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.
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Fourteen NCLs have been described, each with its own identified lipo-protein ultrastructural aggregate and causative gene mutation.
“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]
The Introduction section on primary lysosomal pH dysregulation identifies CLN1 neuronal ceroid lipofuscinosis as caused by loss-of-function mutations in the PPT gene. It does not state that 14 NCLs have been described or that each has a distinct identified lipoprotein ultrastructural aggregate and causative mutation. (LLM, conf=0.82)
Experimental — accuracy not yet measuredPrevious work has linked disruptions to autophagy and lysosomal biology with AD.
“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]
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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 · see citing works
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
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 · see citing works
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 · see citing works
Protein aggregation and neurodegenerative disease
Ross, C. A., & Poirier, M. A. (2004) · Nature Medicine · doi:10.1038/nm1066 · Cited by 3,454 · 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
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
The Roles of PINK1, Parkin, and Mitochondrial Fidelity in Parkinson’s Disease
Pickrell, A. M., & Youle, R. J. (2015) · Neuron · doi:10.1016/j.neuron.2014.12.007 · Cited by 2,310 · 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
The role of autophagy in neurodegenerative disease
Nixon, R. A. (2013) · Nature Medicine · doi:10.1038/nm.3232 · Cited by 2,059 · see citing works
Self-citationZoncu, R., Bar-Peled, L., Efeyan, A., Wang, S., Sancak, Y., & Sabatini, D. M. (2011) · Science · doi:10.1126/science.1207056 · Cited by 1,673 · see citing works
Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology
Forgac, M. D. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2272 · Cited by 1,626 · see citing works
Lysosomes as dynamic regulators of cell and organismal homeostasis
Ballabio, A., & Bonifacino, J. S. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0185-4 · Cited by 1,469 · see citing works
Lysosomal calcium signalling regulates autophagy through calcineurin and TFEB
Medina, D. L., Paola, S. D., Peluso, I., Armani, A., Stefani, D. D., Venditti, R., Montefusco, S., Rosato, A. S., Prezioso, C., Forrester, A. R., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3114 · Cited by 1,405 · see citing works
Yoshimori, T., Yamamoto, A., Moriyama, Y., Futai, M., & Tashiro, Y. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)47429-2 · Cited by 1,334 · see citing works
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
Self-citationRamirez, A., Heimbach, A., Gründemann, J., Stiller, B., Hampshire, D., Cid, L. P., Goebel, I., Mubaidin, A. F., Wriekat, A.-L., Roeper, J., et al. (2006) · Nature Genetics · doi:10.1038/ng1884 · Cited by 1,208 · see citing works
The vacuolar (H+)-ATPases — nature's most versatile proton pumps
Nishi, T., & Forgac, M. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm729 · Cited by 1,197 · see citing works
Autophagy and Neurodegeneration: Pathogenic Mechanisms and Therapeutic Opportunities
Menzies, F. M., Fleming, A., Caricasole, A., Bento, C. F., Andrews, S. P., Ashkenazi, A., Füllgrabe, J., Jackson, A., Jimenez Sanchez, M., Karabiyik, C., et al. (2017) · Neuron · doi:10.1016/j.neuron.2017.01.022 · Cited by 1,134 · cited 1× · see citing works
“Much activity has focused on identifying drugs to induce auto-phagosome formation and improve lysosome function 4,267,268 .”
Self-citationDiscovery 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
Phosphoproteomics reveals that Parkinson's disease kinase LRRK2 regulates a subset of Rab GTPases
Steger, M., Tonelli, F., Ito, G., Davies, P., Trost, M., Vetter, M., Wachter, S., Lorentzen, E., Duddy, G., Wilson, S., et al. (2016) · eLife · doi:10.7554/elife.12813 · Cited by 990 · see citing works
Regulation of endoplasmic reticulum turnover by selective autophagy
Khaminets, A., Heinrich, T., Mari, M., Grumati, P., Huebner, A. K., Akutsu, M., Liebmann, L., Stolz, A., Nietzsche, S., Koch, N., et al. (2015) · Nature · doi:10.1038/nature14498 · Cited by 956 · see citing works
Plasma membrane contributes to the formation of pre-autophagosomal structures
Ravikumar, B., Moreau, K., Jahreiss, L., Puri, C., & Rubinsztein, D. C. (2010) · Nature Cell Biology · doi:10.1038/ncb2078 · Cited by 902 · see citing works
Self-citationLysosomal positioning coordinates cellular nutrient responses
Korolchuk, V. I., Saiki, S., Lichtenberg, M., Siddiqi, F. H., Roberts, E. A., Imarisio, S., Jahreiss, L., Sarkar, S., Futter, M., Menzies, F. M., et al. (2011) · Nature Cell Biology · doi:10.1038/ncb2204 · Cited by 891 · see citing works
Self-citationDooley, H. C., Razi, M., Polson, H. E. J., Girardin, S. E., Wilson, M. I., & Tooze, S. A. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.05.021 · Cited by 886 · see citing works
Cargo recognition failure is responsible for inefficient autophagy in Huntington’s disease
Martinez-Vicente, M., Talloczy, Z., Wong, E., Tang, G., Koga, H., Kaushik, S., de Vries, R., Arias, E., Harris, S., Sulzer, D., et al. (2010) · Nature Neuroscience · doi:10.1038/nn.2528 · Cited by 885 · see citing works
ROS and Autophagy: Interactions and Molecular Regulatory Mechanisms
Li, L., Tan, J., Miao, Y., Lei, P., & Zhang, Q. (2015) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-015-0166-x · Cited by 876 · see citing works
α-Synuclein impairs macroautophagy: implications for Parkinson’s disease
Winslow, A. R., Chen, C.-W., Corrochano, S., Acevedo-Arozena, A., Gordon, D. E., Peden, A. A., Lichtenberg, M., Menzies, F. M., Ravikumar, B., Imarisio, S., et al. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201003122 · Cited by 825 · see citing works
Self-citationPathogenic Lysosomal Depletion in Parkinson's Disease
Dehay, B., Bové, J., Rodríguez-Muela, N., Perier, C., Recasens, A., Boya, P., & Vila, M. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.1920-10.2010 · Cited by 825 · see citing works
Wang, S., Tsun, Z., Wolfson, R. L., Shen, K., Wyant, G., Plovanich, M. E., Yuan, E. D., Jones, T. D., Chantranupong, L., Comb, W. C., et al. (2015) · Science · doi:10.1126/science.1257132 · Cited by 772 · see citing works
Lysosomes as a therapeutic target
Bonam, S. R., Wang, F., & Muller, S. (2019) · Nature Reviews Drug Discovery · doi:10.1038/s41573-019-0036-1 · Cited by 764 · see citing works
Autophagy as a promoter of longevity: insights from model organisms
Hansen, M., Rubinsztein, D. C., & Walker, D. W. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0033-y · Cited by 754 · see citing works
Self-citationTFEB-mediated autophagy rescues midbrain dopamine neurons from α-synuclein toxicity
Decressac, M., Mattsson, B., Weikop, P., Lundblad, M., Jakobsson, J., & Björklund, A. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1305623110 · Cited by 753 · see citing works
β-Secretase Protein and Activity Are Increased in the Neocortex in Alzheimer Disease
Fukumoto, H. (2002) · Archives of Neurology · doi:10.1001/archneur.59.9.1381 · Cited by 694 · see citing works
SLC38A9 is a component of the lysosomal amino acid sensing machinery that controls mTORC1
Rebsamen, M., Pochini, L., Stasyk, T., de Araújo, M. E. G., Galluccio, M., Kandasamy, R. K., Snijder, B., Fauster, A., Rudashevskaya, E. L., Bruckner, M., et al. (2015) · Nature · doi:10.1038/nature14107 · Cited by 673 · see citing works
Autophagy Inhibition Compromises Degradation of Ubiquitin-Proteasome Pathway Substrates
Korolchuk, V. I., Mansilla, A., Menzies, F. M., & Rubinsztein, D. C. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.01.021 · Cited by 657 · see citing works
Self-citationLee, J.-H., Yang, D.-S., Goulbourne, C. N., Im, E., Stavrides, P., Pensalfini, A., Chan, H., Bouchet-Marquis, C., Bleiwas, C., Berg, M. J., et al. (2022) · Nature Neuroscience · doi:10.1038/s41593-022-01084-8 · Cited by 638 · see citing works
Self-citationBasal Mitophagy Occurs Independently of PINK1 in Mouse Tissues of High Metabolic Demand
McWilliams, T. G., Prescott, A. R., Montava-Garriga, L., Ball, G., Singh, F., Barini, E., Muqit, M. M. K., Brooks, S. P., & Ganley, I. G. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2017.12.008 · Cited by 591 · see citing works
Common variants at 7p21 are associated with frontotemporal lobar degeneration with TDP-43 inclusions
Van Deerlin, V. M., Sleiman, P. M. A., Martinez-Lage, M., Chen-Plotkin, A., Wang, L.-S., Graff-Radford, N. R., Dickson, D. W., Rademakers, R., Boeve, B. F., Grossman, M., et al. (2010) · Nature Genetics · doi:10.1038/ng.536 · Cited by 579 · see citing works
Machinery, regulation and pathophysiological implications of autophagosome maturation
Zhao, Y. G., Codogno, P., & Zhang, H. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00392-4 · Cited by 574 · see citing works
Increased expression of the amyloid precursor β‐secretase in Alzheimer's disease
Holsinger, R. M. D., McLean, C. A., Beyreuther, K., Masters, C. L., & Evin, G. (2002) · Annals of Neurology · doi:10.1002/ana.10208 · Cited by 562 · see citing works
MCOLN1 is a ROS sensor in lysosomes that regulates autophagy
Zhang, X., Cheng, X., Yu, L., Yang, J., Calvo, R., Patnaik, S., Hu, X., Gao, Q., Yang, M., Lawas, M., et al. (2016) · Nature Communications · doi:10.1038/ncomms12109 · Cited by 558 · see citing works
Promoting the clearance of neurotoxic proteins in neurodegenerative disorders of ageing
Boland, B., Yu, W. H., Corti, O., Mollereau, B., Henriques, A., Bézard, E., Pastores, G., Rubinsztein, D. C., Nixon, R. A., Duchen, M. R., et al. (2018) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2018.109 · Cited by 552 · see citing works
Self-citationColacurcio, D. J., & Nixon, R. A. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.05.004 · Cited by 548 · see citing works
Self-citationpH-dependent regulation of lysosomal calcium in macrophages
Christensen, K., Myers, J. T., & Swanson, J. A. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.3.599 · Cited by 537 · see citing works
The heritability and genetics of frontotemporal lobar degeneration
Rohrer, J. D., Guerreiro, R., Vandrovcova, J., Uphill, J., Reiman, D., Beck, J., Isaacs, A. M., Authier, A., Ferrari, R., Fox, N. C., et al. (2009) · Neurology · doi:10.1212/wnl.0b013e3181bf997a · Cited by 536 · see citing works
The TFEB orthologue HLH-30 regulates autophagy and modulates longevity in Caenorhabditis elegans
Lapierre, L. R., Filho, C. D. D. M., McQuary, P. R., Chu, C., Visvikis, O., Chang, J. T., Gelino, S., Ong, B., Davis, A. E. M., Irazoqui, J. E., et al. (2013) · Nature Communications · doi:10.1038/ncomms3267 · Cited by 533 · see citing works
Heckmann, B. L., Teubner, B. J. W., Tummers, B., Boada-Romero, E., Harris, L., Yang, M., Guy, C. S., Zakharenko, S. S., & Green, D. R. (2019) · Cell · doi:10.1016/j.cell.2019.05.056 · Cited by 503 · see citing works
Shen, D., Wang, X., Li, X., Zhang, X., Yao, Z., Dibble, S., Dong, X., Yu, T., Lieberman, A. P., Showalter, H. D., et al. (2012) · Nature Communications · doi:10.1038/ncomms1735 · Cited by 497 · see citing works
The Many Substrates of Presenilin/γ-Secretase
Haapasalo, A., & Kovacs, D. M. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-101065 · Cited by 487 · see citing works
The different autophagy degradation pathways and neurodegeneration
Fleming, A., Bourdenx, M., Fujimaki, M., Karabiyik, C., Krause, G. J., Lopez, A., Martín‐Segura, A., Puri, C., Scrivo, A., Skidmore, J., et al. (2022) · Neuron · doi:10.1016/j.neuron.2022.01.017 · Cited by 485 · see citing works
Self-citationLee, S., Satō, Y., & Nixon, R. A. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.6412-10.2011 · Cited by 471 · see citing works
Self-citationThe Ins and Outs of Cathepsins: Physiological Function and Role in Disease Management
Yadati, T., Houben, T., Bitorina, A., & Shiri-Sverdlov, R. (2020) · Cells · doi:10.3390/cells9071679 · Cited by 466 · see citing works
Presenilins and -Secretase: Structure, Function, and Role in Alzheimer DiseasePreprint
Strooper, B. D., Iwatsubo, T., & Wolfe, M. S. (2011) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006304 · Cited by 465 · see citing works
Dynein mutations impair autophagic clearance of aggregate-prone proteins
Ravikumar, B., Acevedo‐Arozena, A., Imarisio, S., Berger, Z., Vacher, C., O’Kane, C. J., Brown, S. D. M., & Rubinsztein, D. C. (2005) · Nature Genetics · doi:10.1038/ng1591 · Cited by 458 · see citing works
Self-citationNAADP Mobilizes Ca2+ from Reserve Granules, Lysosome-Related Organelles, in Sea Urchin Eggs
Churchill, G. C., Okada, Y., Thomas, J. M., Genazzani, A. A., Patel, S., & Galione, A. (2002) · Cell · doi:10.1016/s0092-8674(02)01082-6 · Cited by 457 · see citing works
Regulation of TFEB and V‐ATPases by mTORC1
Peña‐Llopis, S., Vega-Rubín-de-Celis, S., Schwartz, J. C., Wolff, N. C., Tran, T. A. T., Zou, L., Xie, X., Corey, D. R., & Brugarolas, J. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.257 · Cited by 456 · see citing works
Alzheimer Disease and Oxidative Stress
Perry, G., Cash, A. D., & Smith, M. A. (2002) · BioMed Research International · doi:10.1155/s1110724302203010 · Cited by 455 · see citing works
The Itinerary of Autophagosomes: From Peripheral Formation to Kiss‐and‐Run Fusion with Lysosomes
Jahreiss, L., Menzies, F. M., & Rubinsztein, D. C. (2008) · Traffic · doi:10.1111/j.1600-0854.2008.00701.x · Cited by 453 · see citing works
Self-citationYang, 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
Self-citationDiverse Autophagosome Membrane Sources Coalesce in Recycling Endosomes
Puri, C., Renna, M., Bento, C. F., Moreau, K., & Rubinsztein, D. C. (2013) · Cell · doi:10.1016/j.cell.2013.08.044 · Cited by 423 · see citing works
Self-citationESCRT-mediated lysosome repair precedes lysophagy and promotes cell survival
Radulovic, M., Bongiovanni, A., Schink, K., Nähse, V., Wenzel, E. M., Lafont, F., & Stenmark, H. (2018) · bioRxiv · doi:10.15252/embj.201899753 · Cited by 423 · see citing works
Duve, C. D. (2005) · Nature Cell Biology · doi:10.1038/ncb0905-847 · Cited by 422 · see citing works
Majumder, S., Richardson, A. G., Strong, R., & Oddo, S. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025416 · Cited by 401 · see citing works
Nixon, R. A. (2017) · The FASEB Journal · doi:10.1096/fj.201700359 · Cited by 400 · cited 1× · see citing works
“Ensuing free radical-mediated and proteotoxic damage to lysosomal membranes promotes the early autophagic–lysosomal death of affected neurons containing amyloid-β aggregates and their transformation into extracellular senile (‘amyloid-β’) plaques 131,132,134–136 (Fig.”
Self-citationMolecular mechanisms of endolysosomal Ca2+ signalling in health and disease
Morgan, A. J., Platt, F. M., Lloyd‐Evans, E., & Galione, A. (2011) · Biochemical Journal · doi:10.1042/bj20110949 · Cited by 397 · see citing works
Wong, Y. C., & Holzbaur, E. L. F. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.1870-13.2014 · Cited by 395 · see citing works
Autophagosome Precursor Maturation Requires Homotypic Fusion
Moreau, K., Ravikumar, B., Renna, M., Puri, C., & Rubinsztein, D. C. (2011) · Cell · doi:10.1016/j.cell.2011.06.023 · Cited by 382 · see citing works
Self-citationDehay, B., Ramı́rez, A., Martínez‐Vicente, M., Perier, C., Canron, M., Doudnikoff, É., Vital, A., Vila, M., Klein, C., & Bézard, E. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1112368109 · Cited by 381 · see citing works
Complex Inhibitory Effects of Nitric Oxide on Autophagy
Sarkar, S., Korolchuk, V. I., Renna, M., Imarisio, S., Fleming, A., Williams, A. J., Garcı́a-Arencibia, M., Rose, C., Luo, S., Underwood, B. R., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.04.029 · Cited by 381 · see citing works
Self-citationA Dynamic Interface between Vacuoles and Mitochondria in Yeast
Elbaz‐Alon, Y., Rosenfeld-Gur, E., Shinder, V., Futerman, A. H., Geiger, T., & Schuldiner, M. (2014) · Developmental Cell · doi:10.1016/j.devcel.2014.06.007 · Cited by 377 · see citing works
Young, M. M., Takahashi, Y., Khan, O. A., Park, S., Hori, T., Yun, J. K., Sharma, A. K., Amin, S., Hu, C., Zhang, J., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.309104 · Cited by 372 · see citing works
An autophagy assay reveals the ESCRT-III component CHMP2A as a regulator of phagophore closure
Takahashi, Y., He, H., Tang, Z., Hattori, T., Liu, Y., Young, M. M., Serfass, J. M., Chen, L., Gebru, M. T., Chen, C., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-05254-w · Cited by 365 · see citing works
Neurodegenerative lysosomal disorders: A continuum from development to late age
Nixon, R. A., Yang, D.-S., & Lee, J.-H. (2008) · Autophagy · doi:10.4161/auto.6259 · Cited by 362 · see citing works
Self-citationLee, J.-H., McBrayer, M. K., Wolfe, D. M., Haslett, L. J., Kumar, A., Sato, Y., Lie, P. P. Y., Mohan, P., Coffey, E. E., Kompella, U., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.07.050 · Cited by 358 · see citing works
Self-citationPolyglutamine tracts regulate beclin 1-dependent autophagy
Ashkenazi, A., Bento, C. F., Ricketts, T., Vicinanza, M., Siddiqi, F., Pavel, M., Squitieri, F., Hardenberg, M. C., Imarisio, S., Menzies, F. M., et al. (2017) · Nature · doi:10.1038/nature22078 · Cited by 357 · see citing works
Self-citationAutophagy 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
Self-citationChaperone-mediated autophagy prevents collapse of the neuronal metastable proteome
Bourdenx, M., Martín-Segura, A., Scrivo, A., Rodriguez-Navarro, J. A., Kaushik, S., Tasset, I., Diaz, A., Storm, N. J., Xin, Q., Juste, Y. R., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.048 · Cited by 337 · see citing works
ATP13A2 deficiency disrupts lysosomal polyamine export
van Veen, S., Martin, S., den Haute, C. V., Benoy, V., Lyons, J. A., Vanhoutte, R., Kahler, J. P., Decuypere, J.-P., Gelders, G., Lambie, E. J., et al. (2020) · Nature · doi:10.1038/s41586-020-1968-7 · Cited by 335 · see citing works
Lysosomal cathepsins and their regulation in aging and neurodegeneration
Stoka, V., Turk, V., & Turk, B. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.04.010 · Cited by 334 · see citing works
Pasternak, S., Bagshaw, R. D., Guiral, M., Zhang, S., Ackerley, C. A., Pak, B. J., Callahan, J. W., & Mahuran, D. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304009200 · Cited by 316 · see citing works
A TRP Channel in the Lysosome Regulates Large Particle Phagocytosis via Focal Exocytosis
Samie, M., Wang, X., Zhang, X., Goschka, A., Li, X., Cheng, X., Gregg, E., Azar, M., Yue, Z., Garrity, A. G., et al. (2013) · Developmental Cell · doi:10.1016/j.devcel.2013.08.003 · Cited by 315 · see citing works
Henderson, M. X., Cornblath, E. J., Darwich, A., Zhang, B., Brown, H., Gathagan, R. J., Sandler, R. M., Bassett, D. S., Trojanowski, J. Q., & Lee, V. M. Y. (2019) · Nature Neuroscience · doi:10.1038/s41593-019-0457-5 · Cited by 310 · see citing works
Regulation of Organelle Acidity
Grabe, M., & OSTER, G. F. (2001) · The Journal of General Physiology · doi:10.1085/jgp.117.4.329 · Cited by 306 · see citing works
Marzia Perluigi, A., Domenico, F. D., & Butterfield, D. A. (2023) · Physiological Reviews · doi:10.1152/physrev.00030.2022 · Cited by 306 · see citing works
Deficiency of ATP13A2 Leads to Lysosomal Dysfunction, α-Synuclein Accumulation, and Neurotoxicity
Usenovic, M., Tresse, E., Mazzulli, J. R., Taylor, J. P., & Krainc, D. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.5575-11.2012 · Cited by 291 · see citing works
Jiang, Y., Mullaney, K. A., Peterhoff, C. M., Che, S., Schmidt, S. D., Boyer‐Boiteau, A., Ginsberg, S. D., Cataldo, A. M., Mathews, P. M., & Nixon, R. A. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908953107 · Cited by 288 · see citing works
Self-citationPICALM modulates autophagy activity and tau accumulation
Moreau, K., Fleming, A., Imarisio, S., Lopez Ramirez, A., Mercer, J. L., Jimenez-Sanchez, M., Bento, C. F., Puri, C., Zavodszky, E., Siddiqi, F., et al. (2014) · Nature Communications · doi:10.1038/ncomms5998 · Cited by 281 · see citing works
Self-citationNPC1 regulates ER contacts with endocytic organelles to mediate cholesterol egress
Höglinger, D., Burgoyne, T., Sánchez-Heras, E., Hartwig, P., Colaço, A., Newton, J. C., Futter, C. E., Spiegel, S., Platt, F. M., & Eden, E. R. (2019) · Nature Communications · doi:10.1038/s41467-019-12152-2 · Cited by 280 · see citing works
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
Self-citationSannerud, R., Esselens, C. W., Ejsmont, P., Mattera, R., Rochin, L., Tharkeshwar, A. K., Baets, G. D., Wever, V. D., Habets, R., Baert, V., et al. (2016) · Cell · doi:10.1016/j.cell.2016.05.020 · Cited by 279 · see citing works
D’Acunzo, P., Pérez‐González, R., Kim, Y., Hargash, T., Miller, C., Alldred, M. J., Erdjument‐Bromage, H., Penikalapati, S. C., Pawlik, M., Saito, M., et al. (2021) · Science Advances · doi:10.1126/sciadv.abe5085 · Cited by 276 · see citing works
Mitochondria are secreted in extracellular vesicles when lysosomal function is impaired
Liang, W., Sagar, S., Ravindran, R., Najor, R. H., Quiles, J. M., Chi, L., Diao, R. Y., Woodall, B. P., Leon, L. J., Zumaya, E., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-40680-5 · Cited by 273 · see citing works
Lysosomes as coordinators of cellular catabolism, metabolic signalling and organ physiology
Settembre, C., & Perera, R. M. (2023) · Nature reviews. Molecular cell biology · doi:10.1038/s41580-023-00676-x · Cited by 269 · see citing works
Amino Acid-Dependent mTORC1 Regulation by the Lysosomal Membrane Protein SLC38A9
Jung, J., Genau, H. M., & Behrends, C. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.00125-15 · Cited by 266 · see citing works
Direct interorganellar transfer of iron from endosome to mitochondrion
Sheftel, A. D., Zhang, A., Brown, C. M., Shirihai, O. S., & Ponka, P. (2007) · Blood · doi:10.1182/blood-2007-01-068148 · Cited by 266 · see citing works
Mutation of the parkinsonism gene ATP13A2 causes neuronal ceroid-lipofuscinosis
Brás, J., Verloès, A., Schneider, S. A., Mole, S., & Guerreiro, R. J. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds089 · Cited by 266 · see citing works
Lysosome trafficking and signaling in health and neurodegenerative diseases
Lie, P. P. Y., & Nixon, R. A. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.05.015 · Cited by 265 · see citing works
Self-citationVaillant-Beuchot, L., Mary, A., Pardossi-Piquard, R., Bourgeois, A., Lauritzen, I., Eysert, F., Kinoshita, P. F., Cazareth, J., Badot, C., Fragaki, K., et al. (2021) · Acta Neuropathologica · doi:10.1007/s00401-020-02234-7 · Cited by 263 · see citing works
Parkinson’s disease-risk protein TMEM175 is a proton-activated proton channel in lysosomes
Hu, M., Li, P., Wang, C., Feng, X., Geng, Q., Chen, W., Marthi, M., Zhang, W., Gao, C., Reid, W., et al. (2022) · Cell · doi:10.1016/j.cell.2022.05.021 · Cited by 254 · see citing works
Functional Modules of the Proteostasis NetworkPreprint
Jayaraj, G. G., Hipp, M. S., & Hartl, F. U. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a033951 · Cited by 249 · see citing works
Jinn, S., Drolet, R. E., Cramer, P. E., Wong, H. K., Toolan, D. M., Gretzula, C. A., Voleti, B., Vassileva, G., Disa, J., Tadin‐Strapps, M., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1616332114 · Cited by 245 · see citing works
The crucial impact of lysosomes in aging and longevity
Carmona‐Gutiérrez, D., Hughes, A. L., Madeo, F., & Ruckenstuhl, C. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.04.009 · Cited by 244 · see citing works
Cellular injury induced by oxidative stress is mediated through lysosomal damage
Öllinger, K., & Brunk, U. T. (1995) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(95)00062-3 · Cited by 243 · see citing works
Leucine Signals to mTORC1 via Its Metabolite Acetyl-Coenzyme A
Son, S. M., Park, S. J., Lee, H., Siddiqi, F. H., Lee, J. E., Menzies, F. M., & Rubinsztein, D. C. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.08.013 · Cited by 243 · see citing works
Self-citationFinch, N., Carrasquillo, M. M., Baker, M., Rutherford, N. J., Coppola, G., DeJesus-Hernandez, M., Crook, R., Hunter, T., Ghidoni, R., Benussi, L., et al. (2011) · Neurology · doi:10.1212/wnl.0b013e31820a0e3b · Cited by 243 · see citing works
Retromer in Alzheimer disease, Parkinson disease and other neurological disorders
Small, S. A., & Petsko, G. A. (2015) · Nature reviews. Neuroscience · doi:10.1038/nrn3896 · Cited by 235 · see citing works
TRP-ML1 Regulates Lysosomal pH and Acidic Lysosomal Lipid Hydrolytic Activity
Soyombo, A. A., Tjon‐Kon‐Sang, S., Rbaibi, Y., Bashllari, E., Bisceglia, J., Muallem, S., & Kiselyov, K. I. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508211200 · Cited by 235 · see citing works
A key role for MAM in mediating mitochondrial dysfunction in Alzheimer disease
Area-Gomez, E., de Groof, A., Bonilla, E., Montesinos, J., Tanji, K., Boldogh, I., Pon, L., & Schon, E. A. (2018) · Cell Death & Disease · doi:10.1038/s41419-017-0215-0 · Cited by 235 · see citing works
Logan, T., Simon, M. J., Rana, A., Cherf, G. M., Srivastava, A., Davis, S. S., Low, R. L. Y., Chiu, C.-L., Fang, M., Huang, F., et al. (2021) · Cell · doi:10.1016/j.cell.2021.08.002 · Cited by 233 · see citing works
Avrahami, L., Farfara, D., Shaham-Kol, M., Vassar, R. J., Frenkel, D., & Eldar-Finkelman, H. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.409250 · Cited by 232 · see citing works
TMEM175 Is an Organelle K+ Channel Regulating Lysosomal Function
Cang, C., Aranda, K., Seo, Y.-J., Gasnier, B., & Ren, D. (2015) · Cell · doi:10.1016/j.cell.2015.08.002 · Cited by 232 · see citing works
Deng, Z., Lim, J., Wang, Q., Purtell, K., Wu, S., Palomo, G. M., Tan, H., Manfredi, G., Zhao, Y., Peng, J., et al. (2019) · Autophagy · doi:10.1080/15548627.2019.1644076 · Cited by 232 · see citing works
LRRK2 mediates tubulation and vesicle sorting from lysosomes
Bonet-Ponce, L., Beilina, A., Williamson, C. D., Lindberg, E., Kluss, J. H., Saez-Atienzar, S., Landeck, N., Kumaran, R., Mamais, A., Bleck, C., et al. (2020) · Science Advances · doi:10.1126/sciadv.abb2454 · Cited by 230 · see citing works
Detection and Clearance of Damaged Lysosomes by the Endo-Lysosomal Damage Response and Lysophagy
Papadopoulos, C., & Meyer, H. (2017) · Current Biology · doi:10.1016/j.cub.2017.11.012 · Cited by 230 · cited 1× · see citing works
“LMP leading to a gradual lysosomal-associated cell death can be mediated by lysosomal hydrolase release directly 245,246 .”
Impaired lysosomal acidification triggers iron deficiency and inflammation in vivo
Yambire, K. F., Rostosky, C. M., Watanabe, T., Pacheu‐Grau, D., Torres-Odio, S., Sanchez-Guerrero, A., Senderovich, O., Meyron‐Holtz, E. G., Milošević, I., Frahm, J., et al. (2019) · eLife · doi:10.7554/elife.51031 · Cited by 229 · see citing works
Mutation in ATG5 reduces autophagy and leads to ataxia with developmental delay
Kim, M., Sandford, E., Gatica, D., Qiu, Y., Liu, X., Zheng, Y., Schulman, B. A., Xu, J., Semple, I., Ro, S.-H., et al. (2016) · eLife · doi:10.7554/elife.12245 · Cited by 225 · see citing works
Tian, Y., Bustos, V., Flajolet, M., & Greengard, P. (2011) · The FASEB Journal · doi:10.1096/fj.10-175158 · Cited by 224 · see citing works
Lauritzen, I., Pardossi-Piquard, R., Bourgeois, A., Pagnotta, S., Biferi, M.-G., Barkats, M., Lacor, P., Klein, W., Bauer, C., & Checler, F. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1577-6 · Cited by 219 · see citing works
Bourdenx, M., Daniel, J., Génin, E., Soria, F. N., Blanchard-Desce, M. H., Bézard, E., & Dehay, B. (2016) · Autophagy · doi:10.1080/15548627.2015.1136769 · Cited by 218 · see citing works
Zheng, Q., Chen, Y., Chen, D., Zhao, H., Feng, Y., Meng, Q., Zhao, Y. G., & Zhang, H. (2022) · Cell · doi:10.1016/j.cell.2022.09.001 · Cited by 214 · see citing works
Jin, L., Maezawa, I., Vincent, I. J., & Bird, T. D. (2004) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63185-9 · Cited by 212 · see citing works
The calpains in aging and aging-related diseases
Nixon, R. A. (2003) · Ageing Research Reviews · doi:10.1016/s1568-1637(03)00029-1 · Cited by 211 · see citing works
Self-citationAutophagic Stress in Neuronal Injury and Disease
Chu, C. T. (2006) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/01.jnen.0000229233.75253.be · Cited by 211 · cited 1× · see citing works
“This phenomenon, termed autophagic stress, reflects an imbalance favouring autophagosome production over the rate of clearance, and its effects on the severity of autophagic vacuole build-up varies in different diseases 241 .”
Regulation and function of V-ATPases in physiology and disease
Collins, M. P., & Forgac, M. D. (2020) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2020.183341 · Cited by 210 · see citing works
Autophagy in Neurodegenerative Diseases: A Hunter for Aggregates
Park, H., Kang, J., & Lee, S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21093369 · Cited by 209 · see citing works
Coen, K., Flannagan, R. S., Baron, S., Carraro-Lacroix, L. R., Wang, D., Vermeire, W., Michiels, C., Munck, S., Baert, V., Sugita, S., et al. (2012) · Journal of Cell Biology · doi:10.1083/jcb.201201076 · Cited by 208 · see citing works
Puri, C., Vicinanza, M., Ashkenazi, A., Gratian, M. J., Zhang, Q., Bento, C. F., Renna, M., Menzies, F. M., & Rubinsztein, D. C. (2018) · Developmental Cell · doi:10.1016/j.devcel.2018.03.008 · Cited by 206 · see citing works
Self-citationBrady, O. A., Zheng, Y., Murphy, K. A., Huang, M. J., & Hu, F. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds475 · Cited by 205 · see citing works
Autophagy enables microglia to engage amyloid plaques and prevents microglial senescence
Choi, I., Wang, M., Yoo, S., Xu, P., Seegobin, S. P., Li, X., Han, X., Wang, Q., Peng, J., Zhang, B., et al. (2023) · Nature Cell Biology · doi:10.1038/s41556-023-01158-0 · Cited by 202 · see citing works
Lauritzen, I., Pardossi-Piquard, R., Bauer, C., Brigham, E., Abraham, J.-D., Ranaldi, S., Fraser, P., St-George-Hyslop, P., Le Thuc, O., Espin, V., et al. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.2775-12.2012 · Cited by 201 · see citing works
Lipids on Trial: The Search for the Offending Metabolite in Niemann-Pick type C Disease
Lloyd‐Evans, E., & Platt, F. M. (2010) · Traffic · doi:10.1111/j.1600-0854.2010.01032.x · Cited by 199 · see citing works
Rosato, A. S., Montefusco, S., Soldati, C., Paola, S. D., Capuozzo, A., Monfregola, J., Polishchuk, E., Amabile, A., Grimm, C. M., Lombardo, A., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-13572-w · Cited by 199 · see citing works
Maetzel, D., Sarkar, S., Wang, H., Abi-Mosleh, L., Xu, P., Cheng, A. W., Gao, Q., Mitalipova, M., & Jaenisch, R. (2014) · Stem Cell Reports · doi:10.1016/j.stemcr.2014.03.014 · Cited by 195 · see citing works
Developmental Consequences of Defective ATG7-Mediated Autophagy in Humans
Collier, J. J., Guissart, C., Oláhová, M., Sasorith, S., Piron‐Prunier, F., Suomi, F., Zhang, D., Martinez-Lopez, N., Leboucq, N., Bahr, A., et al. (2021) · New England Journal of Medicine · doi:10.1056/nejmoa1915722 · Cited by 193 · see citing works
Fischer, P.-D. O. (2009) · Monatsschrift für Psychiatrie und Neurologie · doi:10.1159/000211873 · Cited by 186 · see citing works
Cruchaga, C., Graff, C., Chiang, H., Wang, J., Hinrichs, A. L., Spiegel, N., Bertelsen, S. E., Mayo, K., Norton, J. B., Morris, J. C., et al. (2011) · Archives of Neurology · doi:10.1001/archneurol.2010.350 · Cited by 186 · see citing works
LRRK2 activation controls the repair of damaged endomembranes in macrophages
Herbst, S., Campbell, P., Harvey, J., Bernard, E. M., Papayannopoulos, V., Wood, N. W., Morris, H. R., & Gutierrez, M. G. (2020) · The EMBO Journal · doi:10.15252/embj.2020104494 · Cited by 185 · see citing works
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
Lysosomal exocytosis and lipid storage disorders
Samie, M. A., & Xu, H. (2014) · Journal of Lipid Research · doi:10.1194/jlr.r046896 · Cited by 179 · see citing works
Congenital corneal clouding with abnormal systemic storage bodies: A new variant of mucolipidosis
Berman, E. R., Livni, N., Shapira, E., Merin, S., & Levij, I. S. (1974) · The Journal of Pediatrics · doi:10.1016/s0022-3476(74)80671-2 · Cited by 174 · see citing works
Chen, J. J., Nathaniel, D. L., Raghavan, P., Nelson, M., Tian, R., Tse, E., Hong, J. Y., See, S. K., Mok, S.-A., Hein, M. Y., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.009432 · Cited by 170 · see citing works
Roles of Oxidative Stress in Synaptic Dysfunction and Neuronal Cell Death in Alzheimer’s Disease
Plascencia‐Villa, G., & Perry, G. L. (2023) · Antioxidants · doi:10.3390/antiox12081628 · Cited by 167 · see citing works
Lysosomal Dysfunction in Down Syndrome Is APP-Dependent and Mediated by APP-βCTF (C99)
Jiang, Y., Sato, Y., Im, E., Berg, M., Bordi, M., Darji, S., Kumar, A., Mohan, P. S., Bandyopadhyay, U., Diaz, A., et al. (2019) · The Journal of Neuroscience · doi:10.1523/jneurosci.0578-19.2019 · Cited by 166 · see citing works
Self-citationThe FTLD risk factor TMEM106B and MAP6 control dendritic trafficking of lysosomes
Schwenk, B. M., Lang, C. M., Hogl, S., Tahirović, S., Orozco, D., Rentzsch, K., Lichtenthaler, S. F., Hoogenraad, C. C., Capell, A., Haass, C., et al. (2013) · The EMBO Journal · doi:10.1002/embj.201385857 · Cited by 165 · see citing works
The Role of Cathepsin D in the Pathogenesis of Human Neurodegenerative Disorders
Vidoni, C., Follo, C., Savino, M., Melone, M. A. B., & Isidoro, C. (2016) · Medicinal Research Reviews · doi:10.1002/med.21394 · Cited by 164 · see citing works
Lang, C. M., Fellerer, K., Schwenk, B. M., Kuhn, P., Kremmer, E., Edbauer, D., Capell, A., & Haass, C. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.365098 · Cited by 161 · see citing works
Klein, Z. A., Takahashi, H., Ma, M., Stagi, M., Zhou, M. S., Lam, T. T., & Strittmatter, S. M. (2017) · Neuron · doi:10.1016/j.neuron.2017.06.026 · Cited by 161 · see citing works
HMGB1 is involved in autophagy inhibition caused by SNCA/α-synuclein overexpression
Song, J., Lu, J., Liu, L., Chen, L., Durairajan, S. S. K., Yue, Z., Zhang, H., & Li, M. (2013) · Autophagy · doi:10.4161/auto.26751 · Cited by 160 · see citing works
NAADP: A Universal Ca 2+ Trigger
Guse, A. H., & Lee, H. C. (2008) · Science Signaling · doi:10.1126/scisignal.144re10 · Cited by 159 · see citing works
The Role of Iron in Beta Amyloid Toxicity
Schubert, D. A., & Chevion, M. (1995) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1995.2678 · Cited by 159 · see citing works
Ashraf, A., Clark, M., & So, P. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00065 · Cited by 158 · see citing works
Lysosomal LAMP proteins regulate lysosomal pH by direct inhibition of the TMEM175 channel
Zhang, J., Zeng, W., Han, Y., Lee, W.-R., Liou, J., & Jiang, Y. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.06.004 · Cited by 157 · see citing works
PLD3 affects axonal spheroids and network defects in Alzheimer’s disease
Yuan, P., Zhang, M., Tong, L., Morse, T. M., McDougal, R. A., Ding, H., Chan, D., Cai, Y., & Grutzendler, J. (2022) · Nature · doi:10.1038/s41586-022-05491-6 · Cited by 155 · see citing works
Bagh, M. B., Peng, S., Chandra, G., Zhang, Z., SINGH, S. P., Pattabiraman, N., Liu, A., & Mukherjee, A. B. (2017) · Nature Communications · doi:10.1038/ncomms14612 · Cited by 155 · see citing works
The aging lysosome: An essential catalyst for late-onset neurodegenerative diseases
Nixon, R. A. (2020) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2020.140443 · Cited by 149 · see citing works
Self-citationImpaired proteolysis underlies autophagic dysfunction in Niemann–Pick type C disease
Elrick, M. J., Yu, T., Chung, C., & Lieberman, A. P. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds324 · Cited by 148 · see citing works
Role and mechanism of ferroptosis in neurological diseases
Ou, M., Jiang, Y., Ji, Y., Zhou, Q., Du, Z., Zhu, H., & Zhou, Z. (2022) · Molecular Metabolism · doi:10.1016/j.molmet.2022.101502 · Cited by 148 · see citing works
Annunziata, I., Patterson, A., Helton, D., Hu, H., Moshiach, S., Gomero, E., Nixon, R., & d’Azzo, A. (2013) · Nature Communications · doi:10.1038/ncomms3734 · Cited by 146 · see citing works
Self-citationSchultheis, P. J., Fleming, S. M., Clippinger, A. K., Lewis, J. M., Tsunemi, T., Giasson, B. I., Dickson, D. W., Mazzulli, J. R., Bardgett, M. E., Haik, K. L., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt057 · Cited by 144 · see citing works
Endo-lysosomal dysfunction: a converging mechanism in neurodegenerative diseases
Wang, C., Telpoukhovskaia, M. A., Bahr, B. A., Chen, X., & Gan, L. (2017) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2017.09.005 · Cited by 144 · see citing works
Tamayev, R., Matsuda, S., Arancio, O., & D'Adamio, L. (2012) · EMBO Molecular Medicine · doi:10.1002/emmm.201100195 · Cited by 142 · see citing works
Regulation of lysosomal ion homeostasis by channels and transporters
Xiong, J., & Zhu, M. X. (2016) · Science China Life Sciences · doi:10.1007/s11427-016-5090-x · Cited by 141 · see citing works
Proteostasis and aging of stem cells
Vı́lchez, D., Simic, M., & Dillin, A. G. (2013) · Trends in Cell Biology · doi:10.1016/j.tcb.2013.09.002 · Cited by 140 · see citing works
Altered splicing of ATP6AP2 causes X-linked parkinsonism with spasticity (XPDS)
Korvatska, O., Strand, N. S., Berndt, J. D., Strovas, T., Chen, D.-H., Leverenz, J. B., Kiianitsa, K., Mata, I. F., Karakoc, E., Greenup, J. L., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt180 · Cited by 140 · see citing works
Reed, T. T., Pierce Jr., W. M., Turner, D. M., Markesbery, W. R., & Allan Butterfield, D. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00478.x · Cited by 135 · see citing works
Domenico, F. D., Coccia, R., Cocciolo, A., Murphy, M. P., Cenini, G., Head, E., Butterfield, D. A., Giorgi, A., Schininà, M. E., Mancuso, C., et al. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.04.013 · Cited by 133 · see citing works
Free radical damage, iron, and Alzheimer's disease
Smith, M. A., & Perry, G. L. (1995) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(95)00213-l · Cited by 130 · see citing works
Felodipine induces autophagy in mouse brains with pharmacokinetics amenable to repurposing
Siddiqi, F. H., Menzies, F. M., López, A., Stamatakou, E., Karabiyik, C., Ureshino, R. P., Ricketts, T., Jiménez-Sánchez, M., Esteban, M. A., Lai, L., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-09494-2 · Cited by 129 · see citing works
Self-citationMicroglial-to-neuronal CCR5 signaling regulates autophagy in neurodegeneration
Festa, B. P., Siddiqi, F. H., Jimenez-Sanchez, M., Won, H., Rob, M., Djajadikerta, A., Stamatakou, E., & Rubinsztein, D. C. (2023) · Neuron · doi:10.1016/j.neuron.2023.04.006 · Cited by 129 · see citing works
Self-citationFarias, F., Zeng, R., Johnson, G. S., Wininger, F. A., Taylor, J. F., Schnabel, R. D., McKay, S., Sanders, D. N., Lohi, H., Seppälä, E. H., et al. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.02.009 · Cited by 128 · see citing works
BACE1 and BACE2 enzymatic activities in Alzheimer’s disease
Ahmed, R. R., Holler, C. J., Webb, R. L., Li, F., Beckett, T. L., & Murphy, M. P. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06528.x · Cited by 127 · see citing works
Ubiquilins regulate autophagic flux through mTOR signalling and lysosomal acidification
Şentürk, M., Lin, G., Zuo, Z., Mao, D., Watson, E., Mikos, A. G., & Bellen, H. J. (2019) · Nature Cell Biology · doi:10.1038/s41556-019-0281-x · Cited by 124 · see citing works
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
A growth-factor-activated lysosomal K+ channel regulates Parkinson’s pathology
Wie, J., Liu, Z., Song, H., Tropea, T. F., Yang, L., Wang, H., Liang, Y., Cang, C., Aranda, K., Lohmann, J., et al. (2021) · Nature · doi:10.1038/s41586-021-03185-z · Cited by 120 · see citing works
Dynamic Organization of Endocytic Pathways in Axons of Cultured Sympathetic Neurons
Overly, C. C., & Hollenbeck, P. J. (1996) · Journal of Neuroscience · doi:10.1523/jneurosci.16-19-06056.1996 · Cited by 120 · see citing works
Intracellular amyloid and the neuronal origin of Alzheimer neuritic plaques
Pensalfini, A., Albay, R., Rasool, S., Wu, J. W., Hatami, A., Arai, H., Margol, L., Milton, S., Poon, W. W., Corrada, M. M., et al. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.07.011 · Cited by 120 · see citing works
Park, J., Mehta, P. M., Cooper, A. A., Veivers, D., Heimbach, A., Stiller, B., Kubisch, C., Fung, V. S. C., Krainc, D., Mackay‐Sim, A., et al. (2011) · Human Mutation · doi:10.1002/humu.21527 · Cited by 119 · see citing works
Leucine regulates autophagy via acetylation of the mTORC1 component raptor
Son, S. M., Park, S. J., Stamatakou, E., Vicinanza, M., Menzies, F. M., & Rubinsztein, D. C. (2020) · Nature Communications · doi:10.1038/s41467-020-16886-2 · Cited by 119 · see citing works
Self-citationCalpain inhibition mediates autophagy-dependent protection against polyglutamine toxicity
Menzies, F. M., Garcı́a-Arencibia, M., Imarisio, S., O’Sullivan, N. C., Ricketts, T., Kent, B. A., Rao, M. V., Lam, W., Green-Thompson, Z. W., Nixon, R. A., et al. (2014) · Cell Death and Differentiation · doi:10.1038/cdd.2014.151 · Cited by 117 · see citing works
Self-citationEriksson, I., Wäster, P., & Öllinger, K. M. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-2527-8 · Cited by 116 · see citing works
Yang, D.-S., Stavrides, P., Saito, M., Kumar, A., Rodriguez-Navarro, J. A., Pawlik, M., Huo, C., Walkley, S. U., Saito, M., Cuervo, A. M., et al. (2014) · Brain · doi:10.1093/brain/awu278 · Cited by 114 · see citing works
Self-citationDing, W., Ni, H., Gao, W., Chen, X., Kang, J. H., Stolz, D. B., Liu, J., & Yin, X. (2009) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-08-1169 · Cited by 114 · see citing works
Diepenbroek, M., Casadei, N., Esmer, H., Saido, T. C., Takano, J., Kahle, P. J., Nixon, R. A., Rao, M. V., Melki, R., Pieri, L., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu112 · Cited by 114 · see citing works
Self-citationMass spectrometry and redox proteomics: Applications in disease
Butterfield, D. A., Gu, L., Domenico, F. D., & Robinson, R. A. S. (2013) · Mass Spectrometry Reviews · doi:10.1002/mas.21374 · Cited by 113 · see citing works
D'Arcy, M. (2024) · APOPTOSIS · doi:10.1007/s10495-024-01977-y · Cited by 113 · see citing works
Butterfield, D. A., Domenico, F. D., Swomley, A. M., Head, E., & Marzia Perluigi, A. (2014) · Biochemical Journal · doi:10.1042/bj20140772 · Cited by 111 · see citing works
LRRK2 interacts with the vacuolar-type H+-ATPase pump a1 subunit to regulate lysosomal function
Wallings, R. L., Connor‐Robson, N., & Wade‐Martins, R. (2019) · Human Molecular Genetics · doi:10.1093/hmg/ddz088 · Cited by 110 · see citing works
Marzia Perluigi, A., Domenico, F. D., Giorgi, A., Schininà, M. E., Coccia, R., Cini, C., Bellia, F., Cambria, M. T., Cornelius, C., Butterfield, D. A., et al. (2010) · Journal of Neuroscience Research · doi:10.1002/jnr.22500 · Cited by 109 · see citing works
Sequential dynein effectors regulate axonal autophagosome motility in a maturation-dependent pathway
Cason, S. E., Carman, P. J., Duyne, C. V., Goldsmith, J., Domínguez, R., & Holzbaur, E. L. F. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.202010179 · Cited by 108 · see citing works
The Endolysosomal System and Proteostasis: From Development to Degeneration
Winckler, B., Faúndez, V., Maday, S., Cai, Q., Almeida, C. G., & Zhang, H. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.1665-18.2018 · Cited by 105 · see citing works
Goldsmith, J., Ordureau, A., Harper, J. W., & Holzbaur, E. L. F. (2022) · Neuron · doi:10.1016/j.neuron.2021.12.029 · Cited by 105 · see citing works
The role of lysosome in regulated necrosis
Alu, A., Han, X., Ma, X., Wu, M., Wei, Y., & Wei, X. (2020) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2020.07.003 · Cited by 104 · see citing works
Bodzęta, A., Kahms, M., & Klingauf, J. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.07.040 · Cited by 103 · see citing works
Genetic, Structural, and Functional Evidence Link TMEM175 to Synucleinopathies
Krohn, L., Öztürk, T. N., Vanderperre, B., Bencheikh, B. O. A., Ruskey, J. A., Laurent, S. B., Spiegelman, D., Postuma, R. B., Arnulf, I., Hu, M. T. M., et al. (2019) · Annals of Neurology · doi:10.1002/ana.25629 · Cited by 103 · see citing works
Polyamines in Parkinson's Disease: Balancing Between Neurotoxicity and Neuroprotection
Vrijsen, S., Houdou, M., Cascalho, A. C. C., Eggermont, J., & Vangheluwe, P. (2023) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-071322-021330 · Cited by 100 · see citing works
Rao, M. V., McBrayer, M. K., Campbell, J., Kumar, A., Hashim, A. T., Sershen, H. W., Stavrides, P. H., Ohno, M., Hutton, M., & Nixon, R. A. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.1132-14.2014 · Cited by 99 · see citing works
Self-citation
Flagged first, then by citations
Research works printed but not linked: 5
- [16]Lees MB Basic Neurochemistry 5th edn, Vol. 39 (Raven Press, 1994).
- [87]de Duve C. Lysosomes, a New Group of Cytoplasmic Particle (Ronald Press, 1959).
- [102]Wang S. Metabolism. Lysosomal amino acid transporter SLC38A9 signals arginine sufficiency to mTORC1. Science 347, 188– 194 (2015). 25567906 PMC4295826
- [125]Chou CC Proteostasis and lysosomal quality control deficits in Alzheimer’s disease neurons. Preprint at bioRxiv 10.1101/2023.03.27.534444 (2023). · DOI
- [191]Guse AH & Lee HC NAADP: a universal Ca2+ trigger. Sci. Signal 1, re10 (2008). 18984909
Cited by
Sorted by citations
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Nixon, R. A. (2024) · Acta Neuropathologica · doi:10.1007/s00401-024-02799-7 · Cited by 117 · see citing works
Self-citationLiu, T., Kong, X., Qiao, J., & Wei, J. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103787 · Cited by 108 · see citing works
Lipid metabolism, remodelling and intercellular transfer in the CNS
Vanherle, S., Loix, M., Miron, V. E., Hendriks, J. J. A., & Bogie, J. F. J. (2025) · Nature reviews. Neuroscience · doi:10.1038/s41583-025-00908-3 · Cited by 90 · see citing works
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Zhu, Y., Fujimaki, M., & Rubinsztein, D. C. (2025) · Trends in Cell Biology · doi:10.1016/j.tcb.2025.01.005 · Cited by 63 · see citing works
Self-citationGao, L., Wang, J., & Bi, Y. (2025) · International Journal of Nanomedicine · doi:10.2147/ijn.s549893 · Cited by 52 · see citing works
“166,167 A recent study developed a TPP-functionalized MoS 2 nanocomposite system with catalase and superoxide dismutase mimetic activities, which effectively scavenged ROS in AD models.”
Shang, H., Dai, X., Chen, J., Xing, C., Gao, X., Cao, H., Hu, G., Li, H., Hu, M., & Yang, F. (2025) · Journal of Animal Science and Biotechnology/Journal of animal science and biotechnology · doi:10.1186/s40104-025-01255-0 · Cited by 48 · see citing works
Neuronal autophagy in the control of synapse function
Karpova, A., Hiesinger, P. R., Kuijpers, M., Albrecht, A., Kirstein, J., Andres‐Alonso, M., Biermeier, A. J., Eickholt, B. J., Mikhaylova, M., Maglione, M., et al. (2025) · Neuron · doi:10.1016/j.neuron.2025.01.019 · Cited by 46 · see citing works
Wu, Y., Li, Z., Ding, T., Yang, Y., Wei, C., Zhang, S., & Fan, X. (2025) · Ageing Research Reviews · doi:10.1016/j.arr.2025.102842 · Cited by 40 · see citing works
Exploring Stressors: Impact on Cellular Organelles and Implications for Cellular Functions
Zayani, Z., Matinahmadi, A., Tavakolpournegari, A., & Bidooki, S. H. (2025) · Stresses · doi:10.3390/stresses5020026 · Cited by 34 · see citing works
N7-methylguanosine modification in cancers: from mechanisms to therapeutic potential
Wu, Q., Fu, X., Liu, G., He, X., Li, Y., & Ou, C. (2025) · Journal of Hematology & Oncology · doi:10.1186/s13045-025-01665-7 · Cited by 29 · see citing works
Goel, F. (2025) · Inflammopharmacology · doi:10.1007/s10787-025-01794-y · Cited by 29 · see citing works
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Yi, Y., Jia, P., Xie, P., Peng, X., Zhu, X., Yin, S., Luo, Y., Deng, Y., & Wan, L. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1683876 · Cited by 28 · see citing works
Yu, G., Zhao, J., Zhu, X.-X., Yang, N., Lou, J., Chen, Z., Zhang, H., Chaire, T., Gao, W., Cai, Y., et al. (2026) · International Journal of Surgery · doi:10.1097/js9.0000000000004619 · Cited by 27 · see citing works
Tangavelou, K., & Bhaskar, K. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252212335 · Cited by 24 · see citing works
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Hamzehlouy, A., Dare, M. T., Shahi, F., Dawi, E. A., & Khonakdar, H. A. (2024) · Polymers for Advanced Technologies · doi:10.1002/pat.70008 · Cited by 24 · see citing works
Li, M., Chen, S., Guo, R., Wang, Y., Yang, M., Liu, Y., Zhang, Q., Zhu, S., Li, J., Chen, F., et al. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02453-y · Cited by 23 · see citing works
Ghoochani, A., Heiby, J. C., Rawat, E. S., Medoh, U. N., Fraia, D. D., Dong, W., Gastou, M., Rastogi, M., Hernandez, V., Nyame, K., et al. (2026) · Cell · doi:10.1016/j.cell.2025.12.012 · Cited by 22 · see citing works
Lu, J., Florio, D. N. D., Boya, P., Maday, S., Springer, W., & Chu, C. T. (2025) · Autophagy · doi:10.1080/15548627.2025.2581217 · Cited by 21 · see citing works
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Xu, Y.-Q., Chen, Y., Xing, J., & Yao, J. (2025) · Clinical Epigenetics · doi:10.1186/s13148-025-01820-4 · Cited by 20 · see citing works
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Angst, G., Jia, N., Esqueda, L. T., Fan, Y., Cai, Q., & Wang, C. (2025) · Autophagy Reports · doi:10.1080/27694127.2025.2471677 · Cited by 19 · see citing works
Kutchukian, C., Casas, M., Dixon, R. E., & Dickson, E. J. (2025) · Nature Communications · doi:10.1038/s41467-025-65798-6 · Cited by 18 · see citing works
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Ahmadi, S., Khaledi, S., Ahmadi, K., & Hassanzadeh, K. (2025) · CNS Neuroscience & Therapeutics · doi:10.1002/cns.70688 · Cited by 18 · see citing works
Adlimoghaddam, A., Fayazbakhsh, F., Mohammadi, M., Babaei, Z., Behrooz, A. B., Tabasi, F., Guan, T., Beheshti, I., Aghaei, M., Klionsky, D. J., et al. (2025) · Cell Death Discovery · doi:10.1038/s41420-025-02490-0 · Cited by 17 · see citing works
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Guan, Z.-Y., Li, W.-D., He, Y.-T., & Guo, W.-Z. (2025) · Oncogenesis · doi:10.1038/s41389-025-00587-w · Cited by 16 · see citing works
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Self-citationQiao, Q., Song, A., Jiang, G., Zhou, Y., Ruan, Y., Jia, W., Liu, X., & Xu, Z. (2025) · Angewandte Chemie International Edition · doi:10.1002/anie.202503177 · Cited by 14 · see citing works
Lee, A., Ma, Y., Yu, L., Dawe, R. J., Aubin, C., Arfanakis, K., Mayeux, R. P., Bennett, D. A. A., Klein, H., & Jager, P. L. D. (2026) · iScience · doi:10.1016/j.isci.2026.117038 · Cited by 14 · see citing works
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Ge, R., Chen, M., Li, Q., Liu, M., Zhou, J., & Xie, S. (2025) · Acta Pharmacologica Sinica · doi:10.1038/s41401-025-01538-2 · Cited by 13 · see citing works
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Liang, J., Li, R., Wong, G., & Huang, X. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00879-0 · Cited by 13 · see citing works
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Progress in precision drug delivery systems for neurodegenerative diseases with muscle atrophy
Zhang, G., Hu, F., Zhang, Y., Li, D., Deng, Y., Yang, M., Huang, T., Deng, X., Li, Y., Fu, C., et al. (2026) · Neuropharmacology · doi:10.1016/j.neuropharm.2026.111027 · Cited by 12 · see citing works
Zheng, S., Zhu, J., Wang, C., Wu, Y., Sun, S., Guo, H., Chang, Y., Ma, R., & Li, G. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-024-01872-8 · Cited by 12 · see citing works
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Li, S., Zhou, X., Duan, Q., Niu, S., Li, P., Feng, Y., Zhang, Y., Xu, X., Gong, S., & Cao, H. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26073252 · Cited by 11 · see citing works
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 · see citing works
Hao, Y., Fan, X., Huang, X.-Y., Li, Z., Jing, Z., Zhang, G., Xu, Y., Zhang, N., & Wei, P. (2025) · Biomolecules · doi:10.3390/biom15050728 · Cited by 11 · see citing works
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Santana-Martínez, R. A., McWhirt, J., & Brewer, G. J. (2025) · GeroScience · doi:10.1007/s11357-025-01786-4 · Cited by 11 · see citing works
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Lo, C. H., Cheong, L. Y. T., & Zeng, J. (2025) · Nanomaterials · doi:10.3390/nano15100704 · Cited by 10 · see citing works
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Cui, J., & Cui, Z. (2025) · Discover Neuroscience · doi:10.1186/s13064-025-00210-z · Cited by 10 · see citing works
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Qin, X., Zhang, Y., Wang, Y., Zhang, Y., Jing, J., Zhang, Y., Xu, G., Teng, H., Wang, T., Fu, L., et al. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf996 · Cited by 10 · see citing works
Xu, W., Hu, P., Wang, J., Jiang, H., Wang, T., Liu, J., & Li, H. (2024) · Biomolecules · doi:10.3390/biom14121552 · Cited by 9 · see citing works
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Self-citationAdvances in autophagy for Parkinson’s disease pathogenesis and treatment
Zhang, X., Zhang, H., Dong, J., Cai, H., & Le, W. (2025) · Ageing and Neurodegenerative Diseases · doi:10.20517/and.2024.33 · Cited by 9 · see citing works
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Wang, L., Jia, J., Yu, X., Luo, M., Li, J., Khan, G. J., He, C., Duan, H. Q., & Zhai, K. (2025) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2025.151819 · Cited by 9 · see citing works
Kim, E.-H., Baek, S. M., Kim, D., Choi, S., Kim, W., Bian, Y., Tahmasebi, S., & Bae, O. (2025) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2025.118528 · Cited by 9 · see citing works
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Liu, T., Wu, H., & Wei, J. (2025) · Neuroscience Bulletin · doi:10.1007/s12264-025-01439-8 · Cited by 9 · see citing works
He, H., Ai, R., Fang, E. F., & Palikaras, K. (2025) · npj Aging · doi:10.1038/s41514-025-00257-6 · Cited by 9 · see citing works
Mirfakhar, F. S., Marsh, J. A., Sato, C., Schache, K. J., Minaya, M., Dolle, R. E., Pak, S. C., Silverman, G. A., Perlmutter, D. H., Macauley, S. L., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-70473-5 · Cited by 9 · see citing works
Denus, M., Filaquier, A., Fargues, W., Néel, É., Stewart, S. E., Colladant, M., Curel, T., Mezghrani, A., Marin, P., Claeysen, S., et al. (2025) · Traffic · doi:10.1111/tra.70009 · Cited by 8 · see citing works
Self-citationLiu, Y., Jian, Y., Xiong, M., Zhang, D., Yang, M., & Li, K. (2025) · Analytical Chemistry · doi:10.1021/acs.analchem.4c05844 · Cited by 8 · see citing works
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Zheng, Y., Li, M., Chen, X., Zheng, Z., Chen, Z., Tian, R., & Zhao, Y. G. (2025) · The Journal of Cell Biology · doi:10.1083/jcb.202501007 · Cited by 8 · see citing works
Wei, M., Li, W., Bao, G., Yang, Z., Li, S., & Le, W. (2025) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2025.118918 · Cited by 8 · see citing works
Liu, Y., Zhang, J., Tang, L., Yang, J., Hao, L., Lou, F., & Su, J. (2025) · Archives of Toxicology · doi:10.1007/s00204-025-04174-1 · Cited by 8 · see citing works
Lee, J. H., Chang, W. S., Min, S. S., Song, D., & Yoo, H. (2025) · Cells · doi:10.3390/cells14171342 · Cited by 8 · see citing works
Yuan, M., Nguyen, T. T. T., Gibb, A. J., Xian, Y., & Xu, H. (2025) · Chinese Medicine · doi:10.1186/s13020-025-01204-z · Cited by 8 · see citing works
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Wang, L., Luo, Y., Chen, X., Wang, Y., & Zhang, Y. (2025) · MedComm – Oncology · doi:10.1002/mog2.70041 · Cited by 8 · see citing works
Zhong, R., & Richardson, C. E. (2025) · PLoS Biology · doi:10.1371/journal.pbio.3002957 · Cited by 8 · see citing works
Autophagy–NAD+ axis: emerging insights into neuronal homeostasis and neurodegenerative diseases
Koçak, G., Dimas, M. M., Silva, L., Silva-Amaral, D., Sun, C., Cruddas, S., Barrett, T. G., Martins‐de‐Souza, D., Cunha‐Neto, E., Brocardo, P. S., et al. (2025) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2025.1695486 · Cited by 8 · see citing works
Maintenance and Decline of Neuronal Lysosomal Function in Aging
Zhong, R., & Richardson, C. E. (2025) · Cells · doi:10.3390/cells14241976 · Cited by 8 · see citing works
Dong, Y., Xiao, X., Zhuang, X., Wu, W., Wang, Z.-Y., Zhang, S., Li, J.-T., Zhang, K., Fu, W.-Y., Chen, J., et al. (2026) · Nature Biomedical Engineering · doi:10.1038/s41551-026-01667-x · Cited by 8 · see citing works
Ashkavand, Z., Ryan, K. C., Laboy, J. T., Patel, R., Geller, B., & Norman, K. R. (2025) · Neurobiology of Disease · doi:10.1016/j.nbd.2025.106961 · Cited by 7 · see citing works
Research trends of piezoelectric materials in neurodegenerative disease applications
Wang, X., Sun, Y., Han, C., Meng, X., Wen, K., Wu, J., Min, P., Li, K., & Zhang, Y. (2025) · Bioactive Materials · doi:10.1016/j.bioactmat.2025.06.022 · Cited by 7 · see citing works
ATG16L1 membrane recruitment in autophagy
Wei, F., Qin, N., Chen, Y., Liu, Z., Zhao, X., Yu, X., Feng, Z., Wang, Y., Yang, A., & Cui, H. (2025) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2025.2521321 · Cited by 7 · see citing works
Arnsten, A. F. T., Perone, I., Wang, M., Yang, S., Uchendu, S., Bolat, D., & Datta, D. (2025) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2025.1610350 · Cited by 7 · see citing works
Wang, Y., Luo, Y., Zhou, F., & Li, D. (2025) · Cellular Signalling · doi:10.1016/j.cellsig.2025.112322 · Cited by 7 · see citing works
Lysosome: a critical hub for ferroptosis regulation
Chen, X. (2026) · Trends in Cell Biology · doi:10.1016/j.tcb.2026.03.007 · Cited by 7 · see citing works
Intralysosomal Amyloidogenesis and Proximity Labeling by Cathepsin CPreprint
Elias, R. D., Allen, S., Demiralp, I. I., O'Neill, R. T., Schäfer, J.-H., Siems, H., Montabana, E. A., Ermel, U. H., Ash, C. T., Abdurrob, F., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.12.23.696283 · Cited by 7 · see citing works
Liu, C., Li, X., Chen, M., Liu, Y., Li, K., Wang, D., Yang, Z., Guo, Y., Zhao, Y., Zhao, H., et al. (2025) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2025.119481 · Cited by 6 · see citing works
Luo, Y., Zhang, K., Mao, L., Tan, M., Dong, X., Li, N., Zhou, Y., Chen, C., Zou, Z., & Zhang, J. (2025) · Toxicology · doi:10.1016/j.tox.2025.154101 · Cited by 6 · see citing works
Fourrière, L., & Gleeson, P. A. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1550211 · Cited by 6 · see citing works
BDNF Alleviates Noise-Induced Cochlear Synaptopathy Through Inhibition of Autophagy
Wang, F., Yu, Q., Luo, Y., Guo, R., Wu, L., Song, X., Yang, L., Li, S., Liu, K., & Jiang, X. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-05165-0 · Cited by 6 · see citing works
Luo, W.-C., Zhang, J., Bao, L.-N., Yang, L.-J., Yang, Z.-K., Jiang, M., Yu, X., & Li, X. (2025) · Chemical Engineering Journal · doi:10.1016/j.cej.2025.167986 · Cited by 6 · see citing works
ALDH2 in autophagy and cell death: molecular mechanisms and implications for diseases
Duan, Y., Shan, Z.-C., Pang, J., & Chen, Y. (2025) · Military Medical Research · doi:10.1186/s40779-025-00646-8 · Cited by 6 · see citing works
Xia, Y., Zheng, M., Li, X., Song, K., & Teng, Z. (2025) · iScience · doi:10.1016/j.isci.2025.113526 · Cited by 6 · see citing works
Gu, Y., Hao, M., Wang, L., Alimujiang, A., Gao, J., Ji, W., Xu, W., Xiong, R., Zhang, J., & Yin, Y. (2025) · Nanomedicine · doi:10.1080/17435889.2025.2588421 · Cited by 6 · see citing works
Lin, A., Dai, X., Chen, J., Han, T., Du, Q., Wu, M., Cheng, J., Chen, W., Ye, Q.-Y., Chen, X., et al. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70919 · Cited by 6 · see citing works
The interplay between autophagy and unconventional secretion in neurodegeneration
Renna, M., Bonavita, R., Dixon, G., Verdicchio, L. V., & Fleming, A. (2026) · Cell chemical biology · doi:10.1016/j.chembiol.2025.12.007 · Cited by 6 · see citing works
Wang, D., Li, M., Ma, J., Du, G., Zhou, J., Chen, J., & Guan, X. (2026) · Journal of Advanced Research · doi:10.1016/j.jare.2026.01.065 · Cited by 6 · see citing works
Mandal, N., Das, A., & Datta, R. (2025) · Neurobiology of Disease · doi:10.1016/j.nbd.2025.106825 · Cited by 6 · see citing works
Chen, D., Fasina, O. B., Lin, J., Zeng, J., Manzoor, M., Ohno, H., Xiang, L., & Qi, J. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26062804 · Cited by 6 · see citing works
Barmaki, H., Nourazarian, A., Yousefi, H., Khalilnezhad, A., Shahriyari, E., & Khaki‐Khatibi, F. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-05008-y · Cited by 6 · see citing works
Gene-modified animal models of Parkinson's disease
Peng, Y., Jiang, D., Yao, S., Zhang, X., Sugimoto, K., Liu, J. –., Du, M., Lin, L.-Y., Chen, Q., & Hong, J. (2025) · Experimental Neurology · doi:10.1016/j.expneurol.2025.115287 · Cited by 6 · see citing works
A multi-omics-empowered framework for precision diagnosis and treatment of lysosomal diseases
Yen, N. T. H., Tien, N. T. N., Thu, N. Q., Ducatez, F., Mauhin, W., Lidove, O., Bekri, S., Tebani, A., & Long, N. P. (2025) · Journal of Pharmaceutical Analysis · doi:10.1016/j.jpha.2025.101274 · Cited by 5 · see citing works
Alshahrani, S. M., Al-Kuraishy, H. M., Al-Gareeb, A. I., Albuhadily, A. K., Fawzy, M. N., Kadasah, S. F., Alruwaili, M., Papadakis, M., Alexiou, A. T., & Batiha, G. E. (2025) · Neuropharmacology · doi:10.1016/j.neuropharm.2025.110555 · Cited by 5 · see citing works
The Janus face of CaMKII: from memory consolidation to neurotoxic switch in Alzheimer’s disease
Tang, L., Liu, F., Sun, X., Yang, J., Liu, Y., Pan, X., Hao, L., Lou, F., & Su, J. (2025) · Archives of Toxicology · doi:10.1007/s00204-025-04160-7 · Cited by 5 · see citing works
Riva, A., Volpedo, G., Zara, F., Fassio, A., Striano, P., & Falace, A. (2025) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-025-01453-3 · Cited by 5 · see citing works
Sena, P. P., Friedrich, L., Villarreal, A. E., Fath, F., Sopco, L., Hernández‐Guillamón, M., Pereira, M. L. S., Britton, G. B., Weber, J. J., & Schmidt, T. (2025) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2025.1681079 · Cited by 5 · see citing works
Timosaponin B-II attenuates cerebral ischemia injury by enhancing Parkin-mediated mitophagy
Liu, Y., Shang, H., Zhang, L., Fu, R., Li, Y., Wang, Z., Zhen, Y., Zhang, Q., Zhao, Y., Wang, G., et al. (2025) · Phytomedicine · doi:10.1016/j.phymed.2025.157580 · Cited by 5 · see citing works
Martín-Rico, M., Salgado, B., Beamonte, I., Sastre, I., Bullido, M. J., & Aldudo, J. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27020642 · Cited by 5 · see citing works
- 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 · 2021: 1
- 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
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Health Sciences › Medicine › Physiology › 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
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