Autophagy in Alzheimer’s disease

Zare-shahabadi, Ameneh; Masliah, Eliezer; Johnson, Gail V.W.; Rezaei, Nima

doi:10.1515/revneuro-2014-0076

Cited by 206Autophagy in Disease and TherapyAlzheimer's disease research and treatmentsNeuroinflammation and Neurodegeneration Mechanisms

Autophagy in Alzheimer’s disease

Open access

Zare-shahabadi, Ameneh, Masliah, Eliezer, Johnson, Gail V.W., Rezaei, Nima·2015·Reviews in the Neurosciences

DOI 10.1515/revneuro-2014-0076PMC PMC5039008

Open this paper in CoChat — free account

Abstract

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.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1515/revneuro-2014-0076

Cites

118 of 118 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Impairment of protein degradation pathways, including autophagy, is found in a host of neurodegenerative diseases.
“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]

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

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 · see citing works
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 · see citing works
Induction of the Vitamin D Receptor Attenuates Autophagy Dysfunction-Mediated Cell Death Following Traumatic Brain Injury
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 · see citing works
Anti-Vascular Endothelial Growth Factors Protect Retinal Pigment Epithelium Cells Against Oxidation by Modulating Nitric Oxide Release and Autophagy
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 · see citing works
p62/SQSTM1 Binds Directly to Atg8/LC3 to Facilitate Degradation of Ubiquitinated Protein Aggregates by Autophagy
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 · see citing works
Alzheimer’s disease
Querfurth, H. W., & LaFerla, F. M. (2010) · New England Journal of Medicine · doi:10.1056/nejmra0909142 · Cited by 4,569 · see citing works
Upstream and downstream of mTOR
Hay, N., & Sonenberg, N. (2004) · Genes & Development · doi:10.1101/gad.1212704 · Cited by 4,181 · see citing works
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 · see citing works
p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
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 · see citing works
mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery.
Kim, D.-H., Sarbassov, D., Ali, S. M., King, J. E., Latek, R., Erdjument-Bromage, H., Tempst, P., & Sabatini, D. (2002) · Cell · doi:10.1016/s0092-8674(02)00808-5 · Cited by 3,135 · see citing works
Ragulator-Rag Complex Targets mTORC1 to the Lysosomal Surface and Is Necessary for Its Activation by Amino Acids
Sancak, Y., Bar-Peled, L., Zoncu, R., Markhard, A. L., Nada, S., & Sabatini, D. M. (2010) · Cell · doi:10.1016/j.cell.2010.02.024 · Cited by 2,464 · see citing works
Synapse loss in frontal cortex biopsies in Alzheimer's disease: Correlation with cognitive severity
DeKosky, S. T., & Scheff, S. W. (1990) · Annals of Neurology · doi:10.1002/ana.410270502 · Cited by 2,376 · see citing works
Nutrient-dependent mTORC1 Association with the ULK1–Atg13–FIP200 Complex Required for Autophagy
Hosokawa, N., Hara, T., Kaizuka, T., Kishi, C., Takamura, A., Miura, Y., Iemura, S.-I., Natsume, T., Takehana, K., Yamada, N., et al. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-12-1248 · Cited by 2,076 · see citing works
Selective autophagy mediated by autophagic adapter proteins
Johansen, T., & Lamark, T. (2011) · Autophagy · doi:10.4161/auto.7.3.14487 · Cited by 1,730 · see citing works
The roles of intracellular protein-degradation pathways in neurodegeneration
Rubinsztein, D. C. (2006) · Nature · doi:10.1038/nature05291 · Cited by 1,625 · see citing works
-Synuclein in Parkinson's Disease
Stefanis, L. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a009399 · Cited by 1,446 · see citing works
Autophagy, mitochondria and oxidative stress: cross-talk and redox signalling.
Lee, J., Giordano, S., & Zhang, J. (2012) · Biochemical Journal · doi:10.1042/bj20111451 · Cited by 1,438 · see citing works
A Role for Ubiquitin in Selective Autophagy
Kirkin, V., McEwan, D. G., Novak, I., & Đikić, I. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.04.026 · Cited by 1,227 · see citing works
Lysosomal Proteolysis and Autophagy Require Presenilin 1 and Are Disrupted by Alzheimer-Related PS1 Mutations
Lee, J.-H., Yu, W. H., Kumar, A., Lee, S., Mohan, P. S., Peterhoff, C. M., Wolfe, D. M., Martinez-Vicente, M., Massey, A. C., Sovak, G., et al. (2010) · Cell · doi:10.1016/j.cell.2010.05.008 · Cited by 1,212 · see citing works
The autophagy-related protein beclin 1 shows reduced expression in early Alzheimer disease and regulates amyloid beta accumulation in mice.
Pickford, F., Masliah, E., Britschgi, M., Lucin, K. M., Narasimhan, R., Jaeger, P. A., Small, S., Spencer, B., Rockenstein, E., Levine, B., et al. (2008) · Journal of Clinical Investigation · doi:10.1172/jci33585 · Cited by 1,186 · see citing works
Self-citation
A Role for NBR1 in Autophagosomal Degradation of Ubiquitinated Substrates
Kirkin, V., Lamark, T., Sou, Y., Bjørkøy, G., Nunn, J. A. L., Bruun, J., Shvets, E., McEwan, D. G., Clausen, T. H., Wild, P. S., et al. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.01.020 · Cited by 1,156 · see citing works
Trehalose, a Novel mTOR-independent Autophagy Enhancer, Accelerates the Clearance of Mutant Huntingtin and α-Synuclein
Sarkar, S., Davies, J. E., Huang, Z., Tunnacliffe, A., & Rubinsztein, D. C. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609532200 · Cited by 1,142 · see citing works
Autophagy Induction and Autophagosome Clearance in Neurons: Relationship to Autophagic Pathology in Alzheimer's Disease
Boland, B., Kumar, A., Lee, S., Platt, F. M., Wegiel, J., Yu, W. H., & Nixon, R. A. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.0800-08.2008 · Cited by 1,119 · see citing works
Discovery of Atg5/Atg7-independent alternative macroautophagy
Nishida, Y., Arakawa, S., Fujitani, K., Yamaguchi, H., Mizuta, T., Kanaseki, T., Komatsu, M., Otsu, K., Tsujimoto, Y., & Shimizu, S. (2009) · Nature · doi:10.1038/nature08455 · Cited by 1,103 · see citing works
Inhibition of mTOR by Rapamycin Abolishes Cognitive Deficits and Reduces Amyloid-β Levels in a Mouse Model of Alzheimer's Disease
Spilman, P., Podlutskaya, N., Hart, M. J., Debnath, J., Gorostiza, O., Bredesen, D., Richardson, A., Strong, R., & Galvan, V. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009979 · Cited by 1,033 · see citing works
Hippocampal synaptic loss in early Alzheimer's disease and mild cognitive impairment
Scheff, S. W., Price, D. A., Schmitt, F. A., & Mufson, E. J. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.09.012 · Cited by 1,017 · see citing works
Macroautophagy—a novel β-amyloid peptide-generating pathway activated in Alzheimer's disease
Yu, W. H., Cuervo, A. M., Kumar, A., Peterhoff, C. M., Schmidt, S. D., Lee, J.-H., Mohan, P. S., Mercken, M., Farmery, M. R., Tjernberg, L. O., et al. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200505082 · Cited by 967 · see citing works
Impaired synaptic plasticity and learning in aged amyloid precursor protein transgenic mice
Chapman, P. F., White, G. L., Jones, M. W., Cooper-Blacketer, D., Marshall, V. J., Irizarry, M., Younkin, L., Good, M. A., Bliss, T. V. P., Hyman, B. T., et al. (1999) · Nature Neuroscience · doi:10.1038/6374 · Cited by 946 · see citing works
Molecular Interplay between Mammalian Target of Rapamycin (mTOR), Amyloid-β, and Tau
Caccamo, A., Majumder, S., Richardson, A., Strong, R., & Oddo, S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.100420 · Cited by 881 · see citing works
Microautophagy: lesser-known self-eating
Li, W., Li, J., & Bao, J. (2011) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0865-5 · Cited by 803 · see citing works
Peptide sequences that target cytosolic proteins for lysosomal proteolysis
Dice, J. F. (1990) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(90)90019-8 · Cited by 755 · see citing works
CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation
Petrucelli, L. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh083 · Cited by 735 · cited 1× · see citing works
“There are reports that have demonstrated UPS as a principal τ degradation system (David et al., 2002; Petrucelli et al., 2004; Zhang et al., 2005; Dickey et al., 2007).”
Genome-wide analysis reveals mechanisms modulating autophagy in normal brain aging and in Alzheimer’s disease
Lipinski, M. M., Zheng, B., Lu, T., Yan, Z., Py, B. F., Ng, A., Xavier, R. J., Li, C., Yankner, B. A., Scherzer, C. R., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1009485107 · Cited by 680 · see citing works
The Nutrient-Responsive Transcription Factor TFE3 Promotes Autophagy, Lysosomal Biogenesis, and Clearance of Cellular Debris
Martina, J. A., Diab, H. I., Lishu, L., Jeong-A, L., Patange, S., Raben, N., & Puertollano, R. (2014) · Science Signaling · doi:10.1126/scisignal.2004754 · Cited by 677 · see citing works
Rapamycin alleviates toxicity of different aggregate-prone proteins
Berger, Z., Ravikumar, B., Menzies, F. M., Oroz, L. G., Underwood, B. R., Pangalos, M. N., Schmitt, I., Wullner, U., Evert, B. O., O'Kane, C. J., et al. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddi458 · Cited by 657 · see citing works
AMP-activated Protein Kinase Signaling Activation by Resveratrol Modulates Amyloid-β Peptide Metabolism
Vingtdeux, V., Giliberto, L., Zhao, H., Chandakkar, P., Wu, Q., Simon, J. E., Janle, E. M., Lobo, J., Ferruzzi, M. G., Davies, P. J., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.060061 · Cited by 648 · see citing works
The high-affinity HSP90–CHIP complex recognizes and selectively degrades phosphorylated tau client proteins
Dickey, C. A., Kamal, A., Lundgren, K., Klosak, N., Bailey, R. M., Dunmore, J., Ash, P., Shoraka, S., Zlatkovic, J., Eckman, C. B., et al. (2007) · Journal of Clinical Investigation · doi:10.1172/jci29715 · Cited by 642 · see citing works
Autophagy Failure in Alzheimer's Disease – Locating the Primary Defect
Nixon, R., & Yang, D.-S. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.01.021 · Cited by 634 · see citing works
Tau fragmentation, aggregation and clearance: the dual role of lysosomal processing
Wang, Y., Martinez-Vicente, M., Krüger, U., Kaushik, S., Wong, E., Mandelkow, E.-M., Cuervo, A. M., & Mandelkow, E. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp367 · Cited by 617 · see citing works
Selective inhibition of Alzheimer disease-like tau aggregation by phenothiazines.
Wischik, C. M., Edwards, P. C., Lai, R. Y., Roth, M., & Harrington, C. R. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.20.11213 · Cited by 547 · see citing works
Autophagy as a Stress-Response and Quality-Control Mechanism: Implications for Cell Injury and Human Disease
Murrow, L. M., & Debnath, J. (2012) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathol-020712-163918 · Cited by 526 · see citing works
Proteasome inhibition by paired helical filament‐tau in brains of patients with Alzheimer's disease
Keck, S., Nitsch, R., Grune, T., & Ullrich, O. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01642.x · Cited by 483 · see citing works
Reversal of autophagy dysfunction in the TgCRND8 mouse model of Alzheimer’s disease ameliorates amyloid pathologies and memory deficits
Yang, D.-S., Stavrides, P., Mohan, P. S., Kaushik, S., Kumar, A., Ohno, M., Schmidt, S. D., Wesson, D., Bandyopadhyay, U., Jiang, Y., et al. (2011) · Brain · doi:10.1093/brain/awq341 · Cited by 429 · see citing works
Mechanisms of chaperone-mediated autophagy
Majeski, A. E., & Dice, J. F. (2004) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2004.02.013 · Cited by 411 · see citing works
Inducing Autophagy by Rapamycin Before, but Not After, the Formation of Plaques and Tangles Ameliorates Cognitive Deficits
Majumder, S., Richardson, A. G., Strong, R., & Oddo, S. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025416 · Cited by 401 · see citing works
Impaired autophagy and APP processing in Alzheimer's disease: The potential role of Beclin 1 interactome
Salminen, A., Kaarniranta, K., Kauppinen, A., Ojala, J. O., Haapasalo, A., Soininen, H. S., & Hiltunen, M. O. (2013) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2013.06.002 · Cited by 366 · see citing works
Rapamycin treatment augments motor neuron degeneration in SOD1<sup>G93A</sup>mouse model of amyotrophic lateral sclerosis
Zhang, X., Li, L., Chen, S., Yang, D., Wang, Y., Zhang, X., Wang, Z., & Le, W. (2011) · Autophagy · doi:10.4161/auto.7.4.14541 · Cited by 364 · see citing works
Tau degradation: The ubiquitin–proteasome system versus the autophagy-lysosome system
Lee, M. J., Lee, J. H., & Rubinsztein, D. C. (2013) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2013.03.001 · Cited by 364 · see citing works
<scp>mTOR</scp> regulates tau phosphorylation and degradation: implications for Alzheimer's disease and other tauopathies
Caccamo, A., Magrì, A., Medina, D. X., Wisely, E. V., López‐Aranda, M. F., Silva, A. J., & Oddo, S. (2013) · Aging Cell · doi:10.1111/acel.12057 · Cited by 362 · see citing works
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
Cataldo, A., Hamilton, D. J., Barnett, J. L., Paskevich, P. A., & Nixon, R. A. (1996) · Journal of Neuroscience · doi:10.1523/jneurosci.16-01-00186.1996 · Cited by 350 · see citing works
Autophagy failure in A lzheimer's disease and the role of defective lysosomal acidification
Wolfe, D. M., Lee, J., Kumar, A. R., Lee, S., Orenstein, S. J., & Nixon, R. A. (2013) · European Journal of Neuroscience · doi:10.1111/ejn.12169 · Cited by 348 · see citing works
Biology and pathophysiology of the amyloid precursor protein
Zheng, H., & Koo, E. H. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-27 · Cited by 346 · see citing works
Neuronal loss and brain atrophy in mice lacking cathepsins B and L
Felbor, U., Kessler, B., Mothes, W., Goebel, H. H., Ploegh, H. L., Bronson, R. T., & Olsen, B. R. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.112632299 · Cited by 334 · see citing works
Proteasomal degradation of tau protein
David, D. C., Layfield, R., Serpell, L., Narain, Y., Goedert, M., & Spillantini, M. G. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01137.x · Cited by 327 · see citing works
Nrf2 reduces levels of phosphorylated tau protein by inducing autophagy adaptor protein NDP52
Jo, C., Gundemir, S., Pritchard, S., Jin, Y. N., Rahman, I., & Johnson, G. V. W. (2014) · Nature Communications · doi:10.1038/ncomms4496 · Cited by 323 · see citing works
Self-citation
Modeling ALS with iPSCs reveals that mutant SOD1 misregulates neurofilament balance in motor neurons
Chen, H., Qian, K., Du, Z., Cao, J., Petersen, A., Liu, H., Blackbourn, L. W., Huang, C.-L., Errigo, A., Yin, Y., et al. (2014) · Cell stem cell · doi:10.1016/j.stem.2014.02.004 · Cited by 318 · see citing works
Regulation of autophagy by the inositol trisphosphate receptor
Criollo, A., Maiuri, M. C., Tasdemir, E., Vitale, I., Fiebig, A. A., Andrews, D. W., Molgó, J., Dı́az, J., Lavandero, S., Harper, F., et al. (2007) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402099 · Cited by 305 · see citing works
Autophagy receptors link myosin VI to autophagosomes to mediate Tom1-dependent autophagosome maturation and fusion with the lysosome
Tumbarello, D. A., Waxse, B. J., Arden, S. D., Bright, N. A., Kendrick-Jones, J., & Buss, F. (2012) · Nature Cell Biology · doi:10.1038/ncb2589 · Cited by 301 · see citing works
Autophagic degradation of tau in primary neurons and its enhancement by trehalose
Krüger, U., Wang, Y., Kumar, S., & Mandelkow, E.-M. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.11.009 · Cited by 297 · see citing works
Methylthioninium chloride (methylene blue) induces autophagy and attenuates tauopathy in vitro and in vivo
Congdon, E. E., Wu, J. W., Myeku, N., Figueroa, Y. H., Herman, M., Marinec, P. S., Gestwicki, J. E., Dickey, C. A., Yu, W. H., & Duff, K. E. (2012) · Autophagy · doi:10.4161/auto.19048 · Cited by 297 · see citing works
Autophagic-lysosomal perturbation enhances tau aggregation in transfectants with induced wild-type tau expression
Hamano, T., Gendron, T. F., Causevic, E., Yen, S., Lin, W., Isidoro, C., DeTure, M., & Ko, L. (2008) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2008.06084.x · Cited by 283 · see citing works
Autophagic vacuoles are enriched in amyloid precursor protein-secretase activities: implications for β-amyloid peptide over-production and localization in Alzheimer’s disease
Yu, W. H., Kumar, A., Peterhoff, C., Shapiro Kulnane, L., Uchiyama, Y., Lamb, B. T., Cuervo, A. M., & Nixon, R. A. (2004) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2004.05.010 · Cited by 279 · see citing works
ZKSCAN3 Is a Master Transcriptional Repressor of Autophagy
Chauhan, S., Jinesh, G. G., Chauhan, S. C., Manyam, G. C., Wang, J., Kamat, A. M., & Boyd, D. D. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.01.024 · Cited by 276 · see citing works
Roles of heat-shock protein 90 in maintaining and facilitating the neurodegenerative phenotype in tauopathies
Luo, W., Dou, F., Rodina, A., Chip, S., Kim, J., Zhao, Q., Moulick, K., Aguirre, J., Wu, N. F., Greengard, P., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701055104 · Cited by 274 · see citing works
Mesenchymal stem cells enhance autophagy and increase β-amyloid clearance in Alzheimer disease models
Shin, J. Y., Park, H. J., Kim, H. N., Oh, S. H., Bae, J.-S., Ha, H.-J., & Lee, P. H. (2014) · Autophagy · doi:10.4161/auto.26508 · Cited by 243 · see citing works
Selective degradation of p62 by autophagy
Ichimura, Y., & Komatsu, M. (2010) · Seminars in Immunopathology · doi:10.1007/s00281-010-0220-1 · Cited by 242 · see citing works
Chemical Manipulation of Hsp70 ATPase Activity Regulates Tau Stability
Jinwal, U. K., Miyata, Y., Koren, J., Jones, J. R., Trotter, J. H., Chang, L., O’Leary, J. C., Morgan, D., Lee, D. C., Shults, C. L., et al. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.3345-09.2009 · Cited by 231 · see citing works
Tau clearance mechanisms and their possible role in the pathogenesis of Alzheimer disease.
Chesser, A. S., Pritchard, S. M., & Johnson, G. V. W. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00122 · Cited by 219 · see citing works
Self-citation
Cadmium-induced autophagy and apoptosis are mediated by a calcium signaling pathway
Wang, S. H., Shih, Y. L., Ko, W. C., Wei, Y. H., & Shih, C. M. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8383-9 · Cited by 217 · see citing works
Methylene Blue Inhibits Amyloid Aβ Oligomerization by Promoting Fibrillization
Necula, M., Breydo, L., Milton, S., Kayed, R., van der Veer, W. E., Tone, P., & Glabe, C. G. (2007) · Biochemistry · doi:10.1021/bi700411k · Cited by 213 · see citing works
Chaperone-mediated autophagy at a glance
Kaushik, S., Bandyopadhyay, U., Sridhar, S., Kiffin, R., Martínez‐Vicente, M., Kon, M., Orenstein, S. J., Wong, E. S. P., & Cuervo, A. M. (2011) · Journal of Cell Science · doi:10.1242/jcs.073874 · Cited by 211 · see citing works
Arctigenin Effectively Ameliorates Memory Impairment in Alzheimer's Disease Model Mice Targeting Both -Amyloid Production and Clearance
Zhu, Z., Yan, J., Jiang, W., Yao, X., Chen, J., Chen, L., Li, C., Hu, L., Jiang, H., & Shen, X. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.4790-12.2013 · Cited by 207 · see citing works
Regulation of Amyloid Precursor Protein Processing by the Beclin 1 Complex
Jaeger, P. A., Pickford, F., Sun, C.-H. J., Lucin, K. M., Masliah, E., & Wyss‐Coray, T. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011102 · Cited by 204 · see citing works
Self-citation
Methylene Blue Reduces Aβ Levels and Rescues Early Cognitive Deficit by Increasing Proteasome Activity
Medina, D. X., Caccamo, A., & Oddo, S. (2010) · Brain Pathology · doi:10.1111/j.1750-3639.2010.00430.x · Cited by 194 · see citing works
Chaperone-Mediated Autophagy
Bejarano, E., & Cuervo, A. M. (2010) · Proceedings of the American Thoracic Society · doi:10.1513/pats.200909-102js · Cited by 193 · see citing works
Roles of AMP-activated Protein Kinase in Alzheimer’s Disease
Cai, Z., Yan, L., Li, K., Quazi, S. H., & Zhao, B. (2012) · NeuroMolecular Medicine · doi:10.1007/s12017-012-8173-2 · Cited by 191 · see citing works
Proteases in autophagy
Kaminskyy, V. O., & Zhivotovsky, B. (2011) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2011.05.013 · Cited by 188 · see citing works
Lysosomal alkalization and dysfunction in human fibroblasts with the Alzheimer’s disease-linked presenilin 1 A246E mutation can be reversed with cAMP
Coffey, E. E., Beckel, J. M., Laties, A. M., & Mitchell, C. H. (2014) · Neuroscience · doi:10.1016/j.neuroscience.2014.01.001 · Cited by 183 · see citing works
Phenothiazine-mediated rescue of cognition in tau transgenic mice requires neuroprotection and reduced soluble tau burden
O’Leary, J. C., Li, Q., Marinec, P. S., Blair, L. J., Congdon, E. E., Johnson, A. G., Jinwal, U. K., Koren, J., Jones, J. R., Kraft, C., et al. (2010) · Molecular Neurodegeneration · doi:10.1186/1750-1326-5-45 · Cited by 176 · see citing works
Presenilin 1 mediates the turnover of telencephalin in hippocampal neurons via an autophagic degradative pathway
Esselens, C. W., Oorschot, V. M. J., Baert, V., Raemaekers, T., Spittaels, K., Serneels, L., Zheng, H., Säftig, P., Strooper, B. D., Klumperman, J., et al. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200406060 · Cited by 170 · see citing works
Human umbilical cord mesenchymal stem cell-derived neuron-like cells rescue memory deficits and reduce amyloid-beta deposition in an AβPP/PS1 transgenic mouse model
Yang, H., Xie, Z., Wei, L. F., Yang, H. N., Yang, S. N., Zhu, Z., Wang, P., Zhao, C., & Bi, J. Z. (2013) · Stem Cell Research & Therapy · doi:10.1186/scrt227 · Cited by 166 · see citing works
AMPK-independent induction of autophagy by cytosolic Ca2+ increase
Grotemeier, A., Alers, S., Pfisterer, S. G., Paasch, F., Daubrawa, M., Dieterle, A. M., Viollet, B., Wesselborg, S., Proikas‐Cezanne, T., & Stork, B. (2010) · Cellular Signalling · doi:10.1016/j.cellsig.2010.01.015 · Cited by 153 · see citing works
A Caspase Cleaved Form of Tau Is Preferentially Degraded through the Autophagy Pathway
Dolan, P. J., & Johnson, G. V. W. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.110940 · Cited by 147 · see citing works
Self-citation
Presenilin Is Necessary for Efficient Proteolysis through the Autophagy–Lysosome System in a γ-Secretase-Independent Manner
Neely, K. M., Green, K. N., & LaFerla, F. M. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.5156-10.2010 · Cited by 141 · see citing works
Aβ-induced formation of autophagosomes is mediated by RAGE-CaMKKβ-AMPK signaling
Son, S. M., Jung, E. S., Shin, H. J., Byun, J., & Mook‐Jung, I. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.09.039 · Cited by 140 · see citing works
Localization of sequence variations in PGC-1α influence their modifying effect in Huntington disease
Hong Van, B., Metzger, S., Portal, E., Deyle, C., Rieß, O., & Nguyen, H. P. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-1 · Cited by 136 · see citing works
Class IA PI3K p110β Subunit Promotes Autophagy through Rab5 Small GTPase in Response to Growth Factor Limitation
Dou, Z., Pan, J.-A., Dbouk, H. A., Ballou, L. M., DeLeon, J. L., Fan, Y., Chen, J.-S., Liang, Z., Li, G., Backer, J., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.01.022 · Cited by 130 · see citing works
Autophagy deregulation in neurodegenerative diseases – recent advances and future perspectives
Cheung, Z. H., & Ip, N. Y. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07314.x · Cited by 126 · see citing works
A Role for Presenilins in Autophagy Revisited: Normal Acidification of Lysosomes in Cells Lacking PSEN1 and PSEN2
Zhang, X., Garbett, K., Veeraraghavalu, K., Wilburn, B., Gilmore, R., Mirnics, K., & Sisodia, S. S. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.0556-12.2012 · Cited by 122 · see citing works
O3‐04–07: Tau aggregation inhibitor (TAI) therapy with rember™ arrests disease progression in mild and moderate Alzheimer's disease over 50 weeks
Wischik, C. M., Bentham, P., Wischik, D., & Seng, K. M. (2008) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2008.05.438 · Cited by 118 · see citing works
mTOR-Controlled Autophagy Requires Intracellular Ca2+ Signaling
Decuypere, J.-P., Kindt, D., Luyten, T., Welkenhuyzen, K., Missiaen, L., SMEDT, H. D., Bultynck, G., & Parys, J. B. (2013) · PLoS ONE · doi:10.1371/journal.pone.0061020 · Cited by 115 · see citing works
Mitochondrial Ca2+ signals in autophagy
Cárdenas, C., & Foskett, J. (2012) · Cell Calcium · doi:10.1016/j.ceca.2012.03.001 · Cited by 114 · see citing works
Latrepirdine improves cognition and arrests progression of neuropathology in an Alzheimer's mouse model
Steele, J., Lachenmayer, M. L., Ju, S., Stock, A., Liken, J., Kim, S. H., Delgado, L. M., Alfaro, I. E., Bernales, S., Verdile, G., et al. (2012) · Molecular Psychiatry · doi:10.1038/mp.2012.106 · Cited by 113 · see citing works
Degradative organelles containing mislocalized α- and β-synuclein proliferate in presenilin-1 null neurons
Wilson, C., Murphy, D. D., Giasson, B. I., Zhang, B., Trojanowski, J. Q., & Lee, V. M. ‐. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200403061 · Cited by 106 · see citing works
Autophagy: A double-edged sword in Alzheimer’s disease
Tung, Y.-T., Wang, B., Hu, M., Hsu, W., Lee, H., Huang, W., & Liao, Y. (2012) · Journal of Biosciences · doi:10.1007/s12038-011-9176-0 · Cited by 104 · see citing works
Stimulation of autophagy is neuroprotective in a mouse model of human tauopathy
Schaeffer, V., & Goedert, M. (2012) · Autophagy · doi:10.4161/auto.21488 · Cited by 95 · see citing works
Role of Inositol Trisphosphate Receptors in Autophagy in DT40 Cells
Khan, M. T. M., & Joseph, S. K. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.114207 · Cited by 91 · see citing works
Rapamycin, Autophagy, and Alzheimer's Disease.
Cai, Z., & Yan, L. (2013) · PubMed · Cited by 91 · see citing works
Synergy and antagonism of macroautophagy and chaperone-mediated autophagy in a cell model of pathological tau aggregation
Wang, Y., Martinez-Vicente, M., Krüger, U., Kaushik, S., Wong, E., Mandelkow, E.-M., Cuervo, A. M., & Mandelkow, E. (2010) · Autophagy · doi:10.4161/auto.6.1.10815 · Cited by 90 · see citing works
Regulation of Toll-like receptor signaling by NDP52-mediated selective autophagy is normally inactivated by A20
Inomata, M., Niida, S., Shibata, K., & Into, T. (2011) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0819-y · Cited by 89 · see citing works
The Role of Wnt Signaling in the Development of Alzheimer’s Disease: A Potential Therapeutic Target?
Wan, W., Xia, S., Kalionis, B., Liu, L., & Li, Y. (2014) · BioMed Research International · doi:10.1155/2014/301575 · Cited by 86 · see citing works
Autophagy Dysfunction in Alzheimer’s Disease
Li, L., Zhang, X., & Le, W. (2010) · Neurodegenerative Diseases · doi:10.1159/000276710 · Cited by 81 · see citing works
Presenilin Deficiency or Lysosomal Inhibition Enhances Wnt Signaling through Relocalization of GSK3 to the Late-Endosomal Compartment
Dobrowolski, R., Vick, P., Ploper, D., Gumper, I., Snitkin, H., Sabatini, D. D., & Robertis, E. M. D. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.09.026 · Cited by 79 · see citing works
Alzheimer Disease–Associated Peptide, Amyloid β40, Inhibits Vascular Regeneration With Induction of Endothelial Autophagy
Hayashi, S.-I., Sato, N., Yamamoto, A., Ikegame, Y., Nakashima, S., Ogihara, T., & Morishita, R. (2009) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.109.188516 · Cited by 78 · see citing works
Microtubule-associated protein tau is a substrate of ATP/Mg2+-dependent proteasome protease system
Zhang, J. Y., Liu, S. J., Li, H., & Wang, J. (2004) · Journal of Neural Transmission · doi:10.1007/s00702-004-0196-x · Cited by 73 · see citing works
Extensive proteomic screening identifies the obesity-related NYGGF4 protein as a novel LRP1-interactor, showing reduced expression in early Alzheimer's disease
Kajiwara, Y., Franciosi, S., Takahashi, N., Krug, L., Schmeidler, J., Taddei, K., Haroutunian, V. H., Fried, U., Ehrlich, M. E., Martins, R. N., et al. (2010) · Molecular Neurodegeneration · doi:10.1186/1750-1326-5-1 · Cited by 73 · see citing works
ULK1, Mammalian Target of Rapamycin, and Mitochondria: Linking Nutrient Availability and Autophagy
Kundu, M. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3809 · Cited by 47 · see citing works
Multiple Low-Dose Infusions of Human Umbilical Cord Blood Cells Improve Cognitive Impairments and Reduce Amyloid-β-Associated Neuropathology in Alzheimer Mice
Darlington, D., Deng, J., Giunta, B. N., Hou, H., Sanberg, C. D., Kuzmin‐Nichols, N., Zhou, H., Mori, T., Ehrhart, J. C., Sanberg, P. R., et al. (2012) · Stem Cells and Development · doi:10.1089/scd.2012.0345 · Cited by 46 · see citing works
Autophagy takes an alternative pathway
Shimizu, S., Arakawa, S., & Nishida, Y. (2010) · Autophagy · doi:10.4161/auto.6.2.11127 · Cited by 32 · see citing works
Mitochondrial Complex Enzyme Activities and Cytochrome c Expression Changes in Multiple Sclerosis
Iñarrea, P., Alarcia, R., Álava, M. A., Capablo, J. L., Casanova, A., Íñiguez, C., Iturralde, M., Larrodé, P., Martín, J., Mostacero, E., et al. (2013) · Molecular Neurobiology · doi:10.1007/s12035-013-8481-z · Cited by 29 · see citing works
O1‐06–04: Methylthioninium chloride (MTC) acts as a Tau aggregation inhibitor (TAI) in a cellular model and reverses Tau pathology in transgenic mouse models of Alzheimer's disease
Harrington, C. R., Rickard, J. E., Horsley, D., Harrington, K. A., Hindley, K. P., Riedel, G., Theuring, F., Seng, K. M., & Wischik, C. M. (2008) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2008.05.259 · Cited by 21 · see citing works
New Modularity of DAP-Kinases: Alternative Splicing of the DRP-1 Gene Produces a ZIPk-Like Isoform
Shoval, Y., Berissi, H., Kimchi, A., & Pietrokovski, S. (2011) · PLoS ONE · doi:10.1371/journal.pone.0017344 · Cited by 19 · see citing works
PKD at the crossroads of necrosis and autophagy
Eisenberg‐Lerner, A., & Kimchi, A. (2012) · Autophagy · doi:10.4161/auto.19288 · Cited by 19 · see citing works
HSPCs Get Their Motors Running for Asymmetric Fate Choice
Zheng, Y., & Geiger, H. (2014) · Cell stem cell · doi:10.1016/j.stem.2013.12.002 · Cited by 18 · see citing works
Presenilin-1 Regulates the Expression of p62 to Govern p62-dependent Tau Degradation
Tung, Y.-T., Wang, B.-J., Hsu, W., Hu, M., Her, G. M., Huang, W., & Liao, Y. (2013) · Molecular Neurobiology · doi:10.1007/s12035-013-8482-y · Cited by 14 · see citing works
Phase III CONCERT Trial of Latrepirdine
Sweetlove, M. (2012) · Pharmaceutical Medicine · doi:10.1007/bf03256900 · Cited by 12 · see citing works
AMP kinase: the missing link between type 2 diabetes and neurodegenerative diseases?
Kodiha, M., & Stochaj, U. (2011) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2011.07.001 · Cited by 9 · see citing works
Ultrastrukturänderung leukämischer retikulärer Zellen nach Zusatz von RNS aus normaler Milz zum Kulturmedium
Esposito, S. (1964) · Cellular and Molecular Life Sciences · doi:10.1007/bf02151243 · Cited by 5 · see citing works

Flagged first, then by citations

1 of the 119 references couldn’t be matched to a known paper.

Sorted by citations

Tau-targeting therapies for Alzheimer disease
Congdon, E. E., & Sigurdsson, E. M. (2018) · Nature Reviews Neurology · doi:10.1038/s41582-018-0013-z · Cited by 1,113 · see citing works
Disorders of lysosomal acidification—The emerging role of v-ATPase in aging and neurodegenerative disease
Colacurcio, D. J., & Nixon, R. A. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.05.004 · Cited by 548 · see citing works
Ageing, Cellular Senescence and Neurodegenerative Disease
Kritsilis, M., V. Rizou, S., Koutsoudaki, P. N., Evangelou, K., Gorgoulis, V. G., & Papadopoulos, D. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19102937 · Cited by 448 · see citing works
“This is supported by a number of studies reporting dysregulation in many autophagic/lysosomal pathways in the context of AD [234,235], while the vast majority of AD-associated genes appears to be related to these same pathways [232].”
Background
Machine learning identifies candidates for drug repurposing in Alzheimer’s disease
Rodriguez, S., Hug, C., Todorov, P., Moret, N., Boswell, S. A., Evans, K., Zhou, G., Johnson, N. T., Hyman, B. T., Sorger, P. K., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-21330-0 · Cited by 299 · see citing works
Cellular Senescence in Neurodegenerative Diseases
Martínez‐Cué, C., & Rueda, N. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.00016 · Cited by 285 · see citing works
Clearance of cerebral Aβ in Alzheimer’s disease: reassessing the role of microglia and monocytes
Zuroff, L. R., Daley, D. A., Black, K. L., & Koronyo‐Hamaoui, M. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2463-7 · Cited by 275 · see citing works
Abnormalities of Mitochondrial Dynamics in Neurodegenerative Diseases
Gao, J., Wang, L., Liu, J., Xie, F., Su, B., & Wang, X. (2017) · Antioxidants · doi:10.3390/antiox6020025 · Cited by 250 · see citing works
The role of gut microbiota in pathogenesis of Alzheimer's disease
Bostancıklıoğlu, M. (2019) · Journal of Applied Microbiology · doi:10.1111/jam.14264 · Cited by 200 · see citing works
Novel target for treating Alzheimer’s Diseases: Crosstalk between the Nrf2 pathway and autophagy
Zhang, W., Feng, C., & Jiang, H. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101207 · Cited by 200 · see citing works
Impaired insulin signalling and allostatic load in Alzheimer disease
Felice, F. G. D., Gonçalves, R. A., & Ferreira, S. T. (2022) · Nature reviews. Neuroscience · doi:10.1038/s41583-022-00558-9 · Cited by 180 · see citing works
A small molecule transcription factor EB activator ameliorates beta‐amyloid precursor protein and Tau pathology in Alzheimer's disease models
Song, J., Malampati, S., Zeng, Y. X., Durairajan, S. S. K., Yang, C., Tong, B. C., Iyaswamy, A., Shang, W., Sreenivasmurthy, S. G., Zhu, Z., et al. (2019) · Aging Cell · doi:10.1111/acel.13069 · Cited by 161 · see citing works
Cis P-tau is induced in clinical and preclinical brain injury and contributes to post-injury sequelae
Albayram, Ö., Kondo, A., Mannix, R., Smith, C., Tsai, C.-Y., Li, C., Herbert, M. K., Qiu, J., Monuteaux, M. C., Driver, J. A., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-01068-4 · Cited by 152 · see citing works
Current progress, challenges and future prospects of diagnostic and therapeutic interventions in Alzheimer's disease
Rajasekhar, K., & Govindaraju, T. (2018) · RSC Advances · doi:10.1039/c8ra03620a · Cited by 150 · see citing works
Microglial polarization: novel therapeutic mechanism against Alzheimer’s disease
Yao, K., & Zu, H. (2019) · Inflammopharmacology · doi:10.1007/s10787-019-00613-5 · Cited by 146 · see citing works
Lifestyle Modifications and Nutritional Interventions in Aging-Associated Cognitive Decline and Alzheimer's Disease
Bhatti, G. K., Reddy, A. P., Reddy, P. H., & Bhatti, J. S. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00369 · Cited by 145 · see citing works
Signal pathways in the treatment of Alzheimer’s disease with traditional Chinese medicine
Ding, M.-R., Qu, Y.-J., Hu, B., & An, H. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.113208 · Cited by 144 · see citing works
Selenomethionine Mitigates Cognitive Decline by Targeting Both Tau Hyperphosphorylation and Autophagic Clearance in an Alzheimer's Disease Mouse Model
Zhang, Z.-H., Wu, Q., Zheng, R., Chen, C., Chen, Y., Liu, Q., Hoffmann, P. R., Ni, J., & Song, G.-L. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.3229-16.2017 · Cited by 128 · see citing works
Mechanisms of NLRP3 Inflammasome Activation: Its Role in the Treatment of Alzheimer’s Disease
Zhang, Y., Zhao, Y., Zhang, J., & Yang, G. (2020) · Neurochemical Research · doi:10.1007/s11064-020-03121-z · Cited by 125 · see citing works
Co-Localization of Glia Maturation Factor with NLRP3 Inflammasome and Autophagosome Markers in Human Alzheimer’s Disease Brain
Ahmed, M. E., Iyer, S. S., Thangavel, R., Kempuraj, D., Selvakumar, G. P., Raikwar, S. P., Zaheer, S. A., & Zaheer, A. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170634 · Cited by 120 · see citing works
CORVET, CHEVI and HOPS – multisubunit tethers of the endo-lysosomal system in health and disease
van der Beek, J., Jonker, C. T. H., van der Welle, R. E. N., Liv, N., & Klumperman, J. (2019) · Journal of Cell Science · doi:10.1242/jcs.189134 · Cited by 121 · see citing works
Interaction between autophagy and the NLRP3 inflammasome
Cao, Z., Wang, Y., Long, Z., & He, G. (2019) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmz098 · Cited by 119 · see citing works
Key Aging-Associated Alterations in Primary Microglia Response to Beta-Amyloid Stimulation
Caldeira, C., Cunha, C., Vaz, A. R., Falcão, A. S., Barateiro, A., Seixas, E., Fernandes, A., & Brites, D. (2017) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2017.00277 · Cited by 117 · see citing works
Internalization mechanisms of brain-derived tau oligomers from patients with Alzheimer’s disease, progressive supranuclear palsy and dementia with Lewy bodies
Puangmalai, N., Bhatt, N. N., Montalbano, M., Sengupta, U., Gaikwad, S., Ventura, F. L., McAllen, S., Ellsworth, A., García, S., & Kayed, R. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-2503-3 · Cited by 110 · see citing works
The influence of circular RNAs on autophagy and disease progression
Wang, Y., Mo, Y., Miao, P., Zhang, S., Gong, Z., Yan, Q., Tang, Y., He, Y., Liao, Q., Li, X., et al. (2021) · Autophagy · doi:10.1080/15548627.2021.1917131 · Cited by 99 · see citing works
Therapeutic implication of autophagy in neurodegenerative diseases
Rahman, M. A., & Rhim, H. (2017) · BMB Reports · doi:10.5483/bmbrep.2017.50.7.069 · Cited by 96 · see citing works
Benefit of Oleuropein Aglycone for Alzheimer’s Disease by Promoting Autophagy
Cordero, J. G., García‐Escudero, R., Ávila, J., Gargini, R., & García‐Escudero, V. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/5010741 · Cited by 93 · see citing works
Molecular network of neuronal autophagy in the pathophysiology and treatment of depression
Jia, J., & Le, W. (2015) · Neuroscience Bulletin · doi:10.1007/s12264-015-1548-2 · Cited by 91 · see citing works
Neurodegenerative Pathways in Alzheimer’s Disease: A Review
Ramachandran, A. K., Das, S., Joseph, A., Shenoy, G. G., Alex, A. T., & Mudgal, J. (2020) · Current Neuropharmacology · doi:10.2174/1570159x18666200807130637 · Cited by 94 · see citing works
Design, Synthesis, and Evaluation of Novel Ferulic Acid Derivatives as Multi-Target-Directed Ligands for the Treatment of Alzheimer’s Disease
Sang, Z., Wang, K., Han, X., Cao, M., Tan, Z., & Liu, W. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00530 · Cited by 87 · see citing works
Acrylamide aggravates cognitive deficits at night period via the gut–brain axis by reprogramming the brain circadian clock
Tan, X., Ye, J., Liu, W., Zhao, B., Shi, X., Zhang, C., Liu, Z., & Liu, X. (2018) · Archives of Toxicology · doi:10.1007/s00204-018-2340-7 · Cited by 84 · see citing works
Could Alzheimer’s Disease Originate in the Periphery and If So How So?
Morris, G., Berk, M., Maes, M. H. J., & Puri, B. K. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1092-y · Cited by 83 · see citing works
Sex Differences in Autophagy Contribute to Female Vulnerability in Alzheimer's Disease
Congdon, E. E. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00372 · Cited by 81 · see citing works
Mitochondrial dynamics involves molecular and mechanical events in motility, fusion and fission
Green, A., Hossain, T., & Eckmann, D. M. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.1010232 · Cited by 83 · see citing works
Amyloid cross-seeding raises new dimensions to understanding of amyloidogenesis mechanism
Chaudhuri, P., Prajapati, K. P., Anand, B. G., Dubey, K., & Kar, K. (2019) · Ageing Research Reviews · doi:10.1016/j.arr.2019.100937 · Cited by 80 · see citing works
Pharmacological doses of melatonin impede cognitive decline in tau‐related Alzheimer models, once tauopathy is initiated, by restoring the autophagic flux
Luengo, E., Buendía, I., Fernández‐Mendívil, C., Trigo-Alonso, P., Negredo, P., Michalska, P., Hernández-García, B. J., Sánchez‐Ramos, C., Bernal, J. A., Ikezu, T., et al. (2019) · Journal of Pineal Research · doi:10.1111/jpi.12578 · Cited by 76 · see citing works
Neuroprotection by Walnut-Derived Peptides through Autophagy Promotion via Akt/mTOR Signaling Pathway against Oxidative Stress in PC12 Cells
Zhao, F., Wang, J., Lu, H., Li, F., Qin, H., Liu, C., & Min, W. (2020) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.9b08252 · Cited by 77 · see citing works
Evaluating the Effectiveness of GTM-1, Rapamycin, and Carbamazepine on Autophagy and Alzheimer Disease
Zhang, L., Wang, L., Wang, R., Gao, Y., Che, H., Pan, Y., & Fu, P. (2017) · Medical Science Monitor · doi:10.12659/msm.898679 · Cited by 77 · see citing works
Targeting autophagy in Alzheimer’s disease: Animal models and mechanisms
Zhang, X.-W., 澳门大学中华医药研究院中药质量研究国家重点实验室, 澳. 凼. 9., State Key Laboratory of Quality Research in Chinese Medicine, I. O. C. M. S., Zhu, X.-X., Tang, D.-S., Lu, J.-H., 佛山大学广东省动物分子设计与精准育种重点实验室, 广., & Guangdong Provincial Key Laboratory of Animal Molecular Design and Precise Breeding, G. E. T. C. O. G. P. (2023) · Zoological Research · doi:10.24272/j.issn.2095-8137.2023.294 · Cited by 77 · see citing works
Human Herpesviruses 6A and 6B in Brain Diseases: Association versus Causation
Komaroff, A. L., Pellett, P. E., & Jacobson, S. (2020) · Clinical Microbiology Reviews · doi:10.1128/cmr.00143-20 · Cited by 76 · see citing works
Role of NLRP3 Inflammasome and Its Inhibitors as Emerging Therapeutic Drug Candidate for Alzheimer’s Disease: a Review of Mechanism of Activation, Regulation, and Inhibition
Sharma, B., Satija, G., Madan, A., Garg, M., Alam, M. M., Shaquiquzzaman, M., Khanna, S. M., Tiwari, P., Parvez, S., Iqubal, A., et al. (2022) · Inflammation · doi:10.1007/s10753-022-01730-0 · Cited by 65 · see citing works
When Good Kinases Go Rogue: GSK3, p38 MAPK and CDKs as Therapeutic Targets for Alzheimer’s and Huntington’s Disease
D’Mello, S. R. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115911 · Cited by 77 · see citing works
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 76 · see citing works
Self-citation
Regulation 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 73 · see citing works
Exercise-mediated regulation of autophagy in the cardiovascular system
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 · see citing works
Fasting-mimicking diet cycles reduce neuroinflammation to attenuate cognitive decline in Alzheimer’s models
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 68 · see citing works
HIV-1 Nef counteracts autophagy restriction by enhancing the association between BECN1 and its inhibitor BCL2 in a PRKN-dependent manner
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 66 · see citing works
The Combination of β ‐Asarone and Icariin Inhibits Amyloid‐ β and Reverses Cognitive Deficits by Promoting Mitophagy in Models of Alzheimer’s Disease
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 66 · see citing works
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 67 · see citing works
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 · see citing works
Cannabidiol (CBD) enhanced the hippocampal immune response and autophagy of APP/PS1 Alzheimer's mice uncovered by RNA-seq
Hao, F., & Feng, Y. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.118624 · Cited by 64 · see citing works
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 63 · see citing works
Comprehensive Review Regarding Mercury Poisoning and Its Complex Involvement in Alzheimer’s Disease
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 · see citing works
Autophagy in Myelinating Glia
Belgrad, J., Pace, R. D., & Fields, R. D. (2019) · Journal of Neuroscience · doi:10.1523/jneurosci.1066-19.2019 · Cited by 59 · see citing works
Cannabidiol protects against Alzheimer's disease in C. elegans via ROS scavenging activity of its phenolic hydroxyl groups
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 · see citing works
Initial Steps in Mammalian Autophagosome Biogenesis
Grasso, D., Renna, F. J., & Vaccaro, M. I. (2018) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2018.00146 · Cited by 59 · see citing works
Sex-dependent calcium hyperactivity due to lysosomal-related dysfunction in astrocytes from APOE4 versus APOE3 gene targeted replacement mice
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 · see citing works
Antia, a Natural Antioxidant Product, Attenuates Cognitive Dysfunction in Streptozotocin-Induced Mouse Model of Sporadic Alzheimer’s Disease by Targeting the Amyloidogenic, Inflammatory, Autophagy, and Oxidative Stress Pathways
Sayed, N. S. E., & Ghoneum, M. H. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/4386562 · Cited by 55 · see citing works
Reducing Endogenous α-Synuclein Mitigates the Degeneration of Selective Neuronal Populations in an Alzheimer's Disease Transgenic Mouse Model
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 · see citing works
Self-citation
Functional analyses of major cancer-related signaling pathways in Alzheimer's disease etiology
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 · see citing works
Anthocyanin-rich blueberry extracts and anthocyanin metabolite protocatechuic acid promote autophagy-lysosomal pathway and alleviate neurons damage in in vivo and in vitro models of Alzheimer's disease
Li, H., Zheng, T., Lian, F., Xu, T., Yin, W., & Jiang, Y. (2021) · Nutrition · doi:10.1016/j.nut.2021.111473 · Cited by 54 · see citing works
Leveraging hallmark Alzheimer’s molecular targets using phytoconstituents: Current perspective and emerging trends
Dhage, P. A., Sharbidre, A. A., Dakua, S. P., & Balakrishnan, S. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111634 · Cited by 53 · see citing works
Dynamic changes of autophagic flux induced by Abeta in the brain of postmortem Alzheimer’s disease patients, animal models and cell models
Long, Z., Chen, J., Zhao, Y., Zhou, W. H., Yao, Q., Wang, Y., & He, G. (2020) · Aging · doi:10.18632/aging.103305 · Cited by 52 · see citing works
Antimony, a novel nerve poison, triggers neuronal autophagic death via reactive oxygen species-mediated inhibition of the protein kinase B/mammalian target of rapamycin pathway
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 · see citing works
PROTAC technology for the treatment of Alzheimer’s disease: advances and perspectives
Inuzuka, H., Liu, J., Wei, W., & Rezaeian, A.-H. (2022) · Acta Materia Medica · doi:10.15212/amm-2021-0001 · Cited by 51 · see citing works
EGFR Signaling Stimulates Autophagy to Regulate Stem Cell Maintenance and Lipid Homeostasis in the Drosophila Testis
Demarco, R. S., Uyemura, B. S., & Jones, D. L. (2020) · Cell Reports · doi:10.1016/j.celrep.2019.12.086 · Cited by 47 · see citing works
Targeting and regulation of autophagy in hepatocellular carcinoma: revisiting the molecular interactions and mechanisms for new therapy approaches
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 47 · see citing works
Mediators of mitophagy that regulate mitochondrial quality control play crucial role in diverse pathophysiology
De, R., Mazumder, S., & Bandyopadhyay, U. (2020) · Cell Biology and Toxicology · doi:10.1007/s10565-020-09561-1 · Cited by 46 · see citing works
HHV-6A infection dysregulates autophagy/UPR interplay increasing beta amyloid production and tau phosphorylation in astrocytoma cells as well as in primary neurons, possible molecular mechanisms linking viral infection to Alzheimer's disease
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 · see citing works
Apelin-36 exerts the cytoprotective effect against MPP+-induced cytotoxicity in SH-SY5Y cells through PI3K/Akt/mTOR autophagy pathway
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 · see citing works
Molecular Mechanism of Autophagy: Its Role in the Therapy of Alzheimer’s Disease
Zhao, Y., Zhang, Y., Zhang, J., Zhang, X., & Yang, G. (2020) · Current Neuropharmacology · doi:10.2174/1570159x18666200114163636 · Cited by 40 · see citing works
Empagliflozin Induced Ketosis, Upregulated IGF-1/Insulin Receptors and the Canonical Insulin Signaling Pathway in Neurons, and Decreased the Excitatory Neurotransmitter Glutamate in the Brain of Non-Diabetics
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 39 · see citing works
Brainiac Caspases: Beyond the Wall of Apoptosis
Espinosa‐Oliva, A. M., García‐Revilla, J., Alonso-Bellido, I. M., & Burguillos, M. Á. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00500 · Cited by 39 · see citing works
GPNMB mitigates Alzheimer’s disease and enhances autophagy via suppressing the mTOR signal
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 39 · see citing works
New Insights Into Autophagy Dysfunction Related to Amyloid Beta Toxicity and Neuropathology in Alzheimer's Disease
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 38 · see citing works
Downregulated apoptosis and autophagy after anti‐Aβ immunotherapy in Alzheimer's disease
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 · see citing works
The emerging role of the sigma-1 receptor in autophagy: hand-in-hand targets for the treatment of Alzheimer’s
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 · see citing works
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 37 · see citing works
Levetiracetam alleviates cognitive decline in Alzheimer’s disease animal model by ameliorating the dysfunction of the neuronal network
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 · see citing works
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 · see citing works
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 · see citing works
Transient acceleration of autophagic degradation by pharmacological Nrf2 activation is important for retinal pigment epithelium cell survival
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 · see citing works
DHCR24 Knock-Down Induced Tau Hyperphosphorylation at Thr181, Ser199, Thr231, Ser262, Ser396 Epitopes and Inhibition of Autophagy by Overactivation of GSK3β/mTOR Signaling
Bai, X., Wu, J.-F., Zhang, M., Xu, Y.-X., Duan, L.-J., Yao, K., Zhang, J.-F., Bo, J., Zhao, Y.-F., Xu, G.-X., et al. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.513605 · Cited by 31 · see citing works
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 33 · see citing works
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 · see citing works
Anti-Alzheimer Activity of Combinations of Cocoa with Vinpocetine or Other Nutraceuticals in Rat Model: Modulation of Wnt3/β-Catenin/GSK-3β/Nrf2/HO-1 and PERK/CHOP/Bcl-2 Pathways
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 · see citing works
Therapeutic Implications of a Polymethoxylated Flavone, Tangeretin, in the Management of Cancer via Modulation of Different Molecular Pathways
Arafa, E. A., Shurrab, N. T., & Buabeid, M. A. (2021) · Advances in Pharmacological and Pharmaceutical Sciences · doi:10.1155/2021/4709818 · Cited by 31 · see citing works
Targeting STAT3 signaling pathway in the treatment of Alzheimer’s disease with compounds from natural products
Wen, X., & Hu, J. (2024) · International Immunopharmacology · doi:10.1016/j.intimp.2024.112936 · Cited by 31 · see citing works
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 30 · see citing works
Thermodynamic and Kinetic Studies of the Interaction of Nuclear Receptor Coactivator-4 (NCOA4) with Human Ferritin
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 29 · see citing works
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 28 · see citing works
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 · see citing works
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 28 · see citing works
Targeting Microglia in Neuroinflammation: H3 Receptor Antagonists as a Novel Therapeutic Approach for Alzheimer’s Disease, Parkinson’s Disease, and Autism Spectrum Disorder
Thomas, S. D., Abdalla, S., Eissa, N., Akour, A., Jha, N., Ojha, S., & Sadek, B. (2024) · Pharmaceuticals · doi:10.3390/ph17070831 · Cited by 24 · see citing works
Harnessing the Therapeutic Potential of Peptides for Synergistic Treatment of Alzheimer’s Disease by Targeting Aβ Aggregation, Metal-Mediated Aβ Aggregation, Cholinesterase, Tau Degradation, and Oxidative Stress
Singh, K., Kaur, A., Goyal, B., & Goyal, D. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.4c00246 · Cited by 28 · see citing works
PEG-Ceramide Nanomicelles Induce Autophagy and Degrade Tau Proteins in N2a Cells
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 · see citing works
Increased mitochondrial calcium uptake and concomitant mitochondrial activity by presenilin loss promotes mTORC1 signaling to drive neurodegeneration
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 · see citing works
Iron mineralization and core dissociation in mammalian homopolymeric H-ferritin: Current understanding and future perspectives
Melman, A., & Bou‐Abdallah, F. (2020) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2020.129700 · Cited by 27 · see citing works
The Role of Chronic Inflammatory Bone and Joint Disorders in the Pathogenesis and Progression of Alzheimer's Disease
Culibrk, R. A., & Hahn, M. S. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.583884 · Cited by 27 · see citing works
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 28 · see citing works
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 28 · see citing works

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
ORCID: Zare-shahabadi, Ameneh
Masliah, Eliezer
Johnson, Gail V.W.
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
DOI: 10.1515/revneuro-2014-0076
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: Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
Health Sciences › Medicine › Physiology › 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

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Autophagy in Alzheimer’s disease

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Self-check

Cites

Cited by

Related

Record

About these checks