The Link between Oxidative Stress, Mitochondrial Dysfunction and Neuroinflammation in the Pathophysiology of Alzheimer’s Disease: Therapeutic Implications and Future Perspectives
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Alzheimer’s disease (AD), the most common form of dementia, has increasing incidence, increasing mortality rates, and poses a huge burden on healthcare. None of the currently approved drugs for the treatment of AD influence disease progression. Many clinical trials aiming at inhibiting amyloid plaque formation, increasing amyloid beta clearance, or inhibiting neurofibrillary tangle pathology yielded inconclusive results or failed. Meanwhile, research has identified many interlinked vicious cascades implicating oxidative stress, mitochondrial dysfunction, and chronic neuroinflammation, and has pointed to novel therapeutic targets such as improving mitochondrial bioenergetics and quality control, diminishing oxidative stress, or modulating the neuroinflammatory pathways. Many novel molecules tested in vitro or in animal models have proven efficient, but their translation into clinic needs further research regarding appropriate doses, delivery routes, and possible side effects. Cell-based therapies and extracellular vesicle-mediated delivery of messenger RNAs and microRNAs seem also promising strategies allowing to target specific signaling pathways, but need further research regarding the most appropriate harvesting and culture methods as well as control of the possible tumorigenic side effects. The rapidly developing area of nanotechnology could improve drug delivery and also be used in early diagnosis.
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A significant trigger for astrocyte reactivity is neuroinflammation, involving pro-inflammatory molecules like cytokines and chemokines.
“A significant trigger for astrocyte reactivity is neuroinflammation, involving pro-inflammatory molecules like cytokines and chemokines (11–14).”
From Varicose projection astrocytes: Conserved reactive cells in brain pathology (2026) · cites this paper as [13]
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Takahashi, K., & Yamanaka, S. (2006) · Cell · doi:10.1016/j.cell.2006.07.024 · Cited by 26,673 · see citing works
A Unique Microglia Type Associated with Restricting Development of Alzheimer’s Disease
Keren-Shaul, H., Spinrad, A., Weiner, A., Matcovitch-Natan, O., Dvir-Szternfeld, R., Ulland, T. K., David, E., Baruch, K., Lara-Astaiso, D., Toth, B., et al. (2017) · Cell · doi:10.1016/j.cell.2017.05.018 · Cited by 5,493 · see citing works
Highly efficient neural conversion of human ES and iPS cells by dual inhibition of SMAD signaling
Chambers, S. M., Fasano, C. A., Papapetrou, E. P., Tomishima, M., Sadelain, M., & Studer, L. (2009) · Nature Biotechnology · doi:10.1038/nbt.1529 · Cited by 3,620 · see citing works
2019 Alzheimer’s disease facts and figures.
Alzheimer's Association (2019) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2019.01.010 · Cited by 2,461 · see citing works
Oxidative stress and the amyloid beta peptide in Alzheimer’s disease
Cheignon, C., Tomas, M., Bonnefont-Rousselot, D., Faller, P., Hureau, C., & Collin, F. (2018) · Redox Biology · doi:10.1016/j.redox.2017.10.014 · Cited by 2,185 · see citing works
Oxidative stress, dysfunctional glucose metabolism and Alzheimer disease
Butterfield, D. A., & Halliwell, B. (2019) · Nature Reviews Neuroscience · doi:10.1038/s41583-019-0132-6 · Cited by 1,954 · cited 13× · see citing works
“In cell cultures and animal models of neurodegenerative diseases SS-31 (MTP-131, Elamipretide, Bendavia) upregulated mRNAs for ETC complexes I, IV, and V, for PGC-1α and TFAM, and improved mitochondrial dynamics by upregulating mitochondrial fusion proteins and downregulating proteins regulating fission.”
BackgroundInfluentialNLRP3 inflammasome activation drives tau pathology
Ising, C., Venegas, C., Zhang, S., Scheiblich, H., Schmidt, S. V., Vieira-Saecker, A., Schwartz, S., Albasset, S., McManus, R. M., Tejera, D., et al. (2019) · Nature · doi:10.1038/s41586-019-1769-z · Cited by 1,487 · see citing works
TREM2 Maintains Microglial Metabolic Fitness in Alzheimer’s Disease
Ulland, T. K., Song, W. M., Huang, S. C.-C., Ulrich, J. D., Sergushichev, A., Beatty, W. L., Loboda, A. A., Zhou, Y., Cairns, N. J., Kambal, A., et al. (2017) · Cell · doi:10.1016/j.cell.2017.07.023 · Cited by 1,263 · cited 1× · see citing works
“Detailed studies in mouse models of AD described a subpopulation of transcriptionally distinct microglia, termed disease-associated microglia, which differed from the common homeostatic microglia [154] and supported the glial cells in overcoming the compromised bioenergetic state via mTOR signaling [155].”
BackgroundImpaired Balance of Mitochondrial Fission and Fusion in Alzheimer's Disease
Wang, X., Su, B., Lee, H.-G., Li, X., Perry, G., Smith, M. A., & Zhu, X. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.1357-09.2009 · Cited by 1,224 · see citing works
The role of mitochondria in reactive oxygen species metabolism and signaling
Starkov, A. A. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1427.015 · Cited by 846 · see citing works
The Alzheimer’s disease mitochondrial cascade hypothesis: progress and perspectives
Swerdlow, R. H., Burns, J. M., & Khan, S. M. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.09.010 · Cited by 786 · cited 1× · see citing works
“Although the primary insult leading to AD is still a matter of debate, these metabolic changes indicate a crucial role for mitochondrial dysfunction in AD pathogenesis, leading some researchers to postulate the “mitochondrial cascade hypothesis” [45].”
BackgroundBrain metabolism in health, aging, and neurodegeneration
Camandola, S., & Mattson, M. P. (2017) · The EMBO Journal · doi:10.15252/embj.201695810 · Cited by 752 · see citing works
Mitochondrial Aβ: a potential focal point for neuronal metabolic dysfunction in Alzheimer's disease
Caspersen, C., Wang, N., Yao, J., Sosunov, A., Chen, X., Lustbader, J. W., Xu, H. W., Stern, D., McKhann, G., & Du Yan, S. (2005) · The FASEB Journal · doi:10.1096/fj.05-3735fje · Cited by 738 · see citing works
Alzheimer's disease drug development pipeline: 2018
Cummings, J., Lee, G., Ritter, A., & Zhong, K. (2018) · Alzheimer's & Dementia: Translational Research & Clinical Interventions · doi:10.1016/j.trci.2018.03.009 · Cited by 697 · see citing works
Spangenberg, E. E., Lee, R. J., Najafi, A. R., Rice, R. A., Elmore, M. R. P., Blurton-Jones, M., West, B. L., & Green, K. N. (2016) · Brain · doi:10.1093/brain/aww016 · Cited by 695 · see citing works
Jay, T. R., Miller, C. M., Cheng, P. J., Graham, L. C., Bemiller, S., Broihier, M. L., Xu, G., Margevicius, D., Karlo, J. C., Sousa, G. L., et al. (2015) · Journal of Experimental Medicine · doi:10.1084/jem.20142322 · Cited by 682 · cited 1× · see citing works
“It is still controversial whether TREM2 is important for resident microglia or in promoting infiltration of peripheral myeloid cells [180].”
BackgroundDysken, M. W., Sano, M., Asthana, S., Vertrees, J. E., Pallaki, M., Llorente, M., Love, S., Schellenberg, G. D., McCarten, J. R., Malphurs, J., et al. (2014) · JAMA · doi:10.1001/jama.2013.282834 · Cited by 628 · see citing works
The role of interleukin-1 in neuroinflammation and Alzheimer disease: an evolving perspective
Shaftel, S. S., Griffin, W. S. T., & O'Banion, M. K. (2008) · Journal of Neuroinflammation · doi:10.1186/1742-2094-5-7 · Cited by 565 · see citing works
McManus, M. J., Murphy, M. P., & Franklin, J. L. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.0552-11.2011 · Cited by 432 · see citing works
The multifaceted role of Nrf2 in mitochondrial function
Holmström, K. M., Kostov, R. V., & Dinkova-Kostova, A. T. (2016) · Current Opinion in Toxicology · doi:10.1016/j.cotox.2016.10.002 · Cited by 368 · see citing works
Elucidating the Role of TREM2 in Alzheimer’s Disease
Ulrich, J. D., Ulland, T. K., Colonna, M., & Holtzman, D. M. (2017) · Neuron · doi:10.1016/j.neuron.2017.02.042 · Cited by 325 · see citing works
Song, W., Hooli, B., Mullin, K., Jin, S. C., Cella, M., Ulland, T. K., Wang, Y., Tanzi, R. E., & Colonna, M. (2017) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2016.07.004 · Cited by 297 · see citing works
Pattern Recognition by TREM-2: Binding of Anionic Ligands
Daws, M. R., Sullam, P. M., Niemi, E. C., Chen, T. T., Tchao, N. K., & Seaman, W. E. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.171.2.594 · Cited by 291 · see citing works
Reed, T., Perluigi, M., Sultana, R., Pierce, W. M., Klein, J. B., Turner, D. M., Coccia, R., Markesbery, W. R., & Butterfield, D. A. (2008) · Neurobiology of Disease · doi:10.1016/j.nbd.2007.12.007 · Cited by 257 · see citing works
Di Domenico, F., Tramutola, A., & Butterfield, D. A. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.10.490 · Cited by 253 · see citing works
Shi, J.-Q., Shen, W., Chen, J., Wang, B.-R., Zhong, L.-L., Zhu, Y.-W., Zhu, H.-Q., Zhang, Q.-Q., Zhang, Y.-D., & Xu, J. (2011) · Brain Research · doi:10.1016/j.brainres.2010.10.053 · Cited by 219 · see citing works
Fluid Biomarkers in Alzheimer Disease
Blennow, K., Zetterberg, H., & Fagan, A. M. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006221 · Cited by 208 · see citing works
Molecular Mechanisms and Genetics of Oxidative Stress in Alzheimer’s Disease
Cioffi, F., Adam, R. H. I., & Broersen, K. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190863 · Cited by 204 · cited 2× · see citing works
“With aging, cerebral glucose metabolism progressively declines as a result of changes in brain insulin and cortisol levels [46] and of decreased activity of synaptic ATPases [47], leading to a 45% reduced cerebral glucose utilization [46].”
BackgroundAbbaszadeh, H., Ghorbani, F., Derakhshani, M., Movassaghpour, A., & Yousefi, M. (2020) · Journal of Cellular Physiology · doi:10.1002/jcp.29004 · Cited by 188 · see citing works
TREM2 deficiency reduces the efficacy of immunotherapeutic amyloid clearance
Xiang, X., Werner, G., Bohrmann, B., Liesz, A., Mazaheri, F., Capell, A., Feederle, R., Knuesel, I., Kleinberger, G., & Haass, C. (2016) · EMBO Molecular Medicine · doi:10.15252/emmm.201606370 · Cited by 183 · see citing works
Frozza, R. L., Bernardi, A., Hoppe, J. B., Meneghetti, A. B., Matté, A., Battastini, A. M. O., Pohlmann, A. R., Guterres, S. S., & Salbego, C. (2013) · Molecular Neurobiology · doi:10.1007/s12035-013-8401-2 · Cited by 165 · see citing works
GSK3β and tau protein in Alzheimer's disease and epilepsy
Toral-Rios, D., Pichardo-Rojas, P. S., Alonso-Vanegas, M., & Campos-Peña, V. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.00019 · Cited by 158 · see citing works
Nagpal, K., Singh, S. K., & Mishra, D. N. (2013) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2013.04.024 · Cited by 116 · see citing works
Ojala, J. O., Sutinen, E. M., Salminen, A., & Pirttilä, T. (2008) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2008.09.012 · Cited by 102 · see citing works
The Proteasome and Oxidative Stress in Alzheimer's Disease
Bonet-Costa, V., Pomatto, L. C.-D., & Davies, K. J. A. (2016) · Antioxidants & Redox Signaling · doi:10.1089/ars.2016.6802 · Cited by 99 · see citing works
Derakhshankhah, H., Sajadimajd, S., Jafari, S., Izadi, Z., Sarvari, S., Sharifi, M., Falahati, M., Moakedi, F., Muganda, W. C. A., Müller, M., et al. (2020) · Nanomedicine: Nanotechnology, Biology and Medicine · doi:10.1016/j.nano.2020.102149 · Cited by 48 · see citing works
Flagged first, then by citations
Research works printed but not linked: 227
- [1]Zhang X.X. Tian Y. Wang Z.T. Ma Y.H. Tan L. Yu J.T. The epidemiology of Alzheimer’s disease modifiable risk factors and prevention J. Prev. Alzheimers Dis. 2021 8 313 321 10.14283/jpad.2021.15 34101789 · DOI · Paper page
- [2]Fratiglioni L. Launer L.J. Breteler M.M. Copeland J.R. Dartigues J.F. Lobo A. Martinez-Lage J. Soininen H. Hofman A. Incidence of dementia and major subtypes in Europe: A collaborative study of population-based cohorts. Neurologic diseases in the elderly research group Neurology 2000 54 1015 10854355
- [3]Plassman B.L. Langa K.M. Fisher G.G. Heeringa S.G. Weir D.R. Ofstedal M.B. Burke J.R. Hurd M.D. Potter G.G. Rodgers W.L. Prevalence of dementia in the United States: The aging, demographics, and memory study Neuroepidemiology 2007 29 125 132 10.1159/000109998 17975326 PMC2705925 · DOI · Paper page
- [4]Qiu C. Kivipelto M. von Strauss E. Epidemiology of Alzheimer’s disease: Occurrence, determinants, and strategies toward intervention Dialogues Clin. Neurosci. 2009 11 111 128 10.31887/DCNS.2009.11.2/cqiu 19585947 PMC3181909 · DOI · Paper page
- [6]Scheltens P. Blennow K. Breteler M.M.B. de Strooper B. Frisoni G.B. Salloway S. Van der Flier W.M. Alzheimer’s disease Lancet 2016 388 505 517 10.1016/S0140-6736(15)01124-1 26921134 · DOI · Paper page
- [7]Alafuzoff I. Arzberger T. Al-Sarraj S. Bodi I. Bogdanovic N. Braak H. Bugiani O. Del-Tredici K. Ferrer I. Gelpi E. Staging of neurofibrillary pathology in Alzheimer’s disease: A study of the BrainNet Europe Consortium Brain Pathol. 2008 18 484 496 10.1111/j.1750-3639.2008.00147.x 18371174 PMC2659377 · DOI · Paper page
- [9]Grundke-Iqbal I. Iqbal K. Quinlan M. Tung Y.C. Zaidi M.S. Wisniewski H.M. Microtubule-associated protein tau. A component of Alzheimer paired helical filaments J. Biol. Chem. 1986 261 6084 6089 10.1016/S0021-9258(17)38495-8 3084478 · DOI
- [10]Hardy J.A. Higgins G.A. Alzheimer’s disease: The amyloid cascade hypothesis Science 1992 256 184 185 10.1126/science.1566067 1566067 · DOI · Paper page
- [11]Jurcau A. Insights into the pathogenesis of neurodegenerative diseases: Focus on mitochondrial dysfunction and oxidative stress Int. J. Mol. Sci. 2021 22 11847 10.3390/ijms222111847 34769277 PMC8584731 · DOI
- [12]Drake J. Link C.D. Butterfield D.A. Oxidative stress precedes fibrillar deposition of Alzheimer’s disease amyloid beta-peptide (1-42) in a transgenic Caenorhabditis elegans model Neurobiol. Aging 2003 24 415 420 10.1016/S0197-4580(02)00225-7 12600717 · DOI · Paper page
- [14]Halliwell B. Gutteridge J.M.C. Free Radicals in Biology and Medicine 5th ed. Oxford University Press New York, NY, USA 2015
- [15]Andreyev A.Y. Kushnareva Y.E. Starkov A.A. Mitochondrial metabolism of reactive oxygen species Biochemistry 2005 70 200 214 10.1007/s10541-005-0102-7 15807660 · DOI · Paper page
- [17]Cobley N.J. Fiorello M.L. Bailey D.M. 13 reasons why the brain is susceptible to oxidative stress Redox Biol. 2018 15 490 513 10.1016/j.redox.2018.01.008 29413961 PMC5881419 · DOI · Paper page
- [18]Jurcau A. Simion A. Oxidative stress in the pathogenesis of Alzheimer’s disease and cerebrovascular disease with therapeutic implications CNS Neurol. Disord. Drug Targets 2020 19 24 108 10.2174/1871527319666200303121016 32124703 · DOI
- [19]Harris J.J. Jolivet R. Attwell D. Synaptic energy use and supply Neuron 2012 75 762 777 10.1016/j.neuron.2012.08.019 22958818 · DOI · Paper page
- [20]Ren X. Zou L. Zhang X. Branco V. Wang J. Carvalho C. Holmgren A. Lu J. Redox signaling mediated by thioredoxin and glutathione systems in the central nervous system Antioxid. Redox Signal. 2017 27 989 1010 10.1089/ars.2016.6925 28443683 PMC5649126 · DOI
- [21]Chang C.J. Searching for harmony in transition-metal signaling Nat. Chem. Biol. 2015 11 744 747 10.1038/nchembio.1913 26379012 · DOI
- [22]Zerbinati C. Iuliano L. Cholesterol and related sterols autoxidation Free Radic. Biol. Med. 2017 111 151 155 10.1016/j.freeradbiomed.2017.04.013 28428001 · DOI
- [23]Misrani A. Tabassum S. Yang L. Mitochondrial dysfunction and oxidative stress in Alzheimer’s disease Front. Aging Neurosci. 2021 13 617588 10.3389/fnagi.2021.617588 33679375 PMC7930231 · DOI · Paper page
- [24]Elgainidi I.S. Spiers J.P. Regulation of the phosphoprotein phosphatase 2A system and its modulation during oxidative stress: A potential therapeutic target? Pharmacol. Ther. 2019 198 68 89 10.1016/j.pharmthera.2019.02.011 30797822 · DOI
- [26]Perluigi M. Di Domenico F. Barone E. Butterfield D.A. mTOR in Alzheimer disease and its earlier stages: Links to oxidative damage in the progression of this dementing disorder Free Radic. Biol. Med. 2021 169 382 396 10.1016/j.freeradbiomed.2021.04.025 33933601 PMC8145782 · DOI
- [28]Gamba P. Staurenghi E. Testa G. Giannelli S. Sottero B. Leonarduzzi G. A crosstalk between brain cholesterol oxidation and glucose metabolism in Alzheimer’s disease Front. Neurosci. 2019 13 556 10.3389/fnins.2019.00556 31213973 PMC6554318 · DOI
- [29]Sharma A. Weber D. Raupbach J. Dakal T.C. Fließbach K. Ramirez A. Grune T. Wüllner U. Advanced glycation end products and protein carbonyl levels in plasma reveal sex-specific differences in Parkinson’s and Alzheimer’s disease Redox Biol. 2020 34 101546 10.1016/j.redox.2020.101546 32460130 PMC7251371 · DOI · Paper page
- [30]Youssef P. Chami B. Lim J. Middleton T. Sutherland G.T. Witting P.K. Evidence supporting oxidative stress in a moderately affected area of the brain in Alzheimer’s disease Sci. Rep. 2018 8 11553 10.1038/s41598-018-29770-3 30068908 PMC6070512 · DOI
- [31]Qiu C. Fratiglioni L. Epidemiology of Alzheimer’s disease Alzheimer’s Disease 2nd ed. Waldemar G. Burns A. Oxford University Press Oxford, UK 2017 17 26
- [32]Zia A. Pourbagher-Shahri A.M. Farkhondeh T. Samarghandian S. Molecular and cellular pathways contributing to brain aging Behav. Brain Funct. 2021 17 6 10.1186/s12993-021-00179-9 34118939 PMC8199306 · DOI
- [34]Błaszczyk J.W. Energy metabolism decline in the aging brain–pathogenesis of neurodegenerative disorders Metabolites 2020 10 450 10.3390/metabo10110450 33171879 PMC7695180 · DOI
- [35]Rangaraju V. Lauterbach M. Schuman E.M. Spatially stable mitochondrial compartments fuel local translation during plasticity Cell 2019 176 73 84 10.1016/j.cell.2018.12.013 30612742 · DOI
- [36]Sharma C. Kim S. Nam Y. Jung U.J. Kim S.R. Mitochondrial dysfunction as a driver of cognitive impairment in Alzheimer’s disease Int. J. Mol. Sci. 2021 22 4850 10.3390/ijms22094850 34063708 PMC8125007 · DOI
- [37]Daum B. Walter A. Horst A. Osiewacz H.D. Kühlbrandt W. Age-dependent dissociation of ATP synthase dimers and loss of inner-membrane cristae in mitochondria Proc. Natl. Acad. Sci. USA 2013 110 15301 15306 10.1073/pnas.1305462110 24006361 PMC3780843 · DOI
- [38]Huang Z. Chen Y. Zhang Y. Mitochondrial reactive oxygen species cause major oxidative mitochondrial DNA damages and repair pathways J. Biosci. 2020 45 84 10.1007/s12038-020-00055-0 32661211 · DOI
- [39]Folgueras A.R. Freitas-Rodríguez S. Velasco G. López-Otín C. Mouse models to disentangle the hallmarks of human aging Circ. Res. 2018 123 905 924 10.1161/CIRCRESAHA.118.312204 30355076 · DOI · Paper page
- [40]D’Angelo M.A. Raices M. Panowski S.H. Hetzer M.W. Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells Cell 2009 136 284 295 10.1016/j.cell.2008.11.037 19167330 PMC2805151 · DOI · Paper page
- [41]Covarrubias A.J. Perrone R. Grozio A. Verdin E. NAD+ metabolism and its roles in cellular processes during ageing Nat. Rev. Mol. Cell Biol. 2021 22 119 141 10.1038/s41580-020-00313-x 33353981 PMC7963035 · DOI · Paper page
- [42]Mytych J. Actions of Klotho on hippocampal neuronal cells Vitam. Horm. 2022 118 223 246 35180928
- [43]Veitch D.P. Weiner M.W. Aisen P.S. Beckett L.A. Cairns N.J. Green R.C. Harvey D. Jack C.R. Jr. Jagust W. Morris J.C. Alzheimer’s Disease Neuroimaging Initiative. Understanding disease progression and improving Alzheimer’s disease clinical trials: Recent highlights from the Alzheimer’s Disease Neuroimaging Initiative Alzheimers Dement. 2019 15 106 152 10.1016/j.jalz.2018.08.005 30321505 · DOI · Paper page
- [44]Perez Ortiz J.M. Swerdlow R.H. Mitochondrial dysfunction in Alzheimer’s disease: Role in pathogenesis and novel therapeutic opportunities Br. J. Pharmacol. 2019 176 3489 3507 10.1111/bph.14585 30675901 PMC6715612 · DOI · Paper page
- [47]Ferrari F. Viscardi P. Gorini A. Villa R.F. Synaptic ATPases system of rat frontal cerebral cortex during aging Neurosci. Lett. 2019 694 74 79 10.1016/j.neulet.2018.11.028 30472356 · DOI
- [48]Hoyer S. Nitsch R. Oesterreich K. Predominant abnormality in cerebral glucose utilization in late-onset dementia of the Alzheimer type: A cross-sectional comparison against advanced late-onset and incipient early-onset cases J. Neural Transm. Park. Dis. Dement. Sect. 1991 3 1 14 10.1007/BF02251132 1905936 · DOI
- [49]Casley C.S. Canevari L. Land J.M. Clark J.B. Sharpe M.A. β-amyloid inhibits integrated mitochondrial respiration and key enzyme activities J. Neurochem. 2002 80 91 100 10.1046/j.0022-3042.2001.00681.x 11796747 · DOI
- [50]Texeira J.P. de Castro A.A. Soares F.V. da Cunha E.F.F. Ramalho T.C. Future therapeutic perspectives into the Alzheimer’s disease targeting the oxidative stress hypothesis Molecules 2019 24 4410 10.3390/molecules24234410 31816853 PMC6930470 · DOI
- [51]Sultana R. Poon H.F. Cai J. Pierce W.M. Merchant M. Klein J.B. Markesbery W.R. Butterfield D.A. Identification of nitrated proteins in Alzheimer’s disease brain using a redox proteomics approach Neurobiol. Dis. 2006 22 76 87 10.1016/j.nbd.2005.10.004 16378731 · DOI · Paper page
- [55]Tamagno E. Guglielmotto M. Vasciaveo V. Tabaton M. Oxidative Stress and Beta Amyloid in Alzheimer’s Disease. Which Comes First: The Chicken or the Egg? Antioxidants 2021 10 1479 10.3390/antiox10091479 34573112 PMC8468973 · DOI
- [56]Mosconi L. Berti V. Glodzik L. Pupi A. De Santi S. de Leon M.J. Pre-clinical detection of Alzheimer’s disease using FDG-PET, with or without amyloid imaging J. Alzheimer’s Dis. 2010 20 843 854 10.3233/JAD-2010-091504 20182025 PMC3038340 · DOI
- [57]Jurcau A. Ardelean I.A. Molecular pathophysiological mechanisms of ischemia/reperfusion injuries after recanalization therapy for acute ischemic stroke J. Integr. Neurosci. 2021 20 727 744 34645107
- [58]Palikaras K. Tavernarakis N. Mitochondrial homeostasis: The interplay between mitophagy and mitochondrial biogenesis Exp. Gerontol. 2014 56 182 188 10.1016/j.exger.2014.01.021 24486129 · DOI
- [59]Huang J.B. Hsu S.P. Pan H.Y. Chen S.D. Chen S.F. Lin T.K. Liu X.P. Li J.H. Chen N.C. Liou C.W. Peroxisome proliferator-activated receptor gamma coactivator 1 alpha activates vascular endothelial growth factor that protects against neuronal cell death following status epilepticus through PI3K/AKT and MEK/ERK signaling Int. J. Mol. Sci. 2020 21 7247 10.3390/ijms21197247 33008083 PMC7583914 · DOI
- [60]Tilokani L. Nagashima S. Paupe V. Minczuk M. Mitochondrial dynamics: Overview of molecular mechanisms Essays Biochem. 2018 62 341 360 30030364 PMC6056715
- [61]Losón O.C. Song Z. Chen H. Chan D.C. Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial fission Mol. Biol. Cell 2013 24 659 667 10.1091/mbc.e12-10-0721 23283981 PMC3583668 · DOI · Paper page
- [62]Swerdlow N.S. Wilkins H.M. Mitophagy and the brain Int. J. Mol. Sci. 2020 21 9661 10.3390/ijms21249661 33352896 PMC7765816 · DOI
- [63]Qin W. Haroutunian V. Katsel P. Cardozo C.P. Ho L. Buxbaum J.D. Pasinetti G.M. PGC-1alpha expression decreases in the Alzheimer disease brain as a function of dementia Arch. Neurol. 2009 66 352 361 10.1001/archneurol.2008.588 19273754 PMC3052997 · DOI
- [64]Sajan M. Hansen B. Ivey R. 3rd Sajan J. Ari C. Song S. Braun U. Leitges M. Farese-Higgs M. Farese R.V. Brain insulin signaling is increased in insulin-resistant states and decreases in FOXOs and PGC-1α and increases in Aβ1-40/42 and phospho-tau may abet Alzheimer development Diabetes 2016 65 1892 1903 10.2337/db15-1428 26895791 PMC4915579 · DOI
- [65]Wiedemann N. Pfanner N. Mitochondrial machineries for protein import and assembly Annu. Rev. Biochem. 2017 86 685 714 10.1146/annurev-biochem-060815-014352 28301740 · DOI
- [66]Chai Y.L. Xing H. Chong J.R. Francis P.T. Ballard C.G. Chen C.P. Lai M.K.P. Mitochondrial translocase of the outer membrane alterations may underlie dysfunctional oxidative phosphorylation in Alzheimer’s disease J. Alzheimers Dis. 2018 61 793 801 10.3233/JAD-170613 29254089 · DOI
- [67]Wright G. Terada K. Yano M. Sergeev I. Mori M. Oxidative stress inhibits the mitochondrial import of preproteins and leads to their degradation Exp. Cell. Res. 2001 263 107 117 10.1006/excr.2000.5096 11161710 · DOI
- [69]Zhang L. Trushin S. Christensen T.A. Bachmeier B.V. Gateno B. Schroeder A. Yao J. Itoh K. Sesaki H. Poon W.W. Altered brain energetics induces mitochondrial fission arrest in Alzheimer’s Disease Sci. Rep. 2016 6 18725 10.1038/srep18725 26729583 PMC4700525 · DOI
- [70]Manczak M. Calkins M.J. Reddy P.H. Impaired mitochondrial dynamics and abnormal interaction of amyloid beta with mitochondrial protein Drp1 in neurons from patients with Alzheimer’s disease: Implications for neuronal damage Hum. Mol. Genet. 2011 20 2495 2509 10.1093/hmg/ddr139 21459773 PMC3109997 · DOI
- [71]Jiang S. Shao C. Tang F. Wang W. Zhu X. Dynamin-like protein 1 cleavage by calpain in Alzheimer’s disease Aging Cell 2019 18 e12912 10.1111/acel.12912 30767411 PMC6516178 · DOI
- [72]Cho D.H. Nakamura T. Fang J. Cieplak P. Godzik A. Gu Z. Lipton S.A. S-nitrosylation of Drp1 mediates beta-amyloid-related mitochondrial fission and neuronal injury Science 2009 324 102 105 10.1126/science.1171091 19342591 PMC2823371 · DOI · Paper page
- [73]Manczak M. Reddy P.H. Abnormal interaction between the mitochondrial fission protein Drp1 and hyperphosphorylated tau in Alzheimer’s disease neurons: Implications for mitochondrial dysfunction and neuronal damage Hum. Mol. Genet. 2012 21 2538 2547 10.1093/hmg/dds072 22367970 PMC3349426 · DOI
- [74]Kim D.I. Lee K.H. Gabr A.A. Choi G.E. Kim J.S. Ko S.H. Han H.J. Abeta-induced Drp1 phosphorylation through Akt activation promotes excessive mitochondrial fission leading to neuronal apoptosis Biochim. Biophys. Acta 2016 1863 2820 2834 10.1016/j.bbamcr.2016.09.003 27599716 · DOI
- [75]Kim B. Park J. Chang K.T. Lee D.S. Peroxiredoxin 5 prevents amyloid-beta oligomer-induced neuronal cell death by inhibiting ERK-Drp1-mediated mitochondrial fragmentation Free Radic. Biol. Med. 2016 90 184 194 10.1016/j.freeradbiomed.2015.11.015 26582373 · DOI
- [76]Ishihara N. Fujita Y. Oka T. Mihara K. Regulation of mitochondrial morphology through proteolytic cleavage of OPA1 EMBO J. 2006 25 2966 2977 10.1038/sj.emboj.7601184 16778770 PMC1500981 · DOI · Paper page
- [77]Kandimalla R. Manczak M. Yin X. Wang R. Reddy P.H. Hippocampal phosphorylated tau induced cognitive decline, dendritic spine loss and mitochondrial abnormalities in a mouse model of Alzheimer’s disease Hum. Mol. Genet. 2018 27 30 40 10.1093/hmg/ddx381 29040533 PMC5886218 · DOI
- [78]Jara C. Aránguiz A. Cerpa W. Tapia-Rojas C. Quintanilla R.A. Genetic ablation of tau improves mitochondrial function and cognitive abilities in the hippocampus Redox Biol. 2018 18 279 294 10.1016/j.redox.2018.07.010 30077079 PMC6072970 · DOI
- [79]Rogov V.V. Suzuki H. Marinkovic M. Lang V. Kato R. Kawasaki M. Buljubasic M. Sprung M. Rogova N. Wakatsuki S. Phosphorylation of the mitochondrial autophagy receptor Nix enhances its interaction with LC3 proteins Sci. Rep. 2017 7 1131 10.1038/s41598-017-01258-6 28442745 PMC5430633 · DOI
- [80]Hayakawa K. Esposito E. Wang X. Terasaki Y. Liu Y. Xing C. Ji X. Lo E.H. Transfer of mitochondria from astrocytes to neurons after stroke Nature 2016 535 551 555 10.1038/nature18928 27466127 PMC4968589 · DOI · Paper page
- [81]Wang W. Yin J. Ma X. Zhao F. Siedlak S.L. Wang Z. Torres S. Fujioka H. Xu Y. Perry G. Inhibition of mitochondrial fragmentation protects against Alzheimer’s disease in rodent model Hum. Mol. Genet. 2017 26 4118 4131 10.1093/hmg/ddx299 28973308 PMC5886251 · DOI · Paper page
- [82]Fang E.F. Hou Y. Palikaras K. Adriaanse B.A. Kerr J.S. Yang B. Lautrup S. Hasan-Olive M.M. Caponio D. Dan X. Mitophagy inhibits amyloid-β and tau pathology and reverses cognitive deficits in models of Alzheimer’s disease Nat. Neurosci. 2019 22 401 412 10.1038/s41593-018-0332-9 30742114 PMC6693625 · DOI · Paper page
- [83]Hu Y. Li X.C. Wang Z.H. Luo Y. Zhang X. Liu X.P. Feng Q. Wang Q. Yue Z. Chen Z. Tau accumulation impairs mitophagy via increasing mitochondrial membrane potential and reducing mitochondrial Parkin Oncotarget 2016 7 17356 17368 10.18632/oncotarget.7861 26943044 PMC4951217 · DOI
- [84]Szabo L. Eckert A. Grimm A. Insights into Disease-Associated Tau Impact on Mitochondria Int. J. Mol. Sci. 2020 21 6344 10.3390/ijms21176344 32882957 PMC7503371 · DOI
- [85]Cai Q. Tammineni P. Alterations in mitochondrial quality control in Alzheimer’s disease Front. Cell. Neurosci. 2016 10 24 10.3389/fncel.2016.00024 26903809 PMC4746252 · DOI
- [86]Miller K.E. Sheetz M.P. Axonal mitochondrial transport and potential are correlated J. Cell Sci. 2004 117 2791 2804 10.1242/jcs.01130 15150321 · DOI
- [87]Zheng Y.-R. Zhang X.-N. Chen Z. Mitochondrial transport serves as a mitochondrial quality control strategy in axons: Implications for central nervous system disorders CNS Neurosci. Ther. 2019 25 876 886 10.1111/cns.13122 PMC6566064 30900394 · DOI
- [88]Jurcau A. Molecular pathophysiological mechanisms in Huntington’s disease Biomedicines 2022 10 1432 10.3390/biomedicines10061432 35740453 PMC9219859 · DOI
- [89]Shaw J.L. Chang K.T. Nebula/DSCR1 upregulation delays neurodegeneration and protects against APP-induced axonal transport defects by restoring calcineurin and GSK-3beta signaling PLoS Genet. 2013 9 e1003792 10.1371/journal.pgen.1003792 24086147 PMC3784514 · DOI
- [90]Pickett E.K. Rose J. McCrory C. McKenzie C.A. King D. Smith C. Gillingwater T.H. Henstridge C.M. Spires-Jones T.L. Region-specific depletion of synaptic mitochondria in the brains of patients with Alzheimer’s disease Acta Neuropathol. 2018 136 747 757 10.1007/s00401-018-1903-2 30191401 PMC6208730 · DOI
- [91]Pigino G. Morfini G. Pelsman A. Mattson M.P. Brady S.T. Busciglio J. Alzheimer’s presenilin 1 mutations impair kinesin-based axonal transport J. Neurosci. 2003 23 4499 4508 10.1523/JNEUROSCI.23-11-04499.2003 12805290 PMC6740780 · DOI
- [92]Wang Q. Tian J. Chen H. Du H. Guo L. Amyloid beta-mediated KIF5A deficiency disrupts anterograde axonal mitochondrial movement Neurobiol. Dis. 2019 127 410 418 10.1016/j.nbd.2019.03.021 30923004 · DOI
- [93]Tammineni P. Ye X. Feng T. Aikal D. Cai Q. Impaired retrograde transport of axonal autophagosomes contributes to autophagic stress in Alzheimer’s disease neurons Elife 2017 6 e21776 10.7554/eLife.21776 28085665 PMC5235353 · DOI
- [94]Ebneth A. Godemann R. Stamer K. Illenberger S. Trinczek B. Mandelkow E. Overexpression of tau protein inhibits kinesin-dependent trafficking of vesicles, mitochondria, and endoplasmic reticulum: Implications for Alzheimer’s disease J. Cell Biol. 1998 143 777 794 10.1083/jcb.143.3.777 9813097 PMC2148132 · DOI · Paper page
- [95]Ittner L.M. Ke Y.D. Götz J. Phosphorylated tau interacts with c-Jun N-terminal kinase-interacting protein 1 (JIP1) in Alzheimer disease J. Biol. Chem. 2009 284 20909 20916 10.1074/jbc.M109.014472 19491104 PMC2742856 · DOI
- [96]Mammucari C. Raffaello A. Reane D.V. Gherardi G. De Mario A. Rizzuto R. Mitochondrial calcium uptake in organ physiology: From molecular mechanism to animal models Eur. J. Physiol. 2018 470 1165 1179 10.1007/s00424-018-2123-2 29541860 PMC6060757 · DOI
- [97]Briston T. Selwood D. Szabadkai G. Duchen M.R. Mitochondrial permeability transition: A molecular lesion with multiple drug targets Trends Pharm. Sci. 2019 40 50 70 10.1016/j.tips.2018.11.004 30527591 · DOI
- [98]Palty R. Silverman W.F. Hershfinkel M. Caporale T. Sensi S.L. Parnis J. Nolte C. Fishman D. Shoshan-Barmatz V. Herrmann S. NCLX is an essential component of mitochondrial Na+/Ca2+ exchange Proc. Natl. Acad. Sci. USA 2009 107 436 441 10.1073/pnas.0908099107 20018762 PMC2806722 · DOI
- [99]Paß T. Wiesner R.J. Pla-Martin D. Selective neuron vulnerability in common and rare diseases–mitochondria in the focus Front. Mol. Biosci. 2021 8 676187 10.3389/fmolb.2021.676187 34295920 PMC8290884 · DOI
- [100]Eysert F. Kinoshita P.F. Mary A. Vaillant-Beuchot L. Checler F. Chami M. Molecular dysfunctions of mitochondria-associated membranes (MAMs) in Alzheimer’s disease Int. J. Mol. Sci. 2020 21 9521 10.3390/ijms21249521 33327665 PMC7765134 · DOI
- [101]Szabadkai G. Bianchi K. Várnai P. De Stefani D. Wieckowski M.R. Cavagna D. Nagy A.I. Balla T. Rizzuto R. Chaperone-mediated coupling of endoplasmic reticulum and mitochondrial Ca2+ channels J. Cell Biol. 2006 175 901 911 10.1083/jcb.200608073 17178908 PMC2064700 · DOI · Paper page
- [102]Area-Gomez E. De Groof A.J.C. Boldogh I. Bird T.D. Gibson G.E. Koehler C.M. Yu W.H. Duff K.E. Yaffe M.P. Pon L.A. Presenilins are enriched in endoplasmic reticulum membranes associated with mitochondria Am. J. Pathol. 2009 175 1810 1816 10.2353/ajpath.2009.090219 19834068 PMC2774047 · DOI
- [103]Zampese E. Fasolato C. Kipanyula M.J. Bortolozzi M. Pozzan T. Pizzo P. Presenilin 2 modulates endoplasmic reticulum (ER)-mitochondria interactions and Ca2+ crosstalk Proc. Natl. Acad. Sci. USA 2011 108 2777 2782 10.1073/pnas.1100735108 21285369 PMC3041131 · DOI
- [104]Chan S.L. Mayne M. Holden C.P. Geiger J.D. Mattson M.P. Presenilin-1 mutations increase levels of ryanodine receptors and calcium release in PC12 cells and cortical neurons J. Biol. Chem. 2000 275 18195 18200 10.1074/jbc.M000040200 10764737 · DOI
- [105]Calvo-Rodriguez M. Hou S.S. Snyder A.C. Kharitonova E.K. Russ A.N. Das S. Fan Z. Muzikansky A. Garcia-Alloza M. Serrano-Pozo A. Increased mitochondrial calcium levels associated with neuronal death in a mouse model of Alzheimer’s disease Nat. Commun. 2020 11 2146 10.1038/s41467-020-16074-2 32358564 PMC7195480 · DOI
- [106]Area-Gomez E. Schon E.A. On the pathogenesis of Alzheimer’s disease: The MAM hypothesis FASEB J. 2017 31 864 867 10.1096/fj.201601309 28246299 PMC6191063 · DOI
- [107]Britti E. Ros J. Esteras N. Abramov A.Y. Tau inhibits mitochondrial calcium efflux and makes neurons vulnerable to calcium-induced cell death Cell. Calcium 2020 86 102150 10.1016/j.ceca.2019.102150 31918031 · DOI
- [108]Cao L.L. Guan P.P. Liang Y.Y. Huang X.S. Wang P. Calcium ions stimulate the hyperphosphorylation of tau by activating microsomal prostaglandin E synthase 1 Front. Aging Neurosci. 2019 11 108 10.3389/fnagi.2019.00108 31143112 PMC6521221 · DOI
- [110]Jung T. Grune T. The proteasome and the degradation of oxidized proteins: Part I-structure of proteasomes Redox Biol. 2013 1 178 182 10.1016/j.redox.2013.01.004 24024151 PMC3757679 · DOI
- [111]Stadtmueller B.M. Hill C.P. Proteasome activators Mol. Cell 2011 41 8 19 10.1016/j.molcel.2010.12.020 21211719 PMC3040445 · DOI
- [112]Villavicencio Tejo F. Quintanilla R.A. Contribution of the Nrf2 pathway on oxidative damage and mitochondrial failure in Parkinson and Alzheimer’s disease Antioxidants 2021 10 1069 10.3390/antiox10071069 34356302 PMC8301100 · DOI
- [113]Qu Z. Sun J. Zhang W. Yu J. Zhuang C. Transcription factor NRF2 as a promising therapeutic target for Alzheimer’s disease Free Radic. Biol. Med. 2020 159 87 102 10.1016/j.freeradbiomed.2020.06.028 32730855 · DOI
- [114]Grune T. Catalgol B. Licht A. Ermak G. Pickering A.M. Ngo J.K. Davies K.J. HSP70 mediates dissociation and reassociation of the 26S proteasome during adaptation to oxidative STRESS Free Radic. Biol. Med. 2011 51 1355 1364 10.1016/j.freeradbiomed.2011.06.015 21767633 PMC3172204 · DOI
- [115]Gomez-Fabra Gala M. Vögtle F.N. Mitochondrial proteases in human diseases FEBS Lett. 2021 595 1205 1222 10.1002/1873-3468.14039 33453058 · DOI
- [116]Voos W. Pollecker K. The mitochondrial Lon protease: Novel functions off the beaten track? Biomolecules 2020 10 253 10.3390/biom10020253 32046155 PMC7072132 · DOI
- [117]O’Brien R.J. Wong P.C. Amyloid precursor protein processing and Alzheimer’s disease Annu. Rev. Neurosci. 2011 34 185 204 10.1146/annurev-neuro-061010-113613 21456963 PMC3174086 · DOI · Paper page
- [118]Cao J. Zhong M.B. Toro C.A. Zhang L. Cai D. Endo-lysosomal pathway and ubiquitin-proteasome system dysfunction in Alzheimer’s disease pathogenesis Neurosci Lett. 2019 703 68 78 10.1016/j.neulet.2019.03.016 30890471 PMC6760990 · DOI
- [119]Reddy P.H. Beal M.F. Amyloid beta, mitochondrial dysfunction and synaptic damage: Implications for cognitive decline in aging and Alzheimer’s disease Trends Mol. Med. 2008 14 45 53 10.1016/j.molmed.2007.12.002 18218341 PMC3107703 · DOI · Paper page
- [120]Pandey A.K. Venkatesh S. Protein quality control at the interface of endoplasmic reticulum and mitochondria by Lon protease Br. J. Pharmacol. 2019 176 505 507 10.1111/bph.14543 30536926 PMC6329618 · DOI
- [121]Keck S. Nitsch R. Grune T. Ullrich O. Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimer’s disease J. Neurochem. 2003 85 115 122 10.1046/j.1471-4159.2003.01642.x 12641733 · DOI · Paper page
- [122]Gong B. Radulovic M. Figueiredo-Pereira M.E. Cardozo C. The ubiquitin-proteasome system: Potential therapeutic targets for Alzheimer’s disease and spinal cord injury Front. Mol. Neurosci. 2016 9 4 10.3389/fnmol.2016.00004 26858599 PMC4727241 · DOI
- [123]Vitolo O.V. Sant’Angelo A. Costanzo V. Battaglia F. Arancio O. Shelanski M. Amyloid beta -peptide inhibition of the PKA/CREB pathway and long-term potentiation: Reversibility by drugs that enhance cAMP signaling Proc. Natl. Acad. Sci. USA 2002 99 13217 13221 10.1073/pnas.172504199 12244210 PMC130613 · DOI · Paper page
- [124]Lloret A. Badia M.C. Giraldo E. Ermak G. Alonso M.D. Pallardo F.V. Davies K.J. Vina J. Amyloid-beta toxicity and tau hyperphosphorylation are linked via RCAN1 in Alzheimer’s disease J. Alzheimers Dis. 2011 27 701 709 10.3233/JAD-2011-110890 21876249 PMC3690537 · DOI
- [125]Creamer T.P. Calcineurin Cell Commun. Signal. 2020 18 137 10.1186/s12964-020-00636-4 32859215 PMC7456046 · DOI
- [126]Obakan Yerlikaya P. Arısan E.D. Coker Gurkan A. Okumus O.O. Yenigun T. Ozbey U. Kara M. Palavan Unsal N. Epibrassinolide prevents tau hyperphosphorylation via GSK3β inhibition in vitro and improves Caenorhabditis elegans lifespan and motor deficits in combination with roscovitine Amino Acids 2021 53 1373 1389 10.1007/s00726-021-03027-2 34386848 · DOI
- [127]Martínez-Cué C. Rueda N. Signalling pathways implicated in Alzheimer’s disease neurodegeneration in individuals with and without Down syndrome Int. J. Mol. Sci. 2020 21 6906 10.3390/ijms21186906 32962300 PMC7555886 · DOI
- [128]An F. Xuan X. Liu Z. Bian M. Shen Q. Quan Z. Zhang G. Wei C. Anti-inflammatory activity of 4-(4-(heptyloxy)phenyl)-2,4-dihydro-3H-1,2,4-triazol-3-one via repression of MAPK/NF-κB signaling pathways in β-amyloid-induced Alzheimer’s disease models Molecules 2022 27 5035 10.3390/molecules27155035 35956985 PMC9370156 · DOI
- [129]Lauretti E. Dincer O. Praticò D. Glycogen synthase kinase-3 signaling in Alzheimer’s disease Biochim. Biophys. Acta Mol. Cell. Res. 2020 1867 118664 10.1016/j.bbamcr.2020.118664 32006534 PMC7047718 · DOI
- [130]Meng G. Mei H. Transcriptional dysregulation study reveals a core network involving the progression of Alzheimer’s disease Front. Aging Neurosci. 2019 11 101 10.3389/fnagi.2019.00101 31133844 PMC6513962 · DOI
- [131]Zgorzynska E. Dziedzic B. Walczewska A. An overview of the Nrf2/ARE pathway and its role in neurodegenerative diseases Int. J. Mol. Sci. 2021 22 9592 10.3390/ijms22179592 34502501 PMC8431732 · DOI
- [132]Jurcau A. Ardelean A.I. Oxidative Stress in Ischemia/Reperfusion Injuries following Acute Ischemic Stroke Biomedicines 2022 10 574 10.3390/biomedicines10030574 35327376 PMC8945353 · DOI
- [133]Bloom D.A. Jaiswal A.K. Phosphorylation of Nrf2 at Ser40 by protein kinase C in response to antioxidants leads to the release of Nrf2 from INrf2, but is not required for Nrf2 stabilization/accumulation in the nucleus and transcriptional activation of antioxidant response element J. Biol. Chem. 2003 278 44675 44682 10.1074/jbc.M307633200 12947090 · DOI
- [134]Apopa P.L. He X. Ma Q. Phosphorylation of Nrf2 in the transcription activation domain by casein kinase 2 (CK2) is critical for the nuclear translocation and transcription activation function of Nrf2 in IMR-32 neuroblastoma cells J. Biochem. Mol. Toxicol. 2008 22 63 76 10.1002/jbt.20212 18273910 · DOI
- [135]Hannan M.A. Dash R. Sohag A.A.M. Haque M.N. Moon I.S. Neuroprotection against oxidative stress: Phytochemicals targeting TrkB signaling and the Nrf2-ARE antioxidant system Front. Mol. Neurosci. 2020 13 116 10.3389/fnmol.2020.00116 32714148 PMC7346762 · DOI
- [136]Bellezza I. Mierla A.L. Minelli A. Nrf2 and NF-κB and their concerted modulation in cancer pathogenesis and progression Cancers 2010 2 483 497 10.3390/cancers2020483 24281078 PMC3835087 · DOI
- [137]Bahn G. Park J.-S. Yun U.J. Lee Y.J. Choi Y. Park J.S. Baek S.H. Choi B.Y. Cho Y.S. Kim H.K. NRF2/ARE pathway negatively regulates BACE1 expression and ameliorates cognitive deficits in mouse Alzheimer’s models Proc. Natl. Acad. Sci. USA 2019 116 12516 12523 10.1073/pnas.1819541116 31164420 PMC6589670 · DOI · Paper page
- [138]Ramsey C.P. Glass C.A. Montgomery M.B. Lindl K.A. Ritson G.P. Chia L.A. Hamilton R.L. Chu C.T. Jordan-Sciutto K.L. Expression of nrf2 in neurodegenerative diseases J. Neuropathol. Exp. Neurol. 2007 66 75 85 10.1097/nen.0b013e31802d6da9 17204939 PMC2253896 · DOI · Paper page
- [139]Manczak M. Kandimalla R. Yin X. Reddy P.H. Hippocampal mutant APP and amyloid beta-induced cognitive decline, dendritic spine loss, defective autophagy, mitophagy and mitochondrial abnormalities in a mouse model of Alzheimer’s disease Hum. Mol. Genet. 2018 27 1332 1342 10.1093/hmg/ddy042 29408999 PMC6455948 · DOI
- [141]Numakawa T. Odaka H. Adachi N. Actions of brain-derived neurotrophin factor in the neurogenesis and neuronal function, and its involvement in the pathophysiology of brain diseases Int. J. Mol. Sci. 2018 19 3650 10.3390/ijms19113650 30463271 PMC6274766 · DOI
- [142]Qi G. Mi Y. Wang Y. Li R. Huang S. Li X. Liu X. Neuroprotective action of tea polyphenols on oxidative stress-induced apoptosis through the activation of the TrkB/CREB/BDNF pathway and Keap1/Nrf2 signaling pathway in SH-SY5Y cells and mice brain Food Funct. 2017 8 4421 4432 10.1039/C7FO00991G 29090295 · DOI
- [143]Du Y. Wu H.T. Qin X.Y. Cao C. Liu Y. Cao Z.Z. Cheng Y. Postmortem brain, cerebrospinal fluid, and blood neurotrophic factor levels in Alzheimer’s disease: A systematic review and meta-analysis J. Mol. Neurosci. 2018 65 289 300 10.1007/s12031-018-1100-8 29956088 · DOI
- [144]Numakawa T. Odaka H. Brain-derived neurotrophic factor signaling in the pathophysiology of Alzheimer’s disease: Beneficial effects of flavonoids for neuroprotection Int. J. Mol. Sci. 2021 22 5719 10.3390/ijms22115719 34071978 PMC8199014 · DOI
- [145]Rosa E. Mahendram S. Ke Y.D. Ittner L.M. Ginsberg S.D. Fahnestock M. Tau downregulates BDNF expression in animal and cellular models of Alzheimer’s disease Neurobiol. Aging 2016 48 135 142 10.1016/j.neurobiolaging.2016.08.020 27676333 PMC5159317 · DOI
- [146]Ortí-Casañ N. Wu Y. Naudé P.J.W. De Deyn P.P. Zuhorn I.S. Eisel U.L.M. Targeting TNFR2 as a novel therapeutic strategy for Alzheimer’s disease Front. Neurosci. 2019 13 49 10.3389/fnins.2019.00049 30778285 PMC6369349 · DOI
- [147]Cheng X. Yang L. He P. Li R. Shen Y. Differential activation of tumor necrosis factor receptors distinguishes between brains from Alzheimer’s disease and non-demented patients J. Alzheimers Dis. 2010 19 621 630 10.3233/JAD-2010-1253 20110607 PMC3746510 · DOI
- [148]Vezzani B. Carinci M. Patergnani S. Pasquin M.P. Guarino A. Aziz N. Pinton P. Simonato M. Giorgi C. The dichotomous role of inflammation in the CNS: A mitochondrial point of view Biomolecules 2020 10 1437 10.3390/biom10101437 33066071 PMC7600410 · DOI
- [149]Jurcau A. Simion A. Neuroinflammation in cerebral ischemia and ischemia/reperfusion injuries: From pathophysiology to therapeutic strategies Int. J. Mol. Sci. 2022 23 14 10.3390/ijms23010014 PMC8744548 35008440 · DOI
- [150]Sabatino J.J. Pröbstel A.-K. Zamvil S.S. B cells in autoimmune and neurodegenerative central nervous system diseases Nat. Rev. Neurosci. 2019 20 728 745 10.1038/s41583-019-0233-2 31712781 · DOI
- [151]Jonsson T. Stefansson H. Steinberg S. Jonsdottir I. Jonsson P.V. Snaedal J. Bjornsson S. Huttenlocher J. Levey A.I. Lah J.J. Variant of TREM2 associated with the risk of Alzheimer’s disease N. Engl. J. Med. 2013 368 107 116 10.1056/NEJMoa1211103 23150908 PMC3677583 · DOI · Paper page
- [153]Efthymiou A.G. Goate A.M. Late onset Alzheimer’s disease genetics implicate microglial pathways in disease risk Mol. Neurodegener. 2017 12 43 10.1186/s13024-017-0184-x 28549481 PMC5446752 · DOI · Paper page
- [156]Götzl J.K. Brendel M. Werner G. Parhizkar S. Sebastian Monasor L. Kleinberger G. Colombo A.V. Deussing M. Wagner M. Winkelmann J. Opposite microglial activation stages upon loss of PGRN or TREM2 result in reduced cerebral glucose metabolism EMBO Mol. Med. 2019 11 e9711 10.15252/emmm.201809711 31122931 PMC6554672 · DOI
- [157]Chitnis T. Weiner H.L. CNS inflammation and neurodegeneration J. Clin. Investig. 2017 127 3577 3587 10.1172/JCI90609 28872464 PMC5617655 · DOI
- [158]Behl T. Makkar R. Sehgal A. Singh S. Sharma N. Zengin G. Bungau S. Andronie-Cioara F.L. Munteanu M.A. Brisc M.C. Current trends in neurodegeneration: Cross talks between oxidative stress, cell death, and inflammation Int. J. Mol. Sci. 2021 22 7432 10.3390/ijms22147432 34299052 PMC8306752 · DOI
- [159]Voet S. Srinivasan S. Lamkanfi M. van Loo G. Inflammasomes in neuroinflammatory and neurodegenerative diseases EMBO Mol. Med. 2019 11 e10248 10.15252/emmm.201810248 31015277 PMC6554670 · DOI · Paper page
- [160]Grazioli S. Pugin J. Mitochondrial damage-associated molecular patterns: From inflammatory signaling to human diseases Front. Immunol. 2018 9 832 10.3389/fimmu.2018.00832 29780380 PMC5946030 · DOI
- [161]Shang G. Zhang C. Chen Z.J. Bai X.-C. Zhang X. Cryo-EM structures of STING reveal its mechanism of activation by cyclic GMP-AMP Nature 2019 567 389 393 10.1038/s41586-019-0998-5 30842659 PMC6859894 · DOI
- [162]Srinivasula S.M. Poyet J.-L. Razmara M. Datta P. Zhang Z. Alnemri E.S. The Pyrin-CARD protein ASC is an activating adaptor for caspase-1 J. Biol. Chem. 2002 277 21119 21122 10.1074/jbc.C200179200 11967258 · DOI · Paper page
- [163]Shi J. Zhao Y. Wang K. Shi X. Wang Y. Huang H. Zhuang Y. Cai T. Wang F. Shao F. Cleavage of GSDMD by inflammatory caspases determines pyroptotic cell death Nature 2015 526 660 665 10.1038/nature15514 26375003 · DOI · Paper page
- [164]Heneka M.T. McManus R.M. Latz E. Inflammasome signaling in brain function and neurodegenerative disease Nat. Rev. Neurosci. 2018 19 610 621 10.1038/s41583-018-0055-7 30206330 · DOI · Paper page
- [165]Lewcock J.W. Schlepckow K. Di Paolo G. Tahirovic S. Monroe K.M. Haass C. Emerging microglial biology defines novel therapeutic approaches for Alzheimer’s disease Neuron 2020 108 801 821 10.1016/j.neuron.2020.09.029 33096024 · DOI · Paper page
- [167]Venegas C. Kumar S. Franklin B.S. Dierkes T. Brinkschulte R. Tejera D. Vieira-Saecker A. Schwartz S. Santarelli F. Kummer M.P. Microglia-derived ASC specks cross-seed amyloid-β in Alzheimer’s disease Nature 2017 552 355 361 10.1038/nature25158 29293211 · DOI · Paper page
- [168]Kobylarek D. Iwanowski P. Lewandowska Z. Limphaibool N. Szafranek S. Labryczka A. Kozubski W. Advances in the potential biomarkers of epilepsy Front. Neurol. 2019 10 685 10.3389/fneur.2019.00685 31312171 PMC6614180 · DOI
- [169]González-Reyes R.E. Nava-Mesa M.O. Vargas-Sánchez K. Ariza-Salamanca D. Mora-Muñoz L. Involvement of astrocytes in Alzheimer’s disease from a neuroinflammatory and oxidative stress perspective Front. Mol. Neurosci. 2017 10 427 10.3389/fnmol.2017.00427 29311817 PMC5742194 · DOI
- [172]Toledo J.B. Arnold M. Kastenmüller G. Chang R. Baillie R.A. Han X. Thambisetty M. Tenenbaum J.D. Suhre K. Thompson J.W. Metabolic network failures in Alzheimer’s disease: A biochemical road map Alzheimers Dement. 2017 13 965 984 10.1016/j.jalz.2017.01.020 28341160 PMC5866045 · DOI
- [174]Benitez B.A. Jin S.C. Guerreiro R. Graham R. Lord J. Harold D. Sims R. Lambert J.-C. Gibbs J.R. Bras J. Missense variant in TREML2 protects against Alzheimer’s disease Neurobiol. Aging 2014 35 1510.e19 1510.e326 10.1016/j.neurobiolaging.2013.12.010 24439484 PMC3961557 · DOI
- [176]Colonna M. Wang Y. TREM2 variants: New keys to decipher Alzheimer disease pathogenesis Nat. Rev. Neurosci. 2016 17 201 207 10.1038/nrn.2016.7 26911435 · DOI · Paper page
- [179]Chakrabarty P. Li A. Ceballos-Diaz C. Eddy J.A. Funk C.C. Moore B. DiNunno N. Rosario A.M. Cruz P.E. Verbeeck C. IL-10 alters immunoproteostasis in APP mice, increasing plaque burden and worsening cognitive behavior Neuron 2015 85 519 533 10.1016/j.neuron.2014.11.020 25619653 PMC4320003 · DOI · Paper page
- [181]Yuan P. Condello C. Keene C.D. Wang Y. Bird T.D. Paul S.M. Luo W. Colonna M. Baddeley D. Grutzendler J. TREM2 haplodeficiency in mice and humans impairs the microglia barrier function leading to decreased amyloid compaction and severe axonal dystrophy Neuron 2016 90 724 739 10.1016/j.neuron.2016.05.003 27196974 PMC4898967 · DOI · Paper page
- [182]Lee C.Y.D. Daggett A. Gu X. Jiang L.-L. Langfelder P. Li X. Wang N. Zhao Y. Park C.S. Cooper Y. Elevated TREM2 gene dosage reprograms microglia responsivity and ameliorates pathological phenotypes in Alzheimer’s disease models Neuron 2018 97 1032 1048 10.1016/j.neuron.2018.02.002 29518357 PMC5927822 · DOI · Paper page
- [184]Fagan A.M. Xiong C. Jasielec M.S. Bateman R.J. Goate A.M. Benzinger T.L.S. Ghetti B. Martins R.N. Masters C.L. Mayeux R. Dominantly inherited Alzheimer Network. Longitudinal change in CSF biomarkers in autosomal-dominant Alzheimer’s disease Sci. Transl. Med. 2014 6 226ra30 10.1126/scitranslmed.3007901 24598588 PMC4038930 · DOI · Paper page
- [185]Suárez-Calvet M. Kleinberger G. Araque Caballero M.Á. Brendel M. Rominger A. Alcolea D. Fortea J. Lleó A. Blesa R. Gispert J.D. sTREM2 cerebrospinal fluid levels are a potential biomarker for microglia activity in early-stage Alzheimer’s disease and associate with neuronal injury markers EMBO Mol Med. 2016 8 466 476 10.15252/emmm.201506123 26941262 PMC5120370 · DOI · Paper page
- [186]Cummings J. Aisen P.S. DuBois B. Frölich L. Jack C.R. Jr. Jones R.W. Morris J.C. Raskin J. Dowsett S.A. Scheltens P. Drug development in Alzheimer’s disease: The path to 2025 Alzheimers Res. Ther. 2016 8 39 10.1186/s13195-016-0207-9 27646601 PMC5028936 · DOI · Paper page
- [188]Amigo I. Menezes-Filho S.L. Luevano-Martinez L.A. Chausse B. Kowaltowski A.J. Caloric restriction increases brain mitochondrial calcium retention capacity and protects against excitotxicity Aging Cell 2017 16 73 81 10.1111/acel.12527 27619151 PMC5242290 · DOI · Paper page
- [192]Kryscio R.J. Abner E.L. Caban-Holt A. Lovell M. Goodman P. Darke A.K. Yee M. Crowley J. Schmitt F.A. Association of antioxidant supplement use and dementia in the prevention of Alzheimer’s disease by vitamin E and selenium trial (PREADViSE) JAMA Neurol. 2017 74 567 573 10.1001/jamaneurol.2016.5778 28319243 PMC5506489 · DOI
- [193]Jurcau A. The role of natural antioxidants in the prevention of dementia—Where do we stand and future perspectives Nutrients 2021 13 282 10.3390/nu13020282 33498262 PMC7909256 · DOI
- [194]Zhu C.W. Grossman H. Neugroschl J. Parker S. Burden A. Luo X. Sano M. A randomized, double-blind, placebo-controlled trial of resveratrol with glucose and malate (RGM) to slow the progression of Alzheimer’s disease: A pilot study Alzheimers Dement. (N Y) 2018 4 609 616 10.1016/j.trci.2018.09.009 30480082 PMC6240843 · DOI
- [195]Moussa C. Hebron M. Huang X. Ahn J. Rissman R.A. Aisen P.S. Turner R.S. Resveratrol regulates neuro-inflammation and induces adaptive immunity in Alzheimer’s disease J. Neuroinflamm. 2017 14 1 10.1186/s12974-016-0779-0 28086917 PMC5234138 · DOI
- [196]Ringman J.M. Frautschy S.A. Teng E. Begum A.N. Bardens J. Beigi M. Gylys K.H. Badmaev V. Heath D.D. Apostolova L.G. Oral curcumin for Alzheimer’s disease: Tolerability and efficacy in a 24-week randomized, double blind, placebo-controlled study Alzheimers Res. Ther. 2012 4 43 10.1186/alzrt146 23107780 PMC3580400 · DOI
- [197]Steele H. Gomez-Duran A. Pyle A. Hopton S. Newman J. Stefanetti R.J. Charman S.J. Parikh J.D. He L. Viscomi C. Metabolic effects of bezafibrate in mitochondrial disease EMBO Mol. Med. 2020 12 e11589 10.15252/emmm.201911589 32107855 PMC7059007 · DOI
- [198]Ding X.W. Robinson M. Li R. Aldhowayan H. Geetha T. Babu J.R. Mitochondrial dysfunction and beneficial effects of mitochondria-targeted small peptide SS-31 in diabetes mellitus and Alzheimer’s disease Pharmacol. Res. 2021 171 105783 10.1016/j.phrs.2021.105783 34302976 · DOI
- [199]Manczak M. Kandimalla R. Yin X. Reddy P.H. Mitochondrial division inhibitor 1 reduces dynamin-related protein 1 and mitochondrial fission activity Hum. Mol. Genet. 2019 28 177 199 10.1093/hmg/ddy335 30239719 PMC6322070 · DOI
- [200]Bordt E.A. Clerc P. Roelofs B.A. Saladino A.J. Tretter L. Adam-Vizi V. Cherok E. Khalil A. Yadava N. Ge S.X. The putative Drp1 inhibitor mdivi-1 is a reversible mitochondrial complex I inhibitor that modulates reactive oxygen species Dev. Cell. 2017 40 583 594 10.1016/j.devcel.2017.02.020 28350990 PMC5398851 · DOI
- [201]Kalra J. Crosslink between mutations in mitochondrial genes and brain disorders: Implications for mitochondrial-targeted therapeutic interventions Neural Regen. Res. 2023 18 94 101 10.4103/1673-5374.343884 35799515 PMC9241418 · DOI
- [202]Qi X. Qvit N. Su Y.C. Mochly-Rosen D. A novel Drp1 inhibitor diminishes aberrant mitochondrial fission and neurotoxicity J. Cell Sci. 2013 126 789 802 10.1242/jcs.114439 23239023 PMC3619809 · DOI
- [203]Kuruva C.S. Manczak M. Yin X. Ogunmokun G. Reddy A.P. Reddy P.H. Aqua-soluble DDQ reduces the levels of Drp1 and Abeta and inhibits abnormal interactions between Abeta and Drp1 and protects Alzheimer’s disease neurons from Abeta-induced mitochondrial and synaptic toxicities Hum. Mol. Genet. 2017 26 3375 3395 10.1093/hmg/ddx226 28854701 PMC5886305 · DOI
- [204]Ferreira J.C.B. Campos J.C. Qvit N. Qi X. Bozi L.H.M. Bechara L.R.G. Lima V.M. Queliconi B.B. Disatnik M.H. Dourado P.M.M. A selective inhibitor of mitofusin 1-βIIPKC association improves heart failure outcome in rats Nat. Commun. 2019 10 329 10.1038/s41467-018-08276-6 30659190 PMC6338754 · DOI · Paper page
- [205]Szabo A. Sumegi K. Fekete K. Hocsak E. Debreceni B. Setalo G. Jr. Kovacs K. Deres L. Kengyel A. Kovacs D. Activation of mitochondrial fusion provides a new treatment for mitochondria-related diseases Biochem. Pharmacol. 2018 150 86 96 10.1016/j.bcp.2018.01.038 29378182 · DOI
- [206]Miret-Casals L. Sebastián D. Brea J. Rico-Leo E.M. Palacín M. Fernández-Salguero P.M. Loza M.I. Albericio F. Zorzano A. Identification of new activators of mitochondrial fusion reveals a link between mitochondrial morphology and pyrimidine metabolism Cell. Chem. Biol. 2018 25 268 278 10.1016/j.chembiol.2017.12.001 29290623 · DOI
- [207]Peng K. Yang L. Wang J. Ye F. Dan G. Zhao Y. Cai Y. Cui Z. Ao L. Liu J. The interaction of mitochondrial biogenesis and fission/fusion mediated by PGC-1α regulates rotenone-induced dopaminergic neurotoxicity Mol. Neurobiol. 2017 54 3783 3797 10.1007/s12035-016-9944-9 27271125 · DOI
- [208]Shah S.A. Khan M. Jo M.H. Jo M.G. Amin F.U. Kim M.O. Melatonin stimulates the SIRT1/Nrf2 signaling pathway counteracting lipopolysaccharide (LPS)-induced oxidative stress to rescue postnatal rat brain CNS Neurosci. Ther. 2017 23 33 44 10.1111/cns.12588 27421686 PMC6492734 · DOI
- [209]Nous A. Engelborghs S. Smolders I. Melatonin levels in the Alzheimer’s disease continuum: A systematic review Alzheimers Res. Ther. 2021 13 52 10.1186/s13195-021-00788-6 33622399 PMC7903801 · DOI
- [210]Kwon S.H. Ma S.X. Hwang J.Y. Lee S.Y. Jang C.G. Involvement of the Nrf2/HO-1 signaling pathway in sulfuretin-induced protection against amyloid beta25-35 neurotoxicity Neuroscience 2015 304 14 28 10.1016/j.neuroscience.2015.07.030 26192096 · DOI
- [211]Ali T. Kim T. Rehman S.U. Khan M.S. Amin F.U. Khan M. Ikram M. Kim M.O. Natural dietary supplementation of anthocyanins via PI3K/Akt/Nrf2/HO-1 pathways mitigate oxidative stress, neurodegeneration, and memory impairment in a mouse model of Alzheimer’s disease Mol. Neurobiol. 2018 55 6076 6093 10.1007/s12035-017-0798-6 29170981 · DOI
- [212]Suresh S. Begum R.F. Singh S.A. Chitra V. Anthocyanin as a therapeutic in Alzheimer’s disease: A systematic review of preclinical evidences Ageing Res. Rev. 2022 76 101595 10.1016/j.arr.2022.101595 35217244 · DOI
- [213]Hui Y. Chengyong T. Cheng L. Haixia H. Yuanda Z. Weihua Y. Resveratrol attenuates the cytotoxicity induced by amyloid-β1–42 in PC12 cells by upregulating heme oxygenase-1 via the PI3K/Akt/Nrf2 pathway Neurochem. Res. 2017 43 297 305 10.1007/s11064-017-2421-7 29090409 · DOI
- [214]Ege D. Action mechanisms of curcumin in Alzheimer’s disease and its brain targeted delivery Materials 2021 14 3332 10.3390/ma14123332 34208692 PMC8234049 · DOI
- [215]Rahman M.A. Rahman M.H. Biswas P. Hossain M.S. Islam R. Hannan M.A. Uddin M.J. Rhim H. Potential therapeutic role of phytochemicals to mitigate mitochondrial dysfunctions in Alzheimer’s disease Antioxidants 2021 10 23 10.3390/antiox10010023 33379372 PMC7823298 · DOI
- [216]Khan H. Ullah H. Aschner M. Cheang W.S. Akkol E.K. Neuroprotective effects of Quercetin in Alzheimer’s disease Biomolecules 2020 10 59 10.3390/biom10010059 31905923 PMC7023116 · DOI
- [217]Wang H. Xu Y.S. Wang M.L. Cheng C. Bian R. Yuan H. Wang Y. Guo T. Zhu L.L. Zhou H. Protective effect of naringin against the LPS-induced apoptosis of PC12cells: Implications for the treatment of neurodegenerative disorders Int. J. Mol. Sci. 2017 39 819 830 PMC5360435 28260042
- [218]Lee D.-S. Cha B.-Y. Woo J.-T. Kim Y.-C. Jang J.-H. Acerogenin A from Acer nikoense maxim prevents oxidative stress-induced neuronal cell death through Nrf2-mediated heme oxygenase-1 expression in mouse hippocampal HT22 cell line Molecules 2015 20 12545 12557 10.3390/molecules200712545 26184139 PMC6331826 · DOI
- [219]Lee H. Ko W. Chowdhury A. Li B. Kim S.C. Oh H. Kim Y.C. Woo E.R. Baek N.I. Lee D.S. Brassicaphenanthrene A from Brassica rapa protects HT22 neuronal cells through the regulation of Nrf2-mediated heme oxygenase-1 expression Mol. Med. Rep. 2020 21 493 500 10.3892/mmr.2019.10824 31746357 · DOI
- [220]Fakhri S. Pesce M. Patruno A. Moradi S.Z. Iranpanah A. Farzaei M.H. Sobarzo-Sanchez E. Attenuation of Nrf2/Keap1/ARE in Alzheimer’s disease by plant secondary metabolites: A mechanistic review Molecules 2020 25 4926 10.3390/molecules25214926 33114450 PMC7663041 · DOI
- [221]Wang J. Li L. Wang Z. Cui Y. Tan X. Yuan T. Liu Q. Liu Z. Liu X. Supplementation of lycopene attenuates lipopolysaccharide-induced amyloidogenesis and cognitive impairments via mediating neuroinflammation and oxidative stress J. Nutr. Biochem. 2018 56 16 25 10.1016/j.jnutbio.2018.01.009 29454265 · DOI
- [223]Camargo C.H.F. Justus F.F. Retzlaff G. Blood M.R.Y. Schafranski M.D. Action of anti-TNF-α drugs on the progression of Alzheimer’s disease: A case report Dement. Neuropsychol. 2015 9 196 200 10.1590/1980-57642015DN92000015 29213962 PMC5619359 · DOI
- [224]Tobinick E. Gross H. Weinberger A. Cohen H. TNF-alpha modulation for treatment of Alzheimer’s disease: A 6-month pilot study MedGenMed 2006 8 25 PMC1785182 16926764
- [225]Butchart J. Brook L. Hopkins V. Teeling J. Puntener U. Culliford D. Sharples R. Sharif S. McFarlane B. Raybould R. Etanercept in Alzheimer disease: A randomized, placebo-controlled, double-blind, phase 2 trial Neurology 2015 84 2161 2168 10.1212/WNL.0000000000001617 25934853 PMC4451045 · DOI
- [226]Barnum C.J. Chen X. Chung J. Chang J. Williams M. Grigoryan N. Tesi R.J. Tansey M.G. Peripheral administration of the selective inhibitor of soluble tumor necrosis factor (TNF) XPro®1595 attenuates nigral cell loss and glial activation in 6-OHDA hemiparkinsonian rats J. Park. Dis. 2014 4 349 360 10.3233/JPD-140410 25061061 PMC4154985 · DOI
- [227]MacPherson K.P. Sompol P. Kannarkat G.T. Chang J. Sniffen L. Wildner M.E. Norris C.M. Tansey M.G. Peripheral administration of the soluble TNF inhibitor XPro1595 modifies brain immune cell profiles, decreases beta-amyloid plaque load, and rescues impaired long-term potentiation in 5xFAD mice Neurobiol. Dis. 2017 102 81 95 10.1016/j.nbd.2017.02.010 28237313 PMC5464789 · DOI
- [228]Cavanagh C. Tse Y.C. Nguyen H.B. Krantic S. Breitner J.C. Quirion R. Wong T.P. Inhibiting tumor necrosis factor-α before amyloidosis prevents synaptic deficits in an Alzheimer’s disease model Neurobiol. Aging 2016 47 41 49 10.1016/j.neurobiolaging.2016.07.009 27552480 · DOI · Paper page
- [229]Dong Y. Fischer R. Naudé P.J. Maier O. Nyakas C. Duffey M. Van der Zee E.A. Dekens D. Douwenga W. Herrmann A. Essential protective role of tumor necrosis factor receptor 2 in neurodegeneration Proc. Natl. Acad. Sci. USA 2016 113 12304 12309 10.1073/pnas.1605195113 27791020 PMC5087045 · DOI
- [230]Fischer R. Maier O. Siegemund M. Wajant H. Scheurich P. Pfizenmaier K. A TNF receptor 2 selective agonist rescues human neurons from oxidative stress-induced cell death PLoS ONE 2011 6 e27621 10.1371/journal.pone.0027621 22110694 PMC3215731 · DOI
- [232]Tang Y. Yu P. Cheng L. Current progress in the derivation and therapeutic application of neural stem cells Cell Death Dis. 2017 8 e3108 10.1038/cddis.2017.504 29022921 PMC5682670 · DOI
- [234]Takahashi K. Yamanaka S. Induced pluripotent stem cells in medicine and biology Development 2013 140 2457 2461 10.1242/dev.092551 23715538 · DOI
200 of 227 shown
Cited by
Sorted by citations
Varicose projection astrocytes: Conserved reactive cells in brain pathology
Ciani, C., Pistorio, G., Giancola, S., Mearelli, M., Mongelli, F. E., Forouzeh, D., Campos Soares, L., Gonzalez Martin, M., Lichtenstein, M. E., Mio, L., et al. (2026) · Science Advances · doi:10.1126/sciadv.ady8204 · Cited by 4 · see citing works
- Authors
- Jurcău, M. C., Andronie-Cioara, F. L., Jurcău, A., Marcu, F., Ţiț, D. M., Pașcalău, N., & Nistor-Cseppentö, D. C.
- Affiliations
- University of Oradea (RO)
- Department of Psycho-Neuroscience and Rehabilitation, Faculty of Medicine and Pharmacy, University of Oradea, 410073 Oradea, Romania
- Department of Pharmacy, Faculty of Medicine and Pharmacy, University of Oradea, 410028 Oradea, Romania
- Corresponding author
- Jurcău, Maria Carolina
- ORCID
- Venue
- Antioxidants
- Publisher
- MDPI AG
- Published
- 2022-10-31
- Volume
- 11
- Issue
- 11
- Pages
- 2167
- ISSN
- 2076-3921 (ISSN-L)
- PMC
- PMC9686795
- OpenAlex
- W4308722220
- Cited by
- 226
- References
- 36
- Citations by year
- 2026: 103 · 2025: 76 · 2024: 28 · 2023: 18 · 2022: 1
- FWCI
- 4.23
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Antioxidants (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Keywords
- Alzheimer's disease, oxidative stress, mitochondrial dysfunction, neuroinflammation, mitochondrial bioenergetics, mitochondrial quality control, amyloid-beta, neurofibrillary tangles, therapeutic target, cell therapy, extracellular vesicles, microRNA delivery, mRNA delivery, nanotechnology, drug delivery, early diagnosis
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