Picomolar Amyloid-β Positively Modulates Synaptic Plasticity and Memory in Hippocampus

The Mouse Brain in Stereotaxic Coordinates

Paxinos, G. (2001) · Cited by 12,859

Short-Term Synaptic Plasticity

Zucker, R. S., & Regehr, W. G. (2002) · Annual Review of Physiology · doi:10.1146/annurev.physiol.64.092501.114547 · Cited by 5,068

Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide

Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744

Differential contribution of amygdala and hippocampus to cued and contextual fear conditioning.

Phillips, R. G., & LeDoux, J. E. (1992) · Behavioral Neuroscience · doi:10.1037/0735-7044.106.2.274 · Cited by 3,292

mouse brain in stereotaxic coordinates

Franklin, K. B. J., & Paxinos, G. (1997) · Cited by 3,258

Neurotrophic and Neurotoxic Effects of Amyloid β Protein: Reversal by Tachykinin Neuropeptides

Yankner, B. A., Duffy, L. K., & Kirschner, D. A. (1990) · Science · doi:10.1126/science.2218531 · Cited by 1,975

APP Processing and Synaptic Function

Kamenetz, F., Tomita, T., Hsieh, H., Seabrook, G., Borchelt, D., Iwatsubo, T., Sisodia, S., & Malinow, R. (2003) · Neuron · doi:10.1016/s0896-6273(03)00124-7 · Cited by 1,644

Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid β-protein in both transfected cells and transgenic mice

Citron, M., Westaway, D., Xia, W., Carlson, G., Diehl, T., Levesque, G., Johnson-wood, K., Lee, M., Seubert, P., Davis, A., et al. (1997) · Nature Medicine · doi:10.1038/nm0197-67 · Cited by 1,271

Synaptic Activity Regulates Interstitial Fluid Amyloid-β Levels In Vivo

Cirrito, J. R., Yamada, K. A., Finn, M. B., Sloviter, R. S., Bales, K. R., May, P. C., Schoepp, D. D., Paul, S. M., Mennerick, S., & Holtzman, D. M. (2005) · Neuron · doi:10.1016/j.neuron.2005.10.028 · Cited by 1,265

A Transcriptively Active Complex of APP with Fe65 and Histone Acetyltransferase Tip60

Cao, X., & Südhof, T. C. (2001) · Science · doi:10.1126/science.1058783 · Cited by 1,202

DrosophilaNeprilysins Are Involved in Middle-Term and Long-Term Memory

Turrel, O., Lampin-Saint-Amaux, A., Préat, T., & Goguel, V. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.3730-15.2016 · Cited by 25

The Tyr216 phosphorylated form of GSK3β contributes to tau phosphorylation at PHF-1 epitope in response to Aβ in the nucleus of SH-SY5Y cells

Noël, A., Barrier, L., & Ingrand, S. S. (2016) · Life Sciences · doi:10.1016/j.lfs.2016.06.020 · Cited by 24

Nonamyloidogenic processing of amyloid beta precursor protein is associated with retinal function improvement in aging male APPswe/PS1ΔE9 mice

Joly, S., Lamoureux, S., & Pernet, V. (2017) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2017.02.004 · Cited by 24

Exogenous Aβ1-42 monomers improve synaptic and cognitive function in Alzheimer's disease model mice

Duan, Y., Lv, J., Zhang, Z., Chen, Z., Wu, H., Chen, J., Chen, Z., Yang, J., Wang, D., Liu, Y., et al. (2022) · Neuropharmacology · doi:10.1016/j.neuropharm.2022.109002 · Cited by 24

Amyloid-β in Alzheimer’s disease – front and centre after all?

Weglinski, C., & Jeans, A. F. (2022) · Neuronal Signaling · doi:10.1042/ns20220086 · Cited by 24

Brain Region-Specific Differences in Amyloid-β Plaque Composition in 5XFAD Mice

Bader, A. S., Gnädig, M.-U., Fricke, M., Büschgens, L., Berger, L. J., Klafki, H., Meyer, T., Jahn, O., Weggen, S., & Wirths, O. (2023) · Life · doi:10.3390/life13041053 · Cited by 26

Role of Syndecans in Lipid Metabolism and Human Diseases

Леонова, Е. И., & Galzitskaya, O. V. (2015) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-17344-3_10 · Cited by 26

Reduction of epileptiform activity by valproic acid in a mouse model of Alzheimer's disease is not long-lasting after treatment discontinuation

Ziyatdinova, S., Viswanathan, J., Hiltunen, M. O., Tanila, H., & Pitkänen, A. (2015) · Epilepsy Research · doi:10.1016/j.eplepsyres.2015.02.005 · Cited by 23

Diabetes, Insulin and Alzheimer's Disease

Craft, S., & Christen, Y. (2010) · Research and perspectives in Alzheimer's disease · doi:10.1007/978-3-642-04300-0 · Cited by 24

DrosophilaNeprilysin 1 Rescues Memory Deficits Caused by Amyloid-β Peptide

Turrel, O., Goguel, V., & Préat, T. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.1634-17.2017 · Cited by 24

Bryostatin-1 vs. TPPB: Dose-Dependent APP Processing and PKC-α, -δ, and -ε Isoform Activation in SH-SY5Y Neuronal Cells

Yi, P., Schrott, L. M., Castor, T. P., & Alexander, J. (2012) · Journal of Molecular Neuroscience · doi:10.1007/s12031-012-9816-3 · Cited by 24

Natural Products from Plants and Algae for Treatment of Alzheimer’s Disease: A Review

Klose, J., Griehl, C., Roßner, S., & Schilling, S. (2022) · Biomolecules · doi:10.3390/biom12050694 · Cited by 23

Divergent actions of physiological and pathological amyloid-β on synapses in live human brain slice cultures

McGeachan, R. I., Meftah, S., Taylor, L. W., Catterson, J. H., Negro, D., Bonthron, C., Holt, K., Tulloch, J., Rose, J. L., Gobbo, F., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-58879-z · Cited by 23

Amyloid β: Walking on the dark side of the moon

Fedele, E., Rivera, D., Marengo, B., Pronzato, M. A., & Ricciarelli, R. (2015) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2015.09.001 · Cited by 23

Effects of soluble β-amyloid on the release of neurotransmitters from rat brain synaptosomes

Olivero, G., Grilli, M., Chen, J., Preda, S., Mura, E., Govoni, S. M., & Marchi, M. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00166 · Cited by 23

5-HT4 Receptor Stimulation Leads to Soluble AβPPα Production Through MMP-9 Upregulation

Hashimoto, G., Sakurai, M., Teich, A. F., Saeed, F., Aziz, F., & Arancio, O. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-111235 · Cited by 25

FSTL1-knockdown improves neural oscillation via decreasing neuronal-inflammation regulating apoptosis in Aβ1–42 induced AD model mice

Kumari, E., Xu, A., Chen, R., Yan, Y., Yang, Z. R., & Zhang, T. (2022) · Experimental Neurology · doi:10.1016/j.expneurol.2022.114231 · Cited by 21

The Brain’s Structural Connectome Mediates the Relationship between Regional Neuroimaging Biomarkers in Alzheimer’s Disease

Pandya, S., Initiative, A. D. N., Kuceyeski, A. F., & Raj, A. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160090 · Cited by 24

Cholinergic Homeostatic Synaptic Plasticity Drives the Progression of Aβ-Induced Changes in Neural Activity

Hahm, E.-T., Nagaraja, R. Y., Waro, G., & Tsunoda, S. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.06.029 · Cited by 24

Geriatric epilepsy: Research and clinical directions for the future

Roberson, E. D., Hope, O. A., Martin, R. C., & Schmidt, D. (2011) · Epilepsy & Behavior · doi:10.1016/j.yebeh.2011.04.005 · Cited by 20

Higher baseline levels of CSF inflammation increase risk of incident mild cognitive impairment and Alzheimer's disease dementia

Contreras, J. A., Aslanyan, V., Albrecht, D., Mack, W. J., Initiative, A. D. N., & Pa, J. (2022) · Alzheimer s & Dementia Diagnosis Assessment & Disease Monitoring · doi:10.1002/dad2.12346 · Cited by 20

Nucleic acid aptamer-based electrochemical sensor for the detection of serum P-tau231 and the instant screening test of Alzheimer’s disease

Kong, Q., Liu, C., Zhang, Y., He, Y., Zhang, R., Wang, Y., Zhou, Q., & Cui, F. (2024) · Microchimica Acta · doi:10.1007/s00604-024-06395-0 · Cited by 21

Expression of Phenotypic Astrocyte Marker Is Increased in a Transgenic Mouse Model of Alzheimer’s Disease versus Age-Matched Controls: A Presymptomatic Stage Study

Doméné, A., Cavanagh, C., Page, G., Bodard, S., Klein, C., Delarasse, C., Chalon, S., & Krantic, S. M. (2016) · International Journal of Alzheimer s Disease · doi:10.1155/2016/5696241 · Cited by 21

Brain rhythm attractor breakdown in Alzheimer’s disease: Functional and pathologic implications

Karageorgiou, E., & Vossel, K. A. (2017) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2017.02.003 · Cited by 21

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

Tuning of Glutamate, But Not GABA, Release by an Intrasynaptic Vesicle APP Domain Whose Function Can Be Modulated by β- or α-Secretase Cleavage

Yao, W., Tambini, M. D., Liu, X., & D'adamio, L. (2019) · Journal of Neuroscience · doi:10.1523/jneurosci.0207-19.2019 · Cited by 20

Aη-α and Aη-β peptides impair LTP ex vivo within the low nanomolar range and impact neuronal activity in vivo

Mensch, M., Dunot, J., Yishan, S. M., Harris, S., Blistein, A., Avdiu, A., Pousinha, P. A., Giudici, C., Busche, M. A., Jedlička, P., et al. (2021) · Alzheimer s Research & Therapy · doi:10.1186/s13195-021-00860-1 · Cited by 24

Age-Related Oxidative Redox and Metabolic Changes Precede Intraneuronal Amyloid-β Accumulation and Plaque Deposition in a Transgenic Alzheimer’s Disease Mouse Model

Pontrello, C. G., McWhirt, J., Glabe, C. G., & Brewer, G. J. (2022) · Journal of Alzheimer s Disease · doi:10.3233/jad-220824 · Cited by 20

Implication of the cooking oil-peroxidation product “hydroxynonenal” for Alzheimer’s disease

Yamashima, T., Seike, T., Mochly‐Rosen, D., Chen, C., Kikuchi, M., & Mizukoshi, E. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1211141 · Cited by 20

Statins for Treating Alzheimer's Disease: Truly Ineffective?

Liang, T. B., Li, R., & Cheng, O. (2015) · European Neurology · doi:10.1159/000382128 · Cited by 20

Beta Amyloid Differently Modulate Nicotinic and Muscarinic Receptor Subtypes which Stimulate in vitro and in vivo the Release of Glycine in the Rat Hippocampus

Zappettini, S., Grilli, M., Olivero, G., Mura, E., Preda, S., Govoni, S. M., Salamone, A., & Marchi, M. (2012) · Frontiers in Pharmacology · doi:10.3389/fphar.2012.00146 · Cited by 20

The Role of Ryanodine Receptors in Regulating Neuronal Activity and Its Connection to the Development of Alzheimer’s Disease

Chiantia, G., Hidişoğlu, E., & Marcantoni, A. (2023) · Cells · doi:10.3390/cells12091236 · Cited by 19

A cell autonomous regulator of neuronal excitability modulates tau in Alzheimer’s disease vulnerable neurons

Rodriguez‐Rodriguez, P., Arroyo‐García, L. E., Tsagkogianni, C., Li, L., Wang, W., Végvári, Á., Salas-Allende, I., Plautz, Z., Cedazo-Mı́nguez, Á., Sinha, S. C., et al. (2024) · Brain · doi:10.1093/brain/awae051 · Cited by 18

Evidence that Alzheimer’s Disease Is a Disease of Competitive Synaptic Plasticity Gone Awry

Huang, Z. (2024) · Journal of Alzheimer s Disease · doi:10.3233/jad-240042 · Cited by 20

Comparing α7 nicotinic acetylcholine receptor binding, amyloid‐β deposition, and mitochondria complex‐I function in living brain: A PET study in aged monkeys

Nishiyama, S., Ohba, H., Kanazawa, M., Kakiuchi, T., & Tsukada, H. (2015) · Synapse · doi:10.1002/syn.21842 · Cited by 19

Specific Neuromodulatory Actions of Amyloid-β on Dopamine Release in Rat Nucleus Accumbens and Caudate Putamen

Mura, E., Preda, S., Govoni, S. M., Lanni, C., Trabace, L., Grilli, M., Lagomarsino, F., Pittaluga, A., & Marchi, M. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-1299 · Cited by 19

Improving the Gene Ontology Resource to Facilitate More Informative Analysis and Interpretation of Alzheimer’s Disease Data

Kramarz, B., Roncaglia, P., Meldal, B., Huntley, R. P., Martin, M. J., Orchard, S. E., Parkinson, H., Brough, D., Bandopadhyay, R., Hooper, N. M., et al. (2018) · Genes · doi:10.3390/genes9120593 · Cited by 19

Assessing Neuroprotective Agents for Aβ-Induced Neurotoxicity

Forest, K. H., & Nichols, R. A. (2019) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2019.05.013 · Cited by 19

Alzheimer Disease: The Role of Aβ in the Glutamatergic System

Campos‐Peña, V., & Antônio, M. (2014) · InTech eBooks · doi:10.5772/57367 · Cited by 24

Early hippocampal hyperexcitability and synaptic reorganization in mouse models of amyloidosis

Ray, A., Loghinov, I., Ravindranath, V., & Barth, A. L. (2024) · iScience · doi:10.1016/j.isci.2024.110629 · Cited by 17

Pharmacological and behavioral profile of N-[(3R)-1-azabicyclo[2.2.2]oct-3-yl]-6-chinolincarboxamide (EVP-5141), a novel α7 nicotinic acetylcholine receptor agonist/serotonin 5-HT3 receptor antagonist

Boess, F., Vry, J. D., Erb, C., Fleßner, T., Hendrix, M., Luithle, J. E. A., Methfessel, C., Schnizler, K., van der Staay, F. J., van Kampen, M., et al. (2012) · Psychopharmacology · doi:10.1007/s00213-012-2933-4 · Cited by 18

The effect of crebanine on memory and cognition impairment via the alpha-7 nicotinic acetylcholine receptor

Rojsanga, P., Boonyarat, C., Utsintong, M., Nemecz, Á., Yamauchi, J. G., Talley, T. T., Olson, A. J., Matsumoto, K., & Vajragupta, O. (2012) · Life Sciences · doi:10.1016/j.lfs.2012.06.017 · Cited by 18

Intracerebroventricular injection of Aβ1-42 combined with two-vessel occlusion accelerate Alzheimer’s disease development in rats

Dai, S. J., Zhang, J. Y., Bao, Y. T., Zhou, X. J., Lin, L. N., Fu, Y. B., Zhang, Y. J., Li, C., & Yang, Y. (2018) · Pathology - Research and Practice · doi:10.1016/j.prp.2018.07.020 · Cited by 19

Microglia CREB-Phosphorylation Mediates Amyloid-β-Induced Neuronal Toxicity

Gao, Y., Liu, E.-J., Wang, W.-J., Wang, Y., Li, X., Wang, X., Li, S., Zhang, S., Li, M., Zhou, Q., et al. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-180286 · Cited by 18

Alzheimer β-amyloid blocks epileptiform activity in hippocampal neurons

Sepúlveda, F. J., Opazo, C., & Aguayo, L. G. (2009) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2009.04.012 · Cited by 18

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

Is cerebrospinal fluid amyloid‐β42 a promising biomarker of response to nusinersen in adult spinal muscular atrophy patients?

Introna, A., Milella, G., D’Errico, E., Fraddosio, A., Scaglione, G., Ucci, M., Ruggieri, M., & Simone, I. L. (2021) · Muscle & Nerve · doi:10.1002/mus.27212 · Cited by 18

Regulation of gene expression by the APP family in the adult cerebral cortex

Ji, H. Y., Shen, J., & Kang, J. (2022) · Scientific Reports · doi:10.1038/s41598-021-04027-8 · Cited by 18

Etiology and Clinical Significance of Network Hyperexcitability in Alzheimer’s Disease: Unanswered Questions and Next Steps

Samudra, N. P., Ranasinghe, K. G., Kirsch, H. E., Rankin, K. P., & Miller, B. L. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-220983 · Cited by 18

Unravelling of molecular biomarkers in synaptic plasticity of Alzheimer’s disease: Critical role of the restoration of neuronal circuits

Pinky, P., Neha, N., Ali, M., Tiwari, P., Alam, M. M., Hattiwale, H. M., Jamal, A., & Parvez, S. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.102069 · Cited by 17

Activation of α7 nicotinic receptor affects APP processing by regulating secretase activity in SH-EP1-α7 nAChR-hAPP695 cells.

Nie, H.-Z., Shi, S., Lukas, R., Zhao, W.-J., Sun, Y.-N., & Yin, M. (2010) · Brain Research · doi:10.1016/j.brainres.2010.07.110 · Cited by 17

Atlas stumbled: Kinesin light chain‐1 variant E triggers a vicious cycle of axonal transport disruption and amyloid‐β generation in Alzheimer's disease

Gan, K. J., Morihara, T., & Silverman, M. A. (2014) · BioEssays · doi:10.1002/bies.201400131 · Cited by 17

Prefrontal Cortical GABAergic Dysfunction Contributes to Aberrant UP-State Duration in APP Knockout Mice

Huo, Q., Chen, M., He, Q., Zhang, J., Li, B., Jin, K., Chen, X., Long, C., & Yang, L. (2016) · Cerebral Cortex · doi:10.1093/cercor/bhw218 · Cited by 17

Aβ1-16 controls synaptic vesicle pools at excitatory synapses via cholinergic modulation of synapsin phosphorylation

Anni, D., Weiss, E., Guhathakurta, D., Akdaş, E. Y., Klueva, J., Zeitler, S., Andres‐Alonso, M., Huth, T., & Fejtová, A. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03835-5 · Cited by 18

On the physiological/pathological link between Aβ peptide, cholesterol, calcium ions and membrane deformation: A molecular dynamics study

Pannuzzo, M. (2016) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2016.03.018 · Cited by 17

Possible contributions of a novel form of synaptic plasticity inAplysiato reward, memory, and their dysfunctions in mammalian brainPreprint

Hawkins, R. D. (2013) · Learning & Memory · doi:10.1101/lm.031237.113 · Cited by 17

Cyclopamine Modulates γ-Secretase-mediated Cleavage of Amyloid Precursor Protein by Altering Its Subcellular Trafficking and Lysosomal Degradation

Vorobyeva, A. G., Lee, R., Miller, S., Longen, C., Sharoni, M., Kandelwal, P. J., Kim, F. J., Marenda, D. R., & Saunders, A. J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.591792 · Cited by 16

Elevated amyloid beta disrupts the nanoscale organization and function of synaptic vesicle pools in hippocampal neurons

Biasetti, L., Rey, S. A., Fowler, M. W., Ratnayaka, J. A., Fennell, K., Smith, C. A., Marshall, K. E., Hall, C. N., Vargas‐Caballero, M., Serpell, L. C., et al. (2022) · Cerebral Cortex · doi:10.1093/cercor/bhac134 · Cited by 15

Acute interleukin-6 modulates key enzymes involved in prefrontal cortex and hippocampal amyloid precursor protein processing

Marko, D. M., Finch, M. S., Yang, A. J. T., Castellani, L. N., Peppler, W. T., Wright, D. C., & MacPherson, R. E. K. (2023) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00520.2022 · Cited by 17

Creation and characterization of BAC-transgenic mice with physiological overexpression of epitope-tagged RCAN1 (DSCR1)

Xing, L., Salas, M. C., Zhang, H., Gittler, J. K., Ludwig, T., Lin, C., Murty, V. V. V. S., Silverman, W. P., Arancio, O., & Tycko, B. (2012) · Mammalian Genome · doi:10.1007/s00335-012-9436-9 · Cited by 16

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

New BACE1 Chimeric Peptide Inhibitors Selectively Prevent AβPP-β Cleavage Decreasing Amyloid-β Production and Accumulation in Alzheimer’s Disease Models

Resende, R., Ferreira‐Marques, M., Moreira, P., Coimbra, J. R. M., Baptista, S. J., Isidoro, C., Salvador, J. A. R., Dinis, T. C. P., Pereira, C., & Santos, A. E. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-200381 · Cited by 17

Immunotherapy Targeting Amyloid-ß Peptides in Alzheimer’s Disease

Zampar, S., & Wirths, O. (2020) · Exon Publications eBooks · doi:10.36255/exonpublications.alzheimersdisease.2020.ch2 · Cited by 18

Effects of Low Amyloid-β (Aβ) Concentration on Aβ1–42 Oligomers Binding and GluN2B Membrane Expression

Gilson, V., Mbebi, C., Sellal, F., & de Barry, J. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-142529 · Cited by 17

LC-MS/MS based analytical strategies for the detection of lipid peroxidation products in biological matrices

Fanti, F., Sergi, M., & Compagnone, D. (2025) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/j.jpba.2025.116681 · Cited by 15

Synthetic, Cell-Derived, Brain-Derived, and Recombinant β-Amyloid: Modelling Alzheimer’s Disease for Research and Drug Development

Varshavskaya, K. B., Mitkevich, V. A., Makarov, A. А., & Barykin, E. P. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232315036 · Cited by 18

Inhibitory effects of beta-amyloid on the nicotinic receptors which stimulate glutamate release in rat hippocampus: the glial contribution

Salamone, A., Mura, E., Zappettini, S., Grilli, M., Olivero, G., Preda, S., Govoni, S. M., & Marchi, M. (2013) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2013.11.011 · Cited by 15

Altered Processing of Amyloid Precursor Protein in Cells Undergoing Apoptosis

Fiorelli, T. N., Kirouac, L., & Padmanabhan, J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0057979 · Cited by 15

Preventing the Spread of Alzheimer’s Disease Neuropathology: A Role for Calcilytics?

Chiarini, A., Gardenal, E., Whitfield, J., Chakravarthy, B., Armato, U., & Prà, I. D. (2015) · Current Pharmaceutical Biotechnology · doi:10.2174/1389201016666150505123813 · Cited by 14

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

α7 nicotinic ACh receptors are necessary for memory recovery and neuroprotection promoted by attention training in amyloid‐β‐infused mice

Telles‐Longui, M., Mourelle, D., Schöwe, N. M., Cipolli, G. C., Malerba, H. N., Buck, H. S., & Viel, T. A. (2019) · British Journal of Pharmacology · doi:10.1111/bph.14744 · Cited by 15

Deciphering an interplay of proteins associated with amyloid β 1-42 peptide and molecular mechanisms of Alzheimer’s disease

Hernández-Zimbrón, L. F., & Rivas-Arancibia, S. (2014) · Reviews in the Neurosciences · doi:10.1515/revneuro-2014-0025 · Cited by 17

Viral capsid assembly as a model for protein aggregation diseases: Active processes catalyzed by cellular assembly machines comprising novel drug targets

Marreiros, R., Müller‐Schiffmann, A., Bader, V., Selvarajah, S., Dey, D., Lingappa, V. R., & Korth, C. (2014) · Virus Research · doi:10.1016/j.virusres.2014.10.003 · Cited by 15

Amyloid Beta-Mediated Changes in Synaptic Function and Spine Number of Neocortical Neurons Depend on NMDA Receptors

Back, M. K., Ruggieri, S., Jacobi, E., & von Engelhardt, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22126298 · Cited by 15

Novel crosstalk mechanisms between GluA3 and Epac2 in synaptic plasticity and memory in Alzheimer's disease

Zhang, T., Dolga, A. M., Eisel, U. L. M., & Schmidt, M. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106389 · Cited by 14

Intrahippocampal administration of a domain antibody that binds aggregated amyloid-β reverses cognitive deficits produced by diet-induced obesity

Osborne, D. M., Fitzgerald, D. P., O’Leary, K. E., Anderson, B. M., Lee, C. C., Tessier, P. M., & McNay, E. C. (2016) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2016.03.005 · Cited by 15

Inhibiting and Remodeling Toxic Amyloid-Beta Oligomer Formation Using a Computationally Designed Drug Molecule That Targets Alzheimer’s Disease

Downey, M. A., Giammona, M. J., Lang, C. A., Buratto, S. K., Singh, A. K., & Bowers, M. T. (2018) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-018-1975-1 · Cited by 15

Amyloid-β (25–35) regulates neuronal damage and memory loss via SIRT1/Nrf2 in the cortex of mice

Zhu, L., Lu, F., Jia, X., Yan, Q., Zhang, X., & Mu, P. (2021) · Journal of Chemical Neuroanatomy · doi:10.1016/j.jchemneu.2021.101945 · Cited by 16

The Neuroprotective Beta Amyloid Hexapeptide Core Reverses Deficits in Synaptic Plasticity in the 5xFAD APP/PS1 Mouse Model

Forest, K. H., Taketa, R., Arora, K., Todorovic, C., & Nichols, R. A. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.576038 · Cited by 13

Rescue of Amyloid-Beta-Induced Inhibition of Nicotinic Acetylcholine Receptors by a Peptide Homologous to the Nicotine Binding Domain of the Alpha 7 Subtype

Nery, A. A., Magdesian, M. H., Trujillo, C. A., Sathler, L. B., Juliano, M. A., Juliano, L., Ulrich, H., & Ferreira, S. T. (2013) · PLoS ONE · doi:10.1371/journal.pone.0067194 · Cited by 14

Abelson Kinases Mediate the Depression of Spontaneous Synaptic Activity Induced by Amyloid Beta 1–42 Peptides

Reichenstein, M., Borovok, N., Sheinin, A., Brider, T., & Michaelevski, I. (2020) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-020-00858-7 · Cited by 13

The interplay of aryl hydrocarbon receptor/WNT/CTNNB1/Notch signaling pathways regulate amyloid beta precursor mRNA/protein expression and effected the learning and memory of mice

Keshavarzi, M., Moradbeygi, F., Mobini, K., Ghaffarian‐Bahraman, A., Mohammadi, P., Ghaedi, A., & Mohammadi‐Bardbori, A. (2021) · Toxicology Research · doi:10.1093/toxres/tfab120 · Cited by 14

Na,K-ATPase Acts as a Beta-Amyloid Receptor Triggering Src Kinase Activation

Petrushanko, I. Y., Tverskoi, A. M., Barykin, E. P., Petrovskaya, A. V., Strelkova, M. A., Leonova, O. G., Anashkina, A. A., Tolstova, A. P., Adzhubei, A. A., Bogdanova, A. Y., et al. (2022) · Cells · doi:10.3390/cells11172753 · Cited by 13

Excitation-inhibition imbalance disrupts visual familiarity in amyloid and non-pathology conditions

Niraula, S., Doderer, J. J., Indulkar, S. S., Berry, K., Hauser, W. L., L’Esperance, O. J., Deng, J. Z., Keeter, G., Rouse, A. G., & Subramanian, J. (2023) · Cell Reports · doi:10.1016/j.celrep.2022.111946 · Cited by 13

Alzheimer’s Disease and Alzheimer’s Disease-Related Dementias in African Americans: Focus on Caregivers

Kopel, J. J., Sehar, U., Choudhury, M., & Reddy, P. H. (2023) · Healthcare · doi:10.3390/healthcare11060868 · Cited by 15

Discoveries and future significance of research into amyloid-beta/α7-containing nicotinic acetylcholine receptor (nAChR) interactions

Whiteaker, P., & George, A. A. (2023) · Pharmacological Research · doi:10.1016/j.phrs.2023.106743 · Cited by 14

A Lipid-Raft Theory of Alzheimer's Disease

Rappoport, A. (2024) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-052024-115455 · Cited by 15

Aβ 1–42 C-terminus fragment derived peptides prevent the self-assembly of the parent peptide

Bansal, S., Maurya, I. K., Shenmar, K., Yadav, N., Thota, C. K., Kumar, V., Tikoo, K., Chauhan, V. S., & Jain, R. (2017) · RSC Advances · doi:10.1039/c6ra26295c · Cited by 13

The Role of Mesenchymal Stem Cells in Regulating Astrocytes-Related Synapse Dysfunction in Early Alzheimer’s Disease

Liu, C. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.927256 · Cited by 13

Role of Drosophila Amyloid Precursor Protein in Memory Formation

Préat, T., & Goguel, V. (2016) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2016.00142 · Cited by 13

A Translational Systems Pharmacology Model for Aβ Kinetics in Mouse, Monkey, and Human

Karelina, T., Demin, O. O., Nicholas, T., Lu, Y., Duvvuri, S., & Barton, H. A. (2017) · CPT Pharmacometrics & Systems Pharmacology · doi:10.1002/psp4.12211 · Cited by 13

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

Assessing Reproducibility in Amyloid β Research: Impact of Aβ Sources on Experimental Outcomes

Foley, A. R., & Raskatov, J. A. (2020) · ChemBioChem · doi:10.1002/cbic.202000125 · Cited by 13

Time for a Change in the Research Paradigm for Alzheimer's Disease: The Value of a Chaotic Matrix Modeling Approach

Hunter, S., Friedland, R. P., & Brayne, C. (2010) · CNS Neuroscience & Therapeutics · doi:10.1111/j.1755-5949.2009.00117.x · 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

Methods for the isolation and analysis of Aβ from postmortem brain

Hong, W., Liu, W., DeSousa, A., Young‐Pearse, T. L., & Walsh, D. M. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1108715 · Cited by 12

The neuroprotective N-terminal amyloid-β core hexapeptide reverses reactive gliosis and gliotoxicity in Alzheimer’s disease pathology models

Lantz, M. J., Roberts, A. M., Delgado, D. D., & Nichols, R. A. (2023) · Journal of Neuroinflammation · doi:10.1186/s12974-023-02807-9 · Cited by 13

Effects of the γ-secretase inhibitor semagacestat on hippocampal neuronal network oscillation

Hajós, M., Morozova, E., Siok, C. J., Atchison, K. P., Nolan, C. E., Riddell, D. R., Kiss, T., & Hajós‐Korcsok, É. (2013) · Frontiers in Pharmacology · doi:10.3389/fphar.2013.00072 · Cited by 12

Clinical Pharmacology of Novel Anti-Alzheimer Disease Modifying Medications

Caraci, F., Bosco, P., Leggio, G. M., Malaguarnera, M., Drago, F., Bucolo, C., & Salomone, S. (2013) · Current Topics in Medicinal Chemistry · doi:10.2174/15680266113139990141 · Cited by 12

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

O4‐06–03: Amyloid‐beta peptide is a positive modulator of synaptic plasticity and memory

Arancio, O., Puzzo, D., Privitera, L., Leznik, E., Fà, M., Staniszewski, A., & Palmeri, A. (2008) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2008.05.547 · Cited by 1

S2‐02–04: Amyloid‐beta: From physiology to pathology

Arancio, O. (2008) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2008.05.279

O4‐03‐05: Amyloid‐beta peptide is required for synaptic plasticity and memory

Puzzo, D., Privitera, L., Leznik, E., Fà, M., Staniszewski, A., Hashimoto, G., Aziz, F., Sakurai, M., Ribé, E. M., Mathews, P. M., et al. (2009) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2009.05.535

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

P3‐219: Picomolar Beta‐Amyloid progressively impairs synaptic plasticity over time while simultaneously increases spontaneous neurotransmission

Fà, M., Koppensteiner, P., Trinchese, F., Liu, S., Ninan, I., & Arancio, O. (2011) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2011.05.1660