The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.
Chaperone-mediated autophagy: a unique way to enter the lysosome world
Open accessAbstract
All cellular proteins undergo continuous synthesis and degradation. This permanent renewal is necessary to maintain a functional proteome and to allow for rapid changes in levels of specific proteins with regulatory purposes. Although for a long time lysosomes were considered unable to contribute to the selective degradation of individual proteins, the discovery of chaperone-mediated autophagy (CMA) changed this notion. Here, we review the characteristics that set CMA apart from other types of lysosomal degradation and the subset of molecules that confer cells the capability to identify individual cytosolic proteins and direct them across the lysosomal membrane for degradation.
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.
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
Autophagy fights disease through cellular self-digestion
Mizushima, N., Levine, B., Cuervo, A. M., & Klionsky, D. J. (2008) · Nature · doi:10.1038/nature06639 · Cited by 6,452
Self-citationde Duve, C., & Wattiaux, R. (1966) · Annual Review of Physiology · doi:10.1146/annurev.ph.28.030166.002251 · Cited by 3,033
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-citationMicroautophagy of Cytosolic Proteins by Late Endosomes
Sahu, R., Kaushik, S., Clement, C. C., Cannizzo, E. S., Scharf, B., Follenzi, A., Potolicchio, I., Nieves, E., Cuervo, A. M., & Santambrogio, L. (2011) · Developmental Cell · doi:10.1016/j.devcel.2010.12.003 · Cited by 902
Self-citationCargo 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
Self-citationVogiatzi, T., Xilouri, M., Vekrellis, K., & Stefanis, L. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801992200 · Cited by 683
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
Consequences of the selective blockage of chaperone-mediated autophagy
Massey, A. C., Kaushik, S., Sovak, G., Kiffin, R., & Cuervo, A. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0507436103 · Cited by 529
Self-citationHarnessing chaperone-mediated autophagy for the selective degradation of mutant huntingtin protein
Bauer, P. O., Goswami, A., Wong, H. K., Okuno, M., Kurosawa, M., Yamada, M., Miyazaki, H., Matsumoto, G., Kino, Y., Nagai, Y., et al. (2010) · Nature Biotechnology · doi:10.1038/nbt.1608 · Cited by 280
Kabuta, T., Furuta, A., Aoki, S., Furuta, K., & Wada, K. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801918200 · Cited by 227
Cited by
The role of autophagy in neurodegenerative disease
Nixon, R. A. (2013) · Nature Medicine · doi:10.1038/nm.3232 · Cited by 2,059
Molecular definitions of autophagy and related processes
Galluzzi, L., Baehrecke, E. H., Ballabio, A., Boya, P., Bravo‐San Pedro, J. M., Cecconi, F., Choi, A. M., Chu, C. T., Codogno, P., Colombo, M. I., et al. (2017) · The EMBO Journal · doi:10.15252/embj.201796697 · Cited by 1,646
Self-citationThe Biology of Proteostasis in Aging and Disease
Labbadia, J., & Morimoto, R. I. (2015) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060614-033955 · Cited by 1,472
Degradation of misfolded proteins in neurodegenerative diseases: Therapeutic targets and strategies
Ciechanover, A., & Kwon, Y. T. (2015) · Experimental & Molecular Medicine · doi:10.1038/emm.2014.117 · Cited by 898
The lysosome: from waste bag to potential therapeutic target
Appelqvist, H., Wäster, P., Kågedal, K., & Öllinger, K. (2013) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjt022 · Cited by 772
Autophagy-dependent cell death
Denton, D., & Kumar, S. (2019) · Cell Death & Differentiation · doi:10.1038/s41418-018-0252-y · Cited by 777
The Autophagy–Lysosomal Pathway in Neurodegeneration: A TFEB Perspective
Martini-Stoica, H., Xu, Y., Ballabio, A., & Zheng, H. (2016) · Trends in Neurosciences · doi:10.1016/j.tins.2016.02.002 · Cited by 436
Autophagy and Alzheimer’s Disease: From Molecular Mechanisms to Therapeutic Implications
Uddin, M. S., Stachowiak, A., Mamun, A. A., Tzvetkov, N. T., Takeda, S., Atanasov, A. G., Bergantin, L. B., Abdel-Daim, M. M., & Stankiewicz, A. M. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00004 · Cited by 395
Autophagy in acute kidney injury
Kaushal, G. P., & Shah, S. V. (2016) · Kidney International · doi:10.1016/j.kint.2015.11.021 · Cited by 389
A molecular mechanism to regulate lysosome motility for lysosome positioning and tubulation
Li, X., Rydzewski, N., Hider, A., Zhang, X., Yang, J., Wang, W., Gao, Q., Cheng, X., & Xu, H. (2016) · Nature Cell Biology · doi:10.1038/ncb3324 · Cited by 387
Autophagy in liver diseases: Time for translation?
Allaire, M., Rautou, P.-E., Codogno, P., & Lotersztajn, S. (2019) · Journal of Hepatology · doi:10.1016/j.jhep.2019.01.026 · Cited by 378
An Overview of the Role of Lipofuscin in Age-Related Neurodegeneration
Moreno-García, A., Kun, A., Calero, O., Medina, M., & Calero, M. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00464 · Cited by 372
Deficient Chaperone-Mediated Autophagy in Liver Leads to Metabolic Dysregulation
Schneider, J. L., Suh, Y., & Cuervo, A. M. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.06.009 · Cited by 340
Self-citationMolecular Mechanisms of Autophagy in the Cardiovascular System
Gatica, D., Chiong, M., Lavandero, S., & Klionsky, D. J. (2015) · Circulation Research · doi:10.1161/circresaha.114.303788 · Cited by 272
Transcriptional Regulation of Autophagy: Mechanisms and Diseases
Di Malta, C., Cinque, L., & Settembre, C. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00114 · Cited by 255
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
Self-citationTargeted Protein Degradation by Small Molecules
Bondeson, D. P., & Crews, C. M. (2017) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010715-103507 · Cited by 207
Autophagy and Its Normal and Pathogenic States in the Brain
Yamamoto, A., & Yue, Z. (2014) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-071013-014149 · Cited by 204
Harnessing the Power of Proteolysis for Targeted Protein Inactivation
Verma, R., Mohl, D., & Deshaies, R. J. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.01.010 · Cited by 185
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
Impaired GAPDH‐induced mitophagy contributes to the pathology of Huntington's disease
Hwang, S., Disatnik, M., & Mochly‐Rosen, D. (2015) · EMBO Molecular Medicine · doi:10.15252/emmm.201505256 · Cited by 153
Lysosomal Exocytosis: The Extracellular Role of an Intracellular Organelle
Tancini, B., Buratta, S., Delo, F., Sagini, K., Chiaradia, E., Pellegrino, R. M., Emiliani, C., & Urbanelli, L. (2020) · Membranes · doi:10.3390/membranes10120406 · Cited by 144
Autophagy and Parkinson’s Disease
Lu, J., Wu, M., & Yue, Z. (2020) · Advances in Experimental Medicine and Biology · doi:10.1007/978-981-15-4272-5_2 · Cited by 131
Targeting Lysosomal Degradation Pathways: New Strategies and Techniques for Drug Discovery
Pei, J., Wang, G., Feng, L., Zhang, J., Jiang, T., Sun, Q., & Ouyang, L. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c01689 · Cited by 124
Degradation of HK2 by chaperone-mediated autophagy promotes metabolic catastrophe and cell death
Xia, H.-G., Najafov, A., Geng, J., Galan-Acosta, L., Han, X., Guo, Y., Shan, B., Zhang, Y., Norberg, E., Zhang, T., et al. (2015) · Journal of Cell Biology · doi:10.1083/jcb.201503044 · Cited by 122
Lysosomal multienzyme complex: pros and cons of working together
Bonten, E. J., Annunziata, I., & d’Azzo, A. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1538-3 · Cited by 117
Autophagy and the immune function in aging
Cuervo, A. M., & Macian, F. (2014) · Current Opinion in Immunology · doi:10.1016/j.coi.2014.05.006 · Cited by 112
Self-citationLysosomes: regulators of autophagy in the retinal pigmented epithelium
Sinha, D., Valapala, M., Shang, P., Hose, S., Grebe, R., Lutty, G. A., Zigler, J. S., Kaarniranta, K., & Handa, J. T. (2016) · Experimental Eye Research · doi:10.1016/j.exer.2015.08.018 · Cited by 88
Enhancing autophagy in Alzheimer's disease through drug repositioning
Eshraghi, M., Ahmadi, M., Afshar, S., Lorzadeh, S., Adlimoghaddam, A., Rezvani Jalal, N., West, R., Dastghaib, S., Igder, S., Torshizi, S. R. N., et al. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2022.108171 · Cited by 89
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
Peroxisome degradation in mammals: mechanisms of action, recent advances, and perspectives
Nordgren, M., Wang, B., Apanasets, O., & Fransen, M. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00145 · Cited by 67
Primary cilia and autophagic dysfunction in Huntington’s disease
Kaliszewski, M., Knott, A. B., & Bossy-Wetzel, E. (2015) · Cell Death & Differentiation · doi:10.1038/cdd.2015.80 · Cited by 55
The role of glial autophagy in Alzheimer’s disease
Litwiniuk, A., Juszczak, G. R., Stankiewicz, A. M., & Urbańska, K. (2023) · Molecular Psychiatry · doi:10.1038/s41380-023-02242-5 · Cited by 54
The 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
Chaperone-Mediated Autophagy and Its Emerging Role in Hematological Malignancies
Robert, G., Jacquel, A., & Auberger, P. (2019) · Cells · doi:10.3390/cells8101260 · Cited by 45
Tian, Z., Wang, C., Hu, C., Tian, Y., Liu, J., & Wang, X. (2014) · PLoS ONE · doi:10.1371/journal.pone.0100715 · Cited by 35
The role of lysosomes and autophagosomes in frontotemporal lobar degeneration
Bain, H. D. C., Davidson, Y. S., Robinson, A. C., Ryan, S., Rollinson, S., Richardson, A., Jones, M., Snowden, J. S., Pickering‐Brown, S., & Mann, D. M. A. (2019) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12500 · Cited by 33
Monitoring autophagy in cancer: From bench to bedside
Long, M., & McWilliams, T. G. (2020) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2019.05.016 · Cited by 30
Metadata
- Authors
- Kaushik, S., & Cuervo, A. M.
- Venue
- Trends in Cell Biology
- Publisher
- Elsevier BV
- Published
- 2012-08
- Volume
- 22
- Issue
- 8
- Pages
- 407-417
- ISSN
- 0962-8924 (ISSN-L)
- OpenAlex
- W2021919397
- Cited by
- 850
- References
- 12
- FWCI
- 8.26
- Type
- journal article
- Language
- en
- Open access
- green
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
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.