Cited by 774Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

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Molecular mechanisms of neurodegeneration in Alzheimer's disease

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Crews, L., Masliah, E.·2010·Human Molecular Genetics

DOI 10.1093/hmg/ddq160PMC PMC2875049

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Abstract

Alzheimer's disease (AD) is characterized by cognitive impairment, progressive neurodegeneration and formation of amyloid-beta (Abeta)-containing plaques and neurofibrillary tangles composed of hyperphosphorylated tau. The neurodegenerative process in AD is initially characterized by synaptic damage accompanied by neuronal loss. In addition, recent evidence suggests that alterations in adult neurogenesis in the hippocampus might play a role. Synaptic loss is one of the strongest correlates to the cognitive impairment in patients with AD. Several lines of investigation support the notion that the synaptic pathology and defective neurogenesis in AD are related to progressive accumulation of Abeta oligomers rather than fibrils. Abnormal accumulation of Abeta resulting in the formation of toxic oligomers is the result of an imbalance between the levels of Abeta production, aggregation and clearance. Abeta oligomers might lead to synaptic damage by forming pore-like structures with channel activity; alterations in glutamate receptors; circuitry hyper-excitability; mitochondrial dysfunction; lysosomal failure and alterations in signaling pathways related to synaptic plasticity, neuronal cell and neurogenesis. A number of signaling proteins, including fyn kinase; glycogen synthase kinase-3beta (GSK3beta) and cyclin-dependent kinase-5 (CDK5), are involved in the neurodegenerative progression of AD. Therapies for AD might require the development of anti-aggregation compounds, pro-clearance pathways and blockers of hyperactive signaling pathways.

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Background
Critical role of cPLA2 in Aβ oligomer-induced neurodegeneration and memory deficit
Desbène, C., Malaplate, C., Youssef, I., Garcia, P., Stenger, C., Sauvée, M., Fischer, N., Rimet, D., Koziel, V., Escanyé, M., et al. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.11.008 · Cited by 64
“, 2010) or signaling proteins such as fyn kinase, glycogen synthase kinase-3 , cyclin-dependent kinase-5 (Crews and Masliah, 2010).”
Genome-wide identification of microRNA-related variants associated with risk of Alzheimer’s disease
Ghanbari, M., Ikram, M. A., de Looper, H. W. J., Albert Hofman, D., Erkeland, S. J., Franco, O. H., & Dehghan, A. (2016) · Scientific Reports · doi:10.1038/srep28387 · Cited by 58
Synaptic vesicle cycle and amyloid β: Biting the hand that feeds
Ovsepian, S. V., O’Leary, V. B., Záborszky, L., Ntziachristos, V., & Dolly, J. O. (2018) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2018.01.011 · Cited by 57
“Elucidating the mechanisms of synaptic impairments, thus, are of special interest for a better understanding of AD pathobiology and early therapeutic intervention, before slowing down the onset of irreparable damage with synaptic loss and cognitive decline [27,46].”
Background
Combined administration of cerebrolysin and donepezil induces plastic changes in prefrontal cortex in aged mice
Alcántara-González, F., Mendoza-Perez, C. R., Zaragoza, N., Juárez, I., Arroyo‐García, L. E., Gamboa, C., de la Cruz, F., Zamudio, S., García‐Dolores, F., & Flores, G. (2012) · Synapse · doi:10.1002/syn.21588 · Cited by 56
“…factors (Bertram, 2009; Bertram and Tanzi, 2010; Hardy and Selkoe, 2002); molecular alterations of the processing of b-amyloid and tau proteins (Crews and Masliah, 2010; Iqbal et al., 2009; Ittner and Gotz, 2011; Nelson et al., 2009; Palop and Mucke, 2010); inflammatory and metabolic abnormal…”
Background
Targeting CCR3 to Reduce Amyloid-β Production, Tau Hyperphosphorylation, and Synaptic Loss in a Mouse Model of Alzheimer’s Disease
Zhu, C., Xu, B., Sun, X., Zhu, Q., & Sui, Y. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-0269-5 · Cited by 59
“In the present study, we demonstrate that CCL11 treatment resulted in marked activation of cyclin-dependent kinase 5 (CDK5) and glycogen synthase kinase-3β (GSK-3β), both of which are key regulators in the hyperphosphorylation of tau, leading to neurofibrillary tangle formation, and also important players in the phosp…”
Background
Lychee Seed Saponins Improve Cognitive Function and Prevent Neuronal Injury via Inhibiting Neuronal Apoptosis in a Rat Model of Alzheimer’s Disease
Wang, X., Wu, J., Yu, C., Tang, Y., Liu, J., Chen, H., Jin, B., Mei, Q., Cao, S., & Qin, D. (2017) · Nutrients · doi:10.3390/nu9020105 · Cited by 61
The novel GLP‐1/GIP analogue DA5‐CH reduces tau phosphorylation and normalizes theta rhythm in the icv. STZ rat model of AD
Cheng, L., Liu, W., Li, X., Zhang, Z., Qi, H., Liu, S., Yan, N., Xing, Y., Hölscher, C., & Wang, Z. (2020) · Brain and Behavior · doi:10.1002/brb3.1505 · Cited by 55
“Increased expression of apoptosis-related proteins, typical nuclear apoptotic bodies in neurons, and DNA fragments in neurons were observed in the autopsy the brains of AD patients (Crews & Masliah, 2010; Jellinger, 2001).”
Background
Exercise-Induced Modulation of Neuroinflammation in Models of Alzheimer’s Disease
Kelly, Á. M. (2018) · Brain Plasticity · doi:10.3233/bpl-180074 · Cited by 55
Omics Data and Their Integrative Analysis to Support Stratified Medicine in Neurodegenerative Diseases
Cognata, V. L., Morello, G., & Cavallaro, S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094820 · Cited by 57
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
Mechanisms and Effects Posed by Neurotoxic Products of Cyanobacteria/Microbial Eukaryotes/Dinoflagellates in Algae Blooms: a Review
Mello, F. D., Braidy, N., Marçal, H., Guillemin, G. J., Nabavi, S. M., & Neilan, B. A. (2017) · Neurotoxicity Research · doi:10.1007/s12640-017-9780-3 · Cited by 58
“Neurodegeneration encompasses several types of cellular injury in the central nervous system (CNS), including oxidative stress, excitotoxicity, gliotoxicity, DNA damage, protein accumulation and apoptosis (Crews and Masliah 2010; Heneka et al. 2010; Lau and Tymianski 2010; Wang and Michaelis 2010).”
Background
Identification of Polyphenolic Compounds and Black Tea Extract as Potent Inhibitors of Lipid Membrane Destabilization by Aβ 42 Aggregates
Gauci, A. J., Caruana, M., Giese, A., Scerri, C., & Vassallo, N. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-111061 · Cited by 54
“Nevertheless, great strides have been made in trying to understand the cellular and molecular mechanisms that induce AD [3].”
The Aβ oligomer eliminating D-enantiomeric peptide RD2 improves cognition without changing plaque pathology
van Groen, T., Schemmert, S., Brener, O., Gremer, L., Ziehm, T., Tusche, M., Nagel‐Steger, L., Kadish, I., Schartmann, E., Elfgen, A., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-16565-1 · Cited by 53
“Synthetic and recombinant Aβ(1-42) with >95% purity was purchased as lyophilized powder from Bachem (Germany) and Isoloid (Germany), respectively.”
MethodInfluential
The Molecular Effects of Environmental Enrichment on Alzheimer’s Disease
Liew, A. K. Y., Teo, C. H., & Soga, T. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-03016-w · Cited by 61
“The reduction of neurogenesis throughout the progressive stages has also been recorded [43, 44].”
Background
Discovering Che-1/AATF: a new attractive target for cancer therapy
Iezzi, S., & Fanciulli, M. (2015) · Frontiers in Genetics · doi:10.3389/fgene.2015.00141 · Cited by 53
“This pathology is associated with extracellular aggregates of the β-amyloid peptide (Aβ) and intraneuronal fibrillar tangles of the microtubule binding protein Tau (Crews and Masliah, 2010).”
Background
Palmitate induces transcriptional regulation of BACE1 and presenilin by STAT3 in neurons mediated by astrocytes
Liu, L., Martin, R., Kohler, G., & Chan, C. (2013) · Experimental Neurology · doi:10.1016/j.expneurol.2013.08.004 · Cited by 53
Alzheimer’s Disease: A Molecular View of β-Amyloid Induced Morbific Events
Asik, R. M., Suganthy, N., Aarifa, M. A., Kumar, A., Szigeti, K., Máthé, D., Gulyás, B. Z., Archunan, G., & Padmanabhan, P. (2021) · Biomedicines · doi:10.3390/biomedicines9091126 · Cited by 54
A Reduced Astrocyte Response to β-Amyloid Plaques in the Ageing Brain Associates with Cognitive Impairment
Mathur, R., Ince, P. G., Minett, T., Garwood, C. J., Shaw, P. J., Matthews, F. E., Brayne, C., Simpson, J. E., Wharton, S. B., & on behalf of the MRC Cognitive Function and Ageing Neuropathology Study Group (2015) · PLOS ONE · doi:10.1371/journal.pone.0118463 · Cited by 52
“AD is characterised by early damage to synapses [62,63] and dendritic atrophy [64].”
Background
Insights into intermediate filament regulation from development to ageing
Hyder, C. L., Isoniemi, K. O., Torvaldson, E., & Eriksson, J. (2011) · Journal of Cell Science · doi:10.1242/jcs.041244 · Cited by 56
“Misregulation of Cdk5, one of the kinases targeting NFs, is considered to be important in the pathology of AD (Crews and Masliah, 2010).”
Background
Gastrodin Protects Neural Progenitor Cells Against Amyloid β (1–42)-Induced Neurotoxicity and Improves Hippocampal Neurogenesis in Amyloid β (1–42)-Injected Mice
Li, M. C., & Qian, S. (2016) · Journal of Molecular Neuroscience · doi:10.1007/s12031-016-0758-z · Cited by 50
A soy protein Lunasin can ameliorate amyloid-beta 42 mediated neurodegeneration in Drosophila eye
Sarkar, A., Gogia, N., Glenn, N. W., Singh, A. P., Jones, G. E., Powers, N., Srivastava, A., Singh, A., & Singh, A. (2018) · Scientific Reports · doi:10.1038/s41598-018-31787-7 · Cited by 52
Drosophila Models of Proteinopathies: the Little Fly that Could
Rincón-Limas, D. E., Jensen, K., & Fernández-Fúnez, P. (2012) · Current Pharmaceutical Design · doi:10.2174/138161212799315894 · Cited by 51
“According to the “amyloid hypothesis”, accumulation of the Aß42 peptide initiates the pathogenic cascade in AD, including Tau hyperphosphorylation, aberrant cellular signaling and, ultimately, cell death [26].”
Background
The Pathological Roles of Ganglioside Metabolism in Alzheimer′s Disease: Effects of Gangliosides on Neurogenesis
Ariga, T., Wakade, C. G., & Yu, R. K. (2011) · International Journal of Alzheimer s Disease · doi:10.4061/2011/193618 · Cited by 53
“In addition to the alterations in synaptic plasticity and neuronal integrity in mature neuronal circuitries, the neurodegenerative process in AD has recently been shown to be accompanied by alterations in neurogenesis [103, 104].”
Background
PINK1 enhances insulin-like growth factor-1-dependent Akt signaling and protection against apoptosis
Akundi, R. S., Zhi, L., & Büeler, H. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.08.034 · Cited by 52
BAD-mediated neuronal apoptosis and neuroinflammation contribute to Alzheimer's disease pathology
Zhang, L., Qian, Y., Li, J., Zhou, X., Xu, H. J., Yan, J., Xiang, J., Yuan, X., Sun, B., Sisodia, S. S., et al. (2021) · iScience · doi:10.1016/j.isci.2021.102942 · Cited by 54
“Overwhelming evidence shows that accumulation of Ab plaques induces progressive neuronal degeneration and synaptic loss, resulting in severe neuronal loss and subsequent memory and cognitive deficits in AD patients and animal models (Crews and Masliah, 2010).”
Background
Group 1 Metabotropic Glutamate Receptors in Neurological and Psychiatric Diseases: Mechanisms and Prospective
Su, L., Wang, N., Han, J., & Shen, Y. (2021) · The Neuroscientist · doi:10.1177/10738584211021018 · Cited by 51
“In AD, amyloid hypothesis holds amyloid-β (Aβ) peptide as the prime causative of AD pathology (Hardy and Selkoe 2002; Tanzi and Bertram 2005), as shown by disruptive effects of Aβ40 and Aβ42 on synaptic transmission and brain connectome (Crews and Masliah 2010; Holtzman and others 2012).”
Background
DNA polymerase β decrement triggers death of olfactory bulb cells and impairs olfaction in a mouse model of Alzheimer's disease
Misiak, M., Greeno, R. V., Baptiste, B. A., Sýkora, P., Liu, D., Cordonnier, S. A., Fang, E. F., Croteau, D. L., Mattson, M. P., & Bohr, V. A. (2016) · Aging Cell · doi:10.1111/acel.12541 · Cited by 50
“…(AD) is characterized by dysfunction and degeneration of neurons in brain regions involved in learning and memory, which is associated with accumulations of aggregated extracellular amyloid b-peptide (Ab) and intracellular hyperphosphorylated Tau protein (Mattson, 2004; Crews & Masliah, 2010).”
Background
The neuroprotective effect of deep brain stimulation at nucleus basalis of Meynert in transgenic mice with Alzheimer's disease
Huang, C., Chu, H., Ma, Y., Zhou, Z., Dai, C., Huang, X., Fang, L., Ao, Q., & Huang, D. (2018) · Brain stimulation · doi:10.1016/j.brs.2018.08.015 · Cited by 50
Identification of BACE1 inhibitors from Panax ginseng saponins—An Insilco approach
Veerappan, K., Natarajan, S., Subramaniyam, S., Rasappan, P., Samuel, S., Kim, Y.-J., & Yang, D. (2013) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2013.05.009 · Cited by 49
“Alzheimer's disease (AD), a major progressive neurodegenerative disorder, is the leading cause of dementia threatening the elderly population [1,2].”
Background
Genotoxicity Studies of Titanium Dioxide Nanoparticles (TiO2NPs) in the Brain of Mice
Mohamed, H. R. H., & Hussien, N. A. (2016) · Scientifica · doi:10.1155/2016/6710840 · Cited by 49
“Crews and Masliah [31] referred to previous studies that, in familial forms of AD, PSEN mutations result in an increase of amyloid-β (Aβ) protein production or aggregation that in turn results in plaque formation and synaptotoxicity.”
Background
RETRACTED: A shared comparison of diabetes mellitus and neurodegenerative disorders
Morsi, M., Maher, A., Aboelmagd, O., Johar, D., & Bernstein, L. H. (2017) · Journal of Cellular Biochemistry · doi:10.1002/jcb.26261 · Cited by 52
“In addition, mitochondrial function is impaired, oxidative stress increases, and nigral pathology is enhanced by overexpression of α-synuclein.(4) Respiratory transport chain activity is reduced in HD brains.”
Influential
Retracted
Microbiota Alterations in Alzheimer’s Disease: Involvement of the Kynurenine Pathway and Inflammation
Garcez, M. L., Jacobs, K. R., & Guillemin, G. J. (2019) · Neurotoxicity Research · doi:10.1007/s12640-019-00057-3 · Cited by 51
The Potential Utility of Prebiotics to Modulate Alzheimer’s Disease: A Review of the Evidence
Kang, J. W., & Zivkovic, A. M. (2021) · Microorganisms · doi:10.3390/microorganisms9112310 · Cited by 49
The Neuroprotective Effects and Therapeutic Potential of the Chalcone Cardamonin for Alzheimer’s Disease
Barber, K., Mendonca, P., & Soliman, K. F. A. (2023) · Brain Sciences · doi:10.3390/brainsci13010145 · Cited by 51
“In AD, synaptic dysfunction and faulty neurogenesis are linked to the accumulation of Aβ, an imbalance between the levels of Aβ production, aggregation, and clearance results in the creation of hazardous oligomers [19].”
Background
Faradarmani Consciousness Field Suppresses Alzheimer’s Disease Development in both in vitro and in vivo Models of the Disease
Taheri, M. A., Torabi, S., Nabavi, N., & Semsarha, F. (2022) · ژورنال علمی کازمواینتل · doi:10.61450/joci.v1i2.18 · Cited by 46
Reducing Aβ load and tau phosphorylation: Emerging perspective for treating Alzheimer's disease
Kalra, J., & Khan, A. G. (2015) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2015.07.043 · Cited by 47
“…feature, where as unique lesions, involved in hippocampal formation include hirano bodies and granulovacuolar degeneration (Alzheimer 1907; Serrano-Pozo et al., 2011; Crews and Masliah, 2010) However, onset of clinical signs and symptoms of the disease is insidious evolving over many years.”
Background
Brain metabolism and Alzheimer's disease: The prospect of a metabolite-based therapy
Thomas, S. C., Alhasawi, A. A., Appanna, V. D., Auger, C., & Appanna, V. D. (2014) · The journal of nutrition health & aging · doi:10.1007/s12603-014-0511-7 · Cited by 51
“As individuals age, the primary source of energy shifts from solely glucose to a wide variety of metabolites including lactate, acetate and ketone bodies which support neurons in their cellular functions (21).”
Suppression of a MEF2-KLF6 Survival Pathway by PKA Signaling Promotes Apoptosis in Embryonic Hippocampal Neurons
Salma, J., & McDermott, J. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.3609-11.2012 · Cited by 54
“Modulation of gene expression networks underlying these pivotal cellular events ultimately leading to neurodegeneration is still in its infancy (Crews and Masliah, 2010).”
Background
Marine-Derived Compounds with Anti-Alzheimer’s Disease Activities
Ghoran, S. H., & Kijjoa, A. (2021) · Marine Drugs · doi:10.3390/md19080410 · Cited by 51
“Besides genetic and environmental factors [4,5], to date, several factors, including cholinesterase (acetyl- and butyrylcholinesterase) enzymes [6], proteases with β-site amyloid precursor protein cleaving cascade (β- and γ-secretases) [7], β-amyloid (Aβ) aggregation [3,8], protein kinase C [9], tau protein [3,10], gl…”
Background
Mechanism of synapse redox stress in Okadaic acid (ICV) induced memory impairment: Role of NMDA receptor
Kamat, P. K., Rai, S., Swarnkar, S., Shukla, R., & Nath, C. (2014) · Neurochemistry International · doi:10.1016/j.neuint.2014.06.012 · Cited by 46
“Progressive neurodegeneration in AD is initially characterized by synaptic damage accompanied by neuronal loss, especially in the hippocampus (Crews and Masliah, 2010).”
Background
Genetic interactions associated with 12-month atrophy in hippocampus and entorhinal cortex in Alzheimer's Disease Neuroimaging Initiative
Meda, S. A., Koran, M. E. I., Pryweller, J. R., Vega, J. N., & Thornton‐Wells, T. A. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.09.020 · Cited by 46
“…characterized by decreased synaptic density after injury caused by the accumulation of neuropathologic events such as astrogliosis and microglial cell proliferation, in addition to the observed amyloid and tau pathology (Blurton-Jones and LaFerla, 2006; Crews and Masliah, 2010; LaFerla, 2002 ).”
Background
Proteolytic shedding of the prion protein via activation of metallopeptidase ADAM10 reduces cellular binding and toxicity of amyloid-β oligomers
Jarosz-Griffiths, H., Corbett, N. J., Rowland, H. A., Fisher, K., Jones, A. C., Baron, J., Howell, G. J., Cowley, S. A., Chintawar, S., Cader, M. Z., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005364 · Cited by 45
“A O binding to PrPC activated Fyn kinase and caused an increase in ROS that could be blocked by promoting the shedding of PrPC with acitretin.”
BackgroundInfluential
Neuroligin-1 is altered in the hippocampus of Alzheimer’s disease patients and mouse models, and modulates the toxicity of amyloid-beta oligomers
Dufort‐Gervais, J., Provost, C., Charbonneau, L., Norris, C. M., Calon, F., Mongrain, V., & Brouillette, J. (2020) · Scientific Reports · doi:10.1038/s41598-020-63255-6 · Cited by 48
Activation of CREB‐mediated autophagy by thioperamide ameliorates β‐amyloid pathology and cognition in Alzheimer’s disease
Wang, J., Liu, B., Xu, Y. X., Yang, M., Wang, C., Song, M., Liu, J., Wang, W., You, J., Sun, F., et al. (2021) · Aging Cell · doi:10.1111/acel.13333 · Cited by 47
“…release from histaminergic neurons via negative feedback way (Arrang et al., 1983; Morisset et al., 2000), as well as a heteroreceptor that regulates the release of other neurotransmitters (Clapham & Kilpatrick, 1992; Dai et al., 2007; Hansen et al., 2010; Schlicker et al., 1988, 1989, 1993).”
Background
The Nav1.2 channel is regulated by GSK3
James, T. F., Nenov, M. N., Wildburger, N. C., Lichti, C. F., Luisi, J. D., Vergara, F., Panova-Electronova, N. I., Nilsson, C. L., Rudra, J. S., Green, T. A., et al. (2015) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2015.01.011 · Cited by 45
Anti-Inflammatory and Anti-Migratory Activities of Isoquinoline-1-Carboxamide Derivatives in LPS-Treated BV2 Microglial Cells via Inhibition of MAPKs/NF-κB Pathway
Do, H. T. T., Bui, B. P., Sim, S., Jung, J., Lee, H., & Cho, J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21072319 · Cited by 45
Curcumin and hesperetin attenuate D-galactose-induced brain senescence in vitro and in vivo
Lee, J., Kim, Y. S., Kim, E., Kim, Y., & Kim, Y. (2020) · Nutrition Research and Practice · doi:10.4162/nrp.2020.14.5.438 · Cited by 41
“In addition, neuronal generation is rapidly diminished [7,8].”
Background
Functional Neurophysiological Biomarkers of Early-Stage Alzheimer’s Disease: A Perspective of Network Hyperexcitability in Disease Progression
Tok, S., Ahnaou, A., & Drinkenburg, W. H. I. M. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-210397 · Cited by 45
“Currently, the most accepted pathological features of AD are the presence of extracellular amyloid plaques and intracellular neurofibrillary tangles [9], chronic neuroinflammation [10], and neurodegeneration [11].”
Background
A translational continuum of model systems for evaluating treatment strategies in Alzheimer’s disease: isradipine as a candidate drug
Copenhaver, P. F., Anekonda, T. S., Musashe, D. T., Robinson, K. M., Ramaker, J. M., Swanson, T. L., Wadsworth, T. L., Kretzschmar, D., Woltjer, R. L., & Quinn, J. F. (2011) · Disease Models & Mechanisms · doi:10.1242/dmm.006841 · Cited by 44

Authors: Crews, L., & Masliah, E.
Affiliations: University of California San Diego (US)
Corresponding author: Masliah, E.
ORCID: Crews, L.
Masliah, E.
Venue: Human Molecular Genetics
Publisher: Oxford University Press (OUP)
Published: 2010-04-15
Volume: 19
Issue: R1
Pages: R12-R20
ISSN: 0964-6906 (ISSN-L)
1460-2083
DOI: 10.1093/hmg/ddq160
PMC: PMC2875049
OpenAlex: W2135957529
Cited by: 772
References: 175
Citations by year: 2026: 33 · 2025: 53 · 2024: 56 · 2023: 71 · 2022: 48 · 2021: 76 · 2020: 69 · 2019: 50 · 2018: 47 · 2017: 47 · 2016: 42 · 2015: 34 · 2014: 31 · 2013: 35 · 2012: 40
FWCI: 3.70
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Human Molecular Genetics (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (AG5131, NS4 4233, AG‐18440, AG10435, AG11385)
National Institute on Aging (P01AG010435, AG-11385, P50AG005131, AG-5131, AG 18440, AG10435)
National Institute of Neurological Disorders and Stroke (P01NS044233, NS-44233)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords: Alzheimer's disease, neurodegeneration, amyloid-beta oligomers, amyloid plaques, tau hyperphosphorylation, neurofibrillary tangles, synaptic loss, adult hippocampal neurogenesis, glutamate receptors, excitotoxicity, mitochondrial dysfunction, lysosomal dysfunction, synaptic plasticity, Fyn, glycogen synthase kinase-3β, cyclin-dependent kinase 5, anti-aggregation therapy, amyloid-beta clearance
MeSH terms: Alzheimer Disease, Humans, Amyloid beta-Peptides, Neurogenesis

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