The DOI matches its Crossref record; 286 of the 288 references it cites were found in a registry or an index.
Autophagy and Neurodegeneration: Pathogenic Mechanisms and Therapeutic Opportunities
Open accessAbstract
Autophagy is a conserved pathway that delivers cytoplasmic contents to the lysosome for degradation. Here we consider its roles in neuronal health and disease. We review evidence from mouse knockout studies demonstrating the normal functions of autophagy as a protective factor against neurodegeneration associated with intracytoplasmic aggregate-prone protein accumulation as well as other roles, including in neuronal stem cell differentiation. We then describe how autophagy may be affected in a range of neurodegenerative diseases. Finally, we describe how autophagy upregulation may be a therapeutic strategy in a wide range of neurodegenerative conditions and consider possible pathways and druggable targets that may be suitable for this objective.
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“and permanent or transient endogenous defects in autophagy have been associated with embryonic lethality, developmental defects, and multiple pathological disorders, including (but not limited to) neurodegeneration, cancer, and cardiovascular disorders [812–817].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [813]
In the citing paper
“Molecular and histopathologic analyses of patient tissues demonstrate mislocalized or accumulated autophagy machinery, pathogenic mutations underlying familial neurodegenerative diseases disable known autophagy-related factors, and genetically ablating autophagy effectors produce neurodegeneration in cell and animal model systems [74–81], supporting a role for autophagy dysfunction in the devel”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [80]
In the citing paper
“The autophagic process is essential in preserving the homeostatic requirements of post‐mitotic neurons, both at the central and at the peripheral nervous system levels (Menzies et al, 2017; Scrivo et al, 2018; Mallucci et al, 2020)”
From Autophagy in major human diseases (2021) · cites this paper as Menzies et al, 2017
In the citing paper
“By analogy, a comparable phenotype has been described in Atg16l1 hypomorphic mice (Lv et al, 2014; Wu et al, 2016; Menzies et al, 2017).”
From Autophagy in major human diseases (2021) · cites this paper as Menzies et al, 2017
In the citing paper
“Aβ is targeted for autophagy‐dependent degradation within the lysosome, explaining why activation of autophagy reduces the burden of Aβ plaques in rodents (Boland et al, 2008; Menzies et al, 2017; Meng et al, 2019).”
From Autophagy in major human diseases (2021) · cites this paper as Menzies et al, 2017
In the citing paper
“However, autophagy appears to be causally implicated in the PSEN1 (presenilin 1)‐mediated conversion of APP (amyloid beta precursor protein) into Aβ (Yu et al, 2005), as well as in the non‐canonical secretion of Aβ into the extracellular space (Nilsson et al, 2013; Menzies et al, 2017).”
From Autophagy in major human diseases (2021) · cites this paper as Menzies et al, 2017
In the citing paper
“While autophagy proteins have been shown to impact the clearance of protein aggregates in neurons, most likely by the canonical autophagic process of aggrephagy (Frake et al., 2015; Menzies et al., 2017; Qaisiya et al., 2017; Sarkar et al., 2007; Sarkar et al., 2009; Webb et al., 2003; Yamamoto and Simonsen, 2011), effects in microglia of the CNS are more likely due to LANDO.”
From LC3-Associated Endocytosis Facilitates β-Amyloid Clearance and Mitigates Neurodegeneration in Murine Alzheimer’s Disease (2019) · cites this paper as Menzies et al., 2017
Citations
Cites
mTOR Signaling in Growth Control and Disease
Laplante, M., & Sabatini, D. M. (2012) · Cell · doi:10.1016/j.cell.2012.03.017 · Cited by 8,509
AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
Kim, J., Kundu, M., Viollet, B., & Guan, K.-L. (2011) · Nature Cell Biology · doi:10.1038/ncb2152 · Cited by 7,227
Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
Kitada, T., Asakawa, S., Hattori, N., Matsumine, H., Yamamura, Y., Minoshima, S., Yokochi, M., Mizuno, Y., & Shimizu, N. (1998) · Nature · doi:10.1038/33416 · Cited by 5,227
DeJesus-Hernandez, M., Mackenzie, I. R., Boeve, B. F., Boxer, A. L., Baker, M., Rutherford, N. J., Nicholson, A. M., Finch, N. A., Flynn, H., Adamson, J., et al. (2011) · Neuron · doi:10.1016/j.neuron.2011.09.011 · Cited by 4,936 · cited 1×
“The most common cause of ALS is a hexanucleotide repeat expansion in the C9ORF72 gene (DeJesus-Hernandez et al., 2011; Renton et al., 2011).”
Gage, F. H. (2000) · Science · doi:10.1126/science.287.5457.1433 · Cited by 4,786
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
A Hexanucleotide Repeat Expansion in C9ORF72 Is the Cause of Chromosome 9p21-Linked ALS-FTD
Renton, A. E., Majounie, E., Waite, A., Simón-Sánchez, J., Rollinson, S., Gibbs, J. R., Schymick, J. C., Laaksovirta, H., van Swieten, J. C., Myllykangas, L., et al. (2011) · Neuron · doi:10.1016/j.neuron.2011.09.010 · Cited by 4,409
Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
Narendra, D., Tanaka, A., Suen, D.-F., & Youle, R. J. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200809125 · Cited by 4,026
Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
Hara, T., Nakamura, K., Matsui, M., Yamamoto, A., Nakahara, Y., Suzuki-Migishima, R., Yokoyama, M., Mishima, K., Saito, I., Okano, H., et al. (2006) · Nature · doi:10.1038/nature04724 · Cited by 3,882
Loss of autophagy in the central nervous system causes neurodegeneration in mice
Komatsu, M., Waguri, S., Chiba, T., Murata, S., Iwata, J.-I., Tanida, I., Ueno, T., Koike, M., Uchiyama, Y., Kominami, E., et al. (2006) · Nature · doi:10.1038/nature04723 · Cited by 3,500
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Astrocyte Autophagy in Neurodegenerative Diseases: Current Progress in Mechanisms and Therapeutics
Qian, J., Ren, S., Ren, T., Shi, R., Qiao, L., & Kang, J. (2025) · Neurochemical Research · doi:10.1007/s11064-025-04532-6 · Cited by 3
“TFEB binds to the promoter region of PGC1a, promotes PGC1a transcription, which accelerates down-stream lipid metabolism through the autophagy-lysosomal pathway and reduces the expression of the inflammatory factors, IL-1β and IL-6, among the astrocytes [ 112].”
Sex does not influence neuronal autophagosome biogenesis throughout aging in mice
Rodriguez, M. N., & Stavoe, A. K. (2025) · Molecular Biology of the Cell · doi:10.1091/mbc.e25-07-0312 · Cited by 2
Loss of CHMP2A implicates an ordered assembly of ESCRT-III proteins during cytokinetic abscission
Kamenetsky, N., Nachmias, D., Khan, S., Avinoam, O., Hazan, I., Upcher, A., & Elia, N. (2025) · Molecular Biology of the Cell · doi:10.1091/mbc.e25-06-0279 · Cited by 2
“Mutations or altered expression of CHMP2A contributed to neurodegenerative disorders, like Alzheimer’s and Parkinson’s diseases, potentially by impairing the degradation of toxic protein aggregates, through disruption of phagophore closure (Menzies et al. , 2017; Takahashi et al. , 2018).”
Wang, Y., Xie, X., Zhang, B.-H., Gao, S., Xiang, Y., Sun, Y., & Guan, X. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-05525-w · Cited by 2
“…mammalian target of rapamycin (mTOR) regulates intracellular autophagy, with autophagy modulation closely linked to cognitive processes [21, 23, 24]. mTOR phosphorylation further participates in pathological pathways involving proinflammatory signaling, redox imbalance, programmed cell…”
Shedding light on the function of autophagy in complicated pregnancies
Wan, S., Huang, Y., & Yang, H. (2026) · Cell Death and Disease · doi:10.1038/s41419-025-08311-7 · Cited by 2
“For example, defects in autophagy have been implicated in neurodegenerative disorders [5], metabolic diseases [6], infectious diseases [7], and tumors [8].”
Schober, M. E., Terry, C. R., Monts, J. K., Jones, G. C., Ritzel, R. M., & Loane, D. J. (2026) · Journal of Neurotrauma · doi:10.1177/08977151251393989 · Cited by 2
“72,73 We had hypothesized that neither DHA nor sex would affect protein markers, ROS, nor phagocytic capacity in uninjured controls.”
Targeting UCHL3 attenuates pathological markers in neuronal models of Huntington’s disease
Ishtayeh, H., Battistoni, E., Pochtar, S., McHugh, T. L. M., Tshilenge, K., Rossmiller, B. P., Amer‐Sarsour, F., Berdichevsky, Y., Muchtar, N., Weil, M., et al. (2026) · Brain · doi:10.1093/brain/awag028 · Cited by 2
“9,10 Induction of autophagy decreases aggregate-prone mutant HTT levels, and alleviates its toxicity in cell and mouse models of HD. 11 In the search for new druggable modulators of polyQ aggregation and toxicity, we examined emerging therapeutic cancer targets implicated in protein degradation.”
InfluentialSelf-citationPeng, T., Zhang, Z., Ding, N., & Zhang, J. (2026) · Neural Plasticity · doi:10.1155/np/6718671 · Cited by 2
Presenilin-dependent regulation of neuronal tau pathology via the autophagy and proteasome pathways
del Ser‐Badia, A., Soto-Faguás, C. M., Vecino, R., Vendrell, C., Molina‐Porcel, L., Sánchez‐Valle, R., Rodrı́guez-Álvarez, J., Vicario‐Abejón, C., & Saura, C. A. (2026) · Acta Neuropathologica Communications · doi:10.1186/s40478-026-02270-6 · Cited by 3
“Macroautophagy, hereafter referred as autophagy, is a catabolic cellular process that targets proteins and organelles to autophagosomes for degradation, and plays a central role in neurodegenerative diseases, including tauopathies [30].”
Yang, G., Xu, X., & Xu, Y. (2026) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2026.112057 · Cited by 2
Autophagy and Parkinson’s Disease
Ryan, L., Rob, M., He, J., & Rubinsztein, D. C. (2022) · Springer eBooks · doi:10.1007/978-3-031-15080-7_242 · Cited by 2
Self-citationNew insights into the autophagy-NAD axis in brain disease
Maria Jose Perez, J., & Deleidi, M. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112420 · Cited by 2
Omega-3 Fatty Acids and Ageing Brain
Boga, N. S., & Basak, S. (2023) · Springer eBooks · doi:10.1007/978-981-99-0534-8_6 · Cited by 2
Plants and fungi metabolites as novel autophagy inducers and senescence inhibitors
Ofir, R. (2024) · Exploration of Drug Science · doi:10.37349/eds.2024.00051 · Cited by 2
Lee, C., Kim, S. S., Bae, M. A., & Kim, S. H. (2025) · Neurochemical Research · doi:10.1007/s11064-025-04404-z · Cited by 2
“Thus, healthy activation of autophagy has been considered to the therapeutic approach in neurodegenerative diseases [27, 28].”
Sellitto, S., Caredio, D., Bimbati, M., Mariutti, G., Cerisoli, M., Frick, L. D., Bouris, V., Morales, C. O. O., Vena, D. L., Neupane, S., et al. (2026) · PLoS Pathogens · doi:10.1371/journal.ppat.1014056 · Cited by 2
Sato, R., Koga, M., Iwama, K., Mizuguchi, T., Matsumoto, N., & Kanda, T. (2020) · Rinsho Shinkeigaku · doi:10.5692/clinicalneurol.cn-001324 · Cited by 2
Neuronal functions of clathrin-associated endocytic sorting adaptors – from molecules to disease
Kononenko, N. L., & Haucke, V. (2020) · e-Neuroforum · doi:10.1515/nf-2020-0023 · Cited by 2
Grigsby, J. G., & Derbel, F. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.83159 · Cited by 2
Ильинский, Н. С., Nesterov, S. V., Shestoperova, E. I., Fonin, A. V., Уверский, В. Н., & Gordeliy, V. (2021) · Biochemistry (Moscow) · doi:10.31857/s0320972521030040 · Cited by 2
Frontotemporal lobar degeneration
Kim, B., Viera-Ortiz, A., Phan, J. M., Irwin, D. J., & Lee, E. B. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-85654-6.00041-1 · Cited by 3
Optical Visualization of Red-GQDs’ Organelles Distribution and Localization in Living Cells
Hu, H., Li, P., Qiu, J., Zhao, M.-J., Kuang, M., Zhang, Z., & Wang, D. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.932807 · Cited by 2
“…GTPases, anchoring factors, and SNAREs undergo multiple fusion processes at different stages of the endolysosomal system, finally forming autophagosomes with degradative functions to degrade and recycle phagocytosed substances (Menzies et al., 2017; Lawrence and Zoncu, 2019; Zhao and Zhang, 2019).”
BackgroundVavilova, J. D., Boyko, A. A., Streltsova, M. A., Kust, S. A., Yusubalieva, G. M., Novikova, O. N., Геннадиевна, С. А., Владимирович, Б. М., Iskhakov, R. N., Sapozhnikov, A. M., et al. (2022) · Medical academic journal · doi:10.17816/maj108521 · Cited by 2
Altered autophagy on the path to Parkinson's disease
Sanchez-Mirasierra, I., Hernández-Díaz, S., Ghimire, S., Main, P., & Soukup, S. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-822003-0.00006-1 · Cited by 2
The Aging Epigenome and The Rejuvenation Strategies
Meiliana, A., Dewi, N. M., & Wijaya, A. (2022) · The Indonesian Biomedical Journal · doi:10.18585/inabj.v14i1.1777 · Cited by 1
Prakash, P., Pradhan, A. K., & Sheeba, V. (2022) · Disease Models & Mechanisms · doi:10.1242/dmm.049447 · Cited by 2
Rounding, N. (2018) · White Rose eTheses Online (University of Leeds, The University of Sheffield, University of York) · Cited by 2
Hegde, R. N., Chiki, A., Petricca, L., Martufi, P., Arbez, N., Mouchiroud, L., Auwerx, J., Landles, C., Bates, G., Singh-Bains, M. K., et al. (2019) · bioRxiv · doi:10.1101/869586 · Cited by 2
Self-citationThe G protein-Coupled Metabotropic Glutamate Receptor 1 controls neuronal macroautophagyPreprint
Donoso, M., Speranza, L., Kalinowska, M., Castillo, C., Sanctis, C. D., & Francesconi, A. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.11.02.365783 · Cited by 2
“…(Hara et al., 2006; Komatsu et al., 2006; Komatsu et al., 2007) of neurons is dependent on autophagy and its dysfunction is linked to neurodegenerative conditions including Huntington’s and Alzheimer’s disease and spinocerebellar ataxia (SCA3) among others (Menzies et al., 2017; Nixon, 2013).”
BackgroundZhou, X., Lee, Y.-K., Li, X., Kim, H., Sánchez-Priego, C., Han, X., Tan, H., Zhou, S., Fu, Y., Purtell, K., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.12.04.519029 · Cited by 2
“Furthermore, dysfunctional autophagy may contribute to major neurodegenerative diseases (Menzies et al., 2017; Nixon, 2013; Yamamoto and Yue, 2014).”
BackgroundDow, C. T., & Kidess, L. (2023) · Preprints.org · doi:10.20944/preprints202302.0173.v1 · Cited by 1
Autophagy Mechanisms for Brain Recovery. Keep It Clean, Keep It Alive
Nobili, A., Barbera, L. L., Mastrantonio, R., Palazzo, C., Molinari, M., D’Amelio, M., & Viscomi, M. T. (2023) · Contemporary clinical neuroscience · doi:10.1007/978-3-031-24930-3_2 · Cited by 1
Proximity labeling reveals dynamic changes in the SQSTM1 protein network
Rondón-Ortiz, A. N., Zhang, L., Ash, P. E. A., Basu, A., Puri, S., van der Spek, S. J. F., Wang, Z., Dorrian, L., Emili, A., & Wolozin, B. L. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107621 · Cited by 1
“The interaction of tau protein and SQSTM1 has been widely described (14, 61, 62).”
Proteomic characterization of the medial prefrontal cortex in chronic restraint stress mice
Fu, Y., Gu, Z., Cao, H., Zuo, C., Huang, Y., Song, Y., Miao, J., Jiang, Y., & Wang, F. (2024) · Journal of Proteomics · doi:10.1016/j.jprot.2024.105278 · Cited by 1
Yadav, E., Mandal, A. K., Sah, A. K., Poudel, S., Pathak, P., Khalilullah, H., Jaremko, M., Emwas, A.-H. M., Yadav, P. S., & Verma, A. (2024) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/0118715273298025240905130205 · Cited by 2
Biomarkers for Alzheimer's Disease
Panwar, D., Sharma, P., Sharma, S., Malik, M., & Kaur, J. (2024) · Advances in bioinformatics and biomedical engineering book series · doi:10.4018/979-8-3693-6442-0.ch003 · Cited by 1
Mou, C., Zhou, L., Xiong, J. J., & Lei, L. (2024) · Gene · doi:10.1016/j.gene.2024.149032 · Cited by 1
Morphological analysis of autophagy in axonal degeneration in gracile axonal dystrophy mice
Tokuhara, Y., Ukon, S., Watanabe, S., Tatsumi, Y., Yoshikawa, H., Ohmuraya, M., & Kimura, T. (2024) · EXPERIMENTAL ANIMALS · doi:10.1538/expanim.24-0041 · Cited by 1
“Furthermore, there is increasing evidence that autophagy pathways are affected in various neurodegenerative diseases [12].”
Dilawari, R., Barik, M., & Singh, E. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-28822-7.00003-9 · Cited by 1
Advances in Aggrephagy: Mechanisms, Disease Implications, and Therapeutic Strategies
Zhuang, H., & Ma, X. (2025) · Journal of Cellular Physiology · doi:10.1002/jcp.31512 · Cited by 3
“In the first approach, autophagy activators targeting mTOR, such as rapamycin and its analogs, have demonstrated positive therapeutic effects in animal models of AD, PD, HD, and ALS (Jiang et al. 2014b; Menzies et al. 2010, 2017; Ravikumar et al. 2004).”
Pradhan, N., Shaw, S., & Jana, N. R. (2025) · ACS Applied Nano Materials · doi:10.1021/acsanm.5c00240 · Cited by 1
Baum, P., Ebert, T., Klöting, N., Krupka, S., König, M., Paeschke, S., Stock, P., Bulc, M., Blüher, M., Palus, K., et al. (2025) · Neuroscience Research · doi:10.1016/j.neures.2025.04.002 · Cited by 1
“Generally, autophagy performs a neuroprotective function in the neural tissue by clearance of aggregated and toxic proteins (Menzies et al., 2017).”
Autophagy and Intracellular Membrane Dynamics in Aging and Age-Related Diseases
Minami, S., Nakamura, S., & Yoshimori, T. (2025) · Learning materials in biosciences · doi:10.1007/978-3-031-88121-3_7 · Cited by 1
Yu, Z., & Ueda, T. (2025) · Nutrients · doi:10.3390/nu17183011 · Cited by 2
“Third, TRE may activate autophagy, a conserved intracellular recycling process responsible for clearing damaged organelles and proteins [11,31].”
O’Brien, T. J., Navarro, E. L., Barroso, C., Menzies, L. A., Martínez-Pérez, E., Carling, D., & Brown, A. E. (2025) · BMC Biology · doi:10.1186/s12915-025-02368-8 · Cited by 1
“Furthermore, genetic variants within BORC genes are associated with many neurodegenerative disorders [56] including: Hermansky-Pudlak Syndrome [57], hereditary spastic paraplegia [54, 58, 59], Parkinson’s Disease [60, 61], Huntingdon’s Disease [62], Alzheimer’s [63], amyotrophic lateral sclerosis…”
Clinical Trials and Evidence-Based Nutraceutical Interventions
Ghosh, S., Singh, D. K. K., Raghunath, M., & Sinha, J. K. (2025) · Nutritional neurosciences · doi:10.1007/978-981-95-2790-8_15 · Cited by 1
Fang, H., Liu, S., Qiu, Y., Chang, L., Chen, Y., Enzha, S., Liu, H., Ye, Y., & Yin, Z. (2025) · Experimental Gerontology · doi:10.1016/j.exger.2025.112997 · Cited by 2
Tong, K., Li, S., Chen, G., He, D., Lin, C., Li, Y., & Chen, N. X. (2025) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-25-00544 · Cited by 1
Sharma, C., Ganguly, J., Madan, D., & Chowdhury, S. R. (2026) · Movement Disorders Clinical Practice · doi:10.1002/mdc3.70500 · Cited by 1
Anhydrobiosis as a Model of Aging and Longevity: The Role of Autophagy and Metabolism in Yeast Cells
Jonnagiri, N. P. K. R., & Kieliszek, M. (2026) · Microbial Ecology · doi:10.1007/s00248-026-02782-7 · Cited by 1
Kawachi, Y., Koçak, G., Korolchuk, V. I., Kataura, T., & Sarkar, S. (2026) · Frontiers in Neuroscience · doi:10.3389/fnins.2026.1857866 · Cited by 1
“Indeed, defective autophagy has been reported in several neurodegenerative conditions (Menzies et al., 2017; Seranova et al., 2020).”
Poulin, M., & Golime, R. (2026) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5c00771 · Cited by 2
TDP-43: a critical amplifier of Alzheimer’s disease beyond amyloid and tau
Roy, A., Chhetry, S., Deka, H., Roy, R., Bhattacharya, P., Patel, B. K., & Borah, A. (2026) · Neuroscience · doi:10.1016/j.neuroscience.2026.05.024 · Cited by 1
Sundaresan, Y., Maddineni, P., Arguello, S. R., Kaipa, B. R., Tran, J. D., Li, L., Kodati, B., & Zode, G. S. (2026) · Cell Death and Disease · doi:10.1038/s41419-026-08927-3 · Cited by 1
“Autophagy is an essential quality control mechanism to maintain cellular homeostasis [1 – 3].”
Cellular Senescence and Aging: Mechanisms, Disease Convergence, and Therapeutic Frontiers
Cai, G., Ren, J., Wang, L., Wu, Y., Wang, H., Cao, X., Shang, H., Hou, X., Wang, Y., Xue, H., et al. (2026) · MedComm · doi:10.1002/mco2.70827 · Cited by 2
“…microautophagy, and chaperone-mediated autophagy, macroautophagy (hereafter autophagy) is the dominant pathway for intracellular renewal [ 60 ], capable of engulfing proteins, lipids, damaged organelles, and pathogens within double-membrane autophagosomes for lysosomal degradation [ 123 ].”
Local autophagy impairment triggers brain-wide presynaptic remodeling and resilience
Toppe, D., Huang, S., Lützkendorf, J., Jiang, P., Suárez-Grimalt, R., Neumann, A., Zhao, Z., Lőrincz, P., Scheunemann, L., Juhász, G., et al. (2026) · The EMBO Journal · doi:10.1038/s44318-026-00847-4 · Cited by 1
“…(Aman et al, 2021; Gupta et al, 2013; Lipinski et al, 2010; Ott et al, 2016; Stavoe et al, 2019) and is impaired in numerous neurodegenerative (Guo et al, 2018; Menzies et al, 2017; Nixon, 2013; Nixon and Rubinsztein, 2024) and neurodevelopmental conditions (Deng et al, 2021; Fassio et al, 2020).”
Arbab, S., Ullah, H., Han, Y., Zhou, J., & Li, K. (2026) · Ageing Research Reviews · doi:10.1016/j.arr.2026.103263 · Cited by 1
Abrar, F., & Martin, D. D. O. (2026) · Autophagy · doi:10.1080/15548627.2026.2711593 · Cited by 2
Tsong, H., Waxham, M. N., & Stavoe, A. K. (2026) · iScience · doi:10.1016/j.isci.2026.117518 · Cited by 1
The Missing Link in Polyglutamine Diseases
Aziz, N. A., & Balint, B. (2017) · Movement Disorders Clinical Practice · doi:10.1002/mdc3.12558 · Cited by 1
Selective striatal cell loss is ameliorated by regulated autophagy of the cortex
Cho, K., & Kim, G. W. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.119822 · Cited by 1
Marzia Perluigi, A., Domenico, F. D., & Butterfield, D. A. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-818845-3.00009-8 · Cited by 1
ELEMENTARY PATHOPHYSIOLOGY, TREATMENT, RISK FACTOR OF ALZHEIMER’S DISEASE
(2022) · International Research Journal of Modernization in Engineering Technology and Science · doi:10.56726/irjmets30873 · Cited by 2
Missing WD40 Repeats in ATG16L1 Delays Canonical Autophagy and Inhibits Noncanonical Autophagy
Tang, J., Fang, D., Zhong, J., & Li, M. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25084493 · Cited by 1
“However, mice with WDR-deficient ATG16L1 exhibited symptoms of neurodegenerative disease [40], which is commonly caused by autophagy blockade [55].”
BackgroundOptineurin regulates motor and learning behaviors by affecting dopaminergic neuron survival in mice
Yang, X., Zheng, R., Zhang, H., Ou, Z., Wan, S., Lin, D., Yan, J., Jin, M., & Tan, J. (2024) · Experimental Neurology · doi:10.1016/j.expneurol.2024.115007 · Cited by 1
(−)‐Epicatechin Rescues Memory Deficits by Activation of Autophagy in a Mouse Model of Tauopathies
Wu, Y., Li, T., Jiang, X., Ling, J., Zhao, Z., Zhu, J., Chen, C., Liu, Q., Yang, X., Shen, X., et al. (2025) · MedComm · doi:10.1002/mco2.70144 · Cited by 2
Young, J., Abdennebi, I., Saëc, M. L., Magnin, F., Amazit, L., Kamenický, P., Maione, L., Bouligand, J., & Beau, I. (2025) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/clinem/dgaf640 · Cited by 1
Aging in Drosophila melanogaster
Gumeni, S., & Trougakos, I. P. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-801238-3.11410-2 · Cited by 3
Deficient Autophagy Contributes to the Development of Diabetic Retinopathy
de Faria, J. M. L., & Dátilo, M. N. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.89339 · Cited by 1
“Since the primary function of autophagy is to eliminate harmful components from cells (aggregated proteins, damaged organelles, and pathogens), malfunctioning of this mechanism implicit in diseases—such as Huntington’s and Parkinson’s diseases [34, 35]—results in protein accumulation.”
BackgroundUnderstanding Neurodegeneration and Neuroprotection Through Genetic Screens in Drosophila
Mandya, A. S., Cheramangalam, R. N., & Jaiswal, M. (2019) · Springer eBooks · doi:10.1007/978-981-13-2218-1_3 · Cited by 1
Chang, C. C., Liu, J., Chen, B. C., Jiang, Z. S., Tu, C. T., Su, C. H., Yang, H. H., Liu, Z. Q., Deng, Y. C., Chen, C. Y., et al. (2020) · Cell Transplantation · doi:10.1177/0963689720960185 · Cited by 1
Antipsychotics, versatility in action
Mahapatra, S., & Marques, T. R. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2108946118 · Cited by 1
Autophagy and Parkinson’s Disease
Ryan, L., Rob, M., He, J., & Rubinsztein, D. C. (2021) · Springer eBooks · doi:10.1007/978-3-030-71519-9_242-1 · Cited by 1
Self-citationEffect of caloric restriction on aging and neurodegenerative diseases
Анатольевна, Ф. Ю., & Мурашев, Б. Ю. (2022) · Zhurnal «Patologicheskaia fiziologiia i eksperimental`naia terapiia» · doi:10.25557/0031-2991.2022.03.166-176 · Cited by 1
Vernizzi, L., Paiardi, C., Licata, G., Vitali, T., Santarelli, S., Raneli, M., Manelli, V., Rizzetto, M., Gioria, M., Pasini, M. E., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/618629 · Cited by 1
“Many efforts have been focused to develop therapies to improve neuronal health, particularly those that promote autophagy, a self-cleaning process known to improve the symptoms of neurodegenerative disorders (NDDs) [1], especially for proteinopathies such as Huntington’s disease (HD) where autophagy favors the clearan…”
BackgroundChen, K., Guo, Q., Cui, Y., Kendall, A. K., Hill, T. A., Hall, R. J., Sacharz, J., Norwood, S. J., Xie, B., Leneva, N., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.12.03.410779 · Cited by 1
Ramírez-Jarquín, U. N., Sharma, M., Shahani, N., & Subramaniam, S. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.02.15.431277 · Cited by 1
Autophagic degradation of Mutant Huntingtin by Enhancement of the Complex of VCP/p97-LC3-mHTTPreprint
Li, X., Zhang, Y., Fu, Y., Zhang, H., Li, H., Li, Q., Li, H., Tan, R., Jiang, C., Jiang, W. B., et al. (2020) · doi:10.22541/au.158981339.95731270 · Cited by 1
Roşianu, F., Mihaylov, S. R., Eder, N., Martiniuc, A., Claxton, S., Flynn, H. R., Jalal, S., Domart, M., Collinson, L., Skehel, M. J., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.03.28.486054 · Cited by 1
“…an essential mechanism for neuronal homeostasis that is needed to prevent neurodegeneration and enhancing autophagy is a putative therapeutic avenue for neurodegenerative disorders with misfolded protein accumulations (Djajadikerta et al, 2020; Karabiyik et al, 2017; Menzies et al., 2017).”
BackgroundInfluentialWu, S., Yin, Y., & Du, L. (2022) · Research Square · doi:10.21203/rs.3.rs-1411533/v1 · Cited by 1
Minimized combinatorial CRISPR screens identify genetic interactions in autophagy
Diehl, V. (2022) · Publication Server of Goethe University Frankfurt am Main (Goethe University Frankfurt) · doi:10.21248/gups.67332 · Cited by 1
he, X., Zhou, X., Zhang, L., Wang, N., Niu, X., Zou, C., Li, Y., Wang, L., & Wang, X. (2022) · Research Square · doi:10.21203/rs.3.rs-1566317/v1 · Cited by 1
Raghavan, M., & Mohan, H. M. (2019) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.733757702.793556724 · Cited by 1
Aging Differentially Affects Axonal Autophagosome Formation and MaturationPreprint
Tsong, H., Holzbaur, E. L. F., & Stavoe, A. K. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.08.27.505553 · Cited by 1
Plini, E. R. G., Melnychuk, M. C., Harkin, A., Dahl, M. J., McAuslam, M., Kühn, S., Boyle, R. T., Whelan, R., Andrews, R., Düzel, S., et al. (2023) · Preprints.org · doi:10.20944/preprints202304.0406.v1
Autophagy regulator ATG5 preserves cerebellar function by safeguarding its glycolytic activityPreprint
Tutas, J., Tolve, M., Özer-Yildiz, E., Ickert, L., Klein, I., Hosseini, M., Liebsch, F., Dethloff, F., Gavalisco, P., Endepols, H., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.01.27.577372 · Cited by 1
Autophagy–Cholesterol Axis Remodeling Supports Malignant Progression and Chemoresistance in GliomaPreprint
Shojaei, S., Behrooz, A. B., Naghibzadeh, K., Basso, J. L. M., Alizadeh, J., Dehesh, T., Saberi, R., Bhushan, B., Eshraghi, M., Rosa, S. C., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.01.06.697885 · Cited by 1
Humphries, K. M. (2017) · The Atrium (University of Guelph)
Emerging Connections: Synaptic Autophagy in Brain Aging and Disease
Liang, Y. (2018) · Stem cell biology and regenerative medicine · doi:10.1007/978-3-319-98146-8_9
Unfoldin, A Novel Tool for the Analysis of Protein Misfolding or Neurodegenerative Diseases
Hachiya, N. (2017) · Open access Journal of Neurology & Neurosurgery · doi:10.19080/oajnn.2017.06.555686
Autophagy: a treatment option in neurodegenerative disease
Palmer, S. J. (2019) · Nursing and Residential Care · doi:10.12968/nrec.2019.21.6.322
The endolysosomal system in neuronal physiology and pathology
Sanchez, S. V. (2019)
Alexander-Floyd, J., Haroon, S., Ying, M., Entezari, A., Jaeger, C., Vermulst, M., & Gidalevitz, T. (2019) · bioRxiv · doi:10.1101/670042
“Therefore, activation of autophagy has been thought of as a nearly universal therapeutic approach to neurodegenerative diseases caused by protein aggregation (90).”
BackgroundUncovering active modulators of native macroautophagy through novel high-content screensPreprint
Safren, N., Tank, E., Santoro, N., & Barmada, S. J. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/756973
Regulation of Cav2.1 by Ankyrin B and its variants
Choi, C. (2019) · UVic’s Research and Learning Repository (University of Victoria)
Fusse, E. J. (2019) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/d.17.2019.tde-23102019-162952 · Cited by 1
Luengo, E., Trigo-Alonso, P., Fernández‐Mendívil, C., Núñez, Á., del Campo, M., Porrero, C., García‐Magro, N., Negredo, P., Sánchez‐Ramos, C., Bernal, J. A., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.10.14.338954
“ALP is upregulated in early stages of AD, but ALP-mediated clearance becomes impaired with disease progression, may promote autophagosome accumulation, inclusions of ubiquitinated proteins and neuritic dystrophy (1, 7, 12).”
BackgroundLate adult-onset Hereditary Sensory and Motor Neuropathy due to TECPR2 mutations
de Souza, P. V. S., Badia, B. D. M. L., Gonçalves, E. A., Machado, R. I. L., Filho, J. M. V. D. A., Farias, I. B., Lopes, A. B., Pinto, W. B. V. D. R., & Oliveira, A. S. B. (2020) · Revista Neurociências · doi:10.34024/rnc.2020.v28.11107
From brain to muscle and back : novel approaches to harness the benefits of exercise
Kelahmetoglu, Y. (2020) · Figshare
Metadata
- Authors
- Menzies, F. M., Fleming, A., Caricasole, A., Bento, C. F., Andrews, S. P., Ashkenazi, A., Füllgrabe, J., Jackson, A., Jimenez Sanchez, M., Karabiyik, C., Licitra, F., Lopez Ramirez, A., Pavel, M., Puri, C., Renna, M., Ricketts, T., Schlotawa, L., Vicinanza, M., Won, H., Zhu, Y., Skidmore, J., & Rubinsztein, D. C.
- Affiliations
- University of Cambridge (GB)
- Corresponding author
- Rubinsztein, David C.
- ORCID
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 2017-03
- Volume
- 93
- Issue
- 5
- Pages
- 1015-1034
- ISSN
- 0896-6273 (ISSN-L)
- OpenAlex
- W2592067246
- Cited by
- 1,134
- References
- 288
- Citations by year
- 2026: 68 · 2025: 96 · 2024: 107 · 2023: 119 · 2022: 153 · 2021: 138 · 2020: 145 · 2019: 159 · 2018: 108 · 2017: 39
- FWCI
- 16.37
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- DIGITAL.CSIC (Spanish National Research Council (CSIC)) (acceptedVersion, other-oa)
- Research Portal (King's College London) (submittedVersion, other-oa)
- Apollo (University of Cambridge) (submittedVersion, cc-by-nc-nd)
- Apollo
- Funders
- Tau Consortium
- Alzheimer’s Research UK
- Wellcome Trust (095317/Z/11/Z)
- Cambridge Institute for Medical Research (100140/Z/12/Z)
- NIHR Biomedical Research Unit in Dementia at Addenbrooke’s Hospital
- The Rosetrees Trust
- FEBS
- Addenbrooke’s Charitable Trust
- Sims Scholarship
- James Baird Fund
- 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, neurodegeneration, lysosomal degradation, protein aggregation, neurodegenerative diseases, therapeutic target, druggable targets, mouse knockout models
- MeSH terms
- Animals, Autophagy, Humans, Lysosomes, Motor Neurons, Proteins, Signal Transduction, Neurodegenerative Diseases
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