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Autophagy in Alzheimer’s disease
Open accessAbstract
Autophagy is a vesicle and lysosome-mediated degradative pathway that is essential for protein homeostasis and cell health. In particular, compared to nonneuronal cells, neurons are dependent on high basal autophagy for survival. There is emerging agreement that defects in autophagy are likely to contribute to the neurodegenerative processes in numerous diseases, including Alzheimer’s disease (AD). Autophagy-lysosome defects occur early in the pathogenesis of AD and have been proposed to be a significant contributor to the disease process. Given the fact that autophagy deficits are likely major contributors to the etiology of AD, the focus of this review will be on recent studies that support a role for autophagy deficits in AD.
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“Impairment of protein degradation pathways, including autophagy (reviewed previously66–68), is found in a host of neurodegenerative diseases.”
From Tau-targeting therapies for Alzheimer disease (2018) · cites this paper as [67]
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Repertoires of Autophagy in the Pathogenesis of Ocular Diseases
Li, Y., Jiang, Q. L., Cao, G.-F., Yao, J., & Yan, B. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000373980 · Cited by 16,351
LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing.
Kabeya, Y., Mizushima, N., Ueno, T., Yamamoto, A., Kirisako, T., Noda, T., Kominami, E., Ohsumi, Y., & Yoshimori, T. (2000) · The EMBO Journal · doi:10.1093/emboj/19.21.5720 · Cited by 6,605
Cui, C., Cui, J., Jin, F., Cui, Y., Li, R., Jiang, X., Tian, Y., Wang, R. C., Jiang, P., & Gao, J. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000479571 · Cited by 5,214
Cillà, S. D., Farruggio, S., Vujosevic, S., Raina, G., Filippini, D. A., Gatti, V., Clemente, N., Mary, D., Vezzola, D., Casini, G., et al. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000479441 · Cited by 5,154
Pankiv, S., Clausen, T. H., Lamark, T., Brech, A., Bruun, J.-A., Outzen, H., Øvervatn, A., Bjørkøy, G., & Johansen, T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702824200 · Cited by 4,578
Querfurth, H. W., & LaFerla, F. M. (2010) · New England Journal of Medicine · doi:10.1056/nejmra0909142 · Cited by 4,569
Upstream and downstream of mTOR
Hay, N., & Sonenberg, N. (2004) · Genes & Development · doi:10.1101/gad.1212704 · Cited by 4,181
TFEB Links Autophagy to Lysosomal Biogenesis
Settembre, C., Di Malta, C., Polito, V. A., Arencibia, M. G., Vetrini, F., Erdin, S., Erdin, S. U., Huynh, T., Medina, D., Colella, P., et al. (2011) · Science · doi:10.1126/science.1204592 · Cited by 3,365
Bjørkøy, G., Lamark, T., Brech, A., Outzen, H., Perander, M., Øvervatn, A., Stenmark, H., & Johansen, T. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200507002 · Cited by 3,276
Kim, D., Sarbassov, D. D., Ali, S. M., King, J. E., Latek, R. R., Erdjument‐Bromage, H., Tempst, P., & Sabatini, D. M. (2002) · Cell · doi:10.1016/s0092-8674(02)00808-5 · Cited by 3,051
Research works printed but not linked: 104
- Cai, 2013, Alzheimer disease, autophagy Biochem Pharmacol Res, 1
- Dou, 2013, Class PI β subunit promotes autophagy through in response to growth factor limitation, Small Mol Cell, 50, 110
- Bejarano, 2010, Chaperone mediated Thoracic, autophagy Proc Am Soc, 7
- Cai, 2013, Alzheimer disease, autophagy Biochem Pharmacol Res, 1
- Dou, 2013, Class PI β subunit promotes autophagy through in response to growth factor limitation, Small Mol Cell, 50, 110
- Pankiv, 2007, binds directly to to facilitate degradation of ubiquitinated protein aggregates by autophagy, Biol Chem, 1
- Kaushik, 2011, Chaperone - mediated autophagy at a glance, Cell Sci, 124
- Wischik, 2008, τ aggregation inhibitor therapy with rember arrests disease progression in mild and moderate Alzheimer s disease over weeks Alzheimer, Dementia, 04
- Keck, 2003, Proteasome inhibition by paired helical filament - τ in brains of patients with Alzheimer s disease, Neurochem, 85
- Caccamo, 2013, mTOR regulates τ phosphorylation and degradation : implications for Alzheimer s disease and other tauopathies, Aging Cell, 12, 370, 10.1111/acel.12057 · DOI · Paper page
- Fred Dice, 1990, Peptide sequences that target cytosolic proteins for lysosomal proteolysis Trends, Biochem Sci, 15, 305, 10.1016/0968-0004(90)90019-8 · DOI
- Petrucelli, 2004, CHIP regulate τ ubiquitination degradation aggregation, Hum Mol Genet, 13, 703, 10.1093/hmg/ddh083 · DOI · Paper page
- Wilson, 2004, Degradative organelles containing mislocalized α - and β - synuclein proliferate in presenilin null neurons, Cell Biol, 1
- Nishida, 2009, Discovery of independent alternative macroautophagy, Nature, 461
- Boland, 2008, induction and autophagosome clearance in neurons : relationship to autophagic pathology in Alzheimer s disease, Autophagy Neurosci, 28, 6926
- Tumbarello, 2012, receptors link myosin VI to autophagosomes to mediate Tom - dependent autophagosome maturation and fusion with the lysosome, Autophagy Nat Cell Biol, 14, 1
- Nishida, 2009, Discovery of independent alternative macroautophagy, Nature, 461
- Grotemeier, 2010, independent induction of autophagy by cytosolic Ca increase, Cell Signal, 22, 914, 10.1016/j.cellsig.2010.01.015 · DOI · Paper page
- Stefanis, 2012, α in s disease Cold a, Parkinson Perspect Med, 009399
- Zheng, 2011, Biology and pathophysiology of the amyloid precursor protein, Mol Neurodegener, 6, 1, 10.1186/1750-1326-6-27 · DOI
- Darlington, 2012, Multiple low - dose infusions of human umbilical cord blood cells improve cognitive impairments and reduce amyloid - β - associated neuropathology in Alzheimer mice, Stem Cells Dev, 22, 412, 10.1089/scd.2012.0345 · DOI
- Coffey, 2014, alkalization and dysfunction in human fibroblasts with the Alzheimer s disease - linked presenilin mutation can be reversed with cAMP, Neuroscience, 1
- Querfurth, 2010, Alzheimer disease, Engl J Med, 362
- Zhang, 2005, Microtubule - associated protein τ is a substrate of ATP - dependent proteasome protease system, Neural Transm, 112
- Felbor, 2002, Neuronal loss and brain atrophy in mice lacking cathepsins, Proc Natl Acad Sci USA, 99
- Wang, 2009, τ fragmentation aggregation clearance the dual role of lysosomal processing, Hum Mol Genet, 18, 4153, 10.1093/hmg/ddp367 · DOI · Paper page
- Kirkin, 2009, a role for in autophagosomal degradation of ubiquitinated substrates, Mol Cell, 1
- Hosokawa, 2009, Nutrient - dependent mTORC association with the ULK complex required for, autophagy Mol Biol Cell, 20, 1
- Kundu, 2011, ULK mammalian target of rapamycin mitochondria linking nutrient availability and Antioxidants Signal, autophagy, 14, 1
- Steele, 2013, improves cognition and arrests progression of neuropathology in an Alzheimer s mouse model, Mol Psychiatry, 18, 889, 10.1038/mp.2012.106 · DOI
- Jisun, 2012, mitochondria oxidative stress cross talk redox signalling, Autophagy Biochem J, 441
- Yu, 2004, Autophagic vacuoles are enriched in amyloid precursor protein - secretase activities : implications for β - amyloid peptide over - production and localization in Alzheimer s disease, Int J Biochem Cell Biol, 2531, 10.1016/j.biocel.2004.05.010 · DOI · Paper page
- Salminen, 2013, Impaired processing in Alzheimer s disease : the potential role of interactome, autophagy Prog Neurobiol, 1
- Son, 2012, induced formation of autophagosomes is mediated by RAGE signaling, Aging, 1006
- Yu, 2005, Macroautophagy a novel β - amyloid peptide - generating pathway activated in Alzheimer s disease, Cell Biol, 171
- Bejarano, 2010, Chaperone mediated Thoracic, autophagy Proc Am Soc, 7
- David, 2002, degradation of τ protein, J Neurochem, 176, 10.1046/j.1471-4159.2002.01137.x · DOI · Paper page
- Hosokawa, 2009, Nutrient - dependent mTORC association with the ULK complex required for, autophagy Mol Biol Cell, 20, 1
- Harrington, 2008, Methylthioninium chloride acts as a τ aggregation inhibitor in a cellular model and reverses τ pathology in transgenic mice models of Alzheimer s disease International Conference on Alzheimer s Disease Abstracts
- Wischik, 2008, τ aggregation inhibitor therapy with rember arrests disease progression in mild and moderate Alzheimer s disease over weeks Alzheimer, Dementia, 04
- Wang, 2008, Cadmium - induced autophagy and apoptosis are mediated by a calcium signaling pathway, Cell Mol Life Sci, 3640, 10.1007/s00018-008-8383-9 · DOI
- Necula, 2007, Der Veer Methylene blue inhibits amyloid Aβ oligomerization by promoting fibrillization, Biochemistry Moscow, 8850, 10.1021/bi700411k · DOI · Paper page
- Harrington, 2008, Methylthioninium chloride acts as a τ aggregation inhibitor in a cellular model and reverses τ pathology in transgenic mice models of Alzheimer s disease International Conference on Alzheimer s Disease Abstracts
- Martina, 2014, and The nutrient - responsive transcription factor promotes autophagy lysosomal biogenesis and clearance of cellular debris Signal ra, Sci
- Cataldo, 1996, Properties of the endosomal - lysosomal system in the human central nervous system : disturbances mark most neurons in populations at risk to degenerate in Alzheimer s disease, Neurosci, 16, 186, 10.1523/JNEUROSCI.16-01-00186.1996 · DOI
- Kodiha, 2011, AMP kinase the missing link between type diabetes and neurodegenerative diseases Trends, Mol Med, 17, 613
- Nixon, 2011, failure in Alzheimer s disease locating the primary defect, Autophagy Dis, 43, 38
- Johansen, 2011, Selective autophagy mediated by autophagic adapter proteins, Autophagy, 279, 10.4161/auto.7.3.14487 · DOI
- Chen, 2014, IV Modeling ALS with iPSCs reveals that mutant SOD misregulates neurofilament balance in motor neurons, Cell Stem Cell, 14, 1, 10.1016/j.stem.2014.02.004 · DOI · Paper page
- Li, 2012, lesser known self eating, Cell Mol Life Sci, 69
- Jinwal, 2009, rd Chemical manipulation of hsp activity regulates τ stability, Neurosci, 29, 12079, 10.1523/JNEUROSCI.3345-09.2009 · DOI
- Bjørkøy, 2005, forms protein aggregates degraded by autophagy and has a protective effect on huntingtin - induced cell death, Cell Biol, 1
- Scheff, 2006, Hippocampal synaptic loss in early Alzheimer s disease and mild cognitive impairment, Aging, 27, 1372
- Shimizu, 2010, takes an alternative pathway, Autophagy Autophagy, 290, 10.4161/auto.6.2.11127 · DOI
- Kim, 2002, mTOR interacts with raptor to form a nutrient - sensitive complex that signals to the cell growth machinery, Cell, 110
- Tung, 2012, a double - edged sword in Alzheimer s disease, Autophagy, 37
- Khan, 2010, Role of inositol trisphosphate receptors in autophagy in cells, Biol Chem, 285
- Zhu, 2013, Arctigenin effectively ameliorates memory impairment in Alzheimer s disease model mice targeting both β - amyloid production and clearance, Neurosci, 13138, 10.1523/JNEUROSCI.4790-12.2013 · DOI
- Hamano, 2008, Autophagic - lysosomal perturbation enhances τ aggregation in transfectants with induced wild - type τ expression, Eur J Neurosci, 27, 1119, 10.1111/j.1460-9568.2008.06084.x · DOI · Paper page
- Vingtdeux, 2010, AMP - activated protein kinase signaling activation by resveratrol modulates amyloid - β peptide metabolism, Biol Chem, 285
- Ichimura, 2010, Selective degradation of by, autophagy Immunopathol, 431
- Majeski, 2004, Mechanisms of chaperone mediated, autophagy Int J Biochem Cell Biol, 2435, 10.1016/j.biocel.2004.02.013 · DOI
- Rubinsztein, 2006, The roles of intracellular protein - degradation pathways in neurodegeneration, Nature, 443
- Krüger, 2012, Autophagic degradation of τ in primary neurons and its enhancement by trehalose, Aging, 2291
- Wan, 2014, The role of Wnt signaling in the development of Alzheimer s disease : a potential therapeutic target, Res Int
- Criollo, 2007, Regulation of autophagy by the inositol trisphosphate receptor, Cell Death Differ, 14, 1029, 10.1038/sj.cdd.4402099 · DOI
- Berger, 2006, Rapamycin alleviates toxicity of different aggregate - prone proteins, Hum Mol Genet, 15, 433, 10.1093/hmg/ddi458 · DOI · Paper page
- Dickey, 2007, The high - affinity CHIP complex recognizes and selectively degrades phosphorylated τ client proteins, Clin Invest, 117
- Hayashi, 2009, Alzheimer disease - associated peptide β inhibits vascular regeneration with induction of endothelial autophagy, amyloid Thromb Biol, 29, 1909, 10.1161/ATVBAHA.109.188516 · DOI
- Cai, 2012, Roles of AMP - activated protein kinase in Alzheimer s disease, Med, 14, 1
- Sarkar, 2007, a novel mTOR - independent autophagy enhancer accelerates the clearance of mutant huntingtin and α - synuclein, Biol Chem, 282
- Jo, 2014, reduces levels of phosphorylated τ protein by inducing autophagy adaptor protein, Nat Commun, 3496, 10.1038/ncomms4496 · DOI · Paper page
- Kaminskyy, 2012, Proteases in Proteins, autophagy Biochim Biophys Acta Proteomics, 44, 10.1016/j.bbapap.2011.05.013 · DOI
- Sweetlove, 2012, Phase III CONCERT trial of latrepirdine, Pharm Med, 26, 113, 10.1007/BF03256900 · DOI
- Leary, 2010, rd rd - mediated rescue of cognition in τ transgenic mice requires neuroprotection and reduced soluble τ burden, Mol Neurodegener, 5, 1, 10.1186/1750-1326-5-45 · DOI
- Neely, 2011, Presenilin is necessary for efficient proteolysis through the autophagy - lysosome system in a γ - secretase - independent manner, Neurosci, 31, 2781, 10.1523/JNEUROSCI.5156-10.2010 · DOI · Paper page
- Sancak, 2010, Bar - Rag complex targets mTORC to the lysosomal surface and is necessary for its activation by amino acids, Cell, 1
- Son, 2012, induced formation of autophagosomes is mediated by RAGE signaling, Aging, 1006
- Chauhan, 2013, is a master transcriptional repressor of, autophagy Mol Cell, 50, 16, 10.1016/j.molcel.2013.01.024 · DOI · Paper page
- Dobrowolski, 2012, Presenilin deficiency or lysosomal inhibition enhances Wnt signaling through relocalization of to the late - endosomal compartment, Cell Rep, 29, 1316, 10.1016/j.celrep.2012.09.026 · DOI
- Shin, 2014, Mesenchymal stem cells enhance autophagy and increase β - amyloid clearance in Alzheimer disease models, Autophagy, 10
- Caccamo, 2010, Molecular interplay between mammalian target of rapamycin mTOR β τ effects on cognitive impairments, amyloid Biol Chem, 285
- Yang, 2013, Human umbilical cord mesenchymal stem cell - derived neuron - like cells rescue memory deficits and reduce amyloid - β deposition in an AβPP transgenic mouse model, PS Cell Res Ther, 1
- Pankiv, 2007, binds directly to to facilitate degradation of ubiquitinated protein aggregates by autophagy, Biol Chem, 1
- Lee, 2010, proteolysis and autophagy require presenilin are disrupted by Alzheimer - related mutations, PS Cell, 1
- Esselens, 2004, mediates the turnover of telencephalin in hippocampal neurons via an autophagic degradative pathway, Cell Biol, 1
- Zhang, 2012, role for presenilins in autophagy revisited : normal acidification of lysosomes in cells lacking, Neurosci, 8633, 10.1523/JNEUROSCI.0556-12.2012 · DOI · Paper page
- Li, 2010, dysfunction in Alzheimer s disease, Autophagy Dis, 265
- Querfurth, 2010, Alzheimer disease, Engl J Med, 362
- Pickford, 2008, The autophagy - related protein shows reduced expression in early Alzheimer disease and regulates amyloid β accumulation in mice, Clin Invest, 1
- Medina, 2011, Methylene blue reduces Aβ levels and rescues early cognitive deficit by increasing proteasome activity, Brain Pathol, 21, 140, 10.1111/j.1750-3639.2010.00430.x · DOI
- Lee, 2013, τ degradation : the ubiquitin - proteasome system versus the autophagy - lysosome system, Prog Neurobiol, 105
- Zhang, 2011, Rapamycin treatment augments motor neuron degeneration in SOD mouse model of amyotrophic lateral sclerosis, Autophagy, 1
- Wischik, 1996, Selective inhibition of Alzheimer disease - like τ aggregation by phenothiazines, Proc Natl Acad Sci USA, 11213, 10.1073/pnas.93.20.11213 · DOI · Paper page
- Tung, 2014, regulates the expression of to govern - dependent τ degradation, Mol Neurobiol, 49, 1, 10.1007/s12035-013-8482-y · DOI
- Dolan, 2010, caspase cleaved form of τ is preferentially degraded through the autophagy pathway, Biol Chem, 285
- Cárdenas, 2012, Mitochondrial Ca signals in, autophagy Cell Calcium, 52, 44, 10.1016/j.ceca.2012.03.001 · DOI
- Dekosky, 1990, loss in frontal cortex biopsies in Alzheimer s disease : correlation with cognitive severity, Synapse Ann Neurol, 27, 457, 10.1002/ana.410270502 · DOI · Paper page
- Settembre, 2011, links autophagy to lysosomal biogenesis, Science, 332
- Cheung, 2011, Ip deregulation in neurodegenerative diseases recent advances and future perspectives, Autophagy Neurochem, 317, 10.1111/j.1471-4159.2011.07314.x · DOI
- Inomata, 2012, Into Regulation of Toll - like receptor signaling by mediated selective autophagy is normally inactivated by, Cell Mol Life Sci, 20, 69
- Chapman, 1999, Impaired synaptic plasticity and learning in aged amyloid precursor protein transgenic mice, Nat Neurosci, 271, 10.1038/6374 · DOI · Paper page
- Luo, 2007, Roles of heat - shock protein in maintaining and facilitating the neurodegenerative phenotype in tauopathies, Proc Natl Acad Sci USA, 9511, 10.1073/pnas.0701055104 · DOI
- Kirkin, 2009, role for ubiquitin in selective, autophagy Mol Cell, 259, 10.1016/j.molcel.2009.04.026 · DOI
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Komaroff, A. L., Pellett, P. E., & Jacobson, S. (2020) · Clinical Microbiology Reviews · doi:10.1128/cmr.00143-20 · Cited by 77
Sharma, B., Satija, G., Madan, A., Garg, M., Alam, M. M., Shaquiquzzaman, M., Khanna, S., Tiwari, P., Parvez, S., Iqubal, A., et al. (2022) · Inflammation · doi:10.1007/s10753-022-01730-0 · Cited by 77
D’Mello, S. R. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115911 · Cited by 80
Neurotransmission systems in Parkinson’s disease
Moghaddam, H. S., Zare-Shahabadi, A., Rahmani, F., & Rezaei, N. (2017) · Reviews in the Neurosciences · doi:10.1515/revneuro-2016-0068 · Cited by 78
Self-citationRegulation of autophagy by polyphenols: Paving the road for treatment of neurodegeneration
Nabavi, S. F., Sureda, A., Dehpour, A. R., Shirooie, S., Sanches-Silva, A. T., Devi, K. P., Ahmed, T., Ishaq, N., Hashim, R., Sobarzo‐Sánchez, E., et al. (2017) · Biotechnology Advances · doi:10.1016/j.biotechadv.2017.12.001 · Cited by 74
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Wang, L., Wang, J., Crețoiu, D., Li, G., & Xiao, J. (2019) · Journal of sport and health science/Journal of Sport and Health Science · doi:10.1016/j.jshs.2019.10.001 · Cited by 71
Rangan, P., Lobo, F., Parrella, E., Rochette, N. C., Morselli, M., Stephen, T., Cremonini, A. L., Tagliafico, L., Persia, A., Caffa, I., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111417 · Cited by 71
Castro‐Gonzalez, S., Shi, Y., Colomer-Lluch, M., Song, Y., Mowery, K., Almodóvar, S., Bansal, A., Kirchhoff, F., Sparrer, K. M. J., Liang, C., et al. (2020) · Autophagy · doi:10.1080/15548627.2020.1725401 · Cited by 67
Wang, N., Wang, H., Pan, Q., Kang, J., Liang, Z., & Zhang, R. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/7158444 · Cited by 68
Senescence: A DNA damage response and its role in aging and Neurodegenerative Diseases
Shreeya, T., Ansari, M. S., Kumar, P., Saifi, M., Shati, A. A., Alfaifi, M. Y., & Elbehairi, S. E. I. (2024) · Frontiers in Aging · doi:10.3389/fragi.2023.1292053 · Cited by 72
Brain high-throughput multi-omics data reveal molecular heterogeneity in Alzheimer’s disease
Eteleeb, A. M., Novotny, B. C., Tarraga, C. S., Sohn, C., Dhungel, E., Brase, L., Nallapu, A., Buss, J., Farias, F., Bergmann, K., et al. (2024) · PLOS Biology · doi:10.1371/journal.pbio.3002607 · Cited by 64
Hao, F., & Feng, Y. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.118624 · Cited by 64
Autophagy in neuroinflammatory diseases
Muller, S., Brun, S., René, F., Seze, J. D., Loeffler, J., & Jeltsch‐David, H. (2017) · Autoimmunity Reviews · doi:10.1016/j.autrev.2017.05.015 · Cited by 66
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Paduraru, E., Iacob, D. G., Rarinca, V., Rusu, A., Jijie, R., Ilie, O., Ciobica, A. S., Nicoară, M., & Doroftei, B. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23041992 · Cited by 65
Belgrad, J., Pace, R. D., & Fields, R. D. (2019) · Journal of Neuroscience · doi:10.1523/jneurosci.1066-19.2019 · Cited by 63
Zhang, Y., Li, H., Jin, S., Lu, Y., Peng, Y., Zhao, L., & Wang, X. (2022) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2022.174829 · Cited by 58
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Grasso, D., Renna, F. J., & Vaccaro, M. I. (2018) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2018.00146 · Cited by 62
Larramona-Arcas, R., González-Arias, C., Perea, G., Gutiérrez, A., Vitorica, J., García-Barrera, T., Gómez-Ariza, J. L., Pascua-Maestro, R., Ganfornina, M. D., Kara, E., et al. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00382-8 · Cited by 56
Sayed, N. S. E., & Ghoneum, M. H. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/4386562 · Cited by 55
Spencer, B. J., Desplats, P., Overk, C., Valera, E., Rissman, R. A., Wu, C., Mante, M., Adame, A., Florio, J. B., Rockenstein, E. M., et al. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.0775-16.2016 · Cited by 56
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Guo, J., Cheng, J., North, B. J., & Wei, W. (2017) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2017.07.001 · Cited by 55
Li, H., Zheng, T., Lian, F., Xu, T., Yin, W., & Jiang, Y. (2021) · Nutrition · doi:10.1016/j.nut.2021.111473 · Cited by 54
Dhage, P. A., Sharbidre, A. A., Dakua, S. P., & Balakrishnan, S. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111634 · Cited by 53
Long, Z., Chen, J., Zhao, Y., Zhou, W. H., Yao, Q., Wang, Y., & He, G. (2020) · Aging · doi:10.18632/aging.103305 · Cited by 55
Wang, X., Zhu, P., Xu, S., Liu, Y., Yang, J., Yu, S., Wei, H., Li, J., Zhang, Q., Hasegawa, T., et al. (2019) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2019.105561 · Cited by 50
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Inuzuka, H., Liu, J., Wei, W., & Rezaeian, A.-H. (2022) · Acta Materia Medica · doi:10.15212/amm-2021-0001 · Cited by 52
Demarco, R. S., Uyemura, B. S., & Jones, D. L. (2020) · Cell Reports · doi:10.1016/j.celrep.2019.12.086 · Cited by 47
Hashemi, M., Nadafzadeh, N., Imani, M. H., Rajabi, R., Ziaolhagh, S., Bayanzadeh, S. D., Norouzi, R., Rafiei, R., Koohpar, Z. K., Raei, B., et al. (2023) · Cell Communication and Signaling · doi:10.1186/s12964-023-01053-z · Cited by 52
De, R., Mazumder, S., & Bandyopadhyay, U. (2020) · Cell Biology and Toxicology · doi:10.1007/s10565-020-09561-1 · Cited by 47
Romeo, M. A., Montani, M. S. G., Gaeta, A., D’Orazi, G., Faggioni, A., & Cirone, M. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2019.165647 · Cited by 43
Zhu, J., Dou, S., Jiang, Y., Bai, B., Chen, J., Wang, C., & Cheng, B. (2019) · Life Sciences · doi:10.1016/j.lfs.2019.03.047 · Cited by 42
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Zhao, Y., Zhang, Y., Zhang, J., Zhang, X., & Yang, G. (2020) · Current Neuropharmacology · doi:10.2174/1570159x18666200114163636 · Cited by 40
Avgerinos, K. I., Mullins, R. J., Vreones, M. P., Mustapić, M., Chen, Q., Melvin, D. L., Kapogiannis, D., & Egan, J. M. (2022) · Cells · doi:10.3390/cells11213372 · Cited by 41
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Zhu, Z., Liu, Y., Li, X., Zhang, L., Liu, H., Cui, Y., Wang, Y., & Zhao, D. (2021) · Neuroscience Letters · doi:10.1016/j.neulet.2021.136300 · Cited by 37
Ntsapi, C., Lumkwana, D., Swart, C., du Toit, A., & Loos, B. (2017) · International review of cytology · doi:10.1016/bs.ircmb.2017.07.002 · Cited by 39
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Paquet, C., Nicoll, J. A. R., Love, S., Mouton‐Liger, F., Holmes, C., Hugon, J., & Boche, D. (2017) · Brain Pathology · doi:10.1111/bpa.12567 · Cited by 40
Prasanth, M. I., Malar, D. S., Tencomnao, T., & Brimson, J. M. (2021) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2021.1939681 · Cited by 40
Spleen tyrosine kinase (SYK) blocks autophagic Tau degradation in vitro and in vivo
Schweig, J. E., Yao, H., Coppola, K., Jin, C., Crawford, F., MULLAN, M. J., & Paris, D. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.008033 · Cited by 38
Zheng, X., Lv, Y.-D., Jin, F., Zhang, H., Wu, X., Zhu, J., & Ruan, Y. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.888784 · Cited by 36
Striking a NRF2: The Rusty and Rancid Vulnerabilities Toward Ferroptosis in Alzheimer's Disease
Lane, D. J. R., Alves, F. M., Ayton, S., & Bush, A. I. (2023) · Antioxidants and Redox Signaling · doi:10.1089/ars.2023.0318 · Cited by 36
HyMM: hybrid method for disease-gene prediction by integrating multiscale module structure
Xiang, J., Meng, X., Zhao, Y., Wu, F., & Li, M. (2022) · Briefings in Bioinformatics · doi:10.1093/bib/bbac072 · Cited by 34
Saito, Y., Kuse, Y., Inoue, Y., Nakamura, S., Hara, H., & Shimazawa, M. (2018) · Redox Biology · doi:10.1016/j.redox.2018.09.004 · Cited by 35
Bai, X., Wu, J., Zhang, M., Xu, Y., Duan, L., Yao, K., Zhang, J., Bo, J., Zhao, Y., Xu, G., et al. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.513605 · Cited by 33
Molecular Mechanisms of the Protective Effects of Olive Leaf Polyphenols against Alzheimer’s Disease
Romero‐Márquez, J. M., Forbes-Hernández, T. Y., Navarro‐Hortal, M. D., Quirantes‐Piné, R., Grosso, G., Giampieri, F., Lipari, V., Sánchez‐González, C., Battino, M. A., & Quiles, J. L. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24054353 · Cited by 39
A transition to degeneration triggered by oxidative stress in degenerative disorders
Stern, M., & McNew, J. A. (2020) · Molecular Psychiatry · doi:10.1038/s41380-020-00943-9 · Cited by 33
Abu‐Elfotuh, K., Tolba, A. M. A., Hussein, F. H., Hamdan, A. M., Rabeh, M. A., Alshahri, S. A., Ali, A. A., Mosaad, S. M., Mahmoud, N. A., Elsaied, M. Y., et al. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15082063 · Cited by 32
Arafa, E. A., Shurrab, N. T., & Buabeid, M. A. (2021) · Advances in Pharmacological and Pharmaceutical Sciences · doi:10.1155/2021/4709818 · Cited by 31
Wen, X., & Hu, J. (2024) · International Immunopharmacology · doi:10.1016/j.intimp.2024.112936 · Cited by 32
Based on molecular structures: Amyloid-β generation, clearance, toxicity and therapeutic strategies
Yang, H., Li, J., Li, X., Ma, L., Hou, M., Zhou, H., & Zhou, R. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.927530 · Cited by 33
Srivastava, A. K., Flint, N., Kreckel, H. D., Gryzik, M., Poli, M., Arosio, P., & Bou‐Abdallah, F. (2020) · Biochemistry · doi:10.1021/acs.biochem.0c00246 · Cited by 30
Drosophila as a model to explore secondary injury cascades after traumatic brain injury
Buhlman, L. M., Krishna, G., Jones, T. B., & Thomas, T. C. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.112079 · Cited by 29
Platelet biomarkers identifying mild cognitive impairment in type 2 diabetes patients
Yu, H., Liu, Y., He, T., Zhang, Y., He, J., Li, M., Jiang, B., Gao, Y., Chen, C., Ke, D., et al. (2021) · Aging Cell · doi:10.1111/acel.13469 · Cited by 28
TMEM175: A lysosomal ion channel associated with neurological diseases
Wu, L., Lin, Y., Song, J., Li, L., Rao, X., Wan, W., Wei, G., Hua, F., & Ying, J. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106244 · Cited by 31
Thomas, S. D., Abdalla, S., Eissa, N., Akour, A. A., Jha, N. K., Ojha, S. K., & Sadek, B. S. (2024) · Pharmaceuticals · doi:10.3390/ph17070831 · Cited by 33
Singh, K., Kaur, A., Goyal, B., & Goyal, D. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.4c00246 · Cited by 28
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Gao, J., Chen, X., Ma, T., He, B., Li, P., Zhao, Y., Ma, Y., Zhuang, J., & Yin, Y. (2020) · International Journal of Nanomedicine · doi:10.2147/ijn.s258311 · Cited by 28
Ryan, K. C., Ashkavand, Z., Sarasija, S., Laboy, J. T., Samarakoon, R., & Norman, K. R. (2021) · Aging Cell · doi:10.1111/acel.13472 · Cited by 27
Melman, A., & Bou‐Abdallah, F. (2020) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2020.129700 · Cited by 28
Culibrk, R. A., & Hahn, M. S. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.583884 · Cited by 28
Endosomal‐lysosomal dysfunctions in Alzheimer’s disease: Pathogenesis and therapeutic interventions
Lai, S. S. M., Ng, K. Y., Koh, R. Y., Chok, K. C., & Chye, S. M. (2021) · Metabolic Brain Disease · doi:10.1007/s11011-021-00737-0 · Cited by 31
Autophagic dysfunction of β cell dysfunction in type 2 diabetes, a double-edged sword
Ding, Y., GangYi, Y., & Qi-nan, W. (2020) · Genes & Diseases · doi:10.1016/j.gendis.2020.03.003 · Cited by 29
Metadata
- Authors
- Zare-shahabadi, A., Masliah, E., Johnson, G. V. W., & Rezaei, N.
- Affiliations
- Tehran University of Medical Sciences (IR)
- University of California San Diego (US)
- University of Rochester Medicine (US)
- Universal Scientific Education and Research Network (IR)
- Corresponding author
- Rezaei, Nima
- Venue
- Reviews in the Neurosciences
- Publisher
- Walter de Gruyter GmbH
- Published
- 2015-01-01
- Volume
- 26
- Issue
- 4
- Pages
- 385-95
- ISSN
- 0334-1763 (ISSN-L)
- 2191-0200
- PMC
- PMC5039008
- OpenAlex
- W1992935533
- Cited by
- 204
- References
- 119
- Citations by year
- 2026: 2 · 2025: 10 · 2024: 10 · 2023: 21 · 2022: 27 · 2021: 25 · 2020: 38 · 2019: 27 · 2018: 21 · 2017: 19 · 2016: 3 · 2015: 1
- FWCI
- 1.89
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Reviews in the Neurosciences (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute on Aging (R01AG018440)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- autophagy, Alzheimer's disease, autophagy-lysosome pathway, neurodegeneration, proteostasis, neuronal survival, lysosomal dysfunction
- MeSH terms
- Alzheimer Disease, Animals, Autophagy, Humans, Amyloid beta-Peptides, tau Proteins
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