Alterations in Expression of Glutamatergic Transporters and Receptors in Sporadic Alzheimer's Disease

Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes

Vandesompele, J., De Preter, K., Pattyn, F., Poppe, B., Van Roy, N., De Paepe, A., & Speleman, F. (2002) · Genome Biology · doi:10.1186/gb-2002-3-7-research0034 · Cited by 20,038

High density synthetic oligonucleotide arrays

Lipshutz, R. J., Fodor, S. P. A., Gingeras, T., & Lockhart, D. J. (1999) · Nature Genetics · doi:10.1038/4447 · Cited by 2,204

Frequency of Stages of Alzheimer-Related Lesions in Different Age Categories

Braak, H., & Braak, E. (1997) · Neurobiology of Aging · doi:10.1016/s0197-4580(97)00056-0 · Cited by 1,656

Gene-expression profile of the ageing brain in mice

Lee, C.-K., Weindruch, R., & Prolla, T. A. (2000) · Nature Genetics · doi:10.1038/77046 · Cited by 1,055

Paradigm shift in neuroprotection by NMDA receptor blockade: memantine and beyond

Lipton, S. A. (2006) · Nature Reviews Drug Discovery · doi:10.1038/nrd1958 · Cited by 909

Importance of replication in microarray gene expression studies: Statistical methods and evidence from repetitive cDNA hybridizations

Lee, M. T., Kuo, F. C., Whitmore, G. A., & Sklar, J. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.18.9834 · Cited by 861

Kainic Acid-Mediated Excitotoxicity as a Model for Neurodegeneration

Wang, Q., Yu, S. O., Simonyi, Á., Sun, G. Y., & Sun, A. Y. (2005) · Molecular Neurobiology · doi:10.1385/mn:31:1-3:003 · Cited by 365

Gene expression profiling of parkinsonian substantia nigra pars compacta; alterations in ubiquitin-proteasome, heat shock protein, iron and oxidative stress regulated proteins, cell adhesion/cellular matrix and vesicle trafficking genes

Grünblatt, E., Mandel, S. A., Jacob‐Hirsch, J., Zeligson, S., Amariglo, N., Rechavi, G., Li, J., Ravid, R., Roggendorf, W., Riederer, P. F., et al. (2004) · Journal of Neural Transmission · doi:10.1007/s00702-004-0212-1 · Cited by 355

Pattern of brain destruction in Parkinson's and Alzheimer's diseases

Braak, H., Braak, E., Yilmazer‐Hanke, D., de Vos, R. A. I., Jansen, E. N. H., & Böhl, J. (1996) · Journal of Neural Transmission · doi:10.1007/bf01276421 · Cited by 326

Computational methods for theidentification of differential and coordinated gene expression

Claverie, J. (1999) · Human Molecular Genetics · doi:10.1093/hmg/8.10.1821 · Cited by 287

Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease

Guo, T., Zhang, D., Zeng, Y., Huang, T. Y., Xu, H., & Zhao, Y. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00391-7 · Cited by 994

Soluble Oligomers of Amyloid β Protein Facilitate Hippocampal Long-Term Depression by Disrupting Neuronal Glutamate Uptake

Li, S., Hong, S., Shepardson, N. E., Walsh, D. M., Shankar, G. M., & Selkoe, D. (2009) · Neuron · doi:10.1016/j.neuron.2009.05.012 · Cited by 972

Oligomeric Aβ-induced synaptic dysfunction in Alzheimer’s disease

Tu, S., Okamoto, S., Lipton, S. A., & Xu, H. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-48 · Cited by 613

The Role of NMDA Receptors in Alzheimer’s Disease

Liu, J., Chang, L., Song, Y., Li, H., & Wu, Y. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00043 · Cited by 535

Alzheimer's disease, β‐amyloid, glutamate, NMDA receptors and memantine – searching for the connections

Danysz, W., & Parsons, C. G. (2012) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2012.02057.x · Cited by 500

Molecular and cellular mechanisms of excitotoxic neuronal death

Wang, Y., & Qin, Z. (2010) · APOPTOSIS · doi:10.1007/s10495-010-0481-0 · Cited by 466

Pathological mechanisms and therapeutic strategies for Alzheimer’s disease

Tam, K. Y., & Ju, Y. (2021) · Neural Regeneration Research · doi:10.4103/1673-5374.320970 · Cited by 422

Neuronal hyperexcitability in Alzheimer's disease: what are the drivers behind this aberrant phenotype?

Targa Dias Anastacio, H., Matosin, N., & Ooi, L. (2022) · Translational Psychiatry · doi:10.1038/s41398-022-02024-7 · Cited by 401

Glutamate metabolism and recycling at the excitatory synapse in health and neurodegeneration

Andersen, J. V., Markussen, K. H., Jakobsen, E., Schousboe, A., Waagepetersen, H. S., Rosenberg, P. A., & Aldana, B. I. (2021) · Neuropharmacology · doi:10.1016/j.neuropharm.2021.108719 · Cited by 392

Mechanisms of Glutamate Transport

Vandenberg, R. J., & Ryan, R. M. (2013) · Physiological Reviews · doi:10.1152/physrev.00007.2013 · Cited by 367

Calcium signaling and molecular mechanisms underlying neurodegenerative diseases

Pchitskaya, E. I., Александровна, П. Е., & Борисович, Б. И. (2017) · Cell Calcium · doi:10.1016/j.ceca.2017.06.008 · Cited by 355

The essential elements of Alzheimer’s disease

Lei, P., Ayton, S., & Bush, A. I. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.rev120.008207 · Cited by 344

Astrogliosis: An integral player in the pathogenesis of Alzheimer's disease

Osborn, L. M., Kamphuis, W., Wadman, W. J., & Hol, E. M. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2016.01.001 · Cited by 312

Nicotinic Acetylcholine Receptor Signalling: Roles in Alzheimer’s Disease and Amyloid Neuroprotection

Buckingham, S. D., Jones, A. K., Brown, L. A., & Sattelle, D. B. (2009) · Pharmacological Reviews · doi:10.1124/pr.108.000562 · Cited by 312

Glutamate system, amyloid β peptides and tau protein: functional interrelationships and relevance to Alzheimer disease pathology

Revett, T. J., Baker, G. B., Jhamandas, J. H., & Kar, S. (2012) · Journal of Psychiatry and Neuroscience · doi:10.1503/jpn.110190 · Cited by 308

A mechanistic hypothesis for the impairment of synaptic plasticity by soluble Aβ oligomers from Alzheimer’s brain

Li, S., & Selkoe, D. J. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15007 · Cited by 263

Astrocyte energy and neurotransmitter metabolism in Alzheimer’s disease: Integration of the glutamate/GABA-glutamine cycle

Andersen, J. V., Schousboe, A., & Verkhratsky, A. (2022) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2022.102331 · Cited by 263

Human astrocytes in the diseased brain

Dossi, E., Vasile, F., & Rouach, N. (2018) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2017.02.001 · Cited by 250

Astrocyte dysfunction in Alzheimer disease

Acosta, C., Anderson, H. D., & Anderson, C. M. (2017) · Journal of Neuroscience Research · doi:10.1002/jnr.24075 · Cited by 262

Glymphatic system, AQP4, and their implications in Alzheimer’s disease

Silva, I., Silva, J., Ferreira, R., & Trigo, D. (2021) · Neurological Research and Practice · doi:10.1186/s42466-021-00102-7 · Cited by 246

Recent progress of drug nanoformulations targeting to brain

Khan, A. R., Yang, X., Fu, M., & Zhai, G. (2018) · Journal of Controlled Release · doi:10.1016/j.jconrel.2018.10.004 · Cited by 216

Mitochondrial Dysfunction and Synaptic Transmission Failure in Alzheimer’s Disease

Guo, L., Tian, J., & Du, H. (2017) · Journal of Alzheimer’s Disease · doi:10.3233/jad-160702 · Cited by 211

Glutamate transporter EAAT2: regulation, function, and potential as a therapeutic target for neurological and psychiatric disease

Takahashi, K., Foster, J. B., & Lin, C. G. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-1937-8 · Cited by 227

Dysfunctional synapse in Alzheimer's disease – A focus on NMDA receptors

Mota, S. I., Ferreira, I. L., & Rego, A. C. (2013) · Neuropharmacology · doi:10.1016/j.neuropharm.2013.08.013 · Cited by 215

Glutamate transporter variants reduce glutamate uptake in Alzheimer's disease

Scott, H. A., Gebhardt, F. M., Mitrovic, A. D., Vandenberg, R. J., & Dodd, P. R. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2010.03.008 · Cited by 202

Age-dependent decrease in glutamine synthetase expression in the hippocampal astroglia of the triple transgenic Alzheimer's disease mouse model: mechanism for deficient glutamatergic transmission?

Olabarria, M., Noristani, H. N., Verkhratsky, A., & Rodriguez, J. J. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-55 · Cited by 207

Alzheimer’s disease as a synaptopathy: Evidence for dysfunction of synapses during disease progression

Meftah, S., & Gan, J. (2023) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2023.1129036 · Cited by 205

The Biology and Pathobiology of Glutamatergic, Cholinergic, and Dopaminergic Signaling in the Aging Brain

Gąsiorowska, A., Wydrych, M., Drapich, P., Zadrożny, M., Steczkowska, M., Niewiadomski, W., & Niewiadomska, G. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.654931 · Cited by 199

Amyloid-β 1–42 Slows Clearance of Synaptically Released Glutamate by Mislocalizing Astrocytic GLT-1

Scimemi, A., Meabon, J. S., Woltjer, R. L., Sullivan, J. M., Diamond, J. S., & Cook, D. G. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.5274-12.2013 · Cited by 185

The role of glutamate transporters in the pathophysiology of neuropsychiatric disorders

O'Donovan, S. M., Sullivan, C. R., & McCullumsmith, R. E. (2017) · Schizophrenia · doi:10.1038/s41537-017-0037-1 · Cited by 189

Alzheimer’s disease: Targeting the glutamatergic system

Conway, M. E. (2020) · Biogerontology · doi:10.1007/s10522-020-09860-4 · Cited by 180

Basal Levels of eIF2α Phosphorylation Determine Cellular Antioxidant Status by Regulating ATF4 and xCT Expression

Lewerenz, J., & Maher, P. A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m807325200 · Cited by 173

GluN2B subunit-containing NMDA receptor antagonists prevent Aβ-mediated synaptic plasticity disruption in vivo

Hu, N., Klyubin, I. V., Anwyl, R., & Rowan, M. J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908083106 · Cited by 176

Decreased levels of PSD95 and two associated proteins and increased levels of BCl 2 and caspase 3 in hippocampus from subjects with amnestic mild cognitive impairment: Insights into their potential roles for loss of synapses and memory, accumulation of Aβ, and neurodegeneration in a prodromal stage of Alzheimer's disease

Rukhsana Sultana, A., Banks, W. A., & Butterfield, D. A. (2009) · Journal of Neuroscience Research · doi:10.1002/jnr.22227 · Cited by 171

Deregulation of excitatory neurotransmission underlying synapse failure in Alzheimer's disease

Paula‐Lima, A. C., Brito‐Moreira, J., & Ferreira, S. T. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12304 · Cited by 170

Excitatory Amino Acid Transporters in Physiology and Disorders of the Central Nervous System

Malik, A. R., & Willnow, T. E. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20225671 · Cited by 170

The Regulation of Astrocytic Glutamate Transporters in Health and Neurodegenerative Diseases

Todd, A. C., & Hardingham, G. E. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21249607 · Cited by 172

The Dual Role of Glutamatergic Neurotransmission in Alzheimer’s Disease: From Pathophysiology to Pharmacotherapy

Bukke, V. N., Archana, M., Villani, R., Romano, A. D., Wawrzyniak, A., Balawender, K., Orkisz, S., Beggiato, S., Serviddio, G., & Cassano, T. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21207452 · Cited by 161

GLT-1 Loss Accelerates Cognitive Deficit Onset in an Alzheimer's Disease Animal Model

Mookherjee, P., Green, P. S., Watson, G. S., Marques, M. A., Tanaka, K., Meeker, K. D., Meabon, J. S., Li, N., Zhu, P., Olson, V. G., et al. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-110503 · Cited by 167

Soluble Aβ oligomers impair hippocampal LTP by disrupting glutamatergic/GABAergic balance

Lei, M., Xu, H., Li, Z., Wang, Z., O’Malley, T. T., Zhang, D., Walsh, D. M., Xu, P., Selkoe, D. J., & Li, S. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.10.019 · Cited by 162

Restored glial glutamate transporter EAAT2 function as a potential therapeutic approach for Alzheimer’s disease

Takahashi, K., Kong, Q., Lin, Y., Stouffer, N., Schulte, D. A., Lai, L., Liu, Q., Chang, L., Dominguez, S., Xing, X., et al. (2015) · The Journal of Experimental Medicine · doi:10.1084/jem.20140413 · Cited by 163

The solute carrier transporters and the brain: Physiological and pharmacological implications

Hu, C., Tao, L., Cao, X., & Chen, L. (2019) · Asian Journal of Pharmaceutical Sciences · doi:10.1016/j.ajps.2019.09.002 · Cited by 165

Small-molecule activator of glutamate transporter EAAT2 translation provides neuroprotection

Kong, Q., Chang, L.-C., Takahashi, K., Liu, Q., Schulte, D. A., Lai, L., Ibabao, B., Lin, Y., Stouffer, N., Mukhopadhyay, C. D., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci66163 · Cited by 156

Biomarkers for Alzheimer’s disease and other forms of dementia: Clinical needs, limitations and future aspects

Cedazo-Mínguez, Á., & Winblad, B. G. (2009) · Experimental Gerontology · doi:10.1016/j.exger.2009.09.008 · Cited by 159

Astrocyte calcium dysfunction causes early network hyperactivity in Alzheimer’s disease

Shah, D., Gsell, W., Wahis, J., Luckett, E. S., Jamoulle, T., Vermaercke, B., Preman, P., Moechars, D., Hendrickx, V., Jaspers, T., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111280 · Cited by 164

Ceftriaxone ameliorates tau pathology and cognitive decline via restoration of glial glutamate transporter in a mouse model of Alzheimer's disease

Zumkehr, J., Rodríguez‐Ortiz, C. J., Cheng, D., Kieu, Z., Wai, T., Hawkins, C., Kilian, J., Lim, S., Medeiros, R., & Kitazawa, M. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.04.005 · Cited by 157

The Glutamate/ GABA ‐Glutamine Cycle: Insights, Updates, and Advances

Andersen, J. V. (2025) · Journal of Neurochemistry · doi:10.1111/jnc.70029 · Cited by 170

Glutamate Transporter EAAT2: A New Target For The Treatment Of Neurodegenerative Diseases

Lin, C. G., Kong, Q., Cuny, G. D., & Glicksman, M. A. (2012) · Future Medicinal Chemistry · doi:10.4155/fmc.12.122 · Cited by 154

Target Identification for CNS Diseases by Transcriptional Profiling

Altar, C. A., Vawter, M. P., & Ginsberg, S. D. (2008) · Neuropsychopharmacology · doi:10.1038/npp.2008.172 · Cited by 139

Revisiting the intersection of amyloid, pathologically modified tau and iron in Alzheimer’s disease from a ferroptosis perspective

Derry, P. J., Hegde, M. L., Jackson, G. R., Kayed, R., Tour, J. M., Tsai, A.-L., & Kent, T. A. (2019) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2019.101716 · Cited by 146

Role of Aβ in Alzheimer’s-related synaptic dysfunction

Zhang, H., Jiang, X., Ma, L., Wei, W., Li, Z., Chang, S., Wen, J., Sun, J., & Li, H. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.964075 · Cited by 157

Intracellular Calcium Dysregulation: Implications for Alzheimer’s Disease

Magi, S., Castaldo, P., Macrì, M. L., Maiolino, M., Matteucci, A., Bastioli, G., Gratteri, S., Amoroso, S., & Lariccia, V. (2016) · BioMed Research International · doi:10.1155/2016/6701324 · Cited by 151

Astrocytes in mouse models of tauopathies acquire early deficits and lose neurosupportive functions

Sidoryk‐Wȩgrzynowicz, M., Gerber, Y. N., Ries, M., Sastre, M., Tolkovsky, A. M., & Spillantini, M. G. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0478-9 · Cited by 137

Microglia-astrocyte crosstalk in the amyloid plaque niche of an Alzheimer’s disease mouse model, as revealed by spatial transcriptomics

Mallach, A., Zielonka, M., van Lieshout, V., An, Y., Khoo, J. H., Vanheusden, M., Chen, W.-T., Moechars, D., Arancibia-Carcamo, I. L., Fiers, M., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114216 · Cited by 135

Synaptic dysfunction and septin protein family members in neurodegenerative diseases

Marttinen, M., Kurkinen, K. M. A., Soininen, H. S., Haapasalo, A., & Hiltunen, M. O. (2015) · Molecular Neurodegeneration · doi:10.1186/s13024-015-0013-z · Cited by 138

Oxidative modification to LDL receptor-related protein 1 in hippocampus from subjects with Alzheimer disease: Implications for Aβ accumulation in AD brain

Owen, J. B., Rukhsana Sultana, A., Aluise, C. D., Erickson, M. A., Price, T. O., Bu, G., Banks, W. A., & Butterfield, D. A. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.09.013 · Cited by 132

Amyloid Beta-Related Alterations to Glutamate Signaling Dynamics During Alzheimer’s Disease Progression

Findley, C. A., Bartke, A., Hascup, K. N., & Hascup, E. R. (2019) · ASN NEURO · doi:10.1177/1759091419855541 · Cited by 133

Novel App knock-in mouse model shows key features of amyloid pathology and reveals profound metabolic dysregulation of microglia

Xia, D., Lianoglou, S., Sandmann, T., Calvert, M., Suh, J. H., Thomsen, E., Dugas, J., Pizzo, M. E., DeVos, S. L., Earr, T. K., et al. (2022) · Molecular Neurodegeneration · doi:10.1186/s13024-022-00547-7 · Cited by 124

The Many Faces of Astrocytes in Alzheimer's Disease

Monterey, M. D., Wei, H., Wu, X., & Wu, J. Q. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2021.619626 · Cited by 117

Age and Alzheimer’s disease gene expression profiles reversed by the glutamate modulator riluzole

Pereira, A. C., Gray, J. D., Kogan, J. F., Davidson, R. L., Rubin, T. G., Okamoto, M., Morrison, J. H., & McEwen, B. S. (2017) · Molecular Psychiatry · doi:10.1038/mp.2016.33 · Cited by 116

Contribution of astrocytes to neuropathology of neurodegenerative diseases

Acıoğlu, Ç., Li, L., & Elkabes, S. (2021) · Brain Research · doi:10.1016/j.brainres.2021.147291 · Cited by 119

Susceptibility to calcium dysregulation during brain aging

Kumar, A. (2009) · Frontiers in Aging Neuroscience · doi:10.3389/neuro.24.002.2009 · Cited by 119

Astrocytic Glutamatergic Transmission and Its Implications in Neurodegenerative Disorders

Satarker, S., Bojja, S. L., Gurram, P. C., Mudgal, J., Arora, D. S., & Nampoothiri, M. (2022) · Cells · doi:10.3390/cells11071139 · Cited by 116

Region- and Age-Specific Changes in Glutamate Transport in the AβPP23 Mouse Model for Alzheimer's Disease

Schallier, A., Smolders, I., Van Dam, D., Loyens, E., De Deyn, P. P., Michotte, A., Michotte, Y., & Massie, A. (2011) · Journal of Alzheimer's Disease · doi:10.3233/jad-2011-101005 · Cited by 109

Oxidative stress upregulates the NMDA receptor on cerebrovascular endothelium

Betzen, C., White, R., Zehendner, C. M., Pietrowski, E., Bender, B., Luhmann, H. J., & Kuhlmann, C. R. W. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.07.034 · Cited by 109

Calcineurin and glial signaling: neuroinflammation and beyond

Furman, J. L., & Norris, C. M. (2014) · Journal of Neuroinflammation · doi:10.1186/s12974-014-0158-7 · Cited by 115

Astroglia as a cellular target for neuroprotection and treatment of neuro‐psychiatric disorders

Liu, B., Teschemacher, A. G., & Kasparov, S. (2017) · Glia · doi:10.1002/glia.23136 · Cited by 111

Molecular Profiles of Drinking Alcohol to Intoxication in C57BL/6J Mice

Mulligan, M. K., Rhodes, J. S., Crabbe, J. C., Mayfield, R. D., Harris, R. A., & Ponomarev, I. (2011) · Alcoholism Clinical and Experimental Research · doi:10.1111/j.1530-0277.2010.01384.x · Cited by 106

Translation of Pre-Clinical Studies into Successful Clinical Trials for Alzheimer’s Disease: What are the Roadblocks and How Can They Be Overcome?

Banik, A., Brown, R. E., Bamburg, J., Lahiri, D. K., Khurana, D., Friedland, R. P., Chen, W., Ding, Y., Mudher, A., Padjen, A. L., et al. (2015) · Journal of Alzheimer’s Disease · doi:10.3233/jad-150136 · Cited by 102

Dysregulation of Astrocyte–Neuronal Communication in Alzheimer’s Disease

Nanclares, C., Baraibar, A. M., Araque, A., & Kofuji, P. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22157887 · Cited by 103

The Amyloid Cascade Hypothesis in Alzheimer’s Disease: Should We Change Our Thinking?

Kurkinen, M. T., Fułek, M., Fułek, K., Beszłej, J. A., Kurpas, D., & Leszek, J. (2023) · Biomolecules · doi:10.3390/biom13030453 · Cited by 105

Gene expression deficits in pontine locus coeruleus astrocytes in men with major depressive disorder

Chandley, M., Szebeni, K., Szebeni, A., Crawford, J. D., Stockmeier, C. A., Turecki, G., Miguel-Hidalgo, J. J., & Ordway, G. A. (2013) · Journal of Psychiatry and Neuroscience · doi:10.1503/jpn.120110 · Cited by 101

Glial connexin expression and function in the context of Alzheimer's disease

Koulakoff, A., Mei, X., Orellana, J. A., Sáez, J. C., & Giaume, C. (2011) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2011.10.001 · Cited by 100

Tau-mediated synaptic damage in Alzheimer’s disease

Jadhav, S., Cubinkova, V., Zimova, I., Brezováková, V., Maďari, A., Cigánková, V., & Žilka, N. (2015) · Translational Neuroscience · doi:10.1515/tnsci-2015-0023 · Cited by 97

Modulation of Brain Hyperexcitability: Potential New Therapeutic Approaches in Alzheimer’s Disease

Toniolo, S., Sen, A., & Husain, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21239318 · Cited by 97

Central role for NMDA receptors in redox mediated impairment of synaptic function during aging and Alzheimer’s disease

Foster, T. C., Kyritsopoulos, C., & Kumar, A. (2016) · Behavioural Brain Research · doi:10.1016/j.bbr.2016.05.012 · Cited by 94

Divergent roles of astrocytic versus neuronal EAAT2 deficiency on cognition and overlap with aging and Alzheimer’s molecular signatures

Sharma, A., Kazim, S. F., Larson, C. S., Ramakrishnan, A., Gray, J. D., McEwen, B. S., Rosenberg, P. A., Shen, L., & Pereira, A. C. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1903566116 · Cited by 92

Hyperactivity Induced by Soluble Amyloid-β Oligomers in the Early Stages of Alzheimer's Disease

Hector, A., & Brouillette, J. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.600084 · Cited by 97

Glial Glutamine Homeostasis in Health and Disease

Andersen, J. V., & Schousboe, A. (2022) · Neurochemical Research · doi:10.1007/s11064-022-03771-1 · Cited by 92

Regulation of ferroptosis by bioactive phytochemicals: Implications for medical nutritional therapy

Zheng, K., Dong, Y., Yang, R., Liang, Y., Wu, H., & He, Z. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105580 · Cited by 89

Increased expression of cholesterol 24S‐hydroxylase results in disruption of glial glutamate transporter EAAT2 association with lipid rafts: a potential role in Alzheimer’s disease

Tian, G., Kong, Q., Lai, L., Ray‐Chaudhury, A., & Lin, C. G. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06661.x · Cited by 87

Glutamate transporters

Benarroch, E. E. (2010) · Neurology · doi:10.1212/wnl.0b013e3181cc89e3 · Cited by 86

Excitotoxicity and new antiglutamatergic strategies in Parkinson's disease and Alzheimer's disease

Koutsilieri, E., & Riederer, P. F. (2007) · Parkinsonism & Related Disorders · doi:10.1016/s1353-8020(08)70025-7 · Cited by 84

Integrated multi-omics analysis of Alzheimer’s disease shows molecular signatures associated with disease progression and potential therapeutic targets

Kodam, P., Sai Swaroop, R., Pradhan, S. S., Sivaramakrishnan, V., & Vadrevu, R. (2023) · Scientific Reports · doi:10.1038/s41598-023-30892-6 · Cited by 82

Early Life Stress and Epigenetics in Late-onset Alzheimer’s Dementia: A Systematic Review

Lemche, E. (2018) · Current Genomics · doi:10.2174/1389202919666171229145156 · Cited by 84

The dual face of glutamate: from a neurotoxin to a potential survival factor—metabolic implications in health and disease

Magi, S., Piccirillo, S., & Amoroso, S. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-3002-x · Cited by 79

Post-translational Regulation of GLT-1 in Neurological Diseases and Its Potential as an Effective Therapeutic Target

Peterson, A. R., & Binder, D. K. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00164 · Cited by 82

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Issue Cover (October 2020)

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