Proteome-wide analysis of chaperone-mediated autophagy targeting motifs
Open accessAbstract
Chaperone-mediated autophagy (CMA) contributes to the lysosomal degradation of a selective subset of proteins. Selectivity lies in the chaperone heat shock cognate 71 kDa protein (HSC70) recognizing a pentapeptide motif (KFERQ-like motif) in the protein sequence essential for subsequent targeting and degradation of CMA substrates in lysosomes. Interest in CMA is growing due to its recently identified regulatory roles in metabolism, differentiation, cell cycle, and its malfunctioning in aging and conditions such as cancer, neurodegeneration, or diabetes. Identification of the subset of the proteome amenable to CMA degradation could further expand our understanding of the pathophysiological relevance of this form of autophagy. To that effect, we have performed an in silico screen for KFERQ-like motifs across proteomes of several species. We have found that KFERQ-like motifs are more frequently located in solvent-exposed regions of proteins, and that the position of acidic and hydrophobic residues in the motif plays the most important role in motif construction. Cross-species comparison of proteomes revealed higher motif conservation in CMA-proficient species. The tools developed in this work have also allowed us to analyze the enrichment of motif-containing proteins in biological processes on an unprecedented scale and discover a previously unknown association between the type and combination of KFERQ-like motifs in proteins and their participation in specific biological processes. To facilitate further analysis by the scientific community, we have developed a free web-based resource (KFERQ finder) for direct identification of KFERQ-like motifs in any protein sequence. This resource will contribute to accelerating understanding of the physiological relevance of CMA.
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
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?
This led to the identification of some of the earliest disease-associated genes, including APP, PS1 and PS2 in AD, SNCA and LRRK2 in PD and MAPT and GRN in FTD.
“This subsequently led to the identification of some of the earliest disease-associated genes, including APP, PS1 and PS2 in AD, SNCA and LRRK2 in PD and MAPT and GRN in FTD.79–87”
From The lysosome and proteostatic stress at the intersection of pediatric neurological disorders and adult neurodegenerative diseases (2025) · cites this paper as [86]
The Results section (‘Position of motifs within proteins’; page unavailable) links α-synuclein to Parkinson disease pathology, supporting only a narrow part of the PD association. It does not describe the early identification of disease-associated genes or establish the listed AD and FTD gene associations; the LRRK2 mention is in a reference about autophagy. (LLM, conf=0.72)
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Cytoscape: A software Environment for integrated models of biomolecular interaction networks
Shannon, P., Markiel, A., Ozier, O., Baliga, N. S., Wang, J. T., Ramage, D., Amin, N., Schwikowski, B., & Ideker, T. (2003) · Genome Research · doi:10.1101/gr.1239303 · Cited by 51,888 · see citing works
MUSCLE: multiple sequence alignment with high accuracy and high throughput
Edgar, R. C. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh340 · Cited by 44,662 · see citing works
Matplotlib: a 2D graphics environment
Hunter, J. D. (2007) · Computing in Science & Engineering · doi:10.1109/mcse.2007.55 · Cited by 39,249 · see citing works
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
ggplot2: Elegant Graphics for Data Analysis
Wickham, H. (2009) · doi:10.1007/978-0-387-98141-3 · Cited by 14,447 · see citing works
The NumPy Array: A Structure for Efficient Numerical Computation
van der Walt, S., Colbert, S. C., & Varoquaux, G. P. (2011) · Computing in Science & Engineering · doi:10.1109/mcse.2011.37 · Cited by 10,445 · see citing works
PhosphoSitePlus, 2014: mutations, PTMs and recalibrations
Hornbeck, P. V., Zhang, B., Murray, B., Kornhauser, J. M., Latham, V. M., & Skrzypek, E. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku1267 · Cited by 3,243 · see citing works
Enrichment Map: A Network-Based Method for Gene-Set Enrichment Visualization and Interpretation
Merico, D., Isserlin, R., Stueker, O., Emili, A., & Bader, G. D. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013984 · Cited by 2,235 · 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
Self-citationBio3d: an R package for the comparative analysis of protein structures
Grant, B. J., Rodrigues, A. P. C., ElSawy, K. M., McCammon, J. A., & Caves, L. S. D. (2006) · Bioinformatics · doi:10.1093/bioinformatics/btl461 · Cited by 2,005 · see citing works
Mammalian autophagy: core molecular machinery and signaling regulation
Yang, Z., & Klionsky, D. J. (2010) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.11.014 · Cited by 1,956 · see citing works
JPred4: a protein secondary structure prediction server
Drozdetskiy, A., Cole, C., Procter, J. B., & Barton, G. J. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv332 · Cited by 1,714 · see citing works
The coming of age of chaperone-mediated autophagy
Kaushik, S., & Cuervo, A. M. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0001-6 · Cited by 1,422 · see citing works
Self-citationA Receptor for the Selective Uptake and Degradation of Proteins by Lysosomes
Cuervo, A. M., & Dice, J. F. (1996) · Science · doi:10.1126/science.273.5274.501 · Cited by 979 · see citing works
Self-citationStructure and Dynamics of Micelle-bound Human α-Synuclein
Ulmer, T. S., Bax, A., Cole, N. B., & Nussbaum, R. L. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m411805200 · Cited by 966 · see citing works
Microautophagy 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 · see citing works
Self-citationPeptide sequences that target cytosolic proteins for lysosomal proteolysis
Dice, J. F. (1990) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(90)90019-8 · Cited by 755 · see citing works
Kaushik, S., & Cuervo, A. M. (2015) · Nature Cell Biology · doi:10.1038/ncb3166 · Cited by 719 · see citing works
Self-citationAge-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
Self-citationAttributes of short linear motifs
Davey, N. E., Roey, K. V., Weatheritt, R. J., Toedt, G., Uyar, B., Altenberg, B., Budd, A., Diella, F., Dinkel, H., & Gibson, T. J. (2011) · Molecular BioSystems · doi:10.1039/c1mb05231d · Cited by 626 · see citing works
Activation of Chaperone-mediated Autophagy during Oxidative Stress
Kiffin, R., Christian, C., Knecht, E., & Cuervo, A. M. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-06-0477 · Cited by 611 · see citing works
Self-citationLv, L., Dong, L., Zhao, D., Lin, R., Chu, Y., Zhang, H., Zha, Z., Liu, Y., Li, Z., Xu, Y., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.04.025 · Cited by 605 · 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
Self-citationUbiSite approach for comprehensive mapping of lysine and N-terminal ubiquitination sites
Akimov, V., Barrio‐Hernandez, I., Hansen, S. V. F., Hallenborg, P., Pedersen, A.-K., Bekker‐Jensen, D. B., Puglia, M., Christensen, S. D. K., Vanselow, J. T., Nielsen, M. M., et al. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-018-0084-y · Cited by 466 · see citing works
Toward a Comprehensive Characterization of a Human Cancer Cell Phosphoproteome
Zhou, H., Palma, S. D., Preisinger, C., Peng, M., Polat, A. N., Heck, A. J. R., & Mohammed, S. (2012) · Journal of Proteome Research · doi:10.1021/pr300630k · Cited by 427 · see citing works
Local structural disorder imparts plasticity on linear motifs
Fuxreiter, M., Tompa, P., & Simon, I. (2007) · Bioinformatics · doi:10.1093/bioinformatics/btm035 · Cited by 405 · see citing works
IKK phosphorylates Huntingtin and targets it for degradation by the proteasome and lysosome
Thompson, L. M., Aiken, C. T., Kaltenbach, L. S., Agrawal, N., Illes, K., Khoshnan, A., Martínez‐Vicente, M., Arrasate, M., O’Rourke, J. G., Khashwji, H., et al. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200909067 · Cited by 396 · see citing works
Self-citationChaperone-mediated autophagy and endosomal microautophagy: Jointed by a chaperone
Kosar, A. K. T., & Cuervo, A. M. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.r117.818237 · Cited by 359 · see citing works
Self-citationActivation of a selective pathway of lysosomal proteolysis in rat liver by prolonged starvation
Cuervo, A. M., Knecht, E., Terlecky, S. R., & Dice, J. F. (1995) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1995.269.5.c1200 · Cited by 356 · see citing works
Self-citationDeficient 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 · see citing works
Self-citationMiyoshi, H., Souza, S. C., Zhang, H.-H., Strissel, K. J., Christoffolete, M. A., Kovsan, J., Rudich, A., Kraemer, F. B., Bianco, A. C., Obin, M. S., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601097200 · Cited by 324 · see citing works
Lipid Binding Inhibits α-Synuclein Fibril Formation
Zhu, M., & Fink, A. L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210136200 · Cited by 314 · see citing works
The Role of Cysteine Oxidation in DJ-1 Function and Dysfunction
Wilson, M. A. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3481 · Cited by 304 · see citing works
Unique properties of lamp2a compared to other lamp2 isoforms
Cuervo, A. M., & Dice, J. F. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.24.4441 · Cited by 304 · see citing works
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 · see citing works
Proteomic Analyses Reveal Divergent Ubiquitylation Site Patterns in Murine Tissues
Wagner, S., Beli, P., Weinert, B. T., Scholz, C. W., Kelstrup, C. D., Young, C., Nielsen, M. L., Olsen, J. V., Brakebusch, C., & Choudhary, C. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m112.017905 · Cited by 279 · see citing works
Chaperone-Mediated Autophagy Is Required for Tumor Growth
Kon, M., Kiffin, R., Koga, H., Chapochnick, J., Macián, F., Varticovski, L., & Cuervo, A. M. (2011) · Science Translational Medicine · doi:10.1126/scitranslmed.3003182 · Cited by 260 · see citing works
Self-citationPeptide sequences that target proteins for enhanced degradation during serum withdrawal.
Chiang, H. L., & Dice, J. F. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68713-7 · Cited by 255 · see citing works
Valdor, R., Mocholi, E., Botbol, Y., Guerrero-Ros, I., Chandra, D., Koga, H., Gravekamp, C., Cuervo, A. M., & Macian, F. (2014) · Nature Immunology · doi:10.1038/ni.3003 · Cited by 244 · see citing works
Self-citationChaperone-mediated Autophagy Targets Hypoxia-inducible Factor-1α (HIF-1α) for Lysosomal Degradation
Hubbi, M. E., Hu, H., Gupta, K., Ahmed, I., Levchenko, A., & Semenza, G. L. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.414771 · Cited by 239 · see citing works
Lee, S., Kim, S. J., Kim, I.-K., Ko, J., Jeong, C., Kim, G.-H., Park, C., Kang, S.-O., Suh, P., Lee, H.-S., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304517200 · Cited by 236 · see citing works
Inhibitory effect of dietary lipids on chaperone-mediated autophagy
Rodríguez‐Navarro, J. A., Kaushik, S., Koga, H., Dall’Armi, C., Shui, G., Wenk, M. R., Paolo, G. D., & Cuervo, A. M. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1113036109 · Cited by 228 · see citing works
Self-citationRegulated degradation of Chk1 by chaperone-mediated autophagy in response to DNA damage
Park, C., Suh, Y., & Cuervo, A. M. (2015) · Nature Communications · doi:10.1038/ncomms7823 · Cited by 224 · see citing works
Self-citationA 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
Self-citationMultiomic Analysis of the UV-Induced DNA Damage Response
Boeing, S., Williamson, L. M., Encheva, V., Gori, I., Saunders, R. E., Instrell, R., Aygün, O., Rodríguez‐Martínez, M., Weems, J. C., Kelly, G. P., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.04.047 · Cited by 199 · see citing works
Structure of a Lipid Droplet Protein
Hickenbottom, S. J., Kimmel, A. R., Londos, C., & Hurley, J. H. (2004) · Structure · doi:10.1016/j.str.2004.04.021 · Cited by 193 · see citing works
The jsonlite Package: A Practical and Consistent Mapping Between JSON Data and R ObjectsPreprint
Ooms, J. C. L. (2014) · arXiv (Cornell University) · doi:10.48550/arxiv.1403.2805 · Cited by 183 · see citing works
Wing, S. S., Chiang, H. L., Goldberg, A. L., & Dice, J. F. (1991) · Biochemical Journal · doi:10.1042/bj2750165 · Cited by 154 · see citing works
TreeFam v9: a new website, more species and orthology-on-the-fly
Schreiber, F., Patricio, M., Muffato, M., Pignatelli, M., & Bateman, A. (2013) · Nucleic Acids Res. · doi:10.1093/nar/gkt1055 · Cited by 141 · see citing works
Cuervo, A. M., Terlecky, S. R., Dice, J. F., & Knecht, E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47204-3 · Cited by 138 · see citing works
Self-citationDice, J. F., Chiang, H. L., Spencer, E., & Backer, J. M. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)62694-3 · Cited by 126 · see citing works
Selective endosomal microautophagy is starvation-inducible inDrosophila
Mukherjee, A., Patel, B., Koga, H., Cuervo, A. M., & Jenny, A. (2016) · Autophagy · doi:10.1080/15548627.2016.1208887 · Cited by 121 · see citing works
Self-citationSuppression of chaperone-mediated autophagy in the renal cortex during acute diabetes mellitus
Sooparb, S., Price, S. R., Jin, S., & Franch, H. A. (2004) · Kidney International · doi:10.1111/j.1523-1755.2004.00639.x · Cited by 114 · see citing works
Ferreira, J. V., Soares, A. R., Ramalho, J. S., Pereira, P., & Girão, H. (2015) · Scientific Reports · doi:10.1038/srep10210 · Cited by 99 · see citing works
Regulation of Chk1 Kinase by Autoinhibition and ATR-mediated Phosphorylation
Katsuragi, Y., & Sagata, N. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-12-0874 · Cited by 78 · see citing works
Gough, N. R., Hatem, C. L., & Fambrough, D. M. (1995) · DNA and Cell Biology · doi:10.1089/dna.1995.14.863 · Cited by 71 · see citing works
Structure-Guided Evolution of Potent and Selective CHK1 Inhibitors through Scaffold Morphing
Reader, J. C., Matthews, T. P., Klair, S., Cheung, K.-M. J., Scanlon, J., Proisy, N., Addison, G., Ellard, J. M., Piton, N., Taylor, S., et al. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm2007326 · Cited by 60 · see citing works
Simple, Consistent Wrappers for Common String Operations
Wickham, H. (2015) · Cited by 57 · see citing works
Analysis of Chaperone-Mediated Autophagy
Juste, Y. R., & Cuervo, A. M. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-8873-0_47 · Cited by 55 · see citing works
Self-citationCMA restricted to mammals and birds: myth or reality?
Lescat, L., Herpin, A., Mourot, B., Véron, V., Guiguen, Y., Bobe, J., & Seiliez, I. (2018) · Autophagy · doi:10.1080/15548627.2018.1460021 · Cited by 29 · see citing works
Flagged first, then by citations
2 of the 62 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Klionsky, D. J., Abdel-Aziz, A. K., Abdelfatah, S., Abdellatif, M., Abdoli, A., Abel, S., Abeliovich, H., Abildgaard, M. H., Abudu, Y. P., Acevedo-Arozena, A., et al. (2021) · Autophagy · doi:10.1080/15548627.2020.1797280 · Cited by 2,622 · see citing works
Extracellular Vesicles and Nanoparticles: Emerging Complexities
Jeppesen, D. K., Zhang, Q., Franklin, J. L., & Coffey, R. J. (2023) · Trends in Cell Biology · doi:10.1016/j.tcb.2023.01.002 · Cited by 705 · 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-citationAlquezar, C., Arya, S., & Kao, A. W. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2020.595532 · Cited by 367 · 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
Self-citationAutophagy and the hallmarks of aging
Kaushik, S., Tasset, I., Arias, E., Pampliega, O., Wong, E., Martinez-Vicente, M., & Cuervo, A. M. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101468 · Cited by 285 · see citing works
Self-citationChaperone-mediated autophagy sustains haematopoietic stem-cell function
Dong, S., Wang, Q., Kao, Y.-R., Diaz, A., Tasset, I., Kaushik, S., Thiruthuvanathan, V., Zintiridou, A., Nieves, E., Dzieciatkowska, M., et al. (2021) · Nature · doi:10.1038/s41586-020-03129-z · Cited by 275 · see citing works
Self-citationThe multifaceted role of autophagy in cancer
Russell, R. C., & Guan, K. (2022) · The EMBO Journal · doi:10.15252/embj.2021110031 · Cited by 229 · 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
Self-citationYun, C. W., Jeon, J., Go, G., Lee, J. H., & Lee, S. H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms22010179 · Cited by 208 · see citing works
Proteostasis Failure in Neurodegenerative Diseases: Focus on Oxidative Stress
Höhn, A., Tramutola, A., & Cascella, R. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/5497046 · Cited by 197 · see citing works
Progress in understanding the role of lncRNA in programmed cell death
Jiang, N., Zhang, X., Gu, X., Li, X., & Shang, L. (2021) · Cell Death Discovery · doi:10.1038/s41420-021-00407-1 · Cited by 183 · see citing works
Autophagy in the diabetic heart: A potential pharmacotherapeutic target in diabetic cardiomyopathy
Dewanjee, S., Vallamkondu, J., Kalra, R. S., John, A. A., Reddy, P. H., & Kandimalla, R. J. L. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101338 · Cited by 174 · see citing works
Xu, X., Sun, Y., Cen, X., Shan, B., Zhao, Q., Xie, T., Wang, Z., Hou, T., Xue, Y., Zhang, M., et al. (2021) · Protein & Cell · doi:10.1007/s13238-021-00858-3 · Cited by 171 · see citing works
Limorenko, G., & Lashuel, H. A. (2021) · Chemical Society Reviews · doi:10.1039/d1cs00127b · Cited by 162 · see citing works
Kuo, S.-H., Tasset, I., Cheng, M. M., Diaz, A., Pan, M.-K., Lieberman, O. J., Hutten, S. J., Alcalay, R. N., Kim, S., Ximénez-Embún, P., et al. (2022) · Science Advances · doi:10.1126/sciadv.abm6393 · Cited by 153 · see citing works
Self-citationProtective role of chaperone-mediated autophagy against atherosclerosis
Madrigal‐Matute, J., de Bruijn, J., van Kuijk, K., Riascos‐Bernal, D. F., Díaz, A., Tasset, I., Martín‐Segura, A., Gijbels, M. J., Sander, B., Kaushik, S., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2121133119 · Cited by 105 · see citing works
Self-citationChaperone‐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
Chaperone-mediated autophagy regulates the pluripotency of embryonic stem cells
Xu, Y., Zhang, Y., García‐Cañaveras, J. C., Guo, L., Kan, M., Yu, S., Blair, I. A., Rabinowitz, J. D., & Yang, X. (2020) · Science · doi:10.1126/science.abb4467 · Cited by 99 · see citing works
Through the back door: Unconventional protein secretion
Cohen, M. J., Chirico, W. J., & Lipke, P. N. (2020) · The Cell Surface · doi:10.1016/j.tcsw.2020.100045 · Cited by 97 · see citing works
Wu, J., Han, Y., Xu, H., Sun, H., Wang, R., Ren, H., & Wang, G. (2023) · Science Advances · doi:10.1126/sciadv.adi8343 · Cited by 101 · see citing works
Pros and Cons of Chaperone-Mediated Autophagy in Cancer Biology
Arias, E., & Cuervo, A. M. (2019) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2019.09.007 · Cited by 93 · see citing works
Self-citationChaperone‐mediated autophagy degrades Keap1 and promotes Nrf2‐mediated antioxidative response
Zhu, L., He, S., Huang, L. H., Ren, D., Nie, T., Tao, K. X., Li, X., Lu, F., Mao, Z., & Yang, Q. (2022) · Aging Cell · doi:10.1111/acel.13616 · Cited by 93 · see citing works
Zhao, P., Yin, S., Qiu, Y., Sun, C., & Yu, H. (2025) · Molecular Cancer · doi:10.1186/s12943-024-02217-2 · Cited by 90 · see citing works
The Role of Chaperone-Mediated Autophagy in Cell Cycle Control and Its Implications in Cancer
Andrade-Tomaz, M., de Souza, I., Rocha, C. R. R., & Gomes, L. R. (2020) · Cells · doi:10.3390/cells9092140 · Cited by 82 · see citing works
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
Reciprocal regulation of chaperone-mediated autophagy and the circadian clock
Juste, Y. R., Kaushik, S., Bourdenx, M., Aflakpui, R., Bandyopadhyay, S., Garcı́a, F., Díaz, A., Lindenau, K. L., Tu, V., Krause, G. J., et al. (2021) · Nature Cell Biology · doi:10.1038/s41556-021-00800-z · Cited by 78 · see citing works
Self-citationAdvancing targeted protein degradation for metabolic diseases therapy
Zhou, Q., Xiao, H., Yang, F., Wang, Y., Li, P., & Zheng, Z. (2022) · Pharmacological Research · doi:10.1016/j.phrs.2022.106627 · Cited by 76 · see citing works
Jiang, T., Chen, X., Ren, X., Yang, J., & Cheng, Y. (2021) · Drug Resistance Updates · doi:10.1016/j.drup.2021.100752 · Cited by 72 · see citing works
Gong, Y., Li, Z., Zou, S., Deng, D., Lai, P., Hu, H., Yao, Y., Hu, L., Zhang, S., Li, K., et al. (2021) · Developmental Cell · doi:10.1016/j.devcel.2021.06.011 · Cited by 72 · see citing works
Kluever, V., Russo, B., Mandad, S., Hemandhar-Kumar, N., Alevra, M., Ori, A., Rizzoli, S. O., Urlaub, H., Schneider, A., & Fornasiero, E. F. (2022) · Science Advances · doi:10.1126/sciadv.abn4437 · Cited by 69 · see citing works
Wang, M., Zhang, Z., Chen, M., Lv, Y., Tian, S., Meng, F., Zhang, Y., Guo, X., Chen, Y., Yang, M. G., et al. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-06027-0 · Cited by 67 · see citing works
Zhang, W., Yang, X., Chen, L., Liu, Y.-Y., Venkatarangan, V., Reist, L., Hanson, P., Xu, H.-X., Wang, Y.-Z., & Li, M. (2021) · PLoS Biology · doi:10.1371/journal.pbio.3001361 · Cited by 53 · see citing works
Nucleolin: a cell portal for viruses, bacteria, and toxins
Tonello, F., Massimino, M. L., & Peggion, C. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04300-7 · Cited by 57 · see citing works
Dysfunction 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 55 · see citing works
Gómez‐Sintes, R., Xin, Q., Jiménez‐Loygorri, J. I., McCabe, M., Díaz, A., Garner, T. P., Cotto-Rios, X. M., Wu, Y., Dong, S., Reynolds, C. A., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31869-1 · Cited by 54 · see citing works
Self-citationRole of VAMP7-Dependent Secretion of Reticulon 3 in Neurite Growth
Wojnacki, J., Nola, S., Bun, P., Cholley, B., Filippini, F., Pressé, M. T., Lipecka, J., Lam, S. M., Nguyen, J., Simon, A., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108536 · Cited by 54 · see citing works
Desideri, E., Castelli, S., Dorard, C., Toifl, S., Grazi, G. L., Ciriolo, M. R., & Baccarini, M. (2022) · Autophagy · doi:10.1080/15548627.2022.2063004 · Cited by 53 · see citing works
Ferraz, L. C., Pereira, P., & Ferreira, J. V. (2025) · Advanced Healthcare Materials · doi:10.1002/adhm.202501349 · Cited by 53 · see citing works
Autophagy in farm animals: current knowledge and future challenges
Tesseraud, S., Avril, P., Bonnet, M., Bonnieu, A., Cassar‐Malek, I., Chabi, B., Dessauge, F., Gabillard, J., Perruchot, M., & Seiliez, I. (2020) · Autophagy · doi:10.1080/15548627.2020.1798064 · Cited by 52 · see citing works
Modulating Chaperone-Mediated Autophagy and Its Clinical Applications in Cancer
Hubert, V., Weiss, S., Rees, A. J., & Kain, R. (2022) · Cells · doi:10.3390/cells11162562 · Cited by 50 · see citing works
Pradas, E., & Martínez‐Vicente, M. (2023) · Cells · doi:10.3390/cells12010191 · Cited by 50 · see citing works
Nie, T., Tao, K., Zhu, L., Huang, L. H., Hu, S., Yang, R., Xu, P., Mao, Z., & Yang, Q. (2020) · Autophagy · doi:10.1080/15548627.2020.1848128 · Cited by 49 · see citing works
Wobble tRNA modification and hydrophilic amino acid patterns dictate protein fate
Rapino, F. A., Zhou, Z., Sanchez, A. M. R., Joiret, M., Seca, C., Hachem, N. E., Valenti, G., Latini, S., Shostak, K., Geris, L., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-22254-5 · Cited by 46 · see citing works
Chaperone-mediated autophagy regulates adipocyte differentiation
Kaushik, S., Juste, Y. R., Lindenau, K. L., Dong, S., Macho‐González, A., Santiago‐Fernández, O., McCabe, M., Singh, R., Gavathiotis, E., & Cuervo, A. M. (2022) · Science Advances · doi:10.1126/sciadv.abq2733 · Cited by 46 · see citing works
Self-citationImpact of Chaperone-Mediated Autophagy in Brain Aging: Neurodegenerative Diseases and Glioblastoma
Auzmendi-Iriarte, J., & Matheu, A. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.630743 · Cited by 45 · see citing works
Autophagy and senescence: the molecular mechanisms and implications in liver diseases
Li, Q., Lin, Y., Liang, G., Xiao, N., Zhang, H., Yang, X., Yang, J., & Liu, A. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242316880 · Cited by 43 · see citing works
The Role of Autophagy in Pancreatic Cancer: From Bench to the Dark Bedside
Görgülü, K., Diakopoulos, K. N., Kaya-Aksoy, E., Ciecielski, K. J., Ai, J., Lesina, M., & Algül, H. (2020) · Cells · doi:10.3390/cells9041063 · Cited by 42 · see citing works
Inhibition of class I PI3K enhances chaperone-mediated autophagy
Endicott, S. J., Ziemba, Z., Beckmann, L. J., Boynton, D. N., & Miller, R. A. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.202001031 · Cited by 42 · see citing works
Zavadskiy, S. P., Sologova, S. S., & Moldogazieva, N. T. (2021) · Biochimie · doi:10.1016/j.biochi.2021.12.002 · Cited by 42 · see citing works
Wang, T., Luo, R., Zhang, J., Lan, J., Lu, Z., Zhai, H., Li, L., Sun, Y., & Qiu, H. (2024) · Emerging Microbes & Infections · doi:10.1080/22221751.2024.2333381 · Cited by 39 · see citing works
Li, B., Ming, H., Qin, S., Zhou, L., Huang, Z., Jin, P., Peng, L., Luo, M., Zhang, T., Wang, K., et al. (2023) · Advanced Science · doi:10.1002/advs.202306535 · Cited by 38 · see citing works
Dong, R., Qin, C., Yin, Y., Han, L., Xiao, C., Wang, K., Wei, R., Xia, Y., & Kong, L. (2023) · British Journal of Pharmacology · doi:10.1111/bph.16165 · Cited by 37 · see citing works
The Role of Pericytes in Regulation of Innate and Adaptive Immunity
Dabravolski, S. A., Andreeva, E. R., Eremin, I. I., Markin, A. M., Nadelyaeva, I. I., Orekhov, A. N., & Melnichenko, A. А. (2023) · Biomedicines · doi:10.3390/biomedicines11020600 · Cited by 36 · see citing works
Lysosomes in acute myeloid leukemia: potential therapeutic targets?
Rafiq, S., McKenna, S. L., Muller, S., Tschan, M. P., & Humbert, M. (2021) · Leukemia · doi:10.1038/s41375-021-01388-x · Cited by 34 · see citing works
Gao, Y., Wang, C., Jiang, D. M., An, G., Jin, F. J., Zhang, J., Han, G., Cui, C., & Jiang, P. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.994037 · Cited by 37 · see citing works
Krause, G. J., Diaz, A., Jafari, M., Khawaja, R. R., Agullo‐Pascual, E., Santiago‐Fernández, O., Richards, A. L., Chen, K., Dmitriev, P., Sun, Y., et al. (2022) · Aging Cell · doi:10.1111/acel.13713 · Cited by 35 · see citing works
Self-citationWang, Y., Chen, Y., Gao, G., Zheng, Y.-H., Yu, N., Ouyang, L., Gao, X., Li, N., Wen, S., Huang, S., et al. (2023) · Molecular Therapy · doi:10.1016/j.ymthe.2023.05.015 · Cited by 35 · see citing works
Emerging roles of palmitoylation in pyroptosis
Zhang, N., Yang, Y., & Xu, D. (2024) · Trends in Cell Biology · doi:10.1016/j.tcb.2024.10.005 · Cited by 35 · see citing works
Differential activation of eMI by distinct forms of cellular stress
Mesquita, A., Glenn, J., & Jenny, A. (2020) · Autophagy · doi:10.1080/15548627.2020.1783833 · Cited by 35 · see citing works
Schnebert, S., Goguet, M., Vélez, E. J., Depincé, A., Beaumatin, F., Herpin, A., & Seiliez, I. (2022) · Cells · doi:10.3390/cells11121945 · Cited by 35 · see citing works
Calorie restriction and calorie-restriction mimetics activate chaperone-mediated autophagy
Jafari, M., Macho‐González, A., Díaz, A., Lindenau, K. L., Santiago‐Fernández, O., Zeng, M., Massey, A. C., de Cabo, R., Kaushik, S., & Cuervo, A. M. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2317945121 · Cited by 34 · see citing works
Self-citationKacal, M., Zhang, B., Hao, Y., Norberg, E., & Vakifahmetoglu-Norberg, H. (2021) · Autophagy · doi:10.1080/15548627.2021.1876343 · Cited by 34 · see citing works
Chaperone-Mediated Autophagy of eNOS in Myocardial Ischemia-Reperfusion Injury
Subramani, J., Kundumani‐Sridharan, V., & Das, K. C. (2021) · Circulation Research · doi:10.1161/circresaha.120.317921 · Cited by 32 · see citing works
Retinal Pigment Epithelium Under Oxidative Stress: Chaperoning Autophagy and Beyond
Markitantova, Y. V., & Simirskii, V. N. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26031193 · Cited by 32 · see citing works
Autophagy and Alzheimer’s Disease: Mechanisms and Impact Beyond the Brain
Hein, Z. M., Vishnumukkala, T., Karikalan, B., Alkatiri, A., Hussan, F., Jagadeesan, S., Kamaruzzaman, M. A., Ramli, M. D. C., Nassir, C. M. N. C. M., & Gopalakrishna, P. K. (2025) · Cells · doi:10.3390/cells14120911 · Cited by 36 · see citing works
Chaperone-Mediated Autophagy in the Liver: Good or Bad?
Dash, S., Aydın, Y., & Moroz, K. (2019) · Cells · doi:10.3390/cells8111308 · Cited by 30 · see citing works
TRIM21 Is Targeted for Chaperone-Mediated Autophagy during Salmonella Typhimurium Infection
Hos, N. J., Fischer, J., Hos, D., Hejazi, Z., Calabrese, C., Ganesan, R., Murthy, A. M. V., Rybniker, J., Kumar, S., Krönke, M., et al. (2020) · The Journal of Immunology · doi:10.4049/jimmunol.2000048 · Cited by 30 · see citing works
Losmanová, T., Janser, F. A., Humbert, M., Tokarchuk, I., Schläfli, A. M., Neppl, C., Schmid, R. A., Tschan, M. P., Langer, R., & Berezowska, S. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/8506572 · Cited by 30 · see citing works
Krause, G. J., Kirchner, P., Stiller, B., Morozova, K., Díaz, A., Chen, K.-H., Krogan, N., Agulló-Pascual, E., Clement, C. C., Lindenau, K., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.113529 · Cited by 30 · see citing works
Self-citationChaperone-mediated autophagy and disease: Implications for cancer and neurodegeneration
Gómez‐Sintes, R., & Arias, E. (2021) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2021.101025 · Cited by 29 · see citing works
Dysregulated proteostasis network in neuronal diseases
Tseng, C.-S., Chao, Y.-W., Liu, Y.-H., Huang, Y., & Chao, H. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1075215 · Cited by 28 · see citing works
Cholesterol trafficking, lysosomal function, and atherosclerosis
Skeyni, A., Pradignac, A., Matz, R. L., Terrand, J., & Boucher, P. (2023) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00415.2023 · Cited by 28 · see citing works
Molina, M. L., García‐Bernal, D., Salinas, M. D., Rubio, G., Aparicio, P., Moraleda, J. M., Martı́nez, S., & Valdor, R. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.797945 · Cited by 27 · see citing works
Ma, Y., Huang, X., Wang, Y., Lei, Y., Yu, J., Yu, S., Gao, Y., Yang, J. J., Zhao, F., Yu, H., et al. (2023) · Advanced Science · doi:10.1002/advs.202305907 · Cited by 25 · see citing works
Roles of Stress Response in Autophagy Processes and Aging-Related Diseases
Watanabe, Y., Taguchi, K., & Tanaka, M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241813804 · Cited by 26 · see citing works
Li, X., Sun, W., Huang, M., Gong, L., Zhang, X., Li, Z., Calderon, V., Bian, Z., He, Y., Suh, W., et al. (2024) · Immunity · doi:10.1016/j.immuni.2024.04.023 · Cited by 24 · see citing works
Huang, J., & Wang, J. (2024) · Molecular Medicine Reports · doi:10.3892/mmr.2024.13378 · Cited by 27 · see citing works
Heat therapy: possible benefits for cognitive function and the aging brain
Schulze, A. T. V., Deng, F., Morris, J. K., & Geiger, P. C. (2020) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00168.2020 · Cited by 25 · see citing works
Assessment of mammalian endosomal microautophagy
Krause, G. J., & Cuervo, A. M. (2020) · Methods in cell biology · doi:10.1016/bs.mcb.2020.10.009 · Cited by 25 · see citing works
Self-citationCD4+ T-Cell Legumain Deficiency Attenuates Hypertensive Damage via Preservation of TRAF6
He, Y., Zou, P., Lu, J., Lu, Y., Yuan, S., Zheng, X., Liu, J., Zeng, C. C., Liu, L., Tang, L., et al. (2023) · Circulation Research · doi:10.1161/circresaha.123.322835 · Cited by 25 · see citing works
Autophagy in aquatic animals: mechanisms, implications, and future directions
Kawsar, M. A., Adikari, D., & Zhang, Y. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1612178 · Cited by 25 · see citing works
Heat Treatment Improves Hepatic Mitochondrial Respiratory Efficiency via Mitochondrial Remodeling
Schulze, A. T. V., Deng, F., Fuller, K. N. Z., Franczak, E., Miller, J., Allen, J., McCoin, C. S., Shankar, K., Ding, W., Thyfault, J. P., et al. (2021) · Function · doi:10.1093/function/zqab001 · Cited by 24 · see citing works
Wu, Z., Shu, Y., Jiang, Z., Zhu, Y., Liang, H., Shi, Y., Li, S., Zhang, S., Xu, Y., Hong, C., et al. (2025) · Autophagy · doi:10.1080/15548627.2025.2544287 · Cited by 22 · see citing works
Defining the reference proteomes for small extracellular vesicles and non-vesicular components
Morales‐Sanfrutos, J., Etxeberria-Ugartemendia, J., Barroso‐Gomila, O., Gonzalez, E., Sendino, M., Ximénez‐Embún, P., Garcı́a, F., Zarzuela, E., Falcón‐Pérez, J. M., Peinado, H., et al. (2026) · Nature Cell Biology · doi:10.1038/s41556-026-01878-z · Cited by 23 · see citing works
Li, Q., Yue, T., Du, X., Tang, Z., Cui, J., Wang, W., Xia, W., Ren, B., Kan, S., Li, C., et al. (2022) · Cell Death and Differentiation · doi:10.1038/s41418-022-01068-y · Cited by 22 · see citing works
Cellular Protein Quality Control in Diabetic Cardiomyopathy: From Bench to Bedside
Kaur, N., Raja, R., Ruiz‐Velasco, A., & Liu, W. (2020) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2020.585309 · Cited by 23 · see citing works
Mechanisms and implications of podocyte autophagy in chronic kidney disease
Njeim, R., Merscher, S., & Fornoni, A. (2024) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00415.2023 · Cited by 22 · see citing works
Assessing Autophagy in Archived Tissue or How to Capture Autophagic Flux from a Tissue Snapshot
Humbert, M., Morán, M., de la Cruz‐Ojeda, P., Muntané, J., Wiedmer, T., Apostolova, N., McKenna, S. L., Velasco, G., Balduini, W., Eckhart, L., et al. (2020) · Biology · doi:10.3390/biology9030059 · Cited by 21 · see citing works
Bai, F., Wu, Q.-Q., Wu, Y., Hu, Y., Jiang, Z.-X., Lv, H., Qian, W.-Z., Cai, C., & Wu, J. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-05116-w · Cited by 21 · see citing works
Du, M., Yu, Y., Wang, J., & Ji, C. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms27010366 · Cited by 20 · see citing works
A Crucial Role for the Protein Quality Control System in Motor Neuron Diseases
Cristofani, R., Crippa, V., Cicardi, M. E., Tedesco, B., Ferrari, V., Chierichetti, M., Casarotto, E., Piccolella, M., Messi, E., Galbiati, M., et al. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.00191 · Cited by 20 · see citing works
Rahman, F., Johnson, J. L., Zhang, J., He, J. N., Pestonjamasp, K. N., Cherqui, S., & Catz, S. D. (2021) · Autophagy · doi:10.1080/15548627.2021.1971937 · Cited by 20 · see citing works
PTEN is both an activator and a substrate of chaperone-mediated autophagy
Zhang, K. K., Burns, C. M., Skinner, M. E., Lombard, D. B., Miller, R. A., & Endicott, S. J. (2023) · The Journal of Cell Biology · doi:10.1083/jcb.202208150 · Cited by 20 · see citing works
Choi, Y., Yun, S. H., Yu, J., Mun, Y., Lee, W., Park, C. J., Han, B. W., & Lee, B. (2023) · Molecular Metabolism · doi:10.1016/j.molmet.2023.101784 · Cited by 20 · see citing works
Chaperone-mediated autophagy protects against hyperglycemic stress
Vélez, E. J., Schnebert, S., Goguet, M., Balbuena-Pecino, S., Dias, K., Beauclair, L., Fontagné-Dicharry, S., Véron, V., Depincé, A., Beaumatin, F., et al. (2023) · Autophagy · doi:10.1080/15548627.2023.2267415 · Cited by 20 · see citing works
Late endosomes promote microglia migration via cytosolic translocation of immature protease cathD
Liu, Y.-J., Zhang, T., Cheng, D., Yang, J., Chen, S., Wang, X., Li, X., Duan, D., Lou, H., Zhu, L., et al. (2020) · Science Advances · doi:10.1126/sciadv.aba5783 · Cited by 19 · see citing works
Karampa, A. D., GOUSSIA, A. C., Glantzounis, G. K., Mastoridou, E. M., Anastasopoulos, N.-A., & Charchanti, A. V. (2022) · Cancers · doi:10.3390/cancers14030760 · Cited by 20 · see citing works
New Insights into the Mechanisms of Chaperon-Mediated Autophagy and Implications for Kidney Diseases
Yuan, Z., Wang, S., Tan, X., & Wang, D. (2022) · Cells · doi:10.3390/cells11030406 · Cited by 21 · see citing works
Chaperone mediated autophagy contributes to the newly synthesized histones H3 and H4 quality control
Hormazábal, J., Saavedra, F., Espinoza-Arratia, C., Martínez, N. W., Cruces, T., Alfaro, I. E., & Loyola, A. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkab1296 · Cited by 19 · see citing works
- Authors
- Kirchner, P., Bourdenx, M., Madrigal-Matute, J., Tiano, S., Diaz, A., Bartholdy, B. A., Will, B., & Cuervo, A. M.
- Affiliations
- Albert Einstein College of Medicine (US)
- ORCID
- Venue
- PLOS Biology
- Publisher
- Public Library of Science (PLoS)
- Published
- 2019-05-31
- Volume
- 17
- Issue
- 5
- Pages
- e3000301
- ISSN
- 1544-9173 (ISSN-L)
- 1545-7885
- PMC
- PMC6561683
- OpenAlex
- W2947390945
- Cited by
- 257
- References
- 62
- Citations by year
- 2026: 47 · 2025: 39 · 2024: 30 · 2023: 36 · 2022: 42 · 2021: 36 · 2020: 24 · 2019: 3
- FWCI
- 19.98
- Type
- journal article
- Language
- en
- Update notices
- Open access
- gold
- doi.org
- Licence
- Locations
- PLoS Biology (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Figshare (submittedVersion, cc-by)
- Funders
- National Institute on Aging (AG031782, AG021904, AG038072)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK098408)
- JPB Foundation (Cuervo 1)
- Fondation Leducq (RA15CVD04)
- American Heart Association (17POST33650088)
- Deutsche Forschungemeinschaft (KI 1992/1-1)
- Topics
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- chaperone-mediated autophagy, Hsc70, lysosomal degradation, biological process enrichment
- MeSH terms
- Chaperone-Mediated Autophagy, Amino Acid Sequence, Animals, Drosophila melanogaster, Humans, Saccharomyces cerevisiae, Conserved Sequence, Evolution, Molecular, Proteome, Amino Acid Motifs, NIH 3T3 Cells, Mice
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
