging
Milić, J., Zeković, J., Stankić, D., Henčić, B., Jančić, J., & Samardžić, J. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-818000-6.00033-0 · Cited by 7
Aβ Beyond the AD Pathology: Exploring the Structural Response of Membranes Exposed to Nascent Aβ Peptide
Rondelli, V., Salmona, M., Colombo, L., Fragneto, G., Fadda, G. C., Cantú, L., & Favero, E. D. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218295 · Cited by 7
Alzheimer's Disease; Mechanism, Mutations, and Applications of Nano-Medicine
Maisam, M., Khan, M. T., Lodhi, M. S., Mou, K., Liu, Z., & Wei, D. (2023) · Frontiers in Bioscience-Landmark · doi:10.31083/j.fbl2810258 · Cited by 7
CZ2HF mitigates β-amyloid 25-35 fragment-induced learning and memory impairment through inhibition of neuroinflammation and apoptosis in rats
Zeng, L., Gao, J., Deng, Y., Shi, J., & Gong, Q. (2018) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2018.3952 · Cited by 6
Sinomenine inhibits oxidative stress to attenuate Alzheimer's disease pathology via α7 nicotinic acetylcholine receptor.
Ni, H.-J., Xiong, Y.-Y., Liu, M., Liu, J., Liu, M.-Q., Zhang, L., Zhao, Y., Yi, L., Zhou, R., He, Q., et al. (2026) · Phytomedicine · doi:10.1016/j.phymed.2026.157779 · Cited by 5
Conceptual and Methodological Pitfalls in Experimental Studies: An Overview, and the Case of Alzheimer’s Disease
Puzzo, D., & Conti, F. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.684977 · Cited by 6
Self-citation
The role of Aβ in Alzheimer's Disease as an Evolutionary Outcome of Optimized Innate Immune Defense
Tatar, M. (2022) · The Journal of Prevention of Alzheimer s Disease · doi:10.14283/jpad.2022.68 · Cited by 6
Genetik und Gen-Umwelt-Interaktionen bei psychischen Erkrankungen
Maier, W., Giegling, I., & Rujescu, D. (2017) · Springer eBooks · doi:10.1007/978-3-662-49295-6_5 · Cited by 5
Beyond Amyloid-β: Reevaluating Its Physiological Role to Find Safe Therapies Against Alzheimer’s Disease
Puzzo, D. (2024) · Journal of Alzheimer s Disease · doi:10.3233/jad-240406 · Cited by 3
Self-citation
Towards defining the Mechanisms of Alzheimer's disease based on a contextual analysis of molecular pathways
Richens, J. L., Bramble, J. P., Spencer, H. L., Cantlay, F., Butler, M., & O’Shea, P. (2016) · Global Medical Genetics · doi:10.3934/genet.2016.1.25 · Cited by 3
α7-Nicotinic Acetylcholine Receptors and β-Amyloid Peptides in Alzheimer’s Disease
Lorke, D. E., Petroianu, G. A., & Öz, M. (2016) · Neuromethods · doi:10.1007/978-1-4939-3768-4_10 · Cited by 3
Structure‐Activity Relationship of Fluorinated Benzenesulfonamides as Inhibitors of Amyloid‐β Aggregation
Žvirblis, M., Sakalauskas, A., Alijanvand, S. H., Dudutienė, V., Žiaunys, M., Sniečkutė, R., Otzen, D. E., Smirnovas, V., & Matulis, D. (2024) · Chemistry - A European Journal · doi:10.1002/chem.202402330 · Cited by 2
The Drosophila adult neuromuscular junction as a model for unravelling amyloid peptide influence on synapse dynamics
Torroja, L., López‐Arias, B., Monedero, I., & Turiégano, E. (2017) · Neural Regeneration Research · doi:10.4103/1673-5374.221154 · Cited by 2
High resolution approaches for the identification of amyloid fragments in brain
Ross, J. A., Mathews, P. M., & Bockstaele, E. J. V. (2018) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2018.10.032 · Cited by 2
Amyloid and tau brain pathology in hyppocampal neurons on the activation of entorhinal cortex on the model of Alzheimer’s disease and in the conditions of protection with galarmin
Vardanyan, A. V., Karapetyan, K., & Alieva, M. B. (2017) · Vestnik of Vitebsk State Medical University · doi:10.22263/2312-4156.2017.5.84 · Cited by 1
Administration of amyloid-β oligomer to the buccal ganglia may reduce food intake and cholinergic synaptic responses within the feeding neural circuit in Aplysia kurodai
Nagahama, T., Nakajima, H., Wakuta, M., Kasahara, Y., Narita, K., & Nagahama, S. (2023) · Neuroscience Research · doi:10.1016/j.neures.2023.06.004 · Cited by 1
Cholesterol´s role in membrane organization and nicotinic acetylcholine receptor function: Implications for aging and Alzheimer's disease
Peñalva, D. A., Munafó, J. P., & Antollini, S. S. (2025) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2025.105484 · Cited by 1
Amyloid-β Effects on Peripheral Nerve: A New Model System
Stecker, M. M., Srivastava, A., & Reiss, A. B. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241914488 · Cited by 2

Authors: Puzzo, D., Gulisano, W., Arancio, O., & Palmeri, A.
Affiliations: University of Catania (IT)
Columbia University (US)
Corresponding author: Puzzo, D.
ORCID: Puzzo, D.
Gulisano, W.
Arancio, O.
Palmeri, A.
Venue: Neuroscience
Publisher: Elsevier BV
Published: 2015-10
Volume: 307
Pages: 26-36
ISSN: 0306-4522 (ISSN-L)
DOI: 10.1016/j.neuroscience.2015.08.039
PMC: PMC4591241
OpenAlex: W1149434589
Cited by: 116
References: 181
Citations by year: 2026: 2 · 2025: 5 · 2024: 5 · 2023: 8 · 2022: 7 · 2021: 14 · 2020: 7 · 2019: 15 · 2018: 11 · 2017: 17 · 2016: 23 · 2015: 2
FWCI: 2.21
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Neuroscience (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: Alzheimer’s Association (NIRG-07-59597, IIRG-09-134220)
National Institutes of Health (NS049442, AG034248)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords: Alzheimer's disease pathogenesis, amyloid-beta, amyloid hypothesis, alpha7 nicotinic acetylcholine receptor, negative feedback loop, synaptic plasticity, memory loss, synaptic dysfunction
MeSH terms: Alzheimer Disease, Animals, Humans, Signal Transduction, Amyloid beta-Peptides, Amyloid beta-Protein Precursor

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

The keystone of Alzheimer pathogenesis might be sought in Aβ physiology

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks