Mutant glucocerebrosidase impairs α-synuclein degradation by blockade of chaperone-mediated autophagy

Integrating single-cell transcriptomic data across different conditions, technologies, and species

Butler, A., Hoffman, P., Smibert, P., Papalexi, E., & Satija, R. (2018) · Nature Biotechnology · doi:10.1038/nbt.4096 · Cited by 13,174 · see citing works

Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition).

Klionsky, D. J., Abdelmohsen, K., Abe, A., Abedin, M. J., Abeliovich, H., Acevedo Arozena, A., Adachi, H., Adams, C. M., Adams, P. D., Adeli, K., et al. (2016) · Autophagy · doi:10.1080/15548627.2015.1100356 · Cited by 5,894 · see citing works

Identification of novel risk loci, causal insights, and heritable risk for Parkinson's disease: a meta-analysis of genome-wide association studies

Nalls, M. A., Blauwendraat, C., Vallerga, C. L., Heilbron, K., Bandres-Ciga, S., Chang, D., Tan, M., Kia, D. A., Noyce, A. J., Xue, A., et al. (2019) · The Lancet Neurology · doi:10.1016/s1474-4422(19)30320-5 · Cited by 2,454 · see citing works

Multicenter Analysis of Glucocerebrosidase Mutations in Parkinson's Disease

Sidransky, E., Nalls, M. A., Aasly, J. O., Aharon-Peretz, J., Annesi, G., Barbosa, E. R., Bar-Shira, A., Berg, D., Bras, J., Brice, A., et al. (2009) · New England Journal of Medicine · doi:10.1056/nejmoa0901281 · Cited by 2,135 · see citing works

Impaired Degradation of Mutant α-Synuclein by Chaperone-Mediated Autophagy

Cuervo, A. M., Stefanis, L., Fredenburg, R., Lansbury, P. T., & Sulzer, D. (2004) · Science · doi:10.1126/science.1101738 · Cited by 2,024 · see citing works

Gaucher disease glucocerebrosidase and α-synuclein form a bidirectional pathogenic loop in synucleinopathies

Mazzulli, J. R., Xu, Y.-H., Sun, Y., Knight, A. L., McLean, P. J., Caldwell, G. A., Sidransky, E., Grabowski, G. A., & Krainc, D. (2011) · Cell · doi:10.1016/j.cell.2011.06.001 · Cited by 1,341 · see citing works

Massively parallel single-nucleus RNA-seq with DroNc-seq

Habib, N., Avraham-Davidi, I., Basu, A., Burks, T., Shekhar, K., Hofree, M., Choudhury, S. R., Aguet, F., Gelfand, E., Ardlie, K., et al. (2017) · Nature Methods · doi:10.1038/nmeth.4407 · Cited by 1,069 · see citing works

Integrative single-cell analysis of transcriptional and epigenetic states in the human adult brain

Lake, B. B., Chen, S., Sos, B. C., Fan, J., Kaeser, G. E., Yung, Y. C., Duong, T. E., Gao, D., Chun, J., Kharchenko, P. V., et al. (2018) · Nature Biotechnology · doi:10.1038/nbt.4038 · Cited by 983 · see citing works

A single-cell atlas of entorhinal cortex from individuals with Alzheimer’s disease reveals cell-type-specific gene expression regulation

Grubman, A., Chew, G., Ouyang, J. F., Sun, G., Choo, X. Y., McLean, C., Simmons, R. K., Buckberry, S., Vargas-Landin, D. B., Poppe, D., et al. (2019) · Nature Neuroscience · doi:10.1038/s41593-019-0539-4 · Cited by 956 · see citing works

Dopamine oxidation mediates mitochondrial and lysosomal dysfunction in Parkinson’s disease

Burbulla, L. F., Song, P., Mazzulli, J. R., Zampese, E., Wong, Y. C., Jeon, S., Santos, D. P., Blanz, J., Obermaier, C. D., Strojny, C., et al. (2017) · Science · doi:10.1126/science.aam9080 · Cited by 874 · see citing works

Age-related decline in chaperone-mediated autophagy

Cuervo, A. M., & Dice, J. F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002102200 · Cited by 665 · see citing works

MULTI-seq: sample multiplexing for single-cell RNA sequencing using lipid-tagged indices

McGinnis, C. S., Patterson, D. M., Winkler, J., Conrad, D. N., Hein, M. Y., Srivastava, V., Hu, J. L., Murrow, L. M., Weissman, J. S., Werb, Z., et al. (2019) · Nature Methods · doi:10.1038/s41592-019-0433-8 · Cited by 643 · see citing works

Dopamine-modified α-synuclein blocks chaperone-mediated autophagy

Martínez‐Vicente, M., Tallóczy, Z., Kaushik, S., Massey, A. C., Mazzulli, J. R., Mosharov, E. V., Hodara, R., Fredenburg, R. A., Wu, D.-C., Follenzi, A., et al. (2008) · Journal of Clinical Investigation · doi:10.1172/jci32806 · Cited by 633 · see citing works

Tau fragmentation, aggregation and clearance: the dual role of lysosomal processing

Wang, Y., Martinez-Vicente, M., Krüger, U., Kaushik, S., Wong, E., Mandelkow, E.-M., Cuervo, A. M., & Mandelkow, E. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp367 · Cited by 617 · see citing works

Interplay of LRRK2 with chaperone-mediated autophagy

Orenstein, S. J., Kuo, S.-H., Tasset, I., Arias, E., Koga, H., Fernandez-Carasa, I., Cortes, E., Honig, L. S., Dauer, W., Consiglio, A., et al. (2013) · Nature Neuroscience · doi:10.1038/nn.3350 · Cited by 588 · see citing works

The Chaperone-Mediated Autophagy Receptor Organizes in Dynamic Protein Complexes at the Lysosomal Membrane

Bandyopadhyay, U., Kaushik, S., Varticovski, L., & Cuervo, A. M. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.02070-07 · Cited by 562 · see citing works

[16] Isolation of subcellular organelles

Storrie, B., & Amadden, E. (1990) · Methods in Enzymology · doi:10.1016/0076-6879(90)82018-w · Cited by 555 · see citing works

Interplay between Cytosolic Dopamine, Calcium, and α-Synuclein Causes Selective Death of Substantia Nigra Neurons

Mosharov, E. V., Larsen, K. E., Kanter, E., Phillips, K. A., Wilson, K., Schmitz, Y., Krantz, D. E., Kobayashi, K., Edwards, R. H., & Sulzer, D. L. (2009) · Neuron · doi:10.1016/j.neuron.2009.01.033 · Cited by 530 · see citing works

Chaperone-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

ER retention and degradation as the molecular basis underlying Gaucher disease heterogeneity

Ron, I., & Horowitz, M. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi240 · Cited by 331 · see citing works

CNS expression of glucocerebrosidase corrects α-synuclein pathology and memory in a mouse model of Gaucher-related synucleinopathy

Sardi, S. P., Clarke, J. L., Kinnecom, C., Tamsett, T. J., Li, L., Stanek, L. M., Passini, M. A., Grabowski, G. A., Schlossmacher, M. G., Sidman, R. L., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1108197108 · Cited by 319 · see citing works

Acid β‐glucosidase mutants linked to gaucher disease, parkinson disease, and lewy body dementia alter α‐synuclein processing

Cullen, V., Sardi, S. P., Ng, J., Xu, Y., Sun, Y., Tomlinson, J. J., Kolodziej, P., Kahn, I. L., Säftig, P., Woulfe, J., et al. (2011) · Annals of Neurology · doi:10.1002/ana.22400 · Cited by 303 · see citing works

DAPAR & ProStaR: software to perform statistical analyses in quantitative discovery proteomics

Wieczorek, S., Combes, F., Lazar, C., Gianetto, Q. G., Gatto, L., Dorffer, A., Hesse, A.-M., Couté, Y., Ferro, M., Bruley, C., et al. (2016) · Bioinform. · doi:10.1093/bioinformatics/btw580 · Cited by 286 · see citing works

VPS35 in Dopamine Neurons Is Required for Endosome-to-Golgi Retrieval of Lamp2a, a Receptor of Chaperone-Mediated Autophagy That Is Critical for  -Synuclein Degradation and Prevention of Pathogenesis of Parkinson's Disease

Tang, F.-L., Erion, J. R., Tian, Y., Liu, W., Yin, D.-M., Ye, J., Tang, B., Mei, L., & Xiong, W.-C. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.0042-15.2015 · Cited by 269 · see citing works

Proteome-wide analysis of chaperone-mediated autophagy targeting motifs

Kirchner, P., Bourdenx, M., Madrigal-Matute, J., Tiano, S., Diaz, A., Bartholdy, B. A., Will, B., & Cuervo, A. M. (2019) · PLOS Biology · doi:10.1371/journal.pbio.3000301 · Cited by 257 · see citing works

Augmenting CNS glucocerebrosidase activity as a therapeutic strategy for parkinsonism and other Gaucher-related synucleinopathies

Sardi, S. P., Clarke, J. L., Viel, C., Chan, M., Tamsett, T. J., Treleaven, C. M., Bu, J., Sweet, L., Passini, M. A., Dodge, J. C., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1220464110 · Cited by 252 · see citing works

Aberrant Interaction between Parkinson Disease-associated Mutant UCH-L1 and the Lysosomal Receptor for Chaperone-mediated Autophagy

Kabuta, T., Furuta, A., Aoki, S., Furuta, K., & Wada, K. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801918200 · Cited by 227 · see citing works

Acetylated tau inhibits chaperone-mediated autophagy and promotes tau pathology propagation in mice

Caballero, B., Bourdenx, M., Luengo, E., Diaz, A., Sohn, P. D., Chen, X., Wang, C., Juste, Y. R., Wegmann, S., Patel, B., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-22501-9 · Cited by 223 · see citing works

iPSC-Derived Dopamine Neurons Reveal Differences between Monozygotic Twins Discordant for Parkinson’s Disease

Woodard, C. M., Campos, B. A., Kuo, S., Nirenberg, M. J., Nestor, M. W., Zimmer, M., Mosharov, E. V., Sulzer, D. L., Zhou, H., Paull, D. J., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.10.023 · Cited by 220 · see citing works

A photoconvertible fluorescent reporter to track chaperone-mediated autophagy

Koga, H., Martínez‐Vicente, M., Macián, F., Verkhusha, V. V., & Cuervo, A. M. (2011) · Nature Communications · doi:10.1038/ncomms1393 · Cited by 214 · see citing works

Interplay of pathogenic forms of human tau with different autophagic pathways

Caballero, B., Wang, Y., Diaz, A., Tasset, I., Juste, Y. R., Stiller, B., Mandelkow, E., Mandelkow, E., & Cuervo, A. M. (2018) · Aging Cell · doi:10.1111/acel.12692 · Cited by 213 · see citing works

Loss of hepatic chaperone‐mediated autophagy accelerates proteostasis failure in aging

Schneider, J. L., Villarroya, J., Díaz-Carretero, A. M., Patel, B., Urbanska, A. M., Thi, M. M., Villarroya, F., Santambrogio, L., & Cuervo, A. M. (2015) · Aging Cell · doi:10.1111/acel.12310 · Cited by 192 · see citing works

Stabilization of α-Synuclein Protein with Aging and Familial Parkinson's Disease-Linked A53T Mutation

Li, W., Lesuisse, C., Xu, Y., Troncoso, J. C., Price, D. L., & Lee, M. K. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.1370-04.2004 · Cited by 178 · see citing works

GBA mutations increase risk for Lewy body disease with and without Alzheimer disease pathology

Tsuang, D. W., Leverenz, J. B., López, O. L., Hamilton, R. L., Bennett, D. A., Schneider, J. A., Buchman, A. S., Larson, E. B., Crane, P. K., Kaye, J. A., et al. (2012) · Neurology · doi:10.1212/wnl.0b013e3182735e9a · Cited by 152 · see citing works

Glucocerebrosidase is shaking up the synucleinopathies

Siebert, M., Sidransky, E., & Westbroek, W. (2014) · Brain · doi:10.1093/brain/awu002 · Cited by 142 · see citing works

Phosphorylation of LAMP2A by p38 MAPK couples ER stress to chaperone-mediated autophagy

Li, W., Zhu, J., Dou, J., She, H., Tao, K. X., Xu, H., Yang, Q., & Mao, Z. (2017) · Nature Communications · doi:10.1038/s41467-017-01609-x · Cited by 139 · see citing works

No evidence for substrate accumulation in Parkinson brains with GBA mutations

Gegg, M. E., Sweet, L., Wang, B. H., Shihabuddin, L. S., Sardi, S. P., & Schapira, A. H. V. (2015) · Movement Disorders · doi:10.1002/mds.26278 · Cited by 137 · see citing works

Characterization of the ERAD process of the L444P mutant glucocerebrosidase variant

Bendikov-Bar, I., Ron, I., Filocamo, M., & Horowitz, M. (2010) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2010.10.012 · Cited by 114 · see citing works

Unfolded protein response in Gaucher disease: from human to Drosophila

Maor, G., Rencus‐Lazar, S., Filocamo, M., Steller, H., Segal, D., & Horowitz, M. (2013) · Orphanet Journal of Rare Diseases · doi:10.1186/1750-1172-8-140 · Cited by 111 · see citing works

Essential control of mitochondrial morphology and function by chaperone-mediated autophagy through degradation of PARK7

Wang, B., Cai, Z., Tao, K., Zeng, W., Lu, F., Yang, R., Feng, D., Gao, G., & Yang, Q. (2016) · Autophagy · doi:10.1080/15548627.2016.1179401 · Cited by 107 · see citing works

Interaction between parkin and mutant glucocerebrosidase variants: a possible link between Parkinson disease and Gaucher disease

Ron, I., Rapaport, D., & Horowitz, M. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq292 · Cited by 97 · see citing works

The morbid anatomy of dementia in Parkinson’s disease

Kalaitzakis, M. E., & Pearce, R. K. B. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0597-x · Cited by 89 · see citing works

Methods to study chaperone-mediated autophagy

Patel, B., & Cuervo, A. M. (2015) · Methods · doi:10.1016/j.ymeth.2015.01.003 · Cited by 77 · see citing works

Glucocerebrosidase Mutations alter the endoplasmic reticulum and lysosomes in Lewy body disease

Kurzawa‐Akanbi, M., Hanson, P. S., Blain, P. G., Lett, D. J., McKeith, I. G., Chinnery, P. F., & Morris, C. M. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2012.07879.x · Cited by 69 · see citing works

The Genetic Basis of Cognitive Impairment and Dementia in Parkinson’s Disease

Collins, L., & Williams‐Gray, C. H. (2016) · Frontiers in Psychiatry · doi:10.3389/fpsyt.2016.00089 · Cited by 62 · see citing works

Enriched expression of genes associated with autism spectrum disorders in human inhibitory neurons

Wang, P., Zhao, D., Lachman, H. M., & Zheng, D. (2018) · Translational Psychiatry · doi:10.1038/s41398-017-0058-6 · Cited by 58 · see citing works

Increased 14-3-3 phosphorylation observed in Parkinson's disease reduces neuroprotective potential of 14-3-3 proteins

Slone, S. R., Lavalley, N. J., McFerrin, M., Wang, B., & Yacoubian, T. A. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.02.032 · Cited by 48 · see citing works

Neuronopathic and non‐neuronopathic presentation of Gaucher disease in patients with the third most common mutation (D409H) in Spain

Amparo Chabás, B., Cormand, B., Balcells, S., Gonzàlez‐Duarte, R., Casanova, C. R. M., Colomer, J., Vilageliu, L., & Grinberg, D. (1996) · Journal of Inherited Metabolic Disease · doi:10.1007/bf01799179 · Cited by 25 · see citing works

Overexpression of human glucocerebrosidase containing different-sized leaders

Pasmanik‐Chor, M., Elroy‐Stein, O., Aerts, J. M. F. G., Agmon, V., Gátt, S., & Horowitz, M. (1996) · Biochemical Journal · doi:10.1042/bj3170081 · Cited by 20 · see citing works

Amperometric Detection of Dopamine Exocytosis from Synaptic Terminals

Staal, R. G. W., Rayport, S., & Sulzer, D. L. (2006) · Frontiers in neuroengineering series/Frontiers in neuroengineering · doi:10.1201/9781420005868.ch16 · Cited by 19 · see citing works

Autophagy: Regulator of cell death

Liu, S., Yao, S., Yang, H., Liu, S., & Wang, Y. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-06154-8 · Cited by 1,193 · see citing works

Genetics and Pathogenesis of Parkinson's Syndrome

Ye, H., Robak, L. A., Yu, M., Cykowski, M. D., & Shulman, J. M. (2022) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathmechdis-031521-034145 · Cited by 474 · see citing works

GBA Variants and Parkinson Disease: Mechanisms and Treatments

Smith, L., & Schapira, A. H. V. (2022) · Cells · doi:10.3390/cells11081261 · Cited by 263 · see citing works

LAMP2A, LAMP2B and LAMP2C: similar structures, divergent roles

Qiao, L., Hu, J., Qiu, X., Wang, C., Peng, J., Zhang, C., Zhang, M., Lu, H., & Chen, W. (2023) · Autophagy · doi:10.1080/15548627.2023.2235196 · Cited by 174 · see citing works

Autophagic lysosome reformation in health and disease

Nanayakkara, R., Gurung, R., Rodgers, S. J., Eramo, M. J., Ramm, G., Mitchell, C. A., & McGrath, M. J. (2022) · Autophagy · doi:10.1080/15548627.2022.2128019 · Cited by 104 · see citing works

Chaperone‐mediated autophagy: Molecular mechanisms, biological functions, and diseases

Yao, R., & Shen, J. (2023) · MedComm · doi:10.1002/mco2.347 · Cited by 111 · see citing works

Lysosomal lipid alterations caused by glucocerebrosidase deficiency promote lysosomal dysfunction, chaperone-mediated-autophagy deficiency, and alpha-synuclein pathology

Navarro-Romero, A., Fernández-González, I., Riera, J., Montpeyó, M., Albert-Bayo, M., López‐Royo, T., Castillo-Sanchez, P., Carnicer-Cáceres, C., Arranz, J. A., Castillo‐Ribelles, L., et al. (2022) · npj Parkinson s Disease · doi:10.1038/s41531-022-00397-6 · Cited by 100 · see citing works

Interactions of dopamine, iron, and alpha-synuclein linked to dopaminergic neuron vulnerability in Parkinson's disease and Neurodegeneration with Brain Iron Accumulation disorders

Wise, R. M., Wagener, A., Fietzek, U. M., Klopstock, T., Mosharov, E. V., Zucca, F. A., Sulzer, D. L., Zecca, L., & Burbulla, L. F. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105920 · Cited by 95 · see citing works

Impaired degradation of PLCG1 by chaperone-mediated autophagy promotes cellular senescence and intervertebral disc degeneration

Cheng, Z., Gan, W., Xiang, Q., Zhao, K., Gao, H., Chen, Y., Shi, P., Zhang, A., Li, G., Song, Y., et al. (2024) · Autophagy · doi:10.1080/15548627.2024.2395797 · Cited by 81 · see citing works

Targeting the GBA1 pathway to slow Parkinson disease: Insights into clinical aspects, pathogenic mechanisms and new therapeutic avenues

Menozzi, E., Toffoli, M., & Schapira, A. H. V. (2023) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2023.108419 · Cited by 70 · see citing works

The Hidden Cell-to-Cell Trail of α-Synuclein Aggregates

Neupane, S., Cecco, E. D., & Aguzzi, A. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167930 · Cited by 67 · see citing works

Lysosomal functions and dysfunctions: Molecular and cellular mechanisms underlying Gaucher disease and its association with Parkinson disease

Horowitz, M., Braunstein, H., Zimran, A., Revel‐Vilk, S., & Göker-Alpan, Ö. (2022) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2022.114402 · Cited by 63 · see citing works

Clinical, mechanistic, biomarker, and therapeutic advances in GBA1-associated Parkinson’s disease

Zhang, X., Wu, H., Tang, B., & Guo, J. (2024) · Translational Neurodegeneration · doi:10.1186/s40035-024-00437-6 · Cited by 64 · see citing works

Glucocerebrosidase mutations and Parkinson disease

Vieira, S. R. L., & Schapira, A. H. V. (2022) · Journal of Neural Transmission · doi:10.1007/s00702-022-02531-3 · Cited by 61 · see citing works

Chaperone-Mediated Autophagy in Neurodegenerative Diseases: Molecular Mechanisms and Pharmacological Opportunities

Wang, Y.-T., & Lu, J. (2022) · Cells · doi:10.3390/cells11142250 · Cited by 60 · see citing works

More than meets the eye in Parkinson’s disease and other synucleinopathies: from proteinopathy to lipidopathy

Flores‐León, M., & Outeiro, T. F. (2023) · Acta Neuropathologica · doi:10.1007/s00401-023-02601-0 · Cited by 60 · see citing works

The contribution of altered neuronal autophagy to neurodegeneration

Filippone, A., Esposito, E., Mannino, D., Lyssenko, N., & Praticò, D. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2022.108178 · Cited by 55 · see citing works

Gaucher disease provides a unique window into Parkinson disease pathogenesis

Hertz, E., Chen, Y., & Sidransky, E. (2024) · Nature Reviews Neurology · doi:10.1038/s41582-024-00999-z · Cited by 56 · see citing works

GBA1 Variants and Parkinson’s Disease: Paving the Way for Targeted Therapy

Huh, Y. E., Usnich, T., Scherzer, C. R., Klein, C., & Chung, S. J. (2023) · Journal of Movement Disorders · doi:10.14802/jmd.23023 · Cited by 51 · see citing works

The Consequences of GBA Deficiency in the Autophagy–Lysosome System in Parkinson’s Disease Associated with GBA

Pradas, E., & Martínez‐Vicente, M. (2023) · Cells · doi:10.3390/cells12010191 · Cited by 50 · see citing works

A Mouse Model to Test Novel Therapeutics for Parkinson's Disease: an Update on the Thy1-aSyn (“line 61”) Mice

Richter, F., Stanojlović, M., Käufer, C., Gericke, B., & Feja, M. (2023) · Neurotherapeutics · doi:10.1007/s13311-022-01338-0 · Cited by 50 · see citing works

GBA1 Gene Mutations in α-Synucleinopathies—Molecular Mechanisms Underlying Pathology and Their Clinical Significance

Granek, Z., Barczuk, J., Siwecka, N., Rozpędek‐Kamińska, W., Kucharska, E., & Majsterek, I. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24032044 · Cited by 47 · see citing works

Cell biology of Parkinson's disease: Mechanisms of synaptic, lysosomal, and mitochondrial dysfunction

Brooker, S. M., Naylor, G. E., & Krainc, D. (2024) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2024.102841 · Cited by 47 · see citing works

Glucosylceramide accumulation in microglia triggers STING-dependent neuroinflammation and neurodegeneration in mice

Wang, R., Sun, H., Cao, Y., Zhang, Z., Chen, Y., Wang, X., Liu, L., Wu, J., Xu, H., Wu, D., et al. (2024) · Science Signaling · doi:10.1126/scisignal.adk8249 · Cited by 44 · see citing works

GBA1-Associated Parkinson’s Disease Is a Distinct Entity

Skrahin, A., Horowitz, M., Istaiti, M., Skrahina, V., Lukáš, J., Yahalom, G., Cohen, M. E., Revel‐Vilk, S., Göker-Alpan, Ö., Becker‐Cohen, M., et al. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25137102 · Cited by 42 · see citing works

Deregulation of mTORC1-TFEB axis in human iPSC model of GBA1-associated Parkinson’s disease

Mubariz, F., Saadin, A., Lingenfelter, N., Sarkar, C., Banerjee, A., Lipinski, M. M., & Awad, O. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1152503 · Cited by 37 · see citing works

α-Synuclein oligomers and fibrils: partners in crime in synucleinopathies

Bigi, A., Cascella, R., & Cecchi, C. (2023) · Neural Regeneration Research · doi:10.4103/1673-5374.371345 · Cited by 36 · see citing works

Recent developments in gene therapy for Parkinson’s disease

Szunyogh, S., Carroll, E., & Wade‐Martins, R. (2025) · Molecular Therapy · doi:10.1016/j.ymthe.2025.03.030 · Cited by 35 · see citing works

The Role of Chaperone-Mediated Autophagy in Tissue Homeostasis and Disease Pathogenesis

Valdor, R., & Martínez‐Vicente, M. (2024) · Biomedicines · doi:10.3390/biomedicines12020257 · Cited by 34 · see citing works

Pathogenesis of Parkinson’s Disease

Xiao, B., Zhou, Z., Chao, Y., & Tan, E.-K. (2025) · Neurologic Clinics · doi:10.1016/j.ncl.2024.12.003 · Cited by 36 · see citing works

Mechanisms of Glucocerebrosidase Dysfunction in Parkinson’s Disease

Chatterjee, D., & Krainc, D. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168023 · Cited by 34 · see citing works

ACO2 deficiency increases vulnerability to Parkinson’s disease via dysregulating mitochondrial function and histone acetylation-mediated transcription of autophagy genes

Zhu, J., Xu, F., Lai, H., Yuan, H., Li, X., Hu, J., Li, W., Liu, L., & Wang, C. (2023) · Communications Biology · doi:10.1038/s42003-023-05570-y · Cited by 33 · see citing works

Neuronopathic Gaucher disease: Beyond lysosomal dysfunction

Arévalo, N. B., Lamaizon, C. M., Cavieres, V. A., Burgos, P. V., Alvarez, A. R., Yañez, M. J., & Zanlungo, S. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.934820 · Cited by 31 · see citing works

Autophagy and neurodegeneration: Unraveling the role of C9ORF72 in the regulation of autophagy and its relationship to ALS-FTD pathology

Diab, R., Pilotto, F., & Saxena, S. (2023) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2023.1086895 · Cited by 31 · see citing works

Targeting the Interplay Between Autophagy and the Nrf2 Pathway in Parkinson’s Disease with Potential Therapeutic Implications

Liu, M., Liu, S., Lin, Z.-H., Chen, X., Jiao, Q., Du, X., & Jiang, H. F. (2025) · Biomolecules · doi:10.3390/biom15010149 · Cited by 30 · see citing works

Lewy pathology formation in patient-derived GBA1 Parkinson’s disease midbrain organoids

Frattini, E., Faustini, G., Lopez, G., Carsana, E. V., Tosi, M., Trezzi, I., Magni, M., Soldà, G., Straniero, L., Facchi, D., et al. (2024) · Brain · doi:10.1093/brain/awae365 · Cited by 30 · see citing works

Interplay of α-Synuclein Oligomers and Endoplasmic Reticulum Stress in Parkinson'S Disease: Insights into Cellular Dysfunctions

Zeng, H., Liu, Y., Liu, X., Li, J., Lu, L., Cheng, X., Wu, X., Zhang, X., Zheng, Z., & Lu, G. (2024) · Inflammation · doi:10.1007/s10753-024-02156-6 · Cited by 29 · see citing works

Activating autophagy to eliminate toxic protein aggregates with small molecules in neurodegenerative diseases

Fu, Y., Zhang, J., Qin, R., Ren, Y., Zhou, T., Han, B., & Liu, B. (2025) · Pharmacological Reviews · doi:10.1016/j.pharmr.2025.100053 · Cited by 28 · see citing works

PINK1 is a target of T cell responses in Parkinson’s disease

Williams, G. P., Freuchet, A., Michaelis, T., Frazier, A., Tran, N. K., Lima-Júnior, J. R., Phillips, E. J., Mallal, S. A., Litvan, I., Goldman, J. G., et al. (2024) · Journal of Clinical Investigation · doi:10.1172/jci180478 · Cited by 33 · see citing works

Neuronal activity promotes secretory autophagy for the extracellular release of α-synuclein

Nakamura, Y., Sawai, T., Kakiuchi, K., & Arawaka, S. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107419 · Cited by 25 · see citing works

Misfolded GBA/β-glucocerebrosidase impairs ER-quality control by chaperone-mediated autophagy in Parkinson disease

Kuo, S.-H., Tasset, I., Cuervo, A. M., & Sulzer, D. L. (2022) · Autophagy · doi:10.1080/15548627.2022.2071383 · Cited by 24 · see citing works

Neuronal LAMP2A-mediated reduction of adenylyl cyclases induces acute neurodegenerative responses and neuroinflammation after ischemic stroke

Shi, D., Bai, Y., Long, R., Xia, J., Xu, W., Qin, D., Yang, X., Ding, M., & Hou, X. (2024) · Cell Death and Differentiation · doi:10.1038/s41418-024-01389-0 · Cited by 23 · see citing works

African ancestry neurodegeneration risk variant disrupts an intronic branchpoint in GBA1

Jerez, P. Á., Crea, P. W., Ramos, D. M., Gustavsson, E. K., Radefeldt, M., Damianov, A., Makarious, M. B., Ojo, O. O., Billingsley, K. J., Malik, L., et al. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01423-2 · Cited by 23 · see citing works

Parkinson's Disease: The Epidemiology, Risk Factors, Molecular Pathogenesis, Prevention, and Therapy

Guo, X., Song, D., Wu, M., Zhang, J., Li, J., & Yuan, L. (2025) · MedComm · doi:10.1002/mco2.70540 · Cited by 26 · see citing works

New insights into the role of the Golgi apparatus in the pathogenesis and therapeutics of human diseases

Choi, W., Kang, S., & Kim, J. (2022) · Archives of Pharmacal Research · doi:10.1007/s12272-022-01408-z · Cited by 23 · see citing works

Glucocerebrosidase mutations disrupt the lysosome and now the mitochondria

Klein, A. D., & Outeiro, T. F. (2023) · Nature Communications · doi:10.1038/s41467-023-42107-7 · Cited by 23 · see citing works

Lysosomal storage, impaired autophagy and innate immunity in Gaucher and Parkinson's diseases: insights for drug discovery

Hull, A. J., Atilano, M. L., Gergi, L., & Kinghorn, K. J. (2024) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2022.0381 · Cited by 23 · see citing works

A partial Drp1 knockout improves autophagy flux independent of mitochondrial function

Fan, R. Z., Sportelli, C., Lai, Y., Salehe, S. S., Pinnell, J. R., Brown, H. J., Richardson, J. R., Luo, S., & Tieu, K. (2024) · Molecular Neurodegeneration · doi:10.1186/s13024-024-00708-w · Cited by 23 · see citing works

Regulation and function of endoplasmic reticulum autophagy in neurodegenerative diseases

Zhao, X., Xu, D.-E., Wu, M.-L., Liu, J.-C., Shi, Z.-L., & Ma, Q. (2024) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-23-00995 · Cited by 21 · see citing works

Study protocol of the GRoningen early-PD Ambroxol treatment (GREAT) trial: a randomized, double-blind, placebo-controlled, single center trial with ambroxol in Parkinson patients with a GBA mutation

Siemeling, O., Slingerland, S., van der Zee, S., & van Laar, T. (2024) · BMC Neurology · doi:10.1186/s12883-024-03629-9 · Cited by 21 · see citing works

Apigenin enhances Nrf2-induced chaperone-mediated autophagy and mitigates α-synuclein pathology: Implications for Parkinson's disease therapy

Huang, Y.-B., Tian, L.-L., Zhu, Z., Zhou, K.-G., Lai, X., Peng, Y.-Z., Wu, Z., Tong, W., Wang, H., Wang, X., et al. (2025) · Phytomedicine · doi:10.1016/j.phymed.2025.156652 · Cited by 21 · see citing works

Clinical Sphingolipids Pathway in Parkinson’s Disease: From GCase to Integrated-Biomarker Discovery

Esfandiary, A., Finkelstein, D. I., Voelcker, N. H., & Rudd, D. A. (2022) · Cells · doi:10.3390/cells11081353 · Cited by 21 · see citing works

Selective dopaminergic vulnerability in Parkinson’s disease: new insights into the role of DAT

Harraz, M. M. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1219441 · Cited by 19 · see citing works

Autophagy‑regulating miRNAs: Novel therapeutic targets for Parkinson's disease (Review)

Ma, Z., Liang, H., Hu, B., Cai, S., & Dong, Y. (2023) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2023.5253 · Cited by 19 · see citing works

Large-scale proteomics analysis of five brain regions from Parkinson’s disease patients with a GBA1 mutation

Blumenreich, S., Nehushtan, T., Kupervaser, M., Shalit, T., Gabashvili, A., Joseph, T., Milenković, I., Hardy, J., & Futerman, A. H. (2024) · npj Parkinson s Disease · doi:10.1038/s41531-024-00645-x · Cited by 19 · see citing works

Chaperone-mediated autophagy in neurodegenerative diseases: mechanisms and therapy

Liu, Y., Tan, M., & Tan, M. (2023) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-022-04640-9 · Cited by 18 · see citing works

Targeting chaperone-mediated autophagy in neurodegenerative diseases: mechanisms and therapeutic potential

Wu, J., Xu, W., Su, Y., Wang, G., & Ma, J. (2024) · Acta Pharmacologica Sinica · doi:10.1038/s41401-024-01416-3 · Cited by 17 · see citing works

Ups and downs of lysosomal pH: conflicting roles of LAMP proteins?

Handy, J., MacIntosh, G. C., & Jenny, A. (2023) · Autophagy · doi:10.1080/15548627.2023.2274253 · Cited by 16 · see citing works

α-Synuclein: Multiple pathogenic roles in trafficking and proteostasis pathways in Parkinson’s disease

Zalon, A. J., Quiriconi, D. J., Pitcairn, C., & Mazzulli, J. R. (2024) · The Neuroscientist · doi:10.1177/10738584241232963 · Cited by 16 · see citing works

Chaperone-mediated autophagy: mechanisms and physiological relevance

Jafari, M., McCabe, M., & Cuervo, A. M. (2022) · Current Opinion in Physiology · doi:10.1016/j.cophys.2022.100597 · Cited by 15 · see citing works

Autophagy and Its Association with Genetic Mutations in Parkinson Disease

Erekat, N. S. (2022) · Medical Science Monitor · doi:10.12659/msm.938519 · Cited by 15 · see citing works

Canonical and noncanonical autophagy: involvement in Parkinson’s disease

Sakurai, M., & Kuwahara, T. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1518991 · Cited by 16 · see citing works

iPSC-derived neural precursor cells engineering GBA1 recovers acid β-glucosidase deficiency and diminishes α-synuclein and neuropathology

Peng, Y., Liou, B., Lin, Y., Mayhew, C. N., Fleming, S. M., & Sun, Y. (2023) · Molecular Therapy — Methods & Clinical Development · doi:10.1016/j.omtm.2023.03.007 · Cited by 14 · see citing works

Whole Transcriptome Analysis of Substantia Nigra in Mice with MPTP-Induced Parkinsonism Bearing Defective Glucocerebrosidase Activity

Usenko, T. S., Bezrukova, A. I., Rudenok, M. M., Basharova, K. S., Shadrina, M. I., Slominsky, P. A., Zakharova, E. Y., & Pchelina, S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241512164 · Cited by 14 · see citing works

GBA1 and The Immune System: A Potential Role in Parkinson’s Disease?

Al‐Azzawi, Z. A. M., Arfaie, S., & Gan‐Or, Z. (2022) · Journal of Parkinson s Disease · doi:10.3233/jpd-223423 · Cited by 14 · see citing works

α-Synuclein in Parkinson's Disease: 12 Years LaterPreprint

Vekrellis, K., Emmanouilidou, E., Xilouri, M., & Stefanis, L. (2024) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a041645 · Cited by 14 · see citing works

Biallelic Variants in EPG5 Gene Are Associated with Parkinson's Disease

Sun, Q., Tang, F., Zhou, Y., Pan, H., Zhou, X. C., Zhao, Y., He, R., Zeng, S., Wang, J., Wei, L., et al. (2025) · Annals of Neurology · doi:10.1002/ana.27242 · Cited by 12 · see citing works

Neuroprotective Effects of a Novel Demeclocycline Derivative Lacking Antibiotic Activity: From a Hit to a Promising Lead Compound

Tomas‐Grau, R. H., González‐Lizárraga, F., Ploper, D., Ávila, C. L., Socías, S. B., Besnault, P., Tourville, A., Mella, R. M., Villacé, P., Salado, C., et al. (2022) · Cells · doi:10.3390/cells11172759 · Cited by 12 · see citing works

New evidence on the clinical, genetic, and biochemical bases of GBA1-Parkinson's disease: prospects for treatment

Menozzi, E., Toffoli, M., Deleidi, M., Monte, D. A. D., Blandini, F., Krainc, D., Sidransky, E., & Schapira, A. H. V. (2026) · The Lancet Neurology · doi:10.1016/s1474-4422(26)00090-6 · Cited by 11 · see citing works

Tunicamycin induces depression-like behaviors in male rats, accompanied by initiated chaperon-mediated autophagy and decreased synaptic protein expression in the hippocampus

Yuan, G., Xiao, L., Xie, Y., Si, L., Xu, H. W., Xu, W., & Wang, G. (2023) · Neuroscience Letters · doi:10.1016/j.neulet.2023.137058 · Cited by 11 · see citing works

Characterization of Novel Human β-glucocerebrosidase Antibodies for Parkinson’s Disease Research

Jong, T., Gehrlein, A., Sidransky, E., Jagasia, R., & Chen, Y. (2024) · Journal of Parkinson s Disease · doi:10.3233/jpd-230295 · Cited by 11 · see citing works

Stearoyl-CoA desaturase inhibition normalizes brain lipid saturation, α-synuclein homeostasis, and motor function in mutant Gba1-Parkinson mice

Nuber, S., Hsiang, H. W., Keewan, E. F., Moors, T. E., Reitz, S. J., Tiwari, A., Ho, G. P. H., Su, E., Hahn, W. N., Adom, M.-A., et al. (2025) · JCI Insight · doi:10.1172/jci.insight.188413 · Cited by 10 · see citing works

Converging links between adult-onset neurodegenerative Alzheimer’s disease and early life neurodegenerative neuronal ceroid lipofuscinosis?

Hermey, G., & Klein, M. (2023) · Neural Regeneration Research · doi:10.4103/1673-5374.361544 · Cited by 10 · see citing works

DJ-1 protects cell death from a mitochondrial oxidative stress due to GBA1 deficiency

Nam, Y., Na, J., Ma, S., Park, H., Park, H., Lee, E., Kim, H., Jang, S., Ko, H. S., & Kim, S. (2024) · Genes & Genomics · doi:10.1007/s13258-024-01506-w · Cited by 10 · see citing works

Therapies for lysosomal storage diseases: Principles, practice, and prospects for refinements based on evolving science

Grabowski, G. A., & Mistry, P. K. (2022) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2022.07.014 · Cited by 9 · see citing works

Live cell in situ lysosomal GCase activity correlates to alpha-synuclein levels in human differentiated neurons with LRRK2 and GBA1 mutations

Labrador‐Garrido, A., Zhong, S., Hughes, L. P., Keshiya, S., Kim, W. S., Halliday, G. M., & Dzamko, N. L. (2023) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2023.1229213 · Cited by 10 · see citing works

Evidence of α-Synuclein/Glucocerebrosidase Dual Targeting by Iminosugar Derivatives

Tagliaferro, G., Davighi, M. G., Clemente, F., Turchi, F., Schiavina, M., Matassini, C., Goti, A., Morrone, A., Pierattelli, R., Cardona, F., et al. (2025) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.4c00618 · Cited by 9 · see citing works

The modifying effect of mutant LRRK2 on mutant GBA1 -associated Parkinson disease

Serebryany-Piavsky, V., Egulsky, L., Manoim-Wolkovitz, J. E., Anis, S., Hassin-Baer, S., Parnas, M., & Mia, H. (2025) · Human Molecular Genetics · doi:10.1093/hmg/ddaf062 · Cited by 9 · see citing works

Classification of GBA1 variants and their impact on Parkinson’s disease: an in silico score analysis

Lanore, A., Tesson, C., Basset, A., Lejeune, F., Cogan, G., Mangone, G., Sambin, S., Bertille, N., Anheim, M., Arnulf, I., et al. (2025) · npj Parkinson s Disease · doi:10.1038/s41531-025-01060-6 · Cited by 9 · see citing works

Targeting protein clearance pathways in GBA1-associated Parkinson disease

Chen, C., Hertz, E., Chen, Y., & Sidransky, E. (2022) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2022.2166828 · Cited by 9 · see citing works

Activation and Purification of ß‐Glucocerebrosidase by Exploiting its Transporter LIMP‐2 – Implications for Novel Treatment Strategies in Gaucher's and Parkinson's Disease

Dobert, J. P., Bub, S., Mächtel, R., Januliene, D., Steger, L., Regensburger, M., Wilfling, S., Chen, J., Dejung, M., Plötz, S., et al. (2024) · Advanced Science · doi:10.1002/advs.202401641 · Cited by 9 · see citing works

Golgi damage caused by dysfunction of PiT-2 in primary familial brain calcification

Sun, H., Wang, Z., Zhang, Q., Chen, N., Tang, M., Yang, Z., Xu, Y., Kang, J., & Wang, Y. (2022) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2022.12.050 · Cited by 8 · see citing works

ZEB1-AS1 as a TRPML1 Inhibitor to Cause Lysosome Dysfunction and Cardiac Damage in Aged Mice

Liu, H., Zhang, H., Lou, H., Wang, J., Hao, S., Chen, H., Chen, C., Wang, L., Li, H., Meng, Z., et al. (2024) · Engineering · doi:10.1016/j.eng.2024.09.020 · Cited by 8 · see citing works

Interplay of GBA1 with lysosomal dysfunction and inflammation in Parkinson’s disease

Wang, R., Hatano, T., Hattori, N., & Cossu, D. (2025) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-25-01082 · Cited by 8 · see citing works

Multi-omics insights into GBA1-associated Parkinson’s disease: interplay of genomics, transcriptomics, proteomics, and lipidomics

Ni, Y., Cai, H., Shao, Y., & Le, W.-D. (2026) · Molecular Neurodegeneration · doi:10.1186/s13024-026-00931-7 · Cited by 8 · see citing works

Chaperone-mediated autophagy in fish: A key function amid a changing environment

Schnebert, S., Vélez, E. J., Goguet, M., Dias, K., Véron, V., García-Pérez, I., Radler, L. M., Cardona, E., Fontagné-Dicharry, S., Delft, P. V., et al. (2024) · Autophagy Reports · doi:10.1080/27694127.2024.2403956 · Cited by 8 · see citing works

Fiber‐Specific White Matter Alterations in Parkinson's Disease Patients with GBA Gene Mutations

Andica, C., Kamagata, K., Uchida, W., Saito, Y., Takabayashi, K., Hagiwara, A., Takeshige-Amano, H., Hatano, T., Hattori, N., & Aoki, S. (2023) · Movement Disorders · doi:10.1002/mds.29578 · Cited by 8 · see citing works

PINK1 is a target of T cell responses in Parkinson’s diseasePreprint

Williams, G. P., Michaelis, T., Lima-Júnior, J. R., Frazier, A., Tran, N. K., Phillips, E. J., Mallal, S. A., Litvan, I., Goldman, J. G., Alcalay, R. N., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.02.09.579465 · Cited by 8 · see citing works

Polymeric nanoparticle-mediated GBA1 gene therapy is neuroprotective in a preclinical model of Parkinson’s disease

Kwatra, M., Kwak, G., Li, H., Suk, J. S., & Ko, H. S. (2025) · Drug Delivery and Translational Research · doi:10.1007/s13346-025-01944-3 · Cited by 7 · see citing works

Targeting chaperone-mediated autophagy for Parkinson’s disease therapy

Lu, J., & Wang, Y.-T. (2022) · Neural Regeneration Research · doi:10.4103/1673-5374.363831 · Cited by 7 · see citing works

Synaptojanin1 Modifies Endolysosomal Parameters in Cultured Ventral Midbrain Neurons

Zhu, X., Prakash, S. S., McAuliffe, G., & Pan, P.-Y. (2023) · eNeuro · doi:10.1523/eneuro.0426-22.2023 · Cited by 7 · see citing works

Intrinsic link between PGRN and Gba1 D409V mutation dosage in potentiating Gaucher disease

Lin, Y., Zhao, X., Liou, B., Fannin, V., Zhang, W., Setchell, K. D. R., Wang, X., Pan, D., Grabowski, G. A., Liu, C.-J., et al. (2024) · Human Molecular Genetics · doi:10.1093/hmg/ddae113 · Cited by 6 · see citing works

Modulation of autophagy by melatonin and its receptors: implications in brain disorders

Zhu, C., Li, G., Lyu, H.-F., Lu, Y., Li, Y., & Zhang, X. (2024) · Acta Pharmacologica Sinica · doi:10.1038/s41401-024-01398-2 · Cited by 5 · see citing works

Acetal functionalized iminosugars for targeting β-glucocerebrosidase modulation

Davighi, M. G., Clemente, F., Matassini, C., Cacciarini, M., Tanini, D., Goti, A., Morrone, A., Paoli, P., & Cardona, F. (2025) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2025.117529 · Cited by 5 · see citing works

Role of Chaperone-Mediated Autophagy in Ageing Biology and Rejuvenation of Stem Cells

Vitale, E., Perveen, S., Rossin, D., Iacono, M. L., Rastaldo, R., & Giachino, C. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.912470 · Cited by 6 · see citing works

Developing nanobodies as allosteric molecular chaperones of glucocerebrosidase function

Maso, T. D., Sinisgalli, C., Zilio, G., Franzin, E., Tessari, I., Pardon, E., Steyaert, J., Ballet, S., Greggio, E., Versées, W., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-60134-4 · Cited by 4 · see citing works

α-Synuclein expression is required for somatodendritic dopamine release and immediate early gene induction

Choi, S. J., Frank, A. K., Ben-Johny, M., Tang, G., Bendig, J., Fanourakis, S., Hobson, B. D., Somayaji, M., Ramalingam, N., Dettmer, U., et al. (2026) · Science Advances · doi:10.1126/sciadv.ady6978 · Cited by 4 · see citing works

Lipid Metabolism Reprogramming in the Aging Brain: Glial-Mediated Pathogenic Mechanisms and Translational Strategies in Neurodegeneration

Shao, W., Wang, K., Liu, Y., Zhang, H., Sun, Z., & Zhou, R. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27125580 · Cited by 4 · see citing works

Postmortem Human Dura Mater Cells Exhibit Phenotypic, Transcriptomic and Genetic Abnormalities that Impact their Use for Disease Modeling

Argouarch, A. R., Schultz, N., Yang, A. C., Jang, Y., Garcia, K., Cosme, C. G., Corrales, C. I., Nana, A. L., Karydas, A. M., Spina, S., et al. (2022) · Stem Cell Reviews and Reports · doi:10.1007/s12015-022-10416-x · Cited by 4 · see citing works

Genetic modifiers of synucleinopathies—lessons from experimental models

Lee, R. M. Q., & Koh, T. (2023) · Oxford Open Neuroscience · doi:10.1093/oons/kvad001 · Cited by 4 · see citing works

Cytosolic glucocerebrosidase impairs alpha-synuclein degradation by blockade of chaperone-mediated autophagy (P3.050)

Kuo, S.-H., Tasset, I., Cuervo, A. M., & Sulzer, D. L. (2018) · Neurology · doi:10.1212/wnl.90.15_supplement.p3.050

Effect of glucocerebrosidase inhibition on the activities of microautophagy and chaperone-mediated autophagy

Sato, M., Seki, T., Kurauchi, Y., Hisatsune, A., & Katsuki, H. (2019) · Proceedings for Annual Meeting of The Japanese Pharmacological Society · doi:10.1254/jpssuppl.92.0_1-p-046

Lysosomal lipid alterations caused by glucocerebrosidase deficiency promote lysosomal dysfunction, chaperone-mediated-autophagy deficiency, and alpha-synuclein pathology

Navarro-Romero, A., Fernández-González, I., Riera, J., Montpeyó, M., Albert-Bayo, M., López‐Royo, T., Castillo-Sanchez, P., Carnicer-Cáceres, C., Arranz, J. A., Castillo‐Ribelles, L., et al. (2022) · npj Parkinson s Disease · doi:10.1038/s41531-022-00397-6 · Cited by 100 · see citing works

Autophagy-lysosomal pathway dysfunction in Parkinson’s disease

Murphy, K. (2022) · UNSWorks (UNSW Sydney) · doi:10.26190/unsworks/16712

Inhibition or genetic reduction of ASAH1 /acid ceramidase restore α-synuclein clearance in mutant GBA1 dopamine neurons from Parkinson’s patients

Kumar, M., & Feldman, R. A. (2025) · Human Molecular Genetics · doi:10.1093/hmg/ddaf166 · Cited by 3 · see citing works