The DOI matches its Crossref record; 44 of the 44 references it cites were found in a registry or an index.
Wild Type α-Synuclein Is Degraded by Chaperone-mediated Autophagy and Macroautophagy in Neuronal Cells
Open accessAbstract
Alpha-synuclein (ASYN) is crucial in Parkinson disease (PD) pathogenesis. Increased levels of wild type (WT) ASYN expression are sufficient to cause PD in humans. The manner of post-transcriptional regulation of ASYN levels is controversial. Previously, we had shown that WT ASYN can be degraded by chaperone-mediated autophagy (CMA) in isolated liver lysosomes. Whether this occurs in a cellular and, in particular, in a neuronal cell context is unclear. Using a mutant ASYN form that lacks the CMA recognition motif and RNA interference against the rate-limiting step in the CMA pathway, Lamp2a, we show here that CMA is indeed involved in WT ASYN degradation in PC12 and SH-SY5Y cells, and in primary cortical and midbrain neurons. However, the extent of involvement varies between cell types, potentially because of differences in compensatory mechanisms. CMA inhibition leads to an accumulation of soluble high molecular weight and detergent-insoluble species of ASYN, suggesting that CMA dysfunction may play a role in the generation of such aberrant species in PD. ASYN and Lamp2a are developmentally regulated in parallel in cortical neuron cultures and in vivo in the central nervous system, and they physically interact as indicated by co-immunoprecipitation. In contrast to previous reports, inhibition of macroautophagy, but not the proteasome, also leads to WT ASYN accumulation, suggesting that this lysosomal pathway is also involved in normal ASYN turnover. These results indicate that CMA and macroautophagy are important pathways for WT ASYN degradation in neurons and underline the importance of CMA as degradation machinery in the nervous system.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The cited source says what the claim attributes to it.
In the citing paper
“Previous studies suggest that α-synuclein is degraded by macroautophagy, chaperone-mediated autophagy, and the proteasome20–23.”
From Microglia clear neuron-released α-synuclein via selective autophagy and prevent neurodegeneration (2020) · cites this paper as [22]
In the citing paper
“dopamine-modified α-synuclein blocks chaperone-mediated autophagy [109,110], which induces abnormal intracellular accumulation α-synuclein in PD [120].”
From Degradation of Tyrosine Hydroxylase by the Ubiquitin-Proteasome System in the Pathogenesis of Parkinson’s Disease and Dopa-Responsive Dystonia (2020) · cites this paper as [110]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Repertoires of Autophagy in the Pathogenesis of Ocular Diseases
Li, Y., Jiang, Q. L., Cao, G.-F., Yao, J., & Yan, B. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000373980 · Cited by 16,351
Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells
Elbashir, S. M., Harborth, J., Lendeckel, W., Yalcin, A., Weber, K., & Tuschl, T. (2001) · Nature · doi:10.1038/35078107 · Cited by 9,456
Mutation in the α-Synuclein Gene Identified in Families with Parkinson's Disease
Polymeropoulos, M. H., Lavedan, C., Leroy, E., Ide, S. E., Dehejia, A., Dutra, A., Pike, B., Root, H., Rubenstein, J., Boyer, R., et al. (1997) · Science · doi:10.1126/science.276.5321.2045 · Cited by 8,240
AlaSOPro mutation in the gene encoding α-synuclein in Parkinson's disease
Krüger, R., Kuhn, W., Müller, T., Woitalla, D., Graeber, M., Kösel, S., Przuntek, H., Epplen, J. T., Schols, L., & Riess, O. (1998) · Nature Genetics · doi:10.1038/ng0298-106 · Cited by 3,836
Levine, B., & Klionsky, D. J. (2004) · Developmental Cell · doi:10.1016/s1534-5807(04)00099-1 · Cited by 3,728
A Third-Generation Lentivirus Vector with a Conditional Packaging System
Dull, T., Zufferey, R., Kelly, M., Mandel, R. J., Nguyen, M., Trono, D., & Naldini, L. (1998) · Journal of Virology · doi:10.1128/jvi.72.11.8463-8471.1998 · Cited by 3,341
Autophagy in Health and Disease: A Double-Edged Sword
Shintani, T., & Klionsky, D. J. (2004) · Science · doi:10.1126/science.1099993 · Cited by 2,559
Rational siRNA design for RNA interference
Reynolds, A., Leake, D., Boese, Q., Scaringe, S., Marshall, W. S., & Khvorova, A. (2004) · Nature Biotechnology · doi:10.1038/nbt936 · Cited by 2,094
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
Self-citationRubinson, D. A., Dillon, C. P., Kwiatkowski, A. V., Sievers, C., Yang, L., Kopinja, J. E., Rooney, D. L., Zhang, M., Ihrig, M. M., McManus, M. T., et al. (2003) · Nature Genetics · doi:10.1038/ng1117 · Cited by 1,499
Flagged first, then by citations
Research works printed but not linked: 1
- Martinez-Vicente, 2008, J. Clin. Investig., 118, 777
Cited by
Sorted by citations
Items 201–300 of 683
Tumor Cells Induce LAMP2a Expression in Tumor-Associated Macrophage for Cancer Progression
Wang, R., Liu, Y., Liu, L., Chen, M., Wang, X., Yang, H. J., Gong, Y., Ding, B., Wei, Y., & Wei, X. (2018) · EBioMedicine · doi:10.1016/j.ebiom.2019.01.045 · Cited by 76
Mechanisms of alpha-synuclein toxicity: An update and outlook
Brás, I. C., Xylaki, M., & Outeiro, T. F. (2019) · Progress in brain research · doi:10.1016/bs.pbr.2019.10.005 · Cited by 78
Wu, G., Wang, X., Feng, X., Zhang, A., Li, J., Gu, K., Huang, J. A., Pang, S., Dong, H., Gao, H., et al. (2011) · Brain Research · doi:10.1016/j.brainres.2011.04.013 · Cited by 78
GABA transmission via ATP-dependent K + channels regulates α-synuclein secretion in mouse striatum
Emmanouilidou, E., Minakaki, G., Keramioti, M. V., Xylaki, M., Balafas, E., Chrysanthou‐Piterou, M., Kloukina, I., & Vekrellis, K. (2016) · Brain · doi:10.1093/brain/awv403 · Cited by 77
Self-citationKawahata, I., & Fukunaga, K. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21113779 · Cited by 71
Autophagy in Astrocytes and its Implications in Neurodegeneration
Sung, K., & Jiménez-Sánchez, M. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.12.041 · Cited by 78
Pivtoraiko, V. N., Harrington, A. J., Mader, B. J., Luker, A. M., Caldwell, G. A., Caldwell, K. A., Roth, K. A., & Shacka, J. J. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06838.x · Cited by 75
Autophagy protects against aminochrome-induced cell death in substantia nigra-derived cell line.
Paris, I., Muñoz, P., Huenchuguala, S., Couve, E., Sanders, L. H., Greenamyre, J., Caviedes, P., & Segura-Aguilar, J. (2011) · Toxicological Sciences · doi:10.1093/toxsci/kfr060 · Cited by 69
Apoptosis in Parkinson's disease: Is p53 the missing link between genetic and sporadic Parkinsonism?
da Costa, C. A., & Checler, F. (2010) · Cellular Signalling · doi:10.1016/j.cellsig.2010.10.020 · Cited by 75
Sala, G., Stefanoni, G., Arosio, A., Riva, C., Melchionda, L., Saracchi, E., Fermi, S., Brighina, L., & Ferrarese, C. (2013) · Brain Research · doi:10.1016/j.brainres.2013.12.017 · Cited by 75
Wu, J.-Z., Ardah, M. T., Haikal, C., Svanbergsson, A., Diepenbroek, M., Vaikath, N. N., Li, W., Wang, Z., Outeiro, T. F., El‐Agnaf, O. M. A., et al. (2019) · Translational Neurodegeneration · doi:10.1186/s40035-019-0159-7 · Cited by 73
Targeting Sigma Receptors for the Treatment of Neurodegenerative and Neurodevelopmental Disorders
Malar, D. S., Thitilertdecha, P., Ruckvongacheep, K. S., Brimson, S., Tencomnao, T., & Brimson, J. M. (2023) · CNS Drugs · doi:10.1007/s40263-023-01007-6 · Cited by 77
Genetically engineered mouse models of Parkinson's disease
Crabtree, D., & Zhang, J. (2011) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2011.07.019 · Cited by 73
Parkinson's disease: acid‐glucocerebrosidase activity and alpha‐synuclein clearance
Blanz, J., & Säftig, P. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13517 · Cited by 75
Regulation of neuronal autophagy and the implications in neurodegenerative diseases
Cai, Q., & Ganesan, D. (2021) · Neurobiology of Disease · doi:10.1016/j.nbd.2021.105582 · Cited by 70
Malkus, K. A., & Ischiropoulos, H. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2012.03.017 · Cited by 71
Anandhan, A., Rodríguez‐Rocha, H., Bohovych, I., Griggs, A. M., Zavala-Flores, L. M., Reyes‐Reyes, E. M., Seravalli, J., Stanciu, L., Lee, J., Rochet, J., et al. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.11.018 · Cited by 73
Paris, I. B., Perez-Pastene, C., Couve, E., Caviedes, P. A., LeDoux, S. P., & Segura‐Aguilar, J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m900323200 · Cited by 71
Molecular control of chaperone-mediated autophagy
Catarino, S., Pereira, P., & Girão, H. (2017) · Essays in Biochemistry · doi:10.1042/ebc20170057 · Cited by 71
Targeting the Autophagy/Lysosomal Degradation Pathway in Parkinsons Disease
Rivero-Ríos, P., Madero-Pérez, Fernández, B., & Hilfiker, S. (2016) · Current Neuropharmacology · doi:10.2174/1570159x13666151030103027 · Cited by 69
Saturated Fatty Acids Modulate Autophagy’s Proteins in the Hypothalamus
Portovedo, M., Ignácio-Souza, L. M., Bombassaro, B., Coope, A., Reginato, A., Razolli, D. S., Torsoni, M. A., Torsoni, A. S., Leal, R. F., Velloso, L. A., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0119850 · Cited by 69
Wang, X.-W., Yuan, L.-J., Yang, Y., Zhang, M., & Chen, W. (2020) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00071.2020 · Cited by 70
Latrepirdine (Dimebon™) Enhances Autophagy and Reduces Intracellular GFP-Aβ42 Levels in Yeast
Bharadwaj, P. R., Verdile, G., Barr, R. K., Gupta, V. B., Steele, J., Lachenmayer, M. L., Yue, Z., Ehrlich, M. E., Petsko, G. A., Ju, S., et al. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-120178 · Cited by 69
Deregulation of calcium homeostasis mediates secreted α–synuclein-induced neurotoxicity
Melachroinou, K., Xilouri, M., Emmanouilidou, E., Masgrau, R., Papazafiri, P., Stefanis, L., & Vekrellis, K. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.06.006 · Cited by 71
Self-citationLysosomal alterations in peripheral blood mononuclear cells of Parkinson's disease patients
Papagiannakis, N., Xilouri, M., Koros, C., Stamelou, M., Antonelou, R. C., Maniati, M., Papadimitriou, D. A., Moraitou, M., Michelakakis, H., & Stefanis, L. (2015) · Movement Disorders · doi:10.1002/mds.26433 · Cited by 69
Self-citationRegulation of amyloid precursor protein processing by its KFERQ motif
Park, J., Kim, D., & Yoon, S. (2016) · BMB Reports · doi:10.5483/bmbrep.2016.49.6.212 · Cited by 74
Proteolysis of α‐synuclein fibrils in the lysosomal pathway limits induction of inclusion pathology
Sacino, A. N., Brooks, M., Chakrabarty, P., Saha, K., Khoshbouei, H., Golde, T. E., & Giasson, B. I. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13743 · Cited by 71
Emerging novel concept of chaperone therapies for protein misfolding diseases
Suzuki, Y. (2014) · Proceedings of the Japan Academy Series B · doi:10.2183/pjab.90.145 · Cited by 68
Xilouri, M., & Stefanis, L. (2015) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2015.01.003 · Cited by 68
Self-citationZhang, S., Gui, X., Huang, L., Deng, M., Fang, R., Ke, X., He, Y., Li, L., & Fang, Y. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8950-z · Cited by 67
Vekrellis, K., & Stefanis, L. (2012) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2012.674111 · Cited by 68
Self-citationNelson, M. P., Tse, T. E., O’Quinn, D. B., Percival, S. M., Jaimes, E. A., Warnock, D. G., & Shacka, J. J. (2014) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-2-20 · Cited by 69
The Emerging Roles of Autophagy in Human Diseases
Lei, Y., & Klionsky, D. J. (2021) · Biomedicines · doi:10.3390/biomedicines9111651 · Cited by 68
Underlying Mechanism of Lysosomal Membrane Permeabilization in CNS Injury: A Literature Review
Xiang, L., Lou, J., Zhao, J., Geng, Y., Zhang, J., Wu, Y., Zhao, Y., Tao, Z., Yao, L., Qi, J., et al. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-04290-6 · Cited by 71
Yoon, Y.-S., Cho, E.-D., Ahn, W. J., Lee, K. W., Lee, S., & Lee, H.-J. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.501 · Cited by 65
Ottolini, D., Calí, T., Szabó, I., & Brini, M. (2016) · Biological Chemistry · doi:10.1515/hsz-2016-0201 · Cited by 65
Mavroeidi, P., Arvanitaki, F., Karakitsou, A.-K., Vetsi, M., Kloukina, I., Zweckstetter, M., Giller, K., Becker, S., Sorrentino, Z. A., Giasson, B. I., et al. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-02014-y · Cited by 66
Self-citationAutophagy in neuroinflammatory diseases
Muller, S., Brun, S., René, F., Seze, J. D., Loeffler, J., & Jeltsch‐David, H. (2017) · Autoimmunity Reviews · doi:10.1016/j.autrev.2017.05.015 · Cited by 66
Trifluoperazine rescues human dopaminergic cells from wild-type α-synuclein-induced toxicity
Höllerhage, M., Goebel, J. N., de Andrade, A., Hildebrandt, T., Dolga, A. M., Culmsee, C., Oertel, W. H., Hengerer, B., & Höglinger, G. U. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.01.027 · Cited by 66
Cardiomyocyte ryanodine receptor degradation by chaperone-mediated autophagy
Pedrozo, Z., Torrealba, N., Fernández, C., Gatica, D., Toro, B., Quiroga, C., Rodriguez, A. E., Sánchez, G., Gillette, T. G., Hill, J. A., et al. (2013) · Cardiovascular Research · doi:10.1093/cvr/cvt029 · Cited by 63
Dunning, C. J. R., George, S., & Brundin, P. (2013) · Prion · doi:10.4161/pri.23806 · Cited by 66
Manzoni, C., & Lewis, P. A. (2013) · The FASEB Journal · doi:10.1096/fj.12-223842 · Cited by 62
Michelakakis, H., Xiromerisiou, G., Dardiotis, E., Bozi, M., Vassilatis, D., Kountra, P., Patramani, G., Moraitou, M., Papadimitriou, D., Stamboulis, E., et al. (2012) · Movement Disorders · doi:10.1002/mds.24886 · Cited by 64
Self-citationChaperone mediated autophagy in aging: Starve to prosper
Xilouri, M., & Stefanis, L. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.07.001 · Cited by 65
Self-citationNtsapi, C., & Loos, B. (2016) · Experimental Gerontology · doi:10.1016/j.exger.2016.07.014 · Cited by 65
Apelin/APJ system: A novel promising target for neurodegenerative diseases
Luo, H., Han, L., & Xu, J. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.29001 · Cited by 61
Higashi, S., Moore, D. J., Minegishi, M., Kasanuki, K., Fujishiro, H., Kabuta, T., Togo, T., Katsuse, O., Uchikado, H., Furukawa, Y., et al. (2011) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e318211c86a · Cited by 62
Arotçarena, M.-L., Soria, F. N., Cunha, A., Doudnikoff, É., Prévot, G., Daniel, J., Blanchard-Desce, M. H., Barthélémy, P., Bézard, E., Crauste–Manciet, S., et al. (2022) · Aging Cell · doi:10.1111/acel.13584 · Cited by 60
Chaves, R. S., Melo, T. Q., Martins, S. A., & Ferrari, M. (2010) · BMC Neuroscience · doi:10.1186/1471-2202-11-144 · Cited by 63
Wang, Y.-T., & Lu, J. (2022) · Cells · doi:10.3390/cells11142250 · Cited by 62
Kee, T. R., Khan, S. A., Neidhart, M. B., Masters, B. M., Zhao, V. K., Kim, Y. K., Percy, K. C. M., & Woo, J. A. (2024) · Experimental & Molecular Medicine · doi:10.1038/s12276-023-01144-4 · Cited by 68
Autophagy protects the rotenone-induced cell death in α-synuclein overexpressing SH-SY5Y cells
Dadakhujaev, S., Noh, H. S., Jung, E. J., Cha, J. Y., Baek, S. M., Ha, J. H., & Kim, D. R. (2010) · Neuroscience Letters · doi:10.1016/j.neulet.2010.01.053 · Cited by 62
The different roles of selective autophagic protein degradation in mammalian cells
Wang, D., Peng, Z.-J., Ren, G.-F., & Wang, G. (2015) · Oncotarget · doi:10.18632/oncotarget.5776 · Cited by 63
Bonhoure, A., Vallentin, A., Martin, M., Senff‐Ribeiro, A., Amson, R. B., Telerman, A., & Vidal, M. (2017) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2016.12.002 · Cited by 60
The emerging role of retromer in neuroprotection
McMillan, K. J., Korswagen, H. C., & Cullen, P. J. (2017) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2017.02.004 · Cited by 66
Centrality of Early Synaptopathy in Parkinson’s Disease
Imbriani, P., Schirinzi, T., Meringolo, M., Mercuri, N. B., & Pisani, A. (2018) · Frontiers in Neurology · doi:10.3389/fneur.2018.00103 · Cited by 59
Synaptic dysfunction in genetic models of Parkinson's disease: A role for autophagy?
Plowey, E. D., & Chu, C. T. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.10.011 · Cited by 62
Genetic analysis of the ATG7 gene promoter in sporadic Parkinson's disease
Chen, D., Pang, S., Feng, X., Huang, W., Hawley, R. G., & Yan, B. (2013) · Neuroscience Letters · doi:10.1016/j.neulet.2012.12.039 · Cited by 59
Arduíno, D. M., Esteves, A. R., & Cardoso, S. M. (2011) · Parkinson s Disease · doi:10.4061/2011/767230 · Cited by 61
Manzoni, C., & Lewis, P. A. (2017) · Advances in neurobiology · doi:10.1007/978-3-319-49969-7_5 · Cited by 56
Ahlskog, J. E. (2009) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2009.09.010 · Cited by 59
Naoi, M., Maruyama, W., & Shamoto‐Nagai, M. (2020) · Journal of Neural Transmission · doi:10.1007/s00702-020-02150-w · Cited by 58
Gut microbiota produces biofilm-associated amyloids with potential for neurodegeneration
Fernández-Calvet, A., Matilla-Cuenca, L., Izco, M., Navarro, S., Serrano, M., Ventura, S., Blesa, J., Herráiz, M., Alkorta‐Aranburu, G., Galera, S., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-48309-x · Cited by 55
Ali, A. B., Nin, D. S., Tam, J. K. C., & Khan, M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025268 · Cited by 56
Alpha-synuclein, Proteotoxicity and Parkinson's Disease: Search for Neuroprotective Therapy
Ganguly, U., Chakrabarti, S. S., Kaur, U., Mukherjee, A., & Chakrabarti, S. (2018) · Current Neuropharmacology · doi:10.2174/1570159x15666171129100944 · Cited by 58
Treating Parkinson’s Disease with Antibodies: Previous Studies and Future Directions
Castonguay, A.-M., Gravel, C., & Lévesque, M. (2020) · Journal of Parkinson s Disease · doi:10.3233/jpd-202221 · Cited by 55
Protein Transmission, Seeding and Degradation: Key Steps for α-Synuclein Prion-Like Propagation
Oueslati, A., Ximerakis, M., & Vekrellis, K. (2014) · Experimental Neurobiology · doi:10.5607/en.2014.23.4.324 · Cited by 58
Self-citationDysfunction of chaperone-mediated autophagy in human diseases
Liao, Z., Wang, B., Liu, W., Xu, Q., Hou, L., Song, J., Guo, Q., & Li, N. (2021) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-020-04006-z · Cited by 56
Role of Apolipoproteins and α-Synuclein in Parkinson’s Disease
Emamzadeh, F. N. (2017) · Journal of Molecular Neuroscience · doi:10.1007/s12031-017-0942-9 · Cited by 54
Dou, T., Zhou, L., & Kurouski, D. (2021) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.1c00820 · Cited by 54
Jones-Tabah, J., He, K., Karpilovsky, N. C., Senkevich, K. A., Deyab, G., Pietrantonio, I., Goiran, T., Cousineau, Y., Nikanorova, D., Goldsmith, T., et al. (2024) · Molecular Neurodegeneration · doi:10.1186/s13024-024-00779-9 · Cited by 53
Yan, J., Yuan, Y., Gao, Y., Huang, J., Ma, K., Gao, Y., Zhang, W., Guo, X., & Chen, N. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8738-1 · Cited by 56
Wei, C., Chang, C., & Liao, V. H. (2017) · Phytomedicine · doi:10.1016/j.phymed.2017.09.002 · Cited by 54
MicroRNAs and Target Genes As Biomarkers for the Diagnosis of Early Onset of Parkinson Disease
Arshad, A. R., Sulaiman, S. A., Saperi, A. A., Jamal, R., Ibrahim, N. M., & Murad, N. A. A. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00352 · Cited by 54
Proteostasis of α-Synuclein and Its Role in the Pathogenesis of Parkinson’s Disease
Han, D., Zheng, W., Wang, X., & Chen, Z. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.00045 · Cited by 55
Autophagy-Lysosomal Pathway as Potential Therapeutic Target in Parkinson’s Disease
Bonam, S. R., Tranchant, C., & Muller, S. (2021) · Cells · doi:10.3390/cells10123547 · Cited by 54
Lipophagy: a new player in CNS disorders
Haidar, M., Loix, M., Bogie, J. F. J., & Hendriks, J. J. A. (2021) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2021.08.010 · Cited by 55
Dermentzaki, G., Dimitriou, E., Xilouri, M., Michelakakis, H., & Stefanis, L. (2013) · PLoS ONE · doi:10.1371/journal.pone.0060674 · Cited by 56
Self-citationKim, M. J., Deng, H., Wong, Y. C., Siddique, T., & Krainc, D. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw413 · Cited by 52
Shamoto‐Nagai, M., Hisaka, S., Naoi, M., & Maruyama, W. (2018) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.18-25 · Cited by 53
Triptolide, A Potential Autophagy Modulator
Wei, Y., Wang, Y., Xue, H., Luan, Z., Liu, B., & Ren, J. (2018) · Chinese Journal of Integrative Medicine · doi:10.1007/s11655-018-2847-z · Cited by 52
Neurons and Glia Interplay in α-Synucleinopathies
Mavroeidi, P., & Xilouri, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094994 · Cited by 55
Self-citationThe regulatory role of lipophagy in central nervous system diseases
Lan, Z.-Q., Ge, Z.-Y., Lv, S.-K., Zhao, B., & Li, C.-X. (2023) · Cell Death Discovery · doi:10.1038/s41420-023-01504-z · Cited by 49
Regulation of α-synuclein homeostasis and inflammasome activation by microglial autophagy
Choi, I., Heaton, G. R., Lee, Y.-K., & Yue, Z. (2022) · Science Advances · doi:10.1126/sciadv.abn1298 · Cited by 54
Lysosomal dysfunction in α-synuclein pathology: molecular mechanisms and therapeutic strategies
Dai, L., Liu, M., Ke, W., Chen, L., Fang, X., & Zhang, Z. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-024-05419-5 · Cited by 53
Pukaß, K., & Richter‐Landsberg, C. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00163 · Cited by 53
Targeted Suppression of Chaperone-Mediated Autophagy by miR-320a Promotes α-Synuclein Aggregation
Li, G., Yang, H., Zhu, D., Huang, H., Liu, G., & Lun, P. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms150915845 · Cited by 54
van Rensburg, Z. J., Abrahams, S., Bardien, S., & Kenyon, C. P. (2021) · Molecular Neurobiology · doi:10.1007/s12035-021-02516-5 · Cited by 52
Pukaß, K., Goldbaum, O., & Richter‐Landsberg, C. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13256 · Cited by 49
Pantazopoulou, M., Brembati, V., Kanellidi, A., Bousset, L., Melki, R., & Stefanis, L. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15174 · Cited by 50
Self-citationChakraborty, J., Pakrashi, S., Sarbajna, A., Dutta, M., & Bandyopadhyay, J. (2022) · Biological Trace Element Research · doi:10.1007/s12011-022-03093-x · Cited by 50
Pradas, E., & Martínez‐Vicente, M. (2023) · Cells · doi:10.3390/cells12010191 · Cited by 52
Pukaß, K., & Richter‐Landsberg, C. (2013) · Journal of Molecular Neuroscience · doi:10.1007/s12031-013-0154-x · Cited by 48
KLK6 proteolysis is implicated in the turnover and uptake of extracellular alpha-synuclein species
Pampalakis, G., Sykioti, V. S., Ximerakis, M., Stefanakou-Kalakou, I., Melki, R., Vekrellis, K., & Sotiropoulou, G. (2016) · Oncotarget · doi:10.18632/oncotarget.13264 · Cited by 52
Self-citationThe unlikely partnership between LRRK 2 and α‐synuclein in Parkinson's disease
Cresto, N., Gardier, C., Gubinelli, F., Gaillard, M., Liot, G., West Andrew, B., & Brouillet, E. (2018) · European Journal of Neuroscience · doi:10.1111/ejn.14182 · Cited by 49
Eswari, S., & Naik, S. (2019) · Materials Science for Energy Technologies · doi:10.1016/j.mset.2019.10.011 · Cited by 49
Accumulation of α-synuclein mediates podocyte injury in Fabry nephropathy
Braun, F., Abed, A., Sellung, D., Rogg, M., Woidy, M., Eikrem, Ø., Wanner, N., Gambardella, J., Laufer, S. D., Haas, F., et al. (2023) · Journal of Clinical Investigation · doi:10.1172/jci157782 · Cited by 50
Seki, T., Yoshino, K.-I., Tanaka, S., Dohi, E., Onji, T., Yamamoto, K., Hide, I., Paulson, H. L., Saito, N., & Sakai, N. (2012) · PLoS ONE · doi:10.1371/journal.pone.0031232 · Cited by 48
Chaperone-Mediated Autophagy and Its Emerging Role in Hematological Malignancies
Robert, G., Jacquel, A., & Auberger, P. (2019) · Cells · doi:10.3390/cells8101260 · Cited by 43
Alpha-Synuclein and Cognitive Decline in Parkinson Disease
Fan, T.-S., Liu, S. C.-H., & Wu, R. (2021) · Life · doi:10.3390/life11111239 · Cited by 47
Metadata
- Authors
- Vogiatzi, T., Xilouri, M., Vekrellis, K., & Stefanis, L.
- Affiliations
- Biomedical Research Foundation of the Academy of Athens (GR)
- National and Kapodistrian University of Athens (GR)
- Corresponding author
- Stefanis, Leonidas
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2008-08
- Volume
- 283
- Issue
- 35
- Pages
- 23542-23556
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC2527094
- OpenAlex
- W2026175550
- Cited by
- 683
- References
- 44
- Citations by year
- 2026: 28 · 2025: 33 · 2024: 43 · 2023: 44 · 2022: 36 · 2021: 48 · 2020: 56 · 2019: 40 · 2018: 34 · 2017: 32 · 2016: 30 · 2015: 33 · 2014: 39 · 2013: 39 · 2012: 41
- FWCI
- 22.89
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute of Neurological Disorders and Stroke (R21NS055693)
- Topics
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Health Sciences › Medicine › Genetics (clinical) › Lysosomal Storage Disorders Research
- Keywords
- alpha-synuclein, chaperone-mediated autophagy, macroautophagy, Parkinson's disease, LAMP2A, lysosomal degradation, post-transcriptional regulation, PC12 cells, SH-SY5Y cells, cortical neurons, midbrain neurons, protein turnover
- MeSH terms
- Animals, Autophagy, Cerebral Cortex, Humans, Mesencephalon, Neurons, Parkinson Disease, PC12 Cells, Rats, Wistar, Molecular Chaperones, Mice, Rats, alpha-Synuclein, Lysosomal Membrane Proteins, Lysosomal-Associated Membrane Protein 2
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
