Intracellular amyloid-β in Alzheimer's disease

Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein

Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(84)80190-4 · Cited by 5,404

Amyloid plaque core protein in Alzheimer disease and Down syndrome.

Masters, C. L., Simms, G., Weinman, N. A., Multhaup, G., McDonald, B. L., & Beyreuther, K. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.12.4245 · Cited by 4,431

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

Triple-Transgenic Model of Alzheimer’s Disease with Plaques and Tangles

Oddo, S., Caccamo, A., Shepherd, J. D., Murphy, M. P., Golde, T. E., Kayed, R., Metherate, R., Mattson, M. P., Akbari, Y., & LaFerla, F. M. (2003) · Neuron · doi:10.1016/s0896-6273(03)00434-3 · Cited by 4,126

β-Secretase Cleavage of Alzheimer's Amyloid Precursor Protein by the Transmembrane Aspartic Protease BACE

Vassar, R., Bennett, B. D., Babu-Khan, S., Kahn, S., Mendiaz, E. A., Denis, P., Teplow, D. B., Ross, S., Amarante, P., Loeloff, R., et al. (1999) · Science · doi:10.1126/science.286.5440.735 · Cited by 3,876

Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology.

Grundke-Iqbal, I., Iqbal, K., Tung, Y. C., Quinlan, M., Wisniewski, H. M., & Binder, L. I. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.13.4913 · Cited by 3,676

Selective impairment of learning and blockade of long-term potentiation by an N-methyl-D-aspartate receptor antagonist, AP5

Morris, R. G. M., Anderson, E., Lynch, G. S., & Baudry, M. (1986) · Nature · doi:10.1038/319774a0 · Cited by 3,640

Intraneuronal β-Amyloid Aggregates, Neurodegeneration, and Neuron Loss in Transgenic Mice with Five Familial Alzheimer's Disease Mutations: Potential Factors in Amyloid Plaque Formation

Oakley, H., Cole, S. L., Logan, S., Maus, E., Shao, P., Craft, J., Guillozet-Bongaarts, A., Ohno, M., Disterhoft, J., Van Eldik, L., et al. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.1202-06.2006 · Cited by 3,530

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

Schenk, D., Barbour, R., Dunn, W., Gordon, G., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., Khan, K., et al. (1999) · Nature · doi:10.1038/22124 · Cited by 3,160

Aβ-Induced Insulin Resistance and the Effects of Insulin on the Cholesterol Synthesis Pathway and Aβ Secretion in Neural Cells

Najem, D., Bamji‐Mirza, M., Yang, Z., & Zhang, W. (2016) · Neuroscience Bulletin · doi:10.1007/s12264-016-0034-9 · Cited by 32

Tau Derived Hexapeptide AcPHF6 Promotes Beta-Amyloid (Aβ) Fibrillogenesis

Mohamed, T., Gujral, S. S., & Rao, P. P. N. (2017) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.7b00433 · Cited by 31

Donepezil Derivatives Targeting Amyloid-β Cascade in Alzheimer's Disease

Mezeiová, E., Chalupova, K., Nepovimová, E., Górecki, L., Prchal, L., Maliňák, D., Kuča, K., Soukup, O., & Korábečný, J. (2019) · Current Alzheimer Research · doi:10.2174/1567205016666190228122956 · Cited by 31

Glycopeptide Nanofiber Platform for Aβ-Sialic Acid Interaction Analysis and Highly Sensitive Detection of Aβ

Li, L., Geng, R., Xu, Z., Dang, Y., Hu, X., Li, L., Geng, P., Tian, Y., & Zhang, W. (2019) · Analytical Chemistry · doi:10.1021/acs.analchem.9b00377 · Cited by 30

Antiretroviral Drugs Promote Amyloidogenesis by De-Acidifying Endolysosomes

Liang, H., Ye, Y., Soliman, M. L., Lakpa, K. L., Miller, N., Afghah, Z., Geiger, J. D., & Chen, X. (2019) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-019-09862-1 · Cited by 30

Dihydroactinidiolide regulates Nrf2/HO-1 expression and inhibits caspase-3/Bax pathway to protect SH-SY5Y human neuroblastoma cells from oxidative stress induced neuronal apoptosis

Das, M., & Devi, K. P. (2021) · NeuroToxicology · doi:10.1016/j.neuro.2021.02.006 · Cited by 30

The pharmacological effects of Berberine and its therapeutic potential in different diseases: Role of the phosphatidylinositol 3‐kinase/ AKT signaling pathway

Khezri, M. R., Mohammadipanah, S., & Ghasemnejad‐Berenji, M. (2023) · Phytotherapy Research · doi:10.1002/ptr.8040 · Cited by 32

Requirement of α7 nicotinic acetylcholine receptors for amyloid beta protein‐induced depression of hippocampal long‐term potentiation in CA1 region of rats in vivo

Li, S., Wu, M., Wang, X., Yuan, L., Yang, D. U., & Qi, J. (2011) · Synapse · doi:10.1002/syn.20951 · Cited by 30

Involvement of Intracellular and Mitochondrial Aβ in the Ameliorative Effects of Huperzine A against Oligomeric Aβ42-Induced Injury in Primary Rat Neurons

Lei, Y., Yang, L., Ye, C. Y., Qin, M. Y., Yang, H. Y., Jiang, H. L., Tang, X. C., & Zhang, H. (2015) · PLoS ONE · doi:10.1371/journal.pone.0128366 · Cited by 30

Amyloid-β as a biomarker for Alzheimer’s disease: quantification methods in body fluids

Galozzi, S., Marcus, K., & Barkovits, K. (2015) · Expert Review of Proteomics · doi:10.1586/14789450.2015.1065183 · Cited by 30

Defining the minimum substrate and charge recognition model of gamma-secretase

Yan, Y., Xu, T.-H., Melcher, K., & Xu, H. E. (2017) · Acta Pharmacologica Sinica · doi:10.1038/aps.2017.35 · Cited by 30

Functional significance of O-GlcNAc modification in regulating neuronal properties

Hwang, H., & Rhim, H. (2017) · Pharmacological Research · doi:10.1016/j.phrs.2017.12.006 · Cited by 32

Role of methionine 35 in the intracellular Ca2+ homeostasis dysregulation and Ca2+‐dependent apoptosis induced by amyloid β‐peptide in human neuroblastoma IMR32 cells

Piacentini, R., Ripoli, C., Leone, L., Misiti, F., Clementi, M. E., D’Ascenzo, M., Giardina, B., Azzena, G. B., & Grassi, C. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05680.x · Cited by 30

Could a Common Mechanism of Protein Degradation Impairment Underlie Many Neurodegenerative Diseases?

Smith, D. M. (2018) · Journal of Experimental Neuroscience · doi:10.1177/1179069518794675 · Cited by 32

The link between Alzheimer’s disease and stroke: A detrimental synergism

Behl, T., Kaur, I., Sehgal, A., Khandige, P. S., Imran, M., Gulati, M., Anwer, M. K., Elossaily, G. M., Ali, N., Wal, P., et al. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102388 · Cited by 35

Intracellular accumulation of amyloid-ß is a marker of selective neuronal vulnerability in Alzheimer’s disease

Caramello, A., Fancy, N. N., Tournerie, C., Eklund, M., Chau, V. M. N., Adair, E., Papageorgopoulou, M., Willumsen, N., Jackson, J., Hardy, J., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-60328-w · Cited by 37

Identification and characterization of diarylimidazoles as hybrid inhibitors of butyrylcholinesterase and amyloid beta fibril formation

Karlsson, D., Fallarero, A., Brunhofer, G., Guzik, P., Prinz, M., Holzgrabe, U., Erker, T., & Vuorela, P. M. (2011) · European Journal of Pharmaceutical Sciences · doi:10.1016/j.ejps.2011.11.004 · Cited by 29

Systems biology of Alzheimer's disease: How diverse molecular changes result in memory impairment in AD

Juhász, G. D., Földi, I., & Penke, B. (2011) · Neurochemistry International · doi:10.1016/j.neuint.2011.02.008 · Cited by 29

The Amazonian herbal Marapuama attenuates cognitive impairment and neuroglial degeneration in a mouse Alzheimer model

Figueiró, M., Ilha, J., Linck, V. M., Herrmann, A. P., Nardin, P., Menezes, C. B., Achaval, M., Gonçalves, C. A., Porciúncula, L. O., Nunes, D. S., et al. (2010) · Phytomedicine · doi:10.1016/j.phymed.2010.07.013 · Cited by 30

Galangin decreases p‑tau, Aβ42 and β‑secretase levels, and suppresses autophagy in okadaic acid‑induced PC12 cells via an Akt/GSK3β/mTOR signaling‑dependent mechanism

Huang, L., Lin, M., Zhong, X., Yang, H., & Deng, M. (2019) · Molecular Medicine Reports · doi:10.3892/mmr.2019.9824 · Cited by 29

Alzheimer's disease-related amyloid β peptide causes structural disordering of lipids and changes the electric properties of a floating bilayer lipid membrane

Mrđenović, D., Su, Z., Kutner, W., Lipkowski, J., & Pięta, P. (2020) · Nanoscale Advances · doi:10.1039/d0na00292e · Cited by 29

Small-Molecule-Functionalized Hyperbranched Polyglycerol Dendrimers for Inhibiting Protein Aggregation

Mandal, S., Panja, P., Debnath, K., Jana, N. R., & Jana, N. R. (2020) · Biomacromolecules · doi:10.1021/acs.biomac.0c00713 · Cited by 29

Aluminum and Neurofibrillary Tangle Co-Localization in Familial Alzheimer’s Disease and Related Neurological Disorders

Mold, M. J., O’Farrell, A., Morris, B., & Exley, C. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-200838 · Cited by 31

Pathogenic and protective roles of extracellular vesicles in neurodegenerative diseases

Takeuchi, T. (2020) · The Journal of Biochemistry · doi:10.1093/jb/mvaa131 · Cited by 29

Protein misfolding, ER stress and chaperones: an approach to develop chaperone-based therapeutics for Alzheimer’s disease

Singh, R., Kaur, N., Dhingra, N., & Kaur, T. (2021) · International Journal of Neuroscience · doi:10.1080/00207454.2021.1968859 · Cited by 30

How Can Static and Oscillating Electric Fields Serve in Decomposing Alzheimer’s and Other Senile Plaques?

Kalita, S., Bergman, H., Dubey, K. D., & Shaik, S. S. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.2c12305 · Cited by 29

Amyloid-β peptide binds to microtubule-associated protein 1B (MAP1B)

Gevorkian, G., González‐Noriega, A., Acero, G., Ordoñez, J., Michalak, C., Munguía, M. E., Govezensky, T., Cribbs, D. H., & Manoutcharian, K. (2007) · Neurochemistry International · doi:10.1016/j.neuint.2007.10.020 · Cited by 29

Inflammation and aging: Can endocannabinoids help?

Marchalant, Y., Brothers, H. M., & Wenk, G. L. (2008) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2008.02.004 · Cited by 27

Novel Hexapeptide Interacts with Tubulin and Microtubules, Inhibits Aβ Fibrillation, and Shows Significant Neuroprotection

Biswas, A., Kurkute, P., Saleem, S., Jana, B., Mohapatra, S., Mondal, P., Adak, A., Ghosh, S., Saha, A., Bhunia, D., et al. (2015) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5b00149 · Cited by 29

Pannexin hemichannels: A novel promising therapy target for oxidative stress related diseases

Xu, J. H., Chen, L., & Li, L. (2017) · Journal of Cellular Physiology · doi:10.1002/jcp.25906 · Cited by 30

Carbenoxolone Reverses the Amyloid Beta 1–42 Oligomer–Induced Oxidative Damage and Anxiety-Related Behavior in Rats

Sharma, S., Sharma, N., Saini, A., & Nehru, B. (2018) · Neurotoxicity Research · doi:10.1007/s12640-018-9975-2 · Cited by 29

Screening of Some Sulfonamide and Sulfonylurea Derivatives as Anti-Alzheimer’s Agents Targeting BACE1 and PPARγ

Li, N., Wang, Y., Li, W., Li, H., Yang, L., Wang, J., Mahdy, H. A., Mehany, A. B. M., Jaiash, D. A., Santali, E. Y., et al. (2020) · Journal of Chemistry · doi:10.1155/2020/1631243 · Cited by 29

MicroRNA-455–3P as a peripheral biomarker and therapeutic target for mild cognitive impairment and Alzheimer’s disease

Islam, M. A., Sultana, O. F., Bandari, M., Kshirsagar, S., Manna, P. R., & Reddy, P. H. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102459 · Cited by 28

How to bake a brain: yeast as a model neuron

Sarto‐Jackson, I., & Tomáška, Ľ. (2016) · Current Genetics · doi:10.1007/s00294-015-0554-2 · Cited by 29

The involvement of homocysteine in stress-induced Aβ precursor protein misprocessing and related cognitive decline in rats

Xie, F., Zhao, Y. F., Ma, J., Gong, J., Wang, S., Zhang, L., Gao, X., & Qian, L. (2016) · Cell Stress and Chaperones · doi:10.1007/s12192-016-0718-0 · Cited by 27

N-Methyl Mesoporphyrin IX as an Effective Probe for Monitoring Alzheimer’s Disease β-Amyloid Aggregation in Living Cells

Li, M., Zhao, A., Ren, J., & Qu, X. (2017) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.6b00436 · Cited by 28

Biomolecular Corona Dictates Aβ Fibrillation Process

Lotfabadi, A., Hajipour, M. J., Derakhshankhah, H., Peirovi, A., Saffar, S., Shams, E., Fatemi, E., Barzegari, E., Sarvari, S., Moakedi, F., et al. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00076 · Cited by 27

Amyloid-beta oligomers induce Parkin-mediated mitophagy by reducing Miro1

Kam, M. K., Lee, D. G., Kim, B., Huh, J., Lee, H. J., Park, Y., & Lee, D. (2020) · Biochemical Journal · doi:10.1042/bcj20200488 · Cited by 28

Advances in fluorescent probes for detection and imaging of amyloid-β peptides in Alzheimer's disease

Zhang, Y., Ding, C., Li, C., & Wang, X. (2021) · Advances in clinical chemistry · doi:10.1016/bs.acc.2020.08.008 · Cited by 28

Brain energy metabolism and neurodegeneration: hints from CSF lactate levels in dementias

Bonomi, C. G., Lucia, V. D., Mascolo, A. P., Assogna, M., Motta, C., Scaricamazza, E., Sallustio, F., Mercuri, N. B., Koch, G., & Martorana, A. (2021) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2021.05.011 · Cited by 30

α-synuclein-assisted oligomerization of β-amyloid (1–42)

Chau, E., & Kim, J. R. (2022) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2022.109120 · Cited by 30

Design, synthesis and molecular docking simulation of oxindole-based derivatives with dual VEGFR-2 and cholinesterase inhibitory activities

Srour, A. M., Dawood, D. H., Nossier, E. S., El‐Shiekh, R. A., Mahmoud, A. E. E.-D., Hussien, A. G., Omran, M. M., & Ali, M. M. (2022) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2022.134130 · Cited by 28

Oxygen Sensing: A Common Crossroad in Cancer and Neurodegeneration

Quaegebeur, A., & Carmeliet, P. (2010) · Current topics in microbiology and immunology · doi:10.1007/82_2010_83 · Cited by 27

Mitogen-activated protein kinase signaling pathways promote low-density lipoprotein receptor-related protein 1-mediated internalization of beta-amyloid protein in primary cortical neurons

Yang, W., Ma, K., Qian, Y., Zhang, J.-S., Feng, G.-F., Shi, L., Zhang, Z., & Liu, Z. (2015) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2015.04.013 · Cited by 29

Mitophagy in Neurodegeneration: An Opportunity for Therapy?

Santos, R. X., Correia, S. C., Carvalho, C., Cardoso, S., Santos, M. S., & Moreira, P. I. (2011) · Current Drug Targets · doi:10.2174/138945011795528813 · Cited by 29

Detection and structural characterization of insulin prefibrilar oligomers using surface enhanced Raman spectroscopy

Kurouski, D., Sorci, M., Postiglione, T., Belfort, G., & Lednev, I. K. (2013) · Biotechnology Progress · doi:10.1002/btpr.1852 · Cited by 27

Peroxidase to Cytochrome b Type Transition in the Active Site of Heme-Bound Amyloid β Peptides Relevant to Alzheimer’s Disease

Ghosh, C., Mukherjee, S., Seal, M., & Dey, S. G. (2016) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.5b02683 · Cited by 29

Citalopram Ameliorates Impairments in Spatial Memory and Synaptic Plasticity in Female 3xTgAD Mice

Zhang, W., Junhong, G., Niu, X., Jie, W., Zhaojun, W., Meina, W., Yang, W., Zhang, J., & Qi, J. (2017) · BioMed Research International · doi:10.1155/2017/1238687 · Cited by 29

Crafting of Neuroprotective Octapeptide from Taxol-Binding Pocket of β-Tubulin

Mondal, P., Das, G., Khan, J., Pradhan, K., & Ghosh, S. (2017) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.7b00457 · Cited by 31

Peroxiredoxin 4 ameliorates amyloid beta oligomer-mediated apoptosis by inhibiting ER-stress in HT-22 hippocampal neuron cells

Kam, M. K., Lee, D. G., Kim, B., Lee, H., Lee, S., Bae, Y. C., & Lee, D. (2019) · Cell Biology and Toxicology · doi:10.1007/s10565-019-09477-5 · Cited by 29

A scoping review of mathematical models covering Alzheimer's disease progression

Moravveji, S., Doyon, N., Mashreghi, J., & Duchesne, S. (2024) · Frontiers in Neuroinformatics · doi:10.3389/fninf.2024.1281656 · Cited by 27

Taurine reduces microglia activation in the brain of aged senescence-accelerated mice by increasing the level of TREM2

Ahmed, S., Ma, N., Kawanokuchi, J., Matsuoka, K., Oikawa, S., Kobayashi, H., Hiraku, Y., & Murata, M. (2024) · Scientific Reports · doi:10.1038/s41598-024-57973-4 · Cited by 28

Stress and Cognitive Reserve as independent factors of neuropsychological performance in healthy elderly

Cabral, J. C. C., Veleda, G. W., Mazzoleni, M., Colares, E. P., Neiva-Silva, L., & das Neves, V. T. (2016) · Ciência & Saúde Coletiva · doi:10.1590/1413-812320152111.17452015 · Cited by 34

p66Shc Signaling Mediates Diabetes-Related Cognitive Decline

Minami, Y., Sonoda, N., Hayashida, E., Makimura, H., Ide, M., Ikeda, N., Ohgidani, M., Kato, T. A., Seki, Y., Maeda, Y., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-21426-6 · Cited by 27

Dual-Aptamer-Conjugated Molecular Modulator for Detecting Bioactive Metal Ions and Inhibiting Metal-Mediated Protein Aggregation

Wang, J., Wang, Y., Hu, X., Zhu, C., Ma, Q., Liang, L., Li, Z., & Yuan, Q. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.8b03007 · Cited by 27

Novel N-benzylpyridinium moiety linked to arylisoxazole derivatives as selective butyrylcholinesterase inhibitors: Synthesis, biological evaluation, and docking study

Vafadarnejad, F., Karimpour‐Razkenari, E., Sameem, B., Saeedi, M., Firuzi, O., Edraki, N., Mahdavi, M. R., & Akbarzadeh, T. (2019) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2019.103192 · Cited by 27

Icariin Ameliorates Amyloid Pathologies by Maintaining Homeostasis of Autophagic Systems in Aβ1–42-Injected Rats

Jiang, X., Chen, L.-L., Lan, Z., Xiong, F., Xu, X., Yin, Y.-Y., Li, P., & Wang, P. (2019) · Neurochemical Research · doi:10.1007/s11064-019-02889-z · Cited by 28

Aβ42 Double Mutant Inhibits Aβ42-Induced Plasma and Mitochondrial Membrane Disruption in Artificial Membranes, Isolated Organs, and Intact Cells

Oren, O., Ben-Zichri, S., Taube, R., Jelinek, R., & Papo, N. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00638 · Cited by 27

Amyloidosis increase is not attenuated by long-term calorie restriction or related to neuron density in the prefrontal cortex of extremely aged rhesus macaques

Stonebarger, G. A., Urbanski, H. F., Woltjer, R. L., Vaughan, K. L., Ingram, D., Schultz, P., Calderazzo, S. M., Siedeman, J., Mattison, J., Rosene, D. L., et al. (2020) · GeroScience · doi:10.1007/s11357-020-00259-0 · Cited by 27

The Glucose Metabolic Pathway as A Potential Target for Therapeutics: Crucial Role of Glycosylation in Alzheimer’s Disease

Bukke, V. N., Villani, R., Moola, A., Wawrzyniak, A., Balawender, K., Orkisz, S., Ferraro, L., Serviddio, G., & Cassano, T. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21207739 · Cited by 27

Functional Ensemble Survival Tree: Dynamic Prediction of Alzheimer’s Disease Progression Accommodating Multiple Time-Varying Covariates

Jiang, S., Xie, Y., & Colditz, G. A. (2020) · Journal of the Royal Statistical Society Series C (Applied Statistics) · doi:10.1111/rssc.12449 · Cited by 27

The HSP40 chaperone Ydj1 drives amyloid beta 42 toxicity

Ring, J., Tadić, J., Ristic, S., Poglitsch, M., Bergmann, M., Radic, N., Mossmann, D., Liang, Y., Maglione, M., Jerkovic, A., et al. (2022) · EMBO Molecular Medicine · doi:10.15252/emmm.202113952 · Cited by 27

The polyphenol EGCG directly targets intracellular amyloid‐β aggregates and promotes their lysosomal degradation

Secker, C., Motzny, A., Kostova, S., Buntru, A., Helmecke, L., Reus, L., Steinfort, R., Brusendorf, L., Boeddrich, A., Neuendorf, N., et al. (2023) · Journal of Neurochemistry · doi:10.1111/jnc.15842 · Cited by 28

A Novel Mouse Model of Alzheimer's Disease with Chronic Estrogen Deficiency Leads to Glial Cell Activation and Hypertrophy

Prat, A., Behrendt, M., Marcinkiewicz, E., Boridy, S., Sairam, R., Seidah, N. G., & Maysinger, D. (2011) · Journal of Aging Research · doi:10.4061/2011/251517 · Cited by 26

Pathogenic role of mitochondrial amyloid-β peptide

Chen, J. X., & Yan, S. D. (2007) · Expert Review of Neurotherapeutics · doi:10.1586/14737175.7.11.1517 · Cited by 26

A discrete mathematical model for the aggregation of β-Amyloid

Dayeh, M. A., Livadiotis, G., & Elaydi, S. (2018) · PLoS ONE · doi:10.1371/journal.pone.0196402 · Cited by 27

Clathrin mediated endocytosis in Alzheimer’s disease: cell type specific involvement in amyloid beta pathology

Jaye, S., Sandau, U. S., & Saugstad, J. A. (2024) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2024.1378576 · Cited by 26

Omnidirectional improvement of mitochondrial health in Alzheimer's disease by multi-targeting engineered activated neutrophil exosomes

Zhang, L., Lin, J., Xiang, K., Shi, T., & Guo, B. (2024) · Journal of Controlled Release · doi:10.1016/j.jconrel.2024.10.033 · Cited by 26

Enhanced Amyloidogenic Processing of Amyloid Precursor Protein and Cell Death Under Prolonged Endoplasmic Reticulum Stress in Brain Endothelial Cells

Plácido, A. I., Oliveira, C. R., Moreira, P. I., & Pereira, C. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8819-1 · Cited by 26

Plasma membrane Ca 2+ -ATPases in the nervous system during development and ageing

Mata, A. M. (2010) · World Journal of Biological Chemistry · doi:10.4331/wjbc.v1.i7.229 · Cited by 26

Isoflurane Exposure during Mid-Adulthood Attenuates Age-Related Spatial Memory Impairment in APP/PS1 Transgenic Mice

Su, D., Zhao, Y., Xu, H., Wang, B., Chen, X., Chen, J., & Wang, X. (2012) · PLoS ONE · doi:10.1371/journal.pone.0050172 · Cited by 26

Intraneuronal β‐amyloid and its interactions with proteins and subcellular organelles

Penke, B., Tóth, A. M., Földi, I., Szűcs, M., & Janáky, T. (2012) · Electrophoresis · doi:10.1002/elps.201200297 · Cited by 26

Modulation of Amyloid-β Fibrils into Mature Microrod-Shaped Structure by Histidine Functionalized Water-Soluble Perylene Diimide

Balakrishnan, M., Chowdhury, S. R., & Iyer, P. K. (2015) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.5b07260 · Cited by 26

Intraneuronally injected amyloid beta inhibits long-term potentiation in rat hippocampal slices

Nomura, I., Takechi, H., & Kato, N. (2012) · Journal of Neurophysiology · doi:10.1152/jn.00589.2011 · Cited by 27

Glutamate receptor delocalization in postsynaptic membrane and reduced hippocampal synaptic plasticity in the early stage of Alzheimer’s disease

Li, N., Li, Y., Li, L.-J., Zhu, K., Zheng, Y., & Wang, X. (2019) · Neural Regeneration Research · doi:10.4103/1673-5374.250625 · Cited by 28

Ginsenoside Rg1 reduces β‑amyloid levels by inhibiting CD5K‑induced PPARγ phosphorylation in a neuron model of Alzheimer's disease

Quan, Q., Li, X., Feng, J., Hou, J., Li, M., & Zhang, B. (2020) · Molecular Medicine Reports · doi:10.3892/mmr.2020.11424 · Cited by 26

Mechanistic insight into the capacity of natural polar phenolic compounds to abolish Alzheimer's disease-associated pathogenic effects of apoE4 forms

Mountaki, C., Dafnis, I., Panagopoulou, E. A., Vasilakopoulou, P. B., Karvelas, M., Chiou, A., Karathanos, V. Τ., & Chroni, A. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.05.022 · Cited by 28

Neuropathology of Aging in Cats and its Similarities to Human Alzheimer’s Disease

Sordo, L., Martini, A. C., Houston, E. F., Head, E., & Gunn-Moore, D. A. (2021) · Frontiers in Aging · doi:10.3389/fragi.2021.684607 · Cited by 26

Early Cellular, Molecular, Morphological and Behavioral Changes in the Humanized Amyloid-Beta-Knock-In Mouse Model of Late-Onset Alzheimer’s Disease

Kshirsagar, S., Alvir, R. V., Hindle, A., Kumar, S., Vijayan, M., Pradeepkiran, J. A., Reddy, A. P., Ramasubramanian, B., & Reddy, P. H. (2022) · Cells · doi:10.3390/cells11040733 · Cited by 27

Enhancing the Amyloid-β Anti-Aggregation Properties of Curcumin via Arene-Ruthenium(II) Derivatization

Cuccioloni, M., Cecarini, V., Bonfili, L., Pettinari, R., Tombesi, A., Pagliaricci, N., Petetta, L., Angeletti, M., & Eleuteri, A. M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23158710 · Cited by 27

Molecular Mechanisms Linking Osteoarthritis and Alzheimer’s Disease: Shared Pathways, Mechanisms and Breakthrough Prospects

Umoh, I. O., Reis, H. J., & de Oliveira, A. C. P. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25053044 · Cited by 28

Evaluation of the amyloid beta-GFP fusion protein as a model of amyloid beta peptides-mediated aggregation: a study of DNAJB6 chaperone

Hussein, R. M., Hashem, R. M., & Rashed, L. A. (2015) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2015.00040 · Cited by 27

Novel amyloid-beta specific scFv and VH antibody fragments from human and mouse phage display antibody libraries

Medecigo, M., Manoutcharian, K., Vasilevko, V., Govezensky, T., Munguía, M. E., Becerril, B., Luz-Madrigal, A., Vaca, L. A., Cribbs, D. H., & Gevorkian, G. (2010) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2010.03.023 · Cited by 26

Neuroprotective effects of diarylpropionitrile against β-amyloid peptide-induced neurotoxicity in rat cultured cortical neurons

Suwanna, N., Thangnipon, W., & Soi‐ampornkul, R. (2014) · Neuroscience Letters · doi:10.1016/j.neulet.2014.06.029 · Cited by 26

Amyloid Beta Peptides Differentially Affect Hippocampal Theta Rhythms In Vitro

Gutiérrez-Lerma, A. I., Ordaz, B., & Peña‐Ortega, F. (2013) · International Journal of Peptides · doi:10.1155/2013/328140 · Cited by 26

In vivo labelling of hippocampal β‐amyloid in triple‐transgenic mice with a fluorescent acetylcholinesterase inhibitor released from nanoparticles

Härtig, W., Kacza, J., Paulke, B., Grosche, J., Bauer, U. U. I., Hoffmann, A., Elsinghorst, P. W., & Gütschow, M. (2009) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2009.07038.x · Cited by 26

Naphthalene-triazolopyrimidine hybrid compounds as potential multifunctional anti-Alzheimer’s agents

Umar, T., Gusain, S., Raza, M. K., Shalini, S., Kumar, J., Tiwari, M., & Hoda, N. (2019) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2019.06.004 · Cited by 26

Pollution, Particles, and Dementia: A Hypothetical Causative Pathway

Seaton, A., Tran, L., Chen, R., Maynard, R. L., & Whalley, L. J. (2020) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph17030862 · Cited by 26

Phospholipid transfer protein (PLTP) deficiency accelerates memory dysfunction through altering amyloid precursor protein (APP) processing in a mouse model of Alzheimer's disease

Tong, Y., Sun, Y., Tian, X., Zhou, T., Wang, H., Zhang, T., Zhan, R., Zhao, L., Kuerban, B., Li, Z., et al. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv262 · Cited by 26

Reconstituted mother tinctures of Gelsemium sempervirens L. improve memory and cognitive impairment in mice scopolamine-induced dementia model

Palit, P., Mukherjee, D., & Mandal, S. C. (2015) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2014.09.008 · Cited by 25

Effect of β-amyloid on blood-brain barrier properties and function

Petrushanko, I. Y., Mitkevich, V. A., & Makarov, A. А. (2023) · Biophysical Reviews · doi:10.1007/s12551-023-01052-x · Cited by 28

Paradoxes of Cellular SUMOylation Regulation: A Role of Biomolecular Condensates?

Cheng, X., Yang, W., Lin, W., & Mei, F. C. (2023) · Pharmacological Reviews · doi:10.1124/pharmrev.122.000784 · Cited by 25

Aging reduces glial uptake and promotes extracellular accumulation of Aβ from a lentiviral vector

Zhao, W., Zhang, J., Davis, E. G., & Rebeck, G. W. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00210 · Cited by 24

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

Nitration of amyloid-β peptide (1–42) as a protective mechanism for the amyloid-β peptide (1–42) against copper ion toxicity

Zhao, J. J., Gao, W., Yang, Z., Li, H., & Gao, Z. (2018) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2018.10.005 · Cited by 25

Early loss of cerebellar Purkinje cells in human and a transgenic mouse model of Alzheimer’s disease

Chaudhari, K., Wang, L., Kruse, J. J., Winters, A., Sumien, N., Shetty, R. A., Prah, J., Liu, R., Shi, J., Forster, M. J., et al. (2021) · Neurological Research · doi:10.1080/01616412.2021.1893566 · Cited by 24

Factors driving the compositional diversity of Apis mellifera bee venom from a Corymbia calophylla (marri) ecosystem, Southwestern Australia

Scaccabarozzi, D., Dods, K., Le, T. T., Gummer, J. P. A., Lussu, M., Milne, L. A., Campbell, T. W., Wafujian, B. P., & Priddis, C. (2021) · PLoS ONE · doi:10.1371/journal.pone.0253838 · Cited by 25

Profiling the chemical nature of anti-oxytotic/ferroptotic compounds with phenotypic screening

Soriano‐Castell, D., Liang, Z., Maher, P. A., & Currais, A. J. M. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.11.003 · Cited by 25

Impaired autophagy in amyloid-beta pathology: A traditional review of recent Alzheimer's research

Yuan, M., Wang, Y., Huang, Z., Jing, F., Qiao, P., Zou, Q., Li, J., & Cai, Z. (2022) · Journal of Biomedical Research · doi:10.7555/jbr.36.20220145 · Cited by 26

Intracellular A-Beta Amyloid, A Sign for Worse Things to Come?

Echeverría, V., & Cuello, A. C. (2002) · Molecular Neurobiology · doi:10.1385/mn:26:2-3:299 · Cited by 81

Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer’s disease

Gouras, G. K., Tampellini, D., Takahashi, R. H., & Capetillo-Zarate, E. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0679-9 · Cited by 372

The impact of extracellular amyloid-β (Αβ) peptides on cortical neurotransmitters and of intracellular Aβ accumulation on protein expression AC Cuello, KFS Bell, V Echeverria, E Lopez, A Ribeiro-da-Silva, M Szyf

(2005) · CRC Press eBooks · doi:10.1201/b14441-47

Intracellular A? and its Pathological Role in Alzheimer's Disease: Lessons from Cellular to Animal Models

Ji, L., Zhao, X., Lu, W., Zhang, Q. H., & Hua, Z. (2016) · Current Alzheimer Research · doi:10.2174/1567205013666160322142226 · Cited by 23

Intraneuronal Aβ accumulation and origin of plaques in Alzheimer's disease

Gouras, G. K., Almeida, C. G., & Takahashi, R. H. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.05.022 · Cited by 338