Synaptic slaughter in Alzheimer's disease

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

Synapse loss in frontal cortex biopsies in Alzheimer's disease: Correlation with cognitive severity

DeKosky, S. T., & Scheff, S. W. (1990) · Annals of Neurology · doi:10.1002/ana.410270502 · Cited by 2,376

Differences in the pattern of hippocampal neuronal loss in normal ageing and Alzheimer's disease

West, M. J., Coleman, P. D., Flood, D. G., & Troncoso, J. C. (1994) · The Lancet · doi:10.1016/s0140-6736(94)92338-8 · Cited by 1,267 · cited 1×

Neuron numbers and dendritic extent in normal aging and Alzheimer’s disease

Coleman, P. D., & Flood, D. G. (1987) · Neurobiology of Aging · doi:10.1016/0197-4580(87)90127-8 · Cited by 772

A sequence of cytoskeleton changes related to the formation of neurofibrillary tangles and neuropil threads

Braak, F., Braak, H., & Mandelkow, E. (1994) · Acta Neuropathologica · doi:10.1007/bf00293315 · Cited by 769

The molecular machinery for secretion is conserved from yeast to neurons.

Bennett, M. K., & Scheller, R. H. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.7.2559 · Cited by 650

A cDNA that suppresses MPP+ toxicity encodes a vesicular amine transporter

Liu, Y. (1992) · Cell · doi:10.1016/0092-8674(92)90425-c · Cited by 589

Dendritic Growth in the Aged Human Brain and Failure of Growth in Senile Dementia

Buell, S. J., & Coleman, P. D. (1979) · Science · doi:10.1126/science.493989 · Cited by 475

Quantitative assessment of cortical synaptic density in Alzheimer's disease

Scheff, S. W., DeKosky, S. T., & Price, D. A. (1990) · Neurobiology of Aging · doi:10.1016/0197-4580(90)90059-9 · Cited by 446

Clathrin Assembly Lymphoid Myeloid Leukemia (CALM) Protein: Localization in Endocytic-coated Pits, Interactions with Clathrin, and the Impact of Overexpression on Clathrin-mediated Traffic

Tebar, F., Bohlander, S. K., & Sorkin, A. (1999) · Molecular Biology of the Cell · doi:10.1091/mbc.10.8.2687 · Cited by 320

Differential roles of Rap1 and Rap2 small GTPases in neurite retraction and synapse elimination in hippocampal spiny neurons

Fu, Z., Lee, S. H., Simonetta, A., Hansen, J. D., Sheng, M., & Pak, D. T. S. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04195.x · Cited by 83

Alterations in the motor neuron–renshaw cell circuit in the Sod1G93A mouse model

Wootz, H., FitzSimons‐Kantamneni, E., Larhammar, M., Rotterman, T. M., Enjin, A., Patra, K., André, E., van Zundert, B., Kullander, K., & Álvarez, F. J. (2012) · The Journal of Comparative Neurology · doi:10.1002/cne.23266 · Cited by 86

Structure-Toxicity Analysis of Type-2 Alkenes: In Vitro Neurotoxicity

LoPachin, R. M., Barber, D. S., Geohagen, B. C., Gavin, T., He, D., & Das, S. (2006) · Toxicological Sciences · doi:10.1093/toxsci/kfl127 · Cited by 81

Doxycycline counteracts neuroinflammation restoring memory in Alzheimer's disease mouse models

Balducci, C., Santamaria, G., Vitola, P. L., Brandi, E., Grandi, F., Viscomi, A. R., Beeg, M., Gobbi, M., Salmona, M., Ottonello, S., et al. (2018) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2018.06.002 · Cited by 83

Differentiated Alzheimer's Disease Transmitochondrial Cybrid Cell Lines Exhibit Reduced Organelle Movement

Trimmer, P. A., & Borland, M. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.1101 · Cited by 81

The Neurotoxic Role of Extracellular Tau Protein

Sebastián‐Serrano, Á., de Diego-García, L., & Díaz-Hernández, M. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19040998 · Cited by 85

MINK and TNIK Differentially Act on Rap2-Mediated Signal Transduction to Regulate Neuronal Structure and AMPA Receptor Function

Hussain, N. K., Hsin, H., Huganir, R. L., & Sheng, M. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.4124-10.2010 · Cited by 76

Review: Disruption of the Postsynaptic Density in Alzheimer’s Disease and Other Neurodegenerative Dementias

Gong, Y., & Lippa, C. F. (2010) · American Journal of Alzheimer's Disease & Other Dementias® · doi:10.1177/1533317510382893 · Cited by 76

The novel squamosamide derivative FLZ enhances BDNF/TrkB/CREB signaling and inhibits neuronal apoptosis in APP/PS1 mice

Li, N., & Liu, G.-T. (2010) · Acta Pharmacologica Sinica · doi:10.1038/aps.2010.3 · Cited by 76

Imaging Amyloid‐β Membrane Interactions: Ion‐Channel Pores and Lipid‐Bilayer Permeability in Alzheimer's Disease

Viles, J. H. (2023) · Angewandte Chemie International Edition · doi:10.1002/anie.202215785 · Cited by 74

Tau hyperphosphorylation in synaptosomes and neuroinflammation are associated with canine cognitive impairment

Smolek, T., Maďari, A., Farbáková, J., Kandrac, O., Jadhav, S., Cente, M., Brezováková, V., Novák, M., & Žilka, N. (2015) · The Journal of Comparative Neurology · doi:10.1002/cne.23877 · Cited by 76

Postsynaptic density–membrane associated guanylate kinase proteins (PSD–MAGUKs) and their role in CNS disorders

Gardoni, F., Marcello, E. E., & Luca, M. D. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2008.07.068 · Cited by 73

ICV STZ induced impairment in memory and neuronal mitochondrial function: A protective role of nicotinic receptor

Saxena, G., Patro, I. K., & Nath, C. (2011) · Behavioural Brain Research · doi:10.1016/j.bbr.2011.04.039 · Cited by 74

Pharmacological inhibition of HDAC6 reverses cognitive impairment and tau pathology as a result of cisplatin treatment

Ma, J., Huo, X., Jarpe, M. B., Kavelaars, A., & Heijnen, C. J. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0604-3 · Cited by 73

Leptin gene therapy attenuates neuronal damages evoked by amyloid-β and rescues memory deficits in APP/PS1 mice

Pérez‐González, R., Alvira-Botero, X., Avendaño, O. F. R., Antequera, D., Garzón, M., Martín-Moreno, A. M., Brera, B., CEBALLOS, M. L. D., & Carro, E. (2014) · Gene Therapy · doi:10.1038/gt.2013.85 · Cited by 72

Early calcium dysregulation in Alzheimer’s disease: setting the stage for synaptic dysfunction

Chakroborty, S., & Stutzmann, G. E. (2011) · Science China Life Sciences · doi:10.1007/s11427-011-4205-7 · Cited by 71

A Multilevel View of the Development of Alzheimer’s Disease

Ávila, J., & Perry, G. L. (2020) · Neuroscience · doi:10.1016/j.neuroscience.2020.11.015 · Cited by 69

Apolipoprotein E-Mimetics Inhibit Neurodegeneration and Restore Cognitive Functions in a Transgenic Drosophila Model of Alzheimer's Disease

Sarantseva, S. V., Timoshenko, S., Bolshakova, O. I., Karaseva, E., Rodin, D., Schwarzman, A. L., & Vitek, M. P. (2009) · PLoS ONE · doi:10.1371/journal.pone.0008191 · Cited by 70

Moderate decline in select synaptic markers in the prefrontal cortex (BA9) of patients with Alzheimer’s disease at various cognitive stages

Poirel, O., Mella, S., Videau, C., Ramet, L., Davoli, M. A., Herzog, É., Katsel, P., Mechawar, N., Haroutunian, V. H., Epelbaum, J., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-19154-y · Cited by 72

Level of PICALM, a key component of clathrin-mediated endocytosis, is correlated with levels of phosphotau and autophagy-related proteins and is associated with tau inclusions in AD, PSP and Pick disease

Ando, K., Tomimura, K., Sazdovitch, V., Suain, V., Yilmaz, Z., Authelet, M., Ndjim, M., Vergara, C., Belkouch, M., Potier, M., et al. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2016.05.017 · Cited by 71

Alzheimer’s Disease: A Clinical Practice-Oriented Review

Alves, L., Correia, A. S., Miguel, R., Alegria, P., & Bugalho, P. (2012) · Frontiers in Neurology · doi:10.3389/fneur.2012.00063 · Cited by 74

Neuroprotective effects of donepezil against cholinergic depletion

Cutuli, D., Bartolo, P. D., Caporali, P., Tartaglione, A. M., Oddi, D., D'Amato, F. R., Nobili, A., D’Amelio, M., & Petrosini, L. (2013) · Alzheimer s Research & Therapy · doi:10.1186/alzrt215 · Cited by 68

Trehalose against Alzheimer's Disease: Insights into a Potential Therapy

Khalifeh, M., Read, M. I., Barreto, G. E., & Sahebkar, A. (2020) · BioEssays · doi:10.1002/bies.201900195 · Cited by 67

Identification of the Role of miR-142-5p in Alzheimer’s Disease by Comparative Bioinformatics and Cellular Analysis

Song, J., & Kim, Y. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00227 · Cited by 66

Estructura y función de las subunidades del receptor a glutamato tipo NMDA

Flores-Soto, M. E., Chaparro-Huerta, V., Escoto-Delgadillo, M., Vázquez-Valls, E., González-Castañeda, R. E., & Beas‐Zárate, C. (2012) · Neurología · doi:10.1016/j.nrl.2011.10.014 · Cited by 73

Alzheimer’s Disease Pathologic Cascades: Who Comes First, What Drives What

Swerdlow, R. H. (2011) · Neurotoxicity Research · doi:10.1007/s12640-011-9272-9 · Cited by 69

Regulation of Synaptic Amyloid-β Generation through BACE1 Retrograde Transport in a Mouse Model of Alzheimer's Disease

Ye, X., Feng, T., Tammineni, P., Chang, Q., Jeong, Y. Y., Margolis, D. J., Cai, H., Kusnecov, A. W., & Cai, Q. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.2851-16.2017 · Cited by 62

Alzheimer brain-derived amyloid β-protein impairs synaptic remodeling and memory consolidation

Borlikova, G. G., Trejo, M., Mably, A. J., Donald, J. M. M., Frigerio, C. S., Regan, C. M., Murphy, K. J., Masliah, E., & Walsh, D. M. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.10.028 · Cited by 65

Catalpol ameliorates beta amyloid–induced degeneration of cholinergic neurons by elevating brain-derived neurotrophic factors

Wang, Z., Liu, Q., Zhang, R., Liu, S., Xia, Z., & Hu, Y. G. (2009) · Neuroscience · doi:10.1016/j.neuroscience.2009.07.041 · Cited by 66

Structure and function of NMDA-type glutamate receptor subunits

Flores-Soto, M. E., Chaparro-Huerta, V., Escoto-Delgadillo, M., Vázquez-Valls, E., González-Castañeda, R. E., & Beas‐Zárate, C. (2012) · Neurología (English Edition) · doi:10.1016/j.nrleng.2011.10.003 · Cited by 64

Aluminium Induced Endoplasmic Reticulum Stress Mediated Cell Death in SH-SY5Y Neuroblastoma Cell Line Is Independent of p53

Rizvi, S. H. M., Parveen, A., Verma, A., Ahmad, I., Arshad, M., & Mahdi, A. A. (2014) · PLoS ONE · doi:10.1371/journal.pone.0098409 · Cited by 66

Changes in hippocampal synapses and learning-memory abilities in a streptozotocin-treated rat model and intervention by using fasudil hydrochloride

Hou, Y., Zhou, L., Yang, Q. D., Du, X., Li, M., Yuan, M., & Zhou, Z. (2011) · Neuroscience · doi:10.1016/j.neuroscience.2011.10.030 · Cited by 64

Particulate matter (PM2.5) exposure season-dependently induces neuronal apoptosis and synaptic injuries

Chen, M., Li, B., & Sang, N. (2016) · Journal of Environmental Sciences · doi:10.1016/j.jes.2016.10.013 · Cited by 62

Early-Onset and Robust Amyloid Pathology in a New Homozygous Mouse Model of Alzheimer's Disease

Willuweit, A., Velden, J., Godemann, R., Manook, A., Jetzek, F., Tintrup, H., Kauselmann, G., Zevnik, B., Henriksen, G., Drzezga, A. E., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007931 · Cited by 60

Concise Review: Can Stem Cells be Used to Treat or Model Alzheimer's Disease?

Chen, W. W., & Blurton-Jones, M. M. (2012) · Stem Cells · doi:10.1002/stem.1240 · Cited by 62

Accumulation of Intraneuronal β-Amyloid 42 Peptides Is Associated with Early Changes in Microtubule-Associated Protein 2 in Neurites and Synapses

Takahashi, R. H., Capetillo‐Zarate, E., Lin, M. T. S., Milner, T. A., & Gouras, G. K. (2013) · PLoS ONE · doi:10.1371/journal.pone.0051965 · Cited by 62

Neuronal Aβ42 is enriched in small vesicles at the presynaptic side of synapses

Yu, Y., Jans, D. C., Winblad, B. G., Tjernberg, L. O., & Schedin‐Weiss, S. (2018) · Life Science Alliance · doi:10.26508/lsa.201800028 · Cited by 60

Proteolytic Cleavage of Apolipoprotein E4 as the Keystone for the Heightened Risk Associated with Alzheimer’s Disease

Rohn, T. T. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms140714908 · Cited by 58

Physical Exercise During Pregnancy Prevents Cognitive Impairment Induced by Amyloid-β in Adult Offspring Rats

Klein, C. P., Hoppe, J. B., Saccomori, A. B., dos Santos, B. G., Sagini, J. P. N., Crestani, M. S., August, P. M., Hözer, R. M., Grings, M., Parmeggiani, B., et al. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1210-x · Cited by 59

Molecular, Structural, Functional, and Pharmacological Sites for Vesicular Glutamate Transporter Regulation

Pietrancosta, N., Djibo, M., Daumas, S., Mestikawy, S. E., & Erickson, J. D. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-01912-7 · Cited by 64

Neurotoxic Saboteurs: Straws that Break the Hippo’s (Hippocampus) Back Drive Cognitive Impairment and Alzheimer’s Disease

Daulatzai, M. A. (2013) · Neurotoxicity Research · doi:10.1007/s12640-013-9407-2 · Cited by 56

Overexpression of endophilin A1 exacerbates synaptic alterations in a mouse model of Alzheimer’s disease

Yu, Q., Wang, Y., Du, F., Yan, S., Hu, G., Origlia, N., Rutigliano, G., Sun, Q., Yu, H., Ainge, J. A., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-04389-0 · Cited by 60

Early depletion of CA1 neurons and late neurodegeneration in a mouse tauopathy model

Helboe, L., Egebjerg, J., Barkholt, P., & Volbracht, C. (2017) · Brain Research · doi:10.1016/j.brainres.2017.04.002 · Cited by 56

Brain-Derived Neurotrophic Factor: the Link Between Amyloid-β and Memory Loss

Fahnestock, M. L. (2011) · Future Neurology · doi:10.2217/fnl.11.44 · Cited by 57

The Role of Lysosomes in a Broad Disease-Modifying Approach Evaluated across Transgenic Mouse Models of Alzheimer’s Disease and Parkinson’s Disease and Models of Mild Cognitive Impairment

Hwang, J., Estick, C., Ikonne, U. S., Butler, D., Pait, M. C., Elliott, L. H., Ruiz, S., Smith, K., Rentschler, K. M., Mundell, C. T., et al. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20184432 · Cited by 55

Downregulation of TREM2 expression exacerbates neuroinflammatory responses through TLR4-mediated MAPK signaling pathway in a transgenic mouse model of Alzheimer’s disease

Ruganzu, J. B., Peng, X., He, Y., Wu, X., Zheng, Q., Ding, B., Lin, C., Guo, H., Yang, Z., Zhang, X. L., et al. (2021) · Molecular Immunology · doi:10.1016/j.molimm.2021.12.018 · Cited by 56

Synapses, synaptic activity and intraneuronal Aβ in Alzheimer’s disease

Tampellini, D. (2010) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2010.00013 · Cited by 58

The Synaptic Protein Neuroligin-1 Interacts with the Amyloid β-Peptide. Is There a Role in Alzheimer’s Disease?

Dinamarca, M. C., Weinstein, D. B., Monasterio, O., & Inestrosa, N. C. (2011) · Biochemistry · doi:10.1021/bi201246t · Cited by 53

The Potential of CRISPR/Cas9 Gene Editing as a Treatment Strategy for Alzheimer's Disease

Rohn, T. T., Kim, N., Isho, N. F., & Mack, J. M. (2018) · Journal of Alzheimer’s Disease & Parkinsonism · doi:10.4172/2161-0460.1000439 · Cited by 58

Tauopathy models and human neuropathology: similarities and differences

Frank, S., Clavaguera, F., & Tolnay, M. (2007) · Acta Neuropathologica · doi:10.1007/s00401-007-0291-9 · Cited by 59

The B′ Protein Phosphatase 2A Regulatory Subunit well-rounded Regulates Synaptic Growth and Cytoskeletal Stability at the Drosophila Neuromuscular Junction

Viquez, N. M., Li, C. R., Wairkar, Y. P., & DiAntonio, A. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.1740-06.2006 · Cited by 53

Acrylamide in health and disease

Flynn, N. E. (2010) · Frontiers in Bioscience-Scholar · doi:10.2741/s130 · Cited by 52

Decreased rabphilin 3A immunoreactivity in Alzheimer’s disease is associated with Aβ burden

Tan, M. G. K., Lee, C., Lee, J. H., Francis, P. T., Williams, R. J., Ramírez, M. J., Chen, C., Wong, P. T. ‐., & Lai, M. K. P. (2013) · Neurochemistry International · doi:10.1016/j.neuint.2013.10.013 · Cited by 50

The Cerebrospinal Fluid Neurogranin/BACE1 Ratio is a Potential Correlate of Cognitive Decline in Alzheimer’s Disease

Vos, A. D., Struyfs, H., Jacobs, D., Fransén, E., Klewansky, T., Roeck, E. E. D., Robberecht, C., Broeckhoven, C. V., Duyckaerts, C. J., Engelborghs, S., et al. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160227 · Cited by 54

Type-2 alkenes mediate synaptotoxicity in neurodegenerative diseases

LoPachin, R. M., Gavin, T., & Barber, D. S. (2008) · NeuroToxicology · doi:10.1016/j.neuro.2008.04.016 · Cited by 53

Axonal amyloid precursor protein and its fragments undergo somatodendritic endocytosis and processing

Niederst, E. D., Reyna, S. M., & Goldstein, L. S. B. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-06-1049 · Cited by 51

Mass Spectrometric Characterization of Amyloid-β Species in the 7PA2 Cell Model of Alzheimer's Disease

Portelius, E., Olsson, M., Brinkmalm, G., Rüetschi, U., Mattsson, N., Andréasson, U., Gobom, J., Brinkmalm, A., Hölttä, M., Blennow, K., et al. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-120994 · Cited by 51

CoREST Complex-Selective Histone Deacetylase Inhibitors Show Prosynaptic Effects and an Improved Safety Profile To Enable Treatment of Synaptopathies

Fuller, N. O., Pirone, A., Lynch, B. A., Hewitt, M. C., Quinton, M. S., McKee, T. D., & Ivarsson, M. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00620 · Cited by 51

MAGUK proteins: New targets for pharmacological intervention in the glutamatergic synapse

Gardoni, F. (2008) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2008.01.048 · Cited by 53

Impaired NGF/TrkA Signaling Causes Early AD-Linked Presynaptic Dysfunction in Cholinergic Primary Neurons

Latina, V., Caioli, S., Zona, C., Ciotti, M. T., Amadoro, G., & Calissano, P. (2017) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2017.00068 · Cited by 52

Role of Endoplasmic Reticulum Stress and Unfolded Protein Responses in Health and Diseases

Mahdi, A. A., Rizvi, S. H. M., & Parveen, A. (2015) · Indian Journal of Clinical Biochemistry · doi:10.1007/s12291-015-0502-4 · Cited by 52

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

Rohn, T. T. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/860959 · Cited by 51

Synaptic contact number and size in stratum radiatum CA1 of APP/PS1ΔE9 transgenic mice

West, M. J., Bach, G., Søderman, A., & Jensen, J. L. (2009) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2008.01.009 · Cited by 48

The role of fatty acid amide hydrolase enzyme inhibitors in Alzheimer's disease

Jain, S., Bisht, A., Verma, K., Negi, S., Paliwal, S., & Sharma, S. K. (2021) · Cell Biochemistry and Function · doi:10.1002/cbf.3680 · Cited by 53

Cascade of tau toxicity in inducible hippocampal brain slices and prevention by aggregation inhibitors

Messing, L., Decker, J. M., Joseph, M., Mandelkow�, E., & Mandelkow, E.-M. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.10.024 · Cited by 48

The role of synaptic activity in the regulation of amyloid beta levels in Alzheimer's disease

Cheng, X., Wu, J., Geng, M., & Xiong, J. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.11.021 · Cited by 51

Tau Causes Synapse Loss without Disrupting Calcium Homeostasis in the rTg4510 Model of Tauopathy

Kopeikina, K. J., Wegmann, S., Pitstick, R., Carlson, G. A., Bacskai, B. J., Betensky, R. A., Hyman, B. T., & Spires‐Jones, T. L. (2013) · PLoS ONE · doi:10.1371/journal.pone.0080834 · Cited by 48

A SAGE study of apolipoprotein E3/3, E3/4 and E4/4 allele-specific gene expression in hippocampus in Alzheimer disease

Xu, P., Li, Y., Qin, X., Kroner, C. C., Green-Odlum, A., Xu, H., Wang, T.-Y., Schmechel, D. E., Hulette, C. M., Ervin, J. F., et al. (2007) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2007.06.009 · Cited by 48

C3N nanodots inhibits Aβ peptides aggregation pathogenic path in Alzheimer’s disease

Yin, X., Zhou, H., Zhang, M., Su, J., Wang, X. L., Li, S., Yang, Z., Kang, Z., & Zhou, R. (2023) · Nature Communications · doi:10.1038/s41467-023-41489-y · Cited by 50

The Potential Role of Rho GTPases in Alzheimer's Disease Pathogenesis

Bolognin, S., Lorenzetto, E., Diana, G., & Buffelli, M. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8637-5 · Cited by 47

Synaptic Changes in the Dentate Gyrus of APP/PS1 Transgenic Mice Revealed by Electron Microscopy

Alonso-Nanclares, L., Merino-Serrais, P., Gonzalez, S., & DeFelipe, J. (2013) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e31828d41ec · Cited by 45

Apoptosis is secondary to non-apoptotic axonal degeneration in neurons exposed to Aβ in distal axons

Song, M.-S., Saavedra, L., & de Chaves, E. I. P. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.06.007 · Cited by 40

Amyloid-β Protein Modulates Insulin Signaling in Presynaptic Terminals

Heras-Sandoval, D., Ferrera, P., & Arias, C. (2012) · Neurochemical Research · doi:10.1007/s11064-012-0800-7 · Cited by 45

Tetrahydroxystilbene glucoside improves the learning and memory of amyloid-β1–42-injected rats and may be connected to synaptic changes in the hippocampus

Zhou, L., Hou, Y., Yang, Q., Du, X., Li, M., Yuan, M., & Zhou, Z. (2012) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/y2012-121 · Cited by 45

Downregulation of synapse-associated protein expression and loss of homeostatic microglial control in cerebrospinal fluid of infectious patients with delirium and patients with Alzheimer’s disease

van Ton, A. M. P., Verbeek, M. M., Alkema, W. B. L., Pickkers, P., & Abdo, W. F. (2020) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2020.06.027 · Cited by 48

Nitric Oxide and Synaptic Dynamics in the Adult Brain: Physiopathological Aspects

Moreno‐López, B., & Gonzáylez-Forero, D. (2006) · Reviews in the Neurosciences · doi:10.1515/revneuro.2006.17.3.309 · Cited by 46

Dihydrotestosterone treatment delays the conversion from mild cognitive impairment to Alzheimer's disease in SAMP8 mice

Kang, L., Li, S., Xing, Z., Li, J., Su, Y., Fan, P., Wang, L., & Cui, H. (2014) · Hormones and Behavior · doi:10.1016/j.yhbeh.2014.03.017 · Cited by 44

β-amyloid and Oxidative Stress: Perspectives in Drug Development

Caruso, G., Spampinato, S. F., Cardaci, V., Caraci, F., Sortino, M. A., & Merlo, S. (2019) · Current Pharmaceutical Design · doi:10.2174/1381612825666191209115431 · Cited by 45

The role of microRNA-34 family in Alzheimer’s disease: A potential molecular link between neurodegeneration and metabolic disorders

Bazrgar, M., Khodabakhsh, P., Prudencio, M., Mohagheghi, F., & Ahmadiani, A. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105805 · Cited by 45

Tau pathology is associated with synaptic density and longitudinal synaptic loss in Alzheimer’s disease

Wang, J., Huang, Q., Chen, X., You, Z., He, K., Guo, Q., Huang, Y. H., Yang, Y., Lin, Z., Guo, T., et al. (2024) · Molecular Psychiatry · doi:10.1038/s41380-024-02501-z · Cited by 46

Pharmacological and Genetic Reversal of Age-Dependent Cognitive Deficits Attributable to Decreased presenilin Function

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A Novel Therapeutic Approach to Treat Alzheimer’s Disease by Neurotrophic Support During the Period of Synaptic Compensation

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