The DOI matches its Crossref record; 153 of the 153 references it cites were found in a registry or an index.
Autophagy and neurodegeneration
Open accessAbstract
Most neurodegenerative diseases that afflict humans are associated with the intracytoplasmic deposition of aggregate-prone proteins in neurons. Autophagy is a powerful process for removing such proteins. In this Review, we consider how certain neurodegenerative diseases may be associated with impaired autophagy and how this may affect pathology. We also discuss how autophagy induction may be a plausible therapeutic strategy for some conditions and review studies in various models that support this hypothesis. Finally, we briefly describe some of the signaling pathways that may be amenable to therapeutic targeting for these goals.
Overview
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
Cites
Statistics
Verification
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
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 [76]
Experimental — accuracy not yet measuredIn 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 Frake et al., 2015
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
1 retracted
Crews, L. A., Spencer, B. J., Desplats, P., Patrick, C., Paulino, A., Rockenstein, E. M., Hansen, L. A., Adame, A., Galasko, D. R., & Masliah, E. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009313 · Cited by 379
RetractedRepertoires 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
MACDONALD, M. (1993) · Cell · doi:10.1016/0092-8674(93)90585-e · Cited by 8,366
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
Goate, A., Chartier-Harlin, M.-C., Mullan, M., Brown, J., Crawford, F., Fidani, L., Giuffra, L., Haynes, A., Irving, N., James, L., et al. (1991) · Nature · doi:10.1038/349704a0 · Cited by 4,659
α-Synuclein Locus Triplication Causes Parkinson's Disease
Singleton, A. B., Farrer, M., Johnson, J., Singleton, A., Hague, S., Kachergus, J., Hulihan, M., Peuralinna, T., Dutra, A., Nussbaum, R., et al. (2003) · Science · doi:10.1126/science.1090278 · Cited by 4,383
Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease
Sherrington, R., Rogaev, E. I., Liang, Y., Rogaeva, E. A., Levesque, G., Ikeda, M., Chi, H., Lin, C., Li, G., Holman, K., et al. (1995) · Nature · doi:10.1038/375754a0 · Cited by 4,051
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
mTOR: from growth signal integration to cancer, diabetes and ageing
Zoncu, R., Efeyan, A., & Sabatini, D. M. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3025 · Cited by 3,941
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
Cited by
Sorted by citations
Items 201–300 of 332
Ranaghan, M. J., Durney, M. A., Mesleh, M. F., McCarren, P. R., Garvie, C. W., Daniels, D. S., Carey, K. L., Skepner, A. P., Levine, B., & Perez, J. R. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b00936 · Cited by 16
Zhang, D., Yu, D., Mei, X., & Lv, G. (2020) · Neuroscience Letters · doi:10.1016/j.neulet.2020.134747 · Cited by 16
Involvement of Autophagy in Levodopa‐Induced Dyskinesia
Feyder, M. T., Plewnia, C., Lieberman, O. J., Spigolon, G., Piccin, A., Urbina-Treviño, L., Dehay, B., Li, Q., Nilsson, P., Altun, M., et al. (2021) · Movement Disorders · doi:10.1002/mds.28480 · Cited by 17
Takhsha, F. S., Vangestel, C., Tanç, M., Bruycker, S. D., Berg, M., Pintelon, I., Stroobants, S. G., Meyer, G. R. Y. D., der Veken, P. V., & Martinet, W. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.750259 · Cited by 16
Yi, S., Wang, L., Ho, M. S., & Zhang, S. (2023) · Neural Regeneration Research · doi:10.4103/1673-5374.382259 · Cited by 15
Cellular neurobiology of hyperforin
Bouron, A. (2023) · Phytotherapy Research · doi:10.1002/ptr.8063 · Cited by 15
Autophagy: a necessary evil in cancer and inflammation
Mathur, A., Ritu, R., Chandra, P., & Das, A. (2024) · 3 Biotech · doi:10.1007/s13205-023-03864-w · Cited by 16
Lee, T. V., Kaya, H. E. K., Simin, R. T., Baehrecke, E. H., & Bergmann, A. (2016) · Cell Death and Differentiation · doi:10.1038/cdd.2016.40 · Cited by 15
Autophagy in Neurodegeneration: Can’t Digest It, Spit It Out!
Barthet, V. J. A., & Ryan, K. M. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.01.001 · Cited by 14
Impaired proteostasis in rare neurological diseases
Osinalde, N., Duarri, A., Ramírez, J., Barrio, R., de Nanclares, G. P., & Mayor, U. (2018) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2018.10.007 · Cited by 19
Differences in the Autophagy Response to Hypoxia in the Hippocampus and Neocortex of Rats
Churilova, A. V., Зачепило, Т. Г., Baranova, K. A., & Rybnikova, E. A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23148002 · Cited by 13
Targeting the Mitochondrial Pyruvate Carrier for Neuroprotection
Tang, B. L. (2019) · Brain Sciences · doi:10.3390/brainsci9090238 · Cited by 15
Autophagy in white matter disorders of the CNS : mechanisms and therapeutic opportunities
Nutma, E., Marzin, M. C., Cillessen, S. A. G. M., & Amor, S. (2020) · The Journal of Pathology · doi:10.1002/path.5576 · Cited by 15
The impact of diabetes mellitus on the development of psychiatric and neurological disorders
Kelly, O., Sullivan, J., Carris, N., Geci, S., Martinez, A., Liashenko, V., Colvin, J., Misko, E., Vanderlaan, G., He, L., et al. (2024) · Brain Disorders · doi:10.1016/j.dscb.2024.100135 · Cited by 18
Gao, X., Yu, M., Sun, W., Han, Y., Yang, J., Lu, X., Jin, C., Wu, S., & Cai, Y. (2021) · Food and Chemical Toxicology · doi:10.1016/j.fct.2021.112632 · Cited by 14
Melatonin Protects Neural Stem Cells Against Tri-Ortho-Cresyl Phosphate-Induced Autophagy
Liu, C. X., Zhou, W., Li, Z., Ren, J. T., Li, X., Li, S., Liu, Q., Song, F., Hao, A., & Wang, F. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.00025 · Cited by 13
Peroxisome proliferator-activated receptors (PPARs) agonists as promising neurotherapeutics
Ghannam, I. A. Y., Hassan, R. M., & Abdel‐Maksoud, M. S. (2025) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2025.108226 · Cited by 13
Deneubourg, C., Dafsari, H. S., Lowe, S. A., Martinez-Cotrina, A., Mazaud, D., Park, S. H., Vergani, V., Almacellas‐Barbanoj, A., Maroofian, R., Averdunk, L., et al. (2024) · Autophagy · doi:10.1080/15548627.2024.2405956 · Cited by 13
Gyp1 has a dual function as Ypt1 GAP and interaction partner of Atg8 in selective autophagy
Mitter, A. L., Schlotterhose, P., & Krick, R. (2019) · Autophagy · doi:10.1080/15548627.2019.1569929 · Cited by 12
Qu, Y., Cao, J., Wang, D., Wang, S., Li, Y., & Zhu, Y. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.888836 · Cited by 12
Gholami, M., Hayes, A. W., Jamaati, H., Sureda, A., & Motaghinejad, M. (2023) · Molecular Biology Reports · doi:10.1007/s11033-023-08641-9 · Cited by 12
Kuijpers, M., Kochlamazashvili, G., Stumpf, A., Puchkov, D., Swaminathan, A., Lucht, M. T., Krause, E., Maritzen, T., Schmitz, D., & Haucke, V. (2020) · bioRxiv · doi:10.1101/2020.07.06.189522 · Cited by 167
Luo, Y., Hu, B., Yuan, Z., Bi, H., Yu, J., & Pan, Q. (2024) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2024.118785 · Cited by 12
Min, E., Ko, M. Y., Kim, M. J., Park, H.-J., Kim, Y., Kim, K. K., Lee, B., Hyun, S., & Ka, M. (2025) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2025.179546 · Cited by 11
Targeting autophagy in astrocytes: a potential for neurodegenerative disease intervention
Potokar, M., & Jorgačevski, J. (2025) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2025.1584767 · Cited by 14
Ünal, Ö., Akgun-Unal, N., & Baltacı, A. K. (2025) · Biogerontology · doi:10.1007/s10522-025-10254-7 · Cited by 11
Beclin 1, LC3 and P62 Expression in Equine Sarcoids
Martano, M., Altamura, G., Power, K., Liguori, P., Restucci, B., Borzacchiello, G., & Maiolino, P. (2021) · Animals · doi:10.3390/ani12010020 · Cited by 12
Ran, X., Lu, Q.-Y., Li, Y.-Y., Pu, X.-X., Guo, Y., Yuan, M.-R., Guan, S.-P., Sun, M., Jiao, L., Yao, Y., et al. (2023) · Heliyon · doi:10.1016/j.heliyon.2023.e13691 · Cited by 13
Ashraf, G. M., Ebada, M. A., Suhail, M., Ali, A., Uddin, M. S., Bilgrami, A. L., Perveen, A., Husain, A., Tarique, M., Hafeez, A., et al. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/4572471 · Cited by 11
Gil, L., Chi-Ahumada, É., Niño, S. A., Capdeville, G., Méndez-Torres, A. M., Guerrero, C., Poves, A. B. R., Olazabal, I. M., & Jiménez-Capdeville, M. E. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232112873 · Cited by 10
Protein aggregation and biomolecular condensation in hypoxic environments (Review)
Li, C., Hao, B., Yang, H., Wang, K., Fan, L., & Xiao, W. (2024) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2024.5357 · Cited by 10
The effects and mechanism of estrogen on rats with Parkinson's disease in different age groups.
Li, X.-Z., Sui, C., Chen, Q., Zhuang, Y., Zhang, H., & Zhou, X. (2016) · PubMed Central · Cited by 10
Liu, Z., Wang, P., Yin, Z., Lai, K. P., & Li, R. (2023) · Gene · doi:10.1016/j.gene.2023.147191 · Cited by 10
Hayashi, T., Yano, N., Kora, K., Yokoyama, A., Maizuru, K., Kayaki, T., Nishikawa, K., Osawa, M., Niwa, A., Takenouchi, T., et al. (2023) · Human Molecular Genetics · doi:10.1093/hmg/ddad008 · Cited by 10
Autophagy at the synapse, an early site of dysfunction in neurodegeneration
Jasutkar, H. G., & Yamamoto, A. (2023) · Current Opinion in Physiology · doi:10.1016/j.cophys.2023.100631 · Cited by 9
Fontana, C. M., Locatello, L., Sabatelli, P., Facchinello, N., Lidron, E., Maradonna, F., Carnevali, O., Rasotto, M. B., & Valle, L. D. (2021) · Biomedical Journal · doi:10.1016/j.bj.2021.04.002 · Cited by 9
Macroautophagy and normal aging of the nervous system: Lessons from animal models
Kallergi, E., & Nikoletopoulou, V. (2021) · Cell Stress · doi:10.15698/cst2021.10.257 · Cited by 10
ATase inhibition rescues age-associated proteotoxicity of the secretory pathway
Murie, M., Peng, Y., Rigby, M. J., Dieterich, I. A., Farrugia, M. A., Endresen, A., Bhattacharyya, A., & Puglielli, L. (2022) · Communications Biology · doi:10.1038/s42003-022-03118-0 · Cited by 9
Immune complexes suppressed autophagy in glomerular endothelial cells
Wang, L., & Law, H. (2018) · Cellular Immunology · doi:10.1016/j.cellimm.2018.02.013 · Cited by 9
Autophagy promotes cell and organismal survival by maintaining NAD(H) poolsPreprint
Sedlackova, L., Otten, E. G., Scialò, F., Shapira, D., Kataura, T., Carroll, B., Seranova, E., Rabanal‐Ruiz, Y., Kelly, G., Stefanatos, R. K. A., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.01.31.928424 · Cited by 9
Hohm, H. L., Schuster, R., Buciu, V. B., Serban, D.-M., Ciurescu, S., Cornea, A., Sharma, A., Nistor, D., & Kundnani, N. R. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26188817 · Cited by 9
Burkard, T., Juan, M. H. S., Dreis, C., Kiprina, A., Namgaladze, D., Siebenbrodt, K., Luger, S., Foerch, C., Pfeilschifter, J., Weigert, A., et al. (2022) · Clinical and Translational Medicine · doi:10.1002/ctm2.1068 · Cited by 7
Gong, Q., Luo, D., Wang, H., Xu, X., Fan, Y., Zheng, Z. J., & Qian, T. (2023) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2023.119530 · Cited by 9
The autophagy paradox: A new hypothesis in neurodegenerative disorders
Barmaki, H., Nourazarian, A., Shademan, B., & Khaki‐Khatibi, F. (2024) · Neurochemistry International · doi:10.1016/j.neuint.2024.105827 · Cited by 9
Lapierre, J., Karuppan, M. K. M., Pokharel, M. D., Rodriguez, M., & El‐Hage, N. (2021) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-021-10017-4 · Cited by 9
A Therapeutic Target for Inhibition of Neurodegeneration: Autophagy
Pupyshev, A. B., Короленко, Т. А., & Tikhonova, M. A. (2017) · Neuroscience and Behavioral Physiology · doi:10.1007/s11055-017-0519-7 · Cited by 8
Fat cadherins in mouse models of degenerative ataxias
Baron, O., Grieshober, D., Dias, C., & Fanto, M. (2019) · Scientific Reports · doi:10.1038/s41598-019-52684-7 · Cited by 8
Adornetto, A., Laganà, M. L., Satriano, A., Licastro, E., Corasaniti, M. T., Bagetta, G., & Russo, R. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms251910415 · Cited by 7
Tau proteotasis in Alzheimer’s disease
Chinnathambi, S. (2024) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2024.09.003 · Cited by 7
Liu, Y., Huang, X., Chen, W., Chen, Y., Wang, N., & Wu, X. (2020) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2020/6807879 · Cited by 7
Autophagy Modulation for Organelle-Targeting Therapy
Martins, W. K., & Baptista, M. S. (2016) · InTech eBooks · doi:10.5772/63976 · Cited by 7
Rademacher, D. J., Exline, J. E., & Foecking, E. M. (2025) · Biomedicines · doi:10.3390/biomedicines13061400 · Cited by 8
Gambarotto, L., Russo, L., Bresolin, S., Persano, L., D’Amore, R., Ronchi, G., Zen, F. D., Muratori, L., Cani, A., Negro, S., et al. (2024) · Advanced Science · doi:10.1002/advs.202308965 · Cited by 6
Tamang, J. P., Das, S., Lama, S., Utama, G. L., Safitri, R., Balia, R. L., & Thapa, N. (2025) · Food Research International · doi:10.1016/j.foodres.2025.115757 · Cited by 6
Sase, K., Tsukahara, C., Fujita, N., Arizono, I., Takagi, H., & Kitaoka, Y. (2020) · Molecular Biology Reports · doi:10.1007/s11033-020-06008-y · Cited by 6
Sase, K., Tsukahara, C., Fujita, N., Arizono, I., Otsubo, M., & Kitaoka, Y. (2023) · International Ophthalmology · doi:10.1007/s10792-023-02706-1 · Cited by 6
Gholami, M., Klionsky, D. J., & Motaghinejad, M. (2024) · International Journal of Preventive Medicine · doi:10.4103/ijpvm.ijpvm_41_23 · Cited by 6
D’hondt, C., Iyyathurai, J., Welkenhuyzen, K., Himpens, B., Leybaert, L., & Bultynck, G. (2016) · The Journal of Membrane Biology · doi:10.1007/s00232-016-9874-5 · Cited by 6
Effects of caloric restriction on retinal aging and neurodegeneration
Adornetto, A., Morrone, L. A., Satriano, A., Laganà, M. L., Licastro, E., Nucci, C., Corasaniti, M. T., Tonin, P., Bagetta, G., & Russo, R. (2020) · Progress in brain research · doi:10.1016/bs.pbr.2020.07.005 · Cited by 6
Mi, Z., Liu, H., Rose, M. E., Ma, J., Reay, D. P., Ma, X., Henchir, J. J., Dixon, C. E., & Graham, S. H. (2021) · Neuroscience · doi:10.1016/j.neuroscience.2021.09.001 · Cited by 5
Detection of autophagy in Hirschsprung’s disease
Huang, Q., Ge, X., Li, P., Duan, Y., Guo, Z., Zheng, B., Wu, X., Guo, X., & Gao, Y. (2015) · Neuroreport · doi:10.1097/wnr.0000000000000465 · Cited by 5
Neuronal vacuolation and spinocerebellar degeneration associated with altered neurotransmission
Giannakopoulou, A. (2017) · Folia Neuropathologica · doi:10.5114/fn.2017.68580 · Cited by 5
The many connections of UFMylation with Alzheimer’s disease: a comprehensive review
Yan, T., Clarkson, B. D. S., Lou, Z., Springer, W., & Fiesel, F. C. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00855-8 · Cited by 4
Zargani, M., Ramírez‐Campillo, R., & Arabzadeh, E. (2023) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-023-02795-y · Cited by 4
Mariner, B. L., Rodriguez, A. S., Heath, O. C., & McCormick, M. A. (2023) · GeroScience · doi:10.1007/s11357-023-00938-8 · Cited by 4
p62/sequestosome-1 as a severity-reflecting plasma biomarker in Charcot–Marie–Tooth disease type 1A
Yoon, B., Kim, Y. H., Nam, S. H., Lee, H., Oh, S., Kim, N., Kim, K., Jo, Y. R., Kim, J. K., Choi, B., et al. (2024) · Scientific Reports · doi:10.1038/s41598-024-61794-w · Cited by 5
Wide Applications of Chloroquine Other Than Antimalarial
Alani, B. G., Alwash, A. H., & Ibrahim, I. T. (2020) · Pharmacology & Pharmacy · doi:10.4236/pp.2020.1110022 · Cited by 4
Razzaghi, N., Fernandez-Gonzalez, P., Mas‐Sanchez, A., Vila-Julià, G., Pérez, J. J., & Garriga, P. (2021) · Molecules · doi:10.3390/molecules26103032 · Cited by 6
Sase, K., Kitaoka, Y., Tsukahara, C., & Takagi, H. (2018) · Molecular Medicine Reports · doi:10.3892/mmr.2018.9568 · Cited by 7
SQSTM1/p62 drives radiosensitivity in cervical cancer via autophagy-independent mechanisms
Yoshida, M., Nunomura, H., Furuta, A., Yamada, K., Yasuda, I., Takemura, K., Tsuda, S., Yamaki‐Ushijima, A., Shima, T., Ogawa, R., et al. (2025) · Journal of Reproductive Immunology · doi:10.1016/j.jri.2025.104633 · Cited by 3
Lee, S. H., Han, J. W., Yoon, S.-A., Chang, H. S., & Park, T. K. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27021031 · Cited by 3
New Atg9 Phosphorylation Sites Regulate Autophagic Trafficking in Glia
Wang, L., Yi, S., Zhang, S., Tsai, Y.-T., Cheng, Y.-H., Lin, Y.-T., Lin, C.-C., Lee, Y., Wang, H., & Ho, M. S. (2025) · ASN NEURO · doi:10.1080/17590914.2024.2443442 · Cited by 3
Tautou, M., Eddarkaoui, S., Descamps, F., Larchanché, P.-E., Bakali, J. E., Goveas, L. M., Dumoulin, M., Lamarre, C., Blum, D. L., Buée, L., et al. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.679335 · Cited by 5
ECSIT prevents Alzheimer’s disease pathology by regulating neuronal mitochondrial ROS and mitophagyPreprint
Lepelley, A., Vaughn, L. S., Staniszewski, A., Zhang, H., Du, F., Koppensteiner, P., Tomljanovic, Z., Carneiro, F. R. G., Teich, A. F., Ninan, I., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.01.09.900407 · Cited by 3
c-Myc: Central regulator of autophagy and senescence in cancer
Ji, S., Sun, T., Zhang, Q., Wu, M., Cao, Y., Gao, R., Wang, L., Nicot, C., & Sethi, G. (2026) · Cancer Letters · doi:10.1016/j.canlet.2026.218315 · Cited by 2
Novel mutations and molecular pathways identified in patients with brain iron accumulation disorders
Si, L., Wang, Z., Li, X., Yang, S., Yao, T., Xu, E., Wang, X., & Wang, C. (2023) · Neurogenetics · doi:10.1007/s10048-023-00725-9 · Cited by 2
Acetyl-CoA and acetylation in biology and disease
Puglielli, L., Rigby, M. J., & Fernandez-Fuente, G. (2023) · Elsevier eBooks · doi:10.1016/b978-0-323-95582-9.00009-7 · Cited by 2
Spatial selectivity of ATase inhibition in mouse models of Charcot–Marie–Tooth disease
Fernandez-Fuente, G., Farrugia, M. A., Peng, Y., Schneider, A. J., Svaren, J. P., & Puglielli, L. (2024) · Brain Communications · doi:10.1093/braincomms/fcae232 · Cited by 2
Autophagy on the road to longevity and aging
Manifava, M., & Ktistakis, N. T. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-822003-0.00002-4 · Cited by 2
I nnate immunity regulates α‐synuclein clearance
Sawamura, M., Uemura, N., & Takahashi, R. (2016) · Movement Disorders · doi:10.1002/mds.26571 · Cited by 2
Angireddy, R., Karisetty, B. C., Katsura, K. A., Diaz‐Rosado, A., Murali, S., Smith, S. M., Ohl, L., Clark, K., Kossenkov, A. V., & Bhoj, E. J. K. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.30.621078 · Cited by 2
Chen, H., Tan, Q., Hu, Y., Liu, L., Liang, X., & Hou, L. (2026) · Journal of the Formosan Medical Association · doi:10.1016/j.jfma.2026.05.038 · Cited by 1
Chemical and Molecular Strategies in Restoring Autophagic Flux in TDP-43 Proteinopathy
Jamerlan, A., & Hulme, J. (2026) · Molecules · doi:10.3390/molecules31060924 · Cited by 1
Autophagy–Actin Crosstalk: Implications for Cellular Homeostasis and Disease
Fierti, A. O., Rozsa, R. G., Potu, A., Tajammal, A., & Li, H. (2026) · Cells · doi:10.3390/cells15080665 · Cited by 1
Role of ESCRT pathway and autophagy in neurodegenerative diseases
Dongre, S., Soni, N., & Bissa, B. (2026) · International review of neurobiology · doi:10.1016/bs.irn.2026.05.022 · Cited by 1
Wrasidlo, W., & Masliah, E. (2026) · Cells · doi:10.3390/cells15131177 · Cited by 1
Brain Aging in HIV-1 Infection
Santerre, M., & Sawaya, B. E. (2018) · IntechOpen eBooks · doi:10.5772/intechopen.77029 · Cited by 1
Regulation of autophagy by TDP-43
Tomar, A. K., & Yadav, S. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-820066-7.00005-9 · Cited by 1
Neuroprotective effect of Vesatolimod in an experimental autoimmune encephalomyelitis mice model
Jiang, X., Song, Y., Fang, J., Yang, X., Mu, S., & Zhang, J. (2023) · International Immunopharmacology · doi:10.1016/j.intimp.2023.109717 · Cited by 1
Cheng, C.-F., Cheng, E., & Ku, H.-C. (2024) · Tzu-Chi Medical Journal · doi:10.4103/tcmj.tcmj_51_24 · Cited by 1
Lee, K., Kim, H. J., Kim, J. E., Elina, K. C., Kim, S., Park, Y. S., & Kim, H. K. (2025) · Pharmacology Biochemistry and Behavior · doi:10.1016/j.pbb.2025.173966 · Cited by 1
Mechanistic Target of Rapamycin
McKee-Muir, O. C., & Russell, R. C. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-812146-7.00009-3 · Cited by 2
Lou, Y. (2018) · Biomarkers and Applications · doi:10.29011/2576-9588.100030 · Cited by 1
Deneubourg, C., Dafsari, H. S., Lowe, S. A., Martinez-Cotrina, A., Mazaud, D., Park, S. H., Vergani, V., Maroofian, R., Averdunk, L., Karimiani, E. G., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.04.23.590762 · Cited by 1
Tumor acidosis in malignant progression and therapy
Pellegrini, P. (2016) · Figshare
Physiological Role of Autophagy and Implications in Disease
Karanasios, E., & Ktistakis, N. T. (2016) · Springer eBooks · doi:10.1007/978-3-319-33145-4_5
Is Selective Autophagy Distinct from Starvation-Induced Autophagy?
Guillebaud, G., & Germain, M. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802937-4.00005-3
Autophagy and Cancer Chemotherapy: Inhibition or Enhancement?
Santiago‐O’Farrill, J. M., Lü, Z., & Bast, R. C. (2016) · Single Cell Biology · doi:10.4172/2168-9431.1000145
Autophagy inMycobacterium abscessusInfection
Subhadra, B., & Choi, C. H. (2017) · Journal of Bacteriology and Virology · doi:10.4167/jbv.2017.47.3.122
Metadata
- Authors
- Frake, R. A., Ricketts, T., Menzies, F. M., & Rubinsztein, D. C.
- Corresponding author
- Rubinsztein, David C.
- Venue
- Journal of Clinical Investigation
- Published
- 2015-01-02
- Volume
- 125
- Issue
- 1
- Pages
- 65-74
- ISSN
- 0021-9738 (ISSN-L)
- PMC
- PMC4382230
- OpenAlex
- W2029582543
- Cited by
- 332
- References
- 153
- Citations by year
- 2026: 17 · 2025: 14 · 2024: 19 · 2023: 28 · 2022: 18 · 2021: 36 · 2020: 38 · 2019: 30 · 2018: 40 · 2017: 37 · 2016: 36 · 2015: 19
- FWCI
- 5.72
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Clinical Investigation (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Apollo (University of Cambridge) (submittedVersion)
- Funders
- Wellcome Trust (100140, 095317)
- National Institute for Health and Care Research
- Tau Consortium
- Medical Research Council
- Cambridge Institute for Medical Research, University of Cambridge
- 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, neurodegenerative diseases, protein aggregation, protein clearance, autophagy dysfunction, therapeutic targeting, signaling pathways, neuronal pathology
- MeSH terms
- Animals, Autophagy, Humans, Neurodegenerative Diseases, Protein Kinase Inhibitors, TOR Serine-Threonine Kinases
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