The DOI matches its Crossref record; 319 of the 319 references it cites were found in a registry or an index.
Mechanisms of autophagy–lysosome dysfunction in neurodegenerative diseases
Open accessAbstract
Autophagy is a lysosome-based degradative process used to recycle obsolete cellular constituents and eliminate damaged organelles and aggregate-prone proteins. Their postmitotic nature and extremely polarized morphologies make neurons particularly vulnerable to disruptions caused by autophagy-lysosomal defects, especially as the brain ages. Consequently, mutations in genes regulating autophagy and lysosomal functions cause a wide range of neurodegenerative diseases. Here, we review the role of autophagy and lysosomes in neurodegenerative diseases such as Alzheimer disease, Parkinson disease and frontotemporal dementia. We also consider the strong impact of cellular ageing on lysosomes and autophagy as a tipping point for the late-age emergence of related neurodegenerative disorders. Many of these diseases have primary defects in autophagy, for example affecting autophagosome formation, and in lysosomal functions, especially pH regulation and calcium homeostasis. We have aimed to provide an integrative framework for understanding the central importance of autophagic-lysosomal function in neuronal health and disease.
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
“Currently, 14 NCLs have been described, each with their own identified lipo-protein ultrastructural aggregate and causative gene mutation.119”
From The lysosome and proteostatic stress at the intersection of pediatric neurological disorders and adult neurodegenerative diseases (2025) · cites this paper as [119]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“Previous work has linked disruptions to autophagy and lysosomal biology with AD72–74.”
From APOE genotypes differentially remodel the astrocytic lipid droplet proteome to shape lipid droplet dynamics (2026) · cites this paper as [73]
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
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
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
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
Protein aggregation and neurodegenerative disease
Ross, C. A., & Poirier, M. A. (2004) · Nature Medicine · doi:10.1038/nm1066 · Cited by 3,454
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
Self-citationThe role of autophagy during the early neonatal starvation period
Kuma, A., Hatano, M., Matsui, M., Yamamoto, A., Nakaya, H., Yoshimori, T., Ohsumi, Y., Tokuhisa, T., & Mizushima, N. (2004) · Nature · doi:10.1038/nature03029 · Cited by 2,865
The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy
Lazarou, M., Sliter, D. A., Kane, L. A., Sarraf, S. A., Wang, C., Burman, J. L., Sideris, D. P., Fogel, A. I., & Youle, R. J. (2015) · Nature · doi:10.1038/nature14893 · Cited by 2,774
mTOR at the nexus of nutrition, growth, ageing and disease
Liu, G. Y., & Sabatini, D. M. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0199-y · Cited by 2,737
The Beclin 1 network regulates autophagy and apoptosis
Kang, R., Zeh, H. J., Lotze, M. T., & Tang, D. (2011) · Cell Death & Differentiation · doi:10.1038/cdd.2010.191 · Cited by 2,485
Research works printed but not linked: 3
- Lees, M. B. Basic Neurochemistry 5th edn, Vol. 39 (Raven Press, 1994).
- de Duve, C. Lysosomes, a New Group of Cytoplasmic Particle (Ronald Press, 1959).
- Chou, C. C. et al. Proteostasis and lysosomal quality control deficits in Alzheimer’s disease neurons. Preprint at bioRxiv https://doi.org/10.1101/2023.03.27.534444 (2023). · DOI
Cited by
Sorted by citations
Items 301–400 of 433
Meenambal, R., Kruk, T., Warszyński, P., Łopuszyńska, N., Węglarz, W. P., Stan-Głowińska, K., Wojewoda-Budka, J., Jasiński, K., Mąsior, A., & Jantas, D. (2026) · Pharmacological Reports · doi:10.1007/s43440-026-00863-5
Huang, X., Zhang, S., Yuan, M., Zhou, Y., Chen, X., Xia, B., Xu, Z., Yang, X., Yang, B., He, Q., et al. (2026) · Autophagy · doi:10.1080/15548627.2026.2672162
Lysosomal function and homeostasis: From cellular adaptation to disease pathogenesis
Minami, S., & Hamasaki, M. (2026) · International review of cytology · doi:10.1016/bs.ircmb.2026.04.002
Li, J., Wang, T., Zhang, W., Chen, L., Peng, M., Li, N., & Zhang, L. (2026) · Bioelectrochemistry · doi:10.1016/j.bioelechem.2026.109327
Wang, H., Liu, S.-Y., Chiu, C., Yeh, T., Chiu, T.-J., Yeh, Y.-C., Wu, P., & Weng, Y.-H. (2026) · Neurochemistry International · doi:10.1016/j.neuint.2026.106186
Wang, W., & Meng, X. (2026) · Frontiers in Neuroscience · doi:10.3389/fnins.2026.1819002
Zhou, Z. D., Elvira, R., Hou, D., Chao, Y., & Tan, E. K. (2026) · International review of movement disorders · doi:10.1016/bs.irmvd.2026.04.003
Wang, H., Liu, S.-Y., Chiu, C., Yeh, T., Chen, W.-S., Chiu, T.-J., Yeh, Y.-C., Wu, P., & Weng, Y.-H. (2026) · Neurochemical Research · doi:10.1007/s11064-026-04762-2
Xu, X. J., Ni, Z., Wang, Y.-B., Fan, S., Du, Y., Wang, X., & Meng, X. (2026) · Cell Biology and Toxicology · doi:10.1007/s10565-026-10208-w
Gao, Y.-J., Chen, S.-Y., Li, L., Bai, X.-F., Han, N., You, H., Kong, C., Hu, J., Wang, M.-F., Li, T., et al. (2026) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2026.168264
VCP at the crossroads of UPS and autophagy in cancer
Hitchman, C. J., Phillips, J. I., Park, H.-W., & Lu, H. (2026) · Genes & Diseases · doi:10.1016/j.gendis.2026.102264
Sanchez-Mirasierra, I., Hernández-Díaz, S., Barry-Carroll, L., Marti, A. A., Ghimire, S., Delpech, J.-C., & Soukup, S. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.05.26.727892
Early-onset neuroinflammation drives neurodegeneration caused by lysosomal PI(3,5)P2 insufficiency
Wong, B., Payne, M., Silva, A., Kurniawan, E., Eidman, A. S., Pizzo, D. P., Rajupalem, R., Lenk, G. M., Paulo, J. A., Khan, T., et al. (2026) · Neurobiology of Disease · doi:10.1016/j.nbd.2026.107467
D’Angiolini, S., Silvestro, S., Chiricosta, L., Scuruchi, M., & Minuti, A. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27115058
Deubiquitinases at organelle quality control bottlenecks in neurodegeneration
Ellerby, L., & Ashkenazi, A. (2026) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2026.05.006
Zanuttigh, E., Wiśniewska, K., Stöckl, J. B., Brunet, T. A., Gnutti, B., Berti, L., Pierzynowska, K., Doll, S. G., Cavestro, C., Colombo, M. N., et al. (2026) · Research Square · doi:10.21203/rs.3.rs-9437429/v1
Ye, X., Jing, X., Li, Z., Jia, L., Zhong, F., & Luo, X.-G. (2026) · Microbiological Research · doi:10.1016/j.micres.2026.128587
Lipophagy in disease: signaling control, organelle communication, and therapeutic opportunities
Du, Y., Xin-Yao, C., Fang, Y., Wang, Q., Li, J., Guo, T., Lin, J.-N., Fu, J.-Y., Xie, M.-L., Hao, L., et al. (2026) · Cell Communication and Signaling · doi:10.1186/s12964-026-03016-6
Targeting autophagy-related serine/threonine kinases to combat neurodegenerative disorders
Liu, W., & Liu, B. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-44173-8.00016-4
Xing, L., Liu, A., Li, J., Jiang, K., & Li, H. (2026) · Molecular Biology Reports · doi:10.1007/s11033-026-12148-4
Traditional Chinese medicine treatment of asthma: From the insight on programmed cell death
Yao, D., Du, Y., Yuan, X., Zhiyao, Q., Fang, Y., You, M., & He, X. (2026) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2026.122072
Wali, Z., Neha, Shahwan, M. J., Dinislam, K., Shamsi, A., & Anwar, S. (2026) · Biomolecules · doi:10.3390/biom16070944
Cellular clearance mechanisms in neurodegenerative diseases
Velmurugan, G., Mishra, A., & Chinnathambi, S. (2026) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2026.06.004
Wang, X., Zhang, B., Li, X., Xu, Q., Sun, Y., Zhao, K., Zhou, X., Wu, Y., & Zheng, C. (2026) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.71269
The Tau-mitochondria connection and its impact on cellular energy metabolism in Alzheimer’s disease
Singh, A. K., Supraja, M. R., Amal, P. S., Krishnamoorthi, S., Iyaswamy, A., & Durairajan, S. S. K. (2026) · International review of neurobiology · doi:10.1016/bs.irn.2026.06.002
Li, P., Zhang, Y., Wu, J., Li, M., Li, X., Zhao, H., Liu, X. Q., Rong, X., Ma, L., Xu, X., et al. (2026) · Acta Biomaterialia · doi:10.1016/j.actbio.2026.07.009
Abyadeh, M., Zarei‐Kheirabadi, M., Hou, P., Sari, V., Lee, K., Hameed, R., Mehkri, B., Malaugh, E., Newton, J., Kordula, T., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.07.12.738054
Anti-inflammatory CAR-microglia targeting Aβ for Alzheimer’s disease therapy
Ding, X., Hu, X., Xue, W., An, Y., Cheng, W., Zhang, S., Lei, A., & Zhang, J. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1820099
Lactate reprogramming hijacks BDNF neuroprotection to drive hippocampal injury after CO poisoning
Yang, S., Li, S., Xiang, J., Lin, Y., He, Q., Wang, H., Xiang, K., Sun, G., Li, J., Huang, G., et al. (2026) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2026.07.012
Astrocytic lactate shuttle disruption and the energy-starved lysosome in Alzheimer's diseasePreprint
Kim¹, Y., Heo, W., Park, S. J., Kim, Y., & Cho², Y. E. (2026) · Research Square · doi:10.21203/rs.3.rs-10057949/v1
Du, Y., Li, L., Du, M., Xu, Z., Zhang, X., & Cao, W. (2026) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2026.1860821
Altered gene expression in the liver and small intestine of horses with equine neuroaxonal dystrophy
Ryan, S. B., Durbin-Johnson, B., Woolard, K., Miller, A. D., & Finno, C. J. (2026) · Equine Veterinary Journal · doi:10.1002/evj.70216
Xavier, J., Singh, M., Tamhankar, S. P., Griffett, K., & Amin, R. (2026) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.6c00171
Systemic loss of Rubicon aggravates pathological features in the SOD1G93A mouse model
Rodriguez, L., Ojeda, P., Beltrán, S., Muñoz-Palma, E., Rojas‐Rivera, D., Bergmann, C. A., Hernandez, F., Medinas, D. B., Manque, P., & Woehlbier, U. (2026) · Scientific Reports · doi:10.1038/s41598-026-61046-z
KIF1A-mediated trafficking is required for neuronal autophagy in human neuronsPreprint
Borland, C. T., Popolow, J., & Holzbaur, E. L. F. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.07.22.740140
Krauklis, S. A., Keceli, S. K., Campbell, E. M., & Abbineni, P. S. (2026) · Journal of Neurochemistry · doi:10.1111/jnc.70532
Alanazi, S. M., Al‐kuraishy, H. M., Alexiou, A. T., Papadakis, M., Faheem, S. A., & Batiha, G. E. (2026) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2026.111834
CRISPR screening identifies GNPTAB as a noncanonical STING activator driving cellular senescence
Yin, J., Gao, Y., Jing, Y., Xh, J., Wang, F., Cai, Y., Li, M.-H., Cao, T., Wang, M., He, Y., et al. (2026) · Protein & Cell · doi:10.1093/procel/pwag049
Beyond the barrier: Physiological determinants of nanoformulation availability in the aging brain
Teng, R.-D., Sun, J., Yen, T., Taliyan, R., Hsieh, C.-T., & Yang, C.-H. (2026) · Ageing Research Reviews · doi:10.1016/j.arr.2026.103281
CNS limitations in elderly kidney patients
Fadem, S. Z., & Chatterjee, T. S. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-34069-7.00026-4
Yang, F., Gao, W., Wang, J. Z., & Li, H. (2026) · Molecular Neurobiology · doi:10.1007/s12035-026-06098-y
Liu, M., & Ye, S. (2026) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-026-05764-1
Zhou, S., Liu, J., Hu, M., Tian, S., Zhou, J., Li, W., Chen, H., Yin, M., Wang, S., Luo, L., et al. (2026) · Circulation · doi:10.1161/circulationaha.125.077971
Yang, Y., Zhao, M., Feng, Y., Yu, H., Gong, Y., & Liu, Q. (2026) · Antioxidants and Redox Signaling · doi:10.1177/15230864261470736
ARID5A RNA-binding coordinates microglial defense and ferroptosis in iPSC-derived models
Schafer, D. M., Blue, S. M., Xu, S., Mizrahi, O., Gosztyla, M. L., Street, L., Rothamel, K. L., Kopalle, H., Landry, S. B., Rosales, E. K. F., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-76131-0
α-Synuclein Activates Ras–PI3K/AKT/mTOR Signaling to Drive Pathology in Parkinson’s DiseasePreprint
Elhadi, S. A., Congdon-Loeffler, J., Naamneh, L., Khatib, D., Harrosch, E., Maya, O. B. R., Eliassaf, A., Shalev, O., & Sharon, R. (2026) · Research Square · doi:10.21203/rs.3.rs-10524137/v1
Autophagy as a mechanistic link between physical exercise and Alzheimer’s disease
Yu, Z., Wang, Y., & Yang, Y. (2026) · Neuroscience · doi:10.1016/j.neuroscience.2026.08.026
Li, X., Li, L., Liu, X., Liu, S., Yang, W., Gao, J., Kang, S., Wang, L., Li, J., Wang, X., et al. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1865721
Challenges in Studying Synapses in Alzheimer's Disease
Südhof, T. C. (2026) · Annals of Neurology · doi:10.1002/ana.78331
Suri, P., Daartey, A. B., Khan, D. M. I. O., Rayana, N. P., Chilamakuri, R., Godugu, D., Azad, M. G., Reeb, K. L., & Richardson, D. R. (2026) · Pharmacological Reviews · doi:10.1016/j.pharmr.2026.100158
Wang, J., Wang, B., & Chen, L. (2026) · Frontiers in Pediatrics · doi:10.3389/fped.2026.1922943
G3BP1 depletion, observed in Parkinson’s Disease, drives Golgi–lysosome–autophagy defects
Ramakrishna, S., Ryan, L., Son, S. M., & Rubinsztein, D. C. (2026) · Cell Death and Differentiation · doi:10.1038/s41418-026-01853-z
Self-citationZhang, K., Cheng, J., Zhang, J., Tang, L., Wang, F., Chu, X., & Jiang, J. (2026) · Angewandte Chemie International Edition · doi:10.1002/anie.7042721
Atmospheric Aerosol Neurotoxicity and Parkinson's Disease: Mechanisms and Perspectives
Gao, Y., Dong, M., Duan, C., Zheng, X., & Qu, L. (2026) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.71089
Li, J., Li, Y., Bhat, A., Zheng, M., & Zhang, Q. (2026) · Research Square · doi:10.21203/rs.3.rs-10738655/v1
Kim, T. Y., Bhalla, M., Park, U., Hyeon, S. J., Hwang, I., Seo, Y., Youn, W., Lee, J.-A., Lee, J.-H., Lee, B., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.08.23.746508
Pan, N., Cao, P., Zhang, C., Wu, F., & Ning, Y. (2026) · Journal of Alzheimer s Disease Reports · doi:10.1177/25424823261483598
DNA nanodevice-mediated perinuclear accumulation of lysosomes for functional regulation
Yang, W., Wang, Z., Li, X., Shu, D., He, Y., Lian, X., Sun, S., Feng, X., Wu, X., Cui, C., et al. (2026) · Talanta · doi:10.1016/j.talanta.2026.130522
Polysaccharides targeting organelle network dysfunction in Alzheimer's disease: A review
Yu, X., Gao, P., Yao, Q., Yuan, F., & 经维新 (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.154255
Millan, M. J. (2026) · Neuroscience Applied · doi:10.1016/j.nsa.2026.107024
Rebalancing α-Synuclein Clearance: Novel Therapeutic Frontiers in Parkinson’s Disease
Jabeen, M., Hameed, H., Ahmad, S. M., Mushtaq, T., Khan, M. A., & Hameed, A. (2026) · NeuroMolecular Medicine · doi:10.1007/s12017-026-08948-3
Aβ-induced CaMKII hyperactivation is associated with impaired lysosomal maturation and mitophagy
Suh, E. C., Kim, Y. A., Lee, K. E., & Park, E. (2026) · Neurochemistry International · doi:10.1016/j.neuint.2026.106252
MAPT regulates autophagic-lysosomal function and phagocytosis in human microgliaPreprint
Schache, K. J., Zhang, R., Street, A., Starr, E., Marsh, J. A., Kast, D. J. E., Temple, S., Iyer, A. K., & Karch, C. M. M. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.08.27.747662
Wolozin, B. L., Best, M. N., Ellini, M., Ma, Y., Bok, S., Hwang, D., & Filipponi, C. (2026) · Cells · doi:10.3390/cells15171596
Mu, Y., Pan, Z., Zhao, H., Huang, X., Zhang, N., Xu, Z., Yang, B., He, Q., Yang, X., Luo, P., et al. (2026) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2026.118028
Tedesco, B., Chierichetti, M., Cristofani, R., & Poletti, A. (2026) · Journal of Huntington s Disease · doi:10.1177/18796397261478173
Napoletano, F. (2026) · Frontiers in Cell Death · doi:10.3389/fceld.2026.1954383
Zhang, J., Chen, X., Hu, Z., Zhang, J., Wu, T., Zhou, J., Song, B., Xu, Y., Yang, H., & Zhu, X. (2026) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2026.122367
Breaking the self-reinforcing cycle of aging: Biomaterial strategies for aged bone regeneration
Wang, Y., Chen, J., Liu, X., Pei, Y., Chen, S., & Zhou, Y. (2026) · Ageing Research Reviews · doi:10.1016/j.arr.2026.103348
Liu, J., Wang, J., Zeng, Y., Zhao, Z., Zhu, P., Liu, Y., Dong, Q., 赵君朋, Xia, X., Rong, R., et al. (2026) · Journal of Translational Medicine · doi:10.1186/s12967-026-08934-0
Canonical lymphocyte chemokine receptors CXCR3 and CXCR5 modulate neuronal autophagy
Rob, M., Siddiqi, F. H., He, J., Tanaka, Y., & Rubinsztein, D. C. (2026) · Cell Death and Differentiation · doi:10.1038/s41418-026-01865-9
Self-citationLin, R., Ke, Z., Wang, J., Wei, T., Zhang, L., Fang, Y., & Tian, R. (2026) · Neuron · doi:10.1016/j.neuron.2026.08.006
Mitochondrial Homeostasis in Trabecular Meshwork Cells: A Potential Mechanism in Glaucoma
Cao, Y., Xiao, H., Gu, C., Wang, J., Liu, Y., & Yao, J. (2026) · Tissue Engineering Part B Reviews · doi:10.1177/19373368261485522
Retromer-targeted therapy for neurodegenerative diseases
Persico, M., Tuithung, S., Lorenzo, A., Crawford, D., Eleuteri, S., & Simon, D. K. (2026) · Molecular Neurodegeneration · doi:10.1186/s13024-026-00971-z
Estrogen deprivation exacerbates Alzheimer’s disease pathology through neuronal CTSS signaling
Yang, R., Shao, L., Huang, F., He, Y., Yuan, M., Wu, Q., Lin, S., Guo, K., & Zhang, H. (2026) · Journal of Neuroinflammation · doi:10.1186/s12974-026-03970-5
Zhu, Q., Du, W., Wang, C., Corriere, M. A., & Fan, Y. (2026) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2026.121901
Shen, B., Xie, X., Chen, Q., Zhou, Y., Wu, J., Li, B., & Wang, Z. (2026) · Biomedicines · doi:10.3390/biomedicines14092061
Gergian, C., Urbanaviciute, P., Wells, P. M., Transfeld, J. L., Askarova, A., Yaa, R. M., Wu, Y., Ziegler, K. C., Nickl, C. K., Pasillas, M. P., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.09.09.750356
Poulios, E., Papadopoulou, S. Κ., Angelakou, E.-P., Tsourouflis, G., Serdari, A., & Giaginis, C. (2026) · Current Issues in Molecular Biology · doi:10.3390/cimb48090937
Tong-xin, S., Xu, R., Zhai, X.-H., Li, J.-Z., Xu, B., Ning, F.-F., Zhang, X.-Q., Feng, Y., Yang, F.-Y., Liang, D.-L., et al. (2026) · Research Square · doi:10.21203/rs.3.rs-10583104/v1
Autophagy-lysosomal pathway in neurodegeneration
McDonough, S. R., Rao, A. K., McAleer, J. M., Babrowicz, B. M., & Sharma, M. (2026) · Molecular Neurodegeneration Advances · doi:10.1186/s44477-026-00041-0
Yang, H., Matsuhisa, K., Wei, M., Nishi, W., Koh, D. H. Z., Sim, A. Y., Bonne, I., & Saheki, Y. (2026) · Nature Communications · doi:10.1038/s41467-026-77423-1
Advances in calcium transients and autophagy
Xu, J., Tan, X., Li, Y., Zhao, J., Huang, Y., & Luo, Y. (2026) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2026.107025
Visualizing the Golgi apparatus and Golgiphagy in vivo
Zhao, P., Zhang, M., Ding, R., Song, D., Liu, W., Zhang, L., Sang, Y., & Sun, Q. (2026) · The Journal of Cell Biology · doi:10.1083/jcb.202508151
Milky, B., Adams, R., Mazzachi, P., Ali, A. A., Illeperuma, I., Sargeant, T., & Bardy, C. (2026) · Research Square · doi:10.21203/rs.3.rs-10696877/v1
Lu, Y., Wang, Y., Sun, D., Qiao, Z., Wang, Z., Song, S., & Hou, J. (2026) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2026.179368
Saadatpour, F. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-40467-2.00008-7
CDKL5 deficiency impairs TBK1-mediated autophagy and clearance of neuronal protein aggregatesPreprint
Zou, Z., Kahn, B., Sebti, S., Lucavs, J., Rivera‐Cancel, G., & Thinwa, J. W. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.09.13.751248
Testosterone replacement therapy in Parkinson’s disease a narrative review of current evidence
Souza, J. L. S., Rocha, G. S., Bispo, J. M. M., Luz, A. C. A., Silva, R. H., Ribeiro, A. M., Medeiros, K. A. A. L., de Gois, A. M., Freire, M. A. M., & dos Santos, J. R. (2026) · Discover Neuroscience · doi:10.1186/s13064-026-00335-9
Mercer, R. C. C. (2026) · Frontiers in Neuroscience · doi:10.3389/fnins.2026.1941231
Lysosomes as chemical and metabolic organizers of central nervous system injury and repair
Zhao, T., Huang, H., Wang, Y., Zhong, Y., Zhong, Z., Xue, D., Zhu, W., & Xu, K. (2026) · Frontiers in Chemistry · doi:10.3389/fchem.2026.1891677
Corrales, N., Vallejo-Bedia, F., Olivares-Raya, I., Ávila, J., & García‐Escudero, V. (2026) · Applied Sciences · doi:10.3390/app16199488
Jiang, T., Wang, X., 姚旭通, Xia, J., & Liang, J. (2026) · Metabolism · doi:10.1016/j.metabol.2026.156787 · Cited by 1
BmCPV subverts autophagic flux by suppressing TMEM55B to facilitate viral replication
Mo, X., Song, W., Sui, L., Jiang, S., He, H., Zhang, Y., Cheng, J., Qian, P., & Tang, X. (2026) · Gene · doi:10.1016/j.gene.2026.150417
SH3PXD2A LEVELS IN ALZHEIMER’S DISEASE: AN EXPLORATORY STUDY OF A POTENTIAL SYNAPTIC BLOOD BIOMARKER
Ağbektas, T., Tunçbilek, Z., Bulut, T., Taş, A., & Siliğ, Y. (2026) · Bozok Tıp Dergisi · doi:10.16919/bozoktip.1980590
Ma, Y., Hu, Z., Wang, Y., Shi, Y., Zhu, W., Liu, X., & Wu, Y. (2026) · International Immunopharmacology · doi:10.1016/j.intimp.2026.117466
Organelle-targeted DNA nanomaterials: Design, construction, and application
Li, P., Chen, J., Jia, X., Yao, C., Guo, X., & Yang, D. (2026) · Cell Biomaterials · doi:10.1016/j.celbio.2026.100579
Jiang, X., Zhang, Z.-K., Gong, Y.-C., Jiang, T., Liu, J., Hu, J., & Zhou, W.-D. (2026) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2026.120858
Peng, L., Xu, Q., Yuan, L., Li, Q., & Fu, Q. (2026) · Scientific Reports · doi:10.1038/s41598-026-73323-y
Metadata
- Authors
- Nixon, R. A., & Rubinsztein, D. C.
- Affiliations
- Nathan Kline Institute for Psychiatric Research (US)
- University of Cambridge (GB)
- Corresponding author
- Nixon, Ralph A.
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2024-08-06
- Volume
- 25
- Issue
- 11
- Pages
- 926-946
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- PMC
- PMC12239022
- OpenAlex
- W4401363901
- Cited by
- 435
- References
- 319
- Citations by year
- 2026: 260 · 2025: 160 · 2024: 14
- FWCI
- 26.31
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion, cc-by)
- Apollo (University of Cambridge) (submittedVersion, cc-by)
- Apollo (cc-by)
- Funders
- CHDI Foundation
- Rainwater Charitable Foundation
- Alzheimer's Society
- National Institute for Health and Care Research ((NIHR203312)
- Department of Health and Social Care
- Parkinson's UK
- Rosetrees Trust
- UK Dementia Research Institute
- Medical Research Council (NIHR203312)
- NIHR Cambridge Biomedical Research Centre (NIHR 203312)
- National Institute on Aging (P01AG017617, R01AG062376)
- 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 › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
- Keywords
- autophagy, lysosomes, neurodegenerative diseases, Alzheimer's disease, Parkinson's disease, frontotemporal dementia, neuronal aging, autophagosome formation, calcium homeostasis, protein aggregate clearance, lysosomal storage disease
- MeSH terms
- Autophagosomes, Animals, Autophagy, Humans, Lysosomes, Neurons, Neurodegenerative Diseases
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