The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.
TFEB Links Autophagy to Lysosomal Biogenesis
Open accessAbstract
Starvation activates a transcriptional program controlling autophagosome formation, lysosome fusion, and substrate 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.
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 source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Transcription factor E3 (TFE3) and transcription factor EB (TFEB) are two major members of the microphthalmia-transcription factor E (MiT/TFE) subfamily and well characterized as master regulators of lysosome biogenesis and autophagy1–4.”
From PDCD4 triggers α-synuclein accumulation and motor deficits via co-suppressing TFE3 and TFEB translation in a model of Parkinson’s disease (2024) · cites this paper as [1]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“A gene regulatory network, named CLEAR (coordinated lysosomal enhancement and regulation) that controls both lysosome and autophagosome biogenesis was identified using a systemsbiology approach.[463][464][465]”
From Guidelines for the use and interpretation of assays for monitoring autophagy (2012) · cites this paper as [463]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“In a first case, starting from experimental data available in the literature, we identified 20 targets related to autophagy activation and validated them by qPCR: ATG10, ATG14, ATG16L1, ATG3, ATG4, ATG7, ATG9A, BCL2, GABARAP, GABARAPL1, MAP1LC3B, NBR1, OPTN, PINK1, SQSTM1, ULK1, ULK2, UVRAG, WDR45, WIPI1 (Fig. 2) [18–27].”
From A gene toolbox for monitoring autophagy transcription (2021) · cites this paper as [18]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Moreover, retromer-knockout cells display activation of the TFEB transcription factors (Curnock et al., 2019), master regulators of cellular nutrient sensing and energy metabolism (Sardiello et al., 2009; Settembre et al., 2011).”
From Acute inactivation of retromer and ESCPE-1 leads to time-resolved defects in endosomal cargo sorting (2020) · cites this paper as Settembre et al., 2011
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“NRF2 or TFEB pathways were unaltered as shown by the lack of change in the level of NQO-1 and HO-1, two major targets of NRF2, or the intensity of nuclear TFEB in response to hα-Syn46,47 (Supplementary Fig. 4i, j).”
From Microglia clear neuron-released α-synuclein via selective autophagy and prevent neurodegeneration (2020) · cites this paper as [47]
The cited source says what the claim attributes to it.
In the citing paper
“TFEB activity is regulated by starvation, 463 and can thus serve as a new tool for monitoring transcriptional regulation connected with autophagy.”
From Guidelines for the use and interpretation of assays for monitoring autophagy (2012) · cites this paper as [463]
The cited source says what the claim attributes to it.
In the citing paper
“For example, this can be achieved either through overexpression or post-translational activation of the gene encoding TFEB (see Transcriptional and translational regulation), a transcriptional regulator of the biogenesis of both lysosomes and autophagosomes.463,464”
From Guidelines for the use and interpretation of assays for monitoring autophagy (2012) · cites this paper as [463]
The cited source says what the claim attributes to it.
In the citing paper
“This transcription factor regulates expression of lysosome biogenesis genes [31].”
From Microglia specific deletion of miR-155 in Alzheimer’s disease mouse models reduces amyloid-β pathology but causes hyperexcitability and seizures (2023) · cites this paper as [31]
The cited source says what the claim attributes to it.
In the citing paper
“we identified that Tfeb, transcription factor and modulator of lysosome biogenesis [31], may be targeted by miR-155.”
From Microglia specific deletion of miR-155 in Alzheimer’s disease mouse models reduces amyloid-β pathology but causes hyperexcitability and seizures (2023) · cites this paper as [31]
The cited source says what the claim attributes to it.
In the citing paper
“A so called “activation list” has been derived from the comparison of publications, in which we reported conditions of gene up-regulation upon autophagy activation [18–27].”
From A gene toolbox for monitoring autophagy transcription (2021) · cites this paper as [18]
The cited source says what the claim attributes to it.
In the citing paper
“Hence, for the second sub-lists, we identified 26 targets to assess the state of lysosomal biogenesis (Fig. 2) at variance with the autophagy activation list, this sub-list has been realized by only comparing data from recent work, in which mRNA levels of lysosomal genes in response to autophagy enhancement were accurately and experimentally examined [15, 18, 19, 28–30].”
From A gene toolbox for monitoring autophagy transcription (2021) · cites this paper as [18]
The cited source says what the claim attributes to it.
In the citing paper
“The restricted “induction list” for the prediction of autophagy activation state, made by 20 targets, was obtained combining data from previous publications [18–27], in which have been documented the increase of the mRNA expression following autophagy induction.”
From A gene toolbox for monitoring autophagy transcription (2021) · cites this paper as [18]
The cited source says what the claim attributes to it.
In the citing paper
“Similarly, the list for the evaluation of “lysosomal biogenesis” was created from literature by combining data that underwent preceding experimental validation [15, 18, 19, 28–30].”
From A gene toolbox for monitoring autophagy transcription (2021) · cites this paper as [18]
The check wasn’t confident either way, so it gives no verdict — never disputed.
In the citing paper
“NRF2 or TFEB pathways were unaltered as shown by the lack of change in the level of NQO-1 and HO-1, two major targets of NRF2, or the intensity of nuclear TFEB in response to hα-Syn46,47 (Supplementary Fig. 4i, j).”
From Microglia clear neuron-released α-synuclein via selective autophagy and prevent neurodegeneration (2020) · cites this paper as [47]
Experimental — accuracy not yet measuredThe check wasn’t confident either way, so it gives no verdict — never disputed.
In the citing paper
“The “lysosomal biogenesis list” resulted instead from an extensive literature analysis, obtained by combining data that underwent previous experimental validation [15, 18, 19, 28–30].”
From A gene toolbox for monitoring autophagy transcription (2021) · cites this paper as [18]
Experimental — accuracy not yet measuredIn the citing paper
“Global regulation of the myriad effectors and phases of autophagy is overseen by TFEB (transcription factor EB), a basic helix-loop-helix leucine zipper that directs expression of autophagy and lysosomal genes comprising the coordinated lysosomal expression and regulation (CLEAR) network by binding to a conserved promoter motif [47,48].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [48]
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
AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
Kim, J., Kundu, M., Viollet, B., & Guan, K.-L. (2011) · Nature Cell Biology · doi:10.1038/ncb2152 · Cited by 7,227
Autophagy in the Pathogenesis of Disease
Levine, B., & Kroemer, G. (2008) · Cell · doi:10.1016/j.cell.2007.12.018 · Cited by 7,069
Methods in Mammalian Autophagy Research
Mizushima, N., Yoshimori, T., & Levine, B. (2010) · Cell · doi:10.1016/j.cell.2010.01.028 · Cited by 4,497
Autophagy and Viruses: Adversaries or Allies?
Dong, X., & Levine, B. (2013) · Journal of Innate Immunity · doi:10.1159/000346388 · Cited by 4,444
Autophagy: process and functionPreprint
Mizushima, N. (2007) · Genes & Development · doi:10.1101/gad.1599207 · Cited by 4,104
Regulation mechanisms and signaling pathways of autophagy
He, C., & Klionsky, D. J. (2009) · Annual Review of Genetics · doi:10.1146/annurev-genet-102808-114910 · Cited by 3,609
Antimicrobial Autophagy: A Conserved Innate Immune Response in Drosophila
Moy, R. H., & Cherry, S. R. (2013) · Journal of Innate Immunity · doi:10.1159/000350326 · Cited by 3,551
Phosphorylation of ULK1 (hATG1) by AMP-Activated Protein Kinase Connects Energy Sensing to Mitophagy
Egan, D. F., Shackelford, D. B., Mihaylova, M. M., Gelino, S., Kohnz, R. A., Mair, W., Vasquez, D. S., Joshi, A., Gwinn, D. M., Taylor, R., et al. (2011) · Science · doi:10.1126/science.1196371 · Cited by 2,600
A Gene Network Regulating Lysosomal Biogenesis and Function
Sardiello, M., Palmieri, M., di Ronza, A., Medina, D. L., Valenza, M., Gennarino, V. A., Di Malta, C., Donaudy, F., Embrione, V., Polishchuk, R. S., et al. (2009) · Science · doi:10.1126/science.1174447 · Cited by 2,543
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Items 101–200 of 1,018
Hamacher‐Brady, A., & Brady, N. R. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2087-8 · Cited by 410
Zhou, J., Tan, S.-H., Nicolas, V., Bauvy, C., Yang, N., Zhang, J., Xue, Y., Codogno, P., & Shen, H. (2013) · Cell Research · doi:10.1038/cr.2013.11 · Cited by 397
Autophagy: An Essential Degradation Program for Cellular Homeostasis and Life
Chun, Y., & Kim, J. (2018) · Cells · doi:10.3390/cells7120278 · Cited by 396
Proteoglycan Chemical Diversity Drives Multifunctional Cell Regulation and Therapeutics
Karamanos, N. K., Piperigkou, Z., Theocharis, A. D., Watanabe, H., Franchi, M., Baud, S., Brézillon, S., Götte, M., Passi, A. G., Vigetti, D., et al. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00354 · Cited by 380
Sarkar, S. (2013) · Biochemical Society Transactions · doi:10.1042/bst20130134 · Cited by 380
Role of lysosomes in physiological activities, diseases, and therapy
Zhang, Z., Yue, P., Lu, T., Wang, Y., Wei, Y., & Wei, X. (2021) · Journal of Hematology & Oncology · doi:10.1186/s13045-021-01087-1 · Cited by 375
NUFIP1 is a ribosome receptor for starvation-induced ribophagy
Wyant, G. A., Abu-Remaileh, M., Frenkel, E. M., Laqtom, N. N., Dharamdasani, V., Lewis, C. A., Chan, S. H., Heinze, I., Ori, A., & Sabatini, D. M. (2018) · Science · doi:10.1126/science.aar2663 · Cited by 363
Sahani, M. H., Itakura, E., & Mizushima, N. (2014) · Autophagy · doi:10.4161/auto.27344 · Cited by 348
Autophagosome maturation: An epic journey from the ER to lysosomes
Zhao, Y. G., & Zhang, H. (2018) · The Journal of Cell Biology · doi:10.1083/jcb.201810099 · Cited by 375
Autophagy in the renewal, differentiation and homeostasis of immune cells
Clarke, A. J., & Simon, A. K. (2019) · Nature Reviews Immunology · doi:10.1038/s41577-018-0095-2 · Cited by 361
mTOR Regulates Lysosomal ATP-Sensitive Two-Pore Na+ Channels to Adapt to Metabolic State
Cang, C., Zhou, Y., Navarro, B., Seo, Y.-J., Aranda, K., Shi, L. L., Battaglia-Hsu, S.-F., Nissim, I., Clapham, D. E., & Ren, D. (2013) · Cell · doi:10.1016/j.cell.2013.01.023 · Cited by 373
The mTOR–Autophagy Axis and the Control of Metabolism
Deleyto-Seldas, N., & Efeyan, A. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.655731 · Cited by 378
Mycobacterium tuberculosis induces the miR-33 locus to reprogram autophagy and host lipid metabolism
Ouimet, M. I., Köster, S., Sakowski, E. T., Ramkhelawon, B., Solingen, C. V., Oldebeken, S. R., Karunakaran, D., Portal‐Celhay, C., Sheedy, F. J., Ray, T. D., et al. (2016) · Nature Immunology · doi:10.1038/ni.3434 · Cited by 365
Autophagy in Parkinson's Disease
Hou, X., Watzlawik, J. O., Fiesel, F. C., & Springer, W. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.01.037 · Cited by 361
Bordi, M., Berg, M. J., Mohan, P. S., Peterhoff, C. M., Alldred, M. J., Che, S., Ginsberg, S. D., & Nixon, R. A. (2016) · Autophagy · doi:10.1080/15548627.2016.1239003 · Cited by 353
Exploiting macrophage autophagy-lysosomal biogenesis as a therapy for atherosclerosis
Sergin, I., Evans, T. D., Zhang, X., Bhattacharya, S., Stokes, C. J., Song, E., Ali, S., Dehestani, B., Holloway, K. B., Micevych, P. S., et al. (2017) · Nature Communications · doi:10.1038/ncomms15750 · Cited by 351
Self-citationSelective clearance of aberrant tau proteins and rescue of neurotoxicity by transcription factor EB
Polito, V. A., Li, H., Martini‐Stoica, H., Wang, B., Li, Y., Xu, Y., Swartzlander, D. B., Palmieri, M., di Ronza, A., Lee, V. M. ‐., et al. (2014) · EMBO Molecular Medicine · doi:10.15252/emmm.201303671 · Cited by 356
Self-citationRag GTPases mediate amino acid–dependent recruitment of TFEB and MITF to lysosomes
Martina, J. A., & Puertollano, R. (2013) · Journal of Cell Biology · doi:10.1083/jcb.201209135 · Cited by 354
Beige adipocyte maintenance is regulated by autophagy-induced mitochondrial clearance
Altshuler-Keylin, S., Shinoda, K., Hasegawa, Y., Ikeda, K., Hong, H., Kang, Q., Yang, Y., Perera, R. M., Debnath, J., & Kajimura, S. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.08.002 · Cited by 349
Protein kinase C controls lysosome biogenesis independently of mTORC1
Li, Y., Xu, M., Ding, X., Chen, Y., Song, Z., Chen, L., Huang, X., Wang, X., Jian, Y., Tang, G., et al. (2016) · Nature Cell Biology · doi:10.1038/ncb3407 · Cited by 357
Hydroxychloroquine in systemic lupus erythematosus (SLE)
Ponticelli, C. E., & Moroni, G. L. (2016) · Expert Opinion on Drug Safety · doi:10.1080/14740338.2017.1269168 · Cited by 353
Carballo‐Carbajal, I., Laguna, A., Romero‐Giménez, J., Cuadros, T., Bové, J., Martínez‐Vicente, M., Parent, A., González-Sepúlveda, M., Peñuelas, N., Torra, A., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-08858-y · Cited by 345
Self-citationDevelopment of autophagy inducers in clinical medicine
Levine, B., Packer, M., & Codogno, P. (2015) · Journal of Clinical Investigation · doi:10.1172/jci73938 · Cited by 351
Chao, X., Wang, S., Zhao, K., Li, Y., Williams, J. A., Li, T., Chavan, H., Krishnamurthy, P., He, X. C., Li, L., et al. (2018) · Gastroenterology · doi:10.1053/j.gastro.2018.05.027 · Cited by 342
Self-citationPolyamines control eIF5A hypusination, TFEB translation, and autophagy to reverse B cell senescence
Zhang, H., Alsaleh, G., Feltham, J., Sun, Y., Napolitano, G., Riffelmacher, T., Charles, P., Frau, L., Hublitz, P., Yu, Z., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.08.005 · Cited by 341
Self-citationTranscription factor EB (TFEB) is a new therapeutic target for Pompe disease
Spampanato, C., Feeney, E., Li, L., Cardone, M., Lim, J., Annunziata, F., Zare, H., Polishchuk, R., Puertollano, R., Parenti, G., et al. (2013) · EMBO Molecular Medicine · doi:10.1002/emmm.201202176 · Cited by 341
Self-citationLysosomal impairment in Parkinson's disease
Dehay, B., Martinez‐Vicente, M., Caldwell, G. A., Caldwell, K. A., Yue, Z., Cookson, M. R., Klein, C., Vila, M., & Bezard, E. (2013) · Movement Disorders · doi:10.1002/mds.25462 · Cited by 340
Transcriptional and epigenetic regulation of autophagy in aging
Lapierre, L. R., Kumsta, C., Sandri, M., Ballabio, A., & Hansen, M. (2015) · Autophagy · doi:10.1080/15548627.2015.1034410 · Cited by 344
Self-citationPerluigi, M., Di Domenico, F., & Butterfield, D. A. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.03.014 · Cited by 339
Autophagy and Lipid Droplets in the Liver
Martínez-López, N., & Singh, R. (2015) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-071813-105336 · Cited by 345
Autophagy and Autophagy-Related Diseases: A Review
Ichimiya, T., Yamakawa, T., Hirano, T., Yokoyama, Y., Hayashi, Y., Hirayama, D., Wagatsuma, K., Itoi, T., & Nakase, H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21238974 · Cited by 358
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
Hale, A. N., Ledbetter, D., Gawriluk, T. R., & Rucker, E. B. (2013) · Autophagy · doi:10.4161/auto.24273 · Cited by 343
The Metabolic Basis of Kidney Cancer
Linehan, W. M., Schmidt, L. S., Crooks, D. R., Wei, D., Srinivasan, R., Lang, M., & Ricketts, C. J. (2019) · Cancer Discovery · doi:10.1158/2159-8290.cd-18-1354 · Cited by 350
Tai, H., Wang, Z., Gong, H., Han, X., Zhou, J., Wang, X., Wei, X., Ding, Y., Huang, N., Qin, J., et al. (2017) · Autophagy · doi:10.1080/15548627.2016.1247143 · Cited by 334
At the end of the autophagic road: an emerging understanding of lysosomal functions in autophagy
Shen, H., & Mizushima, N. (2013) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2013.12.001 · Cited by 341
The Role of Autophagy and Mitophagy in Bone Metabolic Disorders
Wang, S., Deng, Z., Ma, Y., Jin, J., Qi, F., Li, S., Liu, C., Lyu, F., & Zheng, Q. (2020) · International Journal of Biological Sciences · doi:10.7150/ijbs.46627 · Cited by 333
Selective Autophagy Receptor p62/SQSTM1, a Pivotal Player in Stress and Aging
Kumar, A. V., Mills, J., & Lapierre, L. R. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.793328 · Cited by 365
TFEB and TFE3 cooperate in the regulation of the innate immune response in activated macrophages
Pastore, N., Brady, O. A., Diab, H. I., Martina, J. A., Sun, L., Huynh, T., Lim, J.-A., Zare, H., Raben, N., Ballabio, A., et al. (2016) · Autophagy · doi:10.1080/15548627.2016.1179405 · Cited by 331
Self-citationInnate Host Defense Requires TFEB-Mediated Transcription of Cytoprotective and Antimicrobial Genes
Visvikis, O., Ihuegbu, N., Labed, S. A., Luhachack, L. G., Alves, A.-M. F., Wollenberg, A. C., Stuart, L. M., Stormo, G. D., & Irazoqui, J. E. (2014) · Immunity · doi:10.1016/j.immuni.2014.05.002 · Cited by 337
A substrate-specific mTORC1 pathway underlies Birt–Hogg–Dubé syndrome
Napolitano, G., Di Malta, C., Esposito, A., de Araujo, M. E. G., Pece, S., Bertalot, G., Matarese, M., Benedetti, V., Zampelli, A., Stasyk, T., et al. (2020) · Nature · doi:10.1038/s41586-020-2444-0 · Cited by 341
Self-citationMXL-3 and HLH-30 transcriptionally link lipolysis and autophagy to nutrient availability
O’Rourke, E. J., & Ruvkun, G. (2013) · Nature Cell Biology · doi:10.1038/ncb2741 · Cited by 333
Ubiquitin signaling and autophagy
Grumati, P., & Đikić, I. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.tm117.000117 · Cited by 336
Nutrient regulation of mTORC1 at a glance
Condon, K. J., & Sabatini, D. M. (2019) · Journal of Cell Science · doi:10.1242/jcs.222570 · Cited by 342
Autophagy and Microglia: Novel Partners in Neurodegeneration and Aging
Plaza-Zabala, A., Sierra-Torre, V., & Sierra, A. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18030598 · Cited by 323
SLC38A2 and glutamine signalling in cDC1s dictate anti-tumour immunity
Guo, C., You, Z., Shi, H., Sun, Y., Du, X., Palacios, G. F., Guy, C. S., Yuan, S., Chapman, N. M., Lim, S. A., et al. (2023) · Nature · doi:10.1038/s41586-023-06299-8 · Cited by 325
Transcription Factor EB Controls Metabolic Flexibility during Exercise
Mansueto, G., Armani, A., Viscomi, C., D’Orsi, L., De Cegli, R., Polishchuk, E. V., Lamperti, C., Di Meo, I., Romanello, V., Marchet, S., et al. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2016.11.003 · Cited by 314
Self-citationTFEB and TFE3 are novel components of the integrated stress response
Martina, J. A., Diab, H. I., Brady, O. A., & Puertollano, R. (2016) · The EMBO Journal · doi:10.15252/embj.201593428 · Cited by 314
Regulation of Liver Metabolism by Autophagy
Madrigal‐Matute, J., & Cuervo, A. M. (2015) · Gastroenterology · doi:10.1053/j.gastro.2015.09.042 · Cited by 319
Acetylation in the regulation of autophagy
Xu, Y., & Wan, W. (2023) · Autophagy · doi:10.1080/15548627.2022.2062112 · Cited by 307
Molecular genetics and cellular features of TFE3 and TFEB fusion kidney cancers
KAUFFMAN, E. C., Ricketts, C. J., Rais‐Bahrami, S., Yang, Y., Merino, M. J., Bottaro, D. P., Srinivasan, R., & Linehan, W. M. (2014) · Nature Reviews Urology · doi:10.1038/nrurol.2014.162 · Cited by 319
MiT/TFE transcription factors are activated during mitophagy downstream of Parkin and Atg5
Nezich, C. L., Wang, C., Fogel, A. I., & Youle, R. J. (2015) · Journal of Cell Biology · doi:10.1083/jcb.201501002 · Cited by 309
Targeting the lysosome in cancer
Piao, S., & Amaravadi, R. K. (2015) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.12953 · Cited by 303
Han, X., Tai, H., Wang, X., Wang, Z., Zhou, J., Wei, X., Ding, Y., Gong, H., Mo, C., Zhang, J., et al. (2016) · Aging Cell · doi:10.1111/acel.12446 · Cited by 302
Cancer-associated lysosomal changes: friends or foes?
Kallunki, T., Olsen, O. D., & Jäättelä, M. (2012) · Oncogene · doi:10.1038/onc.2012.292 · Cited by 301
ATG12–ATG3 interacts with Alix to promote basal autophagic flux and late endosome function
Murrow, L. M., Malhotra, R., & Debnath, J. (2015) · Nature Cell Biology · doi:10.1038/ncb3112 · Cited by 314
Autophagy-Dependent Generation of Free Fatty Acids Is Critical for Normal Neutrophil Differentiation
Riffelmacher, T., Clarke, A. J., Richter, F. C., Stranks, A. J., Pandey, S., Danielli, S., Hublitz, P., Yu, Z., Johnson, E., Schwerd, T., et al. (2017) · Immunity · doi:10.1016/j.immuni.2017.08.005 · Cited by 309
mTOR Pathways in Cancer and Autophagy
Paquette, M., El–Houjeiri, L., & Pause, A. (2018) · Cancers · doi:10.3390/cancers10010018 · Cited by 301
O-GlcNAc-modification of SNAP-29 regulates autophagosome maturation
Guo, B., Liang, Q., Li, L., Hu, Z., Wu, F., Zhang, P., Ma, Y., Zhao, B., Kovács, A. L., Zhang, Z., et al. (2014) · Nature Cell Biology · doi:10.1038/ncb3066 · Cited by 295
Molecular logic of mTORC1 signalling as a metabolic rheostat
Valvezan, A. J., & Manning, B. D. (2019) · Nature Metabolism · doi:10.1038/s42255-019-0038-7 · Cited by 310
A comprehensive glossary of autophagy-related molecules and processes (2ndedition)
Klionsky, D. J., Baehrecke, E. H., Brumell, J. H., Chu, C. T., Codogno, P., Cuervo, A. M., Debnath, J., Deretic, V. P., Elazar, Z., Eskelinen, E., et al. (2011) · Autophagy · doi:10.4161/auto.7.11.17661 · Cited by 298
Self-citationLysosomes as coordinators of cellular catabolism, metabolic signalling and organ physiology
Settembre, C., & Perera, R. M. (2023) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-023-00676-x · Cited by 303
Self-citationAutophagy and disease: always two sides to a problem
Sridhar, S., Botbol, Y. M., Macián, F., & Cuervo, A. M. (2011) · The Journal of Pathology · doi:10.1002/path.3025 · Cited by 298
The Emerging Roles of mTORC1 in Macromanaging Autophagy
Dossou, A. S., & Basu, A. (2019) · Cancers · doi:10.3390/cancers11101422 · Cited by 308
NAD+ homeostasis in renal health and disease
Ralto, K. M., Rhee, E. P., & Parikh, S. M. (2019) · Nature Reviews Nephrology · doi:10.1038/s41581-019-0216-6 · Cited by 293
The lysosome as a command-and-control center for cellular metabolism
Lim, C.-Y., & Zoncu, R. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201607005 · Cited by 298
Autophagy 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
Emerging strategies to effectively target autophagy in cancer
Rebecca, V. W., & Amaravadi, R. K. (2015) · Oncogene · doi:10.1038/onc.2015.99 · Cited by 290
Vidal, R. L., Figueroa, A., Court, F. A., Thielen, P., Molina, C., Wirth, C., Caballero, B., Kiffin, R., Segura‐Aguilar, J., Cuervo, A. M., et al. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds040 · Cited by 286
Therapeutic potential of autophagy-enhancing agents in Parkinson’s disease
Moors, T. E., Hoozemans, J. J. M., Ingrassia, A. M. T., Beccari, T., Parnetti, L., Chartier‐Harlin, M., & van de Berg, W. D. J. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0154-3 · Cited by 287
Egan, B., & Sharples, A. P. (2023) · Physiological Reviews · doi:10.1152/physrev.00054.2021 · Cited by 278
ZKSCAN3 Is a Master Transcriptional Repressor of Autophagy
Chauhan, S., Goodwin, J. G., Chauhan, S., Manyam, G., Wang, J., Kamat, A. M., & Boyd, D. D. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.01.024 · Cited by 266
Role of PGC-1α during acute exercise-induced autophagy and mitophagy in skeletal muscle
Vainshtein, A., Tryon, L. D., Pauly, M., & Hood, D. A. (2015) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00380.2014 · Cited by 273
Chourasia, A. H., Boland, M. L., & Macleod, K. F. (2015) · Cancer & Metabolism · doi:10.1186/s40170-015-0130-8 · Cited by 284
Regulation of autophagy by stress-responsive transcription factors
Pietrocola, F., Izzo, V., Niso‐Santano, M., Vacchelli, E., Galluzzi, L., Maiuri, M. C., & Kroemer, G. (2013) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2013.05.008 · Cited by 277
Variations in MHC Class II Antigen Processing and Presentation in Health and Disease
Unanue, E. R., Türk, V., & Neefjes, J. (2016) · Annual Review of Immunology · doi:10.1146/annurev-immunol-041015-055420 · Cited by 276
Goul, C., Peruzzo, R., & Zoncu, R. (2023) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-023-00641-8 · Cited by 280
Mechanisms of silver nanoparticle-induced toxicity and important role of autophagy
Mao, B.-H., Tsai, J., Chen, C.-W., Yan, S., & Wang, Y. (2016) · Nanotoxicology · doi:10.1080/17435390.2016.1189614 · Cited by 271
Emerging Roles for the Lysosome in Lipid Metabolism
Thelen, A. M., & Zoncu, R. (2017) · Trends in Cell Biology · doi:10.1016/j.tcb.2017.07.006 · Cited by 275
Xiao, Q., Yan, P., Ma, X., Liu, H., Perez, R., Zhu, A., Gonzales, E., Burchett, J. M., Schuler, D. R., Cirrito, J. R., et al. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.3788-13.2014 · Cited by 266
Molecular regulation of autophagy machinery by mTOR‐dependent and ‐independent pathways
Al‐Bari, M. A. A., & Xu, P. (2020) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.14305 · Cited by 269
An overview of macroautophagy in yeast
Wen, X., & Klionsky, D. J. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.02.021 · Cited by 261
Lee, J.-W., Nam, H., Kim, L. E., Jeon, Y., Min, H., Ha, S., Lee, Y., Kim, S.-Y., Lee, S. J., Kim, E.-K., et al. (2019) · Autophagy · doi:10.1080/15548627.2018.1556946 · Cited by 260
Genetic perspective on the role of the autophagy-lysosome pathway in Parkinson disease
Gan-Or, Z., Dion, P. A., & Rouleau, G. A. (2015) · Autophagy · doi:10.1080/15548627.2015.1067364 · Cited by 260
AMPK-dependent phosphorylation is required for transcriptional activation of TFEB and TFE3
Paquette, M., El–Houjeiri, L., Zirden, L. C., Puustinen, P., Blanchette, P., Jeong, H., Dejgaard, K., Siegel, P. M., & Pause, A. (2021) · Autophagy · doi:10.1080/15548627.2021.1898748 · Cited by 264
Tan, A., Prasad, R., Lee, C., & Jho, E. (2022) · Cell Death and Differentiation · doi:10.1038/s41418-022-01028-6 · Cited by 262
Eisenberg, T., Schroeder, S., Andryushkova, A., Pendl, T., Küttner, V., Bhukel, A., Mariño, G., Pietrocola, F., Harger, A., Zimmermann, A., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.02.010 · Cited by 256
Rovere, R. M. L. L., Roest, G., Bultynck, G., & Parys, J. B. (2016) · Cell Calcium · doi:10.1016/j.ceca.2016.04.005 · Cited by 266
MicroRNA regulation of autophagy
Frankel, L. B., & Lund, A. H. (2012) · Carcinogenesis · doi:10.1093/carcin/bgs266 · Cited by 261
Autophagy, aging, and age-related neurodegeneration
Palmer, J. E., Wilson, N., Son, S. M., Obrocki, P., Wróbel, L., Rob, M., Takla, M., Korolchuk, V. I., & Rubinsztein, D. C. (2024) · Neuron · doi:10.1016/j.neuron.2024.09.015 · Cited by 277
Self-citationTranscriptional 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
Self-citationTFEB enhances astroglial uptake of extracellular tau species and reduces tau spreading
Martini-Stoica, H., Cole, A. L., Swartzlander, D. B., Chen, F., Wan, Y.-W., Bajaj, L., Bader, D. A., Lee, V. M. Y., Trojanowski, J. Q., Liu, Z., et al. (2018) · Journal of Experimental Medicine · doi:10.1084/jem.20172158 · Cited by 253
Self-citationTargeting autophagy to overcome drug resistance: further developments
Chang, H., & Zou, Z. (2020) · Journal of Hematology & Oncology · doi:10.1186/s13045-020-01000-2 · Cited by 259
Progranulin, lysosomal regulation and neurodegenerative disease
Kao, A. W., McKay, A. S., Singh, P. P., Brunet, A., & Huang, E. J. (2017) · Nature reviews. Neuroscience · doi:10.1038/nrn.2017.36 · Cited by 252
Bromodomain Protein BRD4 Is a Transcriptional Repressor of Autophagy and Lysosomal Function
Sakamaki, J.-I., Wilkinson, S., Hahn, M., Tasdemir, N., O’Prey, J., Clark, W., Hedley, A., Nixon, C., Long, J. S., New, M., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.04.027 · Cited by 249
Autophagy proteins regulate ERK phosphorylation
Martínez-López, N., Athonvarangkul, D., Mishall, P. L., Sahu, S., & Singh, R. (2013) · Nature Communications · doi:10.1038/ncomms3799 · Cited by 254
Emptying the stores: lysosomal diseases and therapeutic strategies
Platt, F. M. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2017.214 · Cited by 257
Trehalose-Induced Activation of Autophagy Improves Cardiac Remodeling After Myocardial Infarction
Sciarretta, S., Yee, D., Nagarajan, N., Bianchi, F., Saito, T., Valenti, V., Tong, M., Re, D. P. D., Vecchione, C., Schirone, L., et al. (2018) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2018.02.066 · Cited by 249
Ageing and neurodegenerative diseases
Hung, C.-W., Chen, Y., Hsieh, W.-L., Chiou, S., & Kao, C.-L. (2010) · Ageing Research Reviews · doi:10.1016/j.arr.2010.08.006 · Cited by 257
Transcriptional activation of RagD GTPase controls mTORC1 and promotes cancer growth
Malta, C. D., Siciliano, D., Calcagnì, A., Monfregola, J., Punzi, S., Pastore, N., Eastes, A., Davis, O. B., Cegli, R. D., Zampelli, A., et al. (2017) · Science · doi:10.1126/science.aag2553 · Cited by 246
Self-citation
Metadata
- Authors
- Settembre, C., Di Malta, C., Polito, V. A., Arencibia, M. G., Vetrini, F., Erdin, S., Erdin, S. U., Huynh, T., Medina, D., Colella, P., Sardiello, M., Rubinsztein, D. C., & Ballabio, A.
- Affiliations
- Baylor College of Medicine (US)
- Telethon Institute of Genetics and Medicine (TIGEM), Via Pietro Castellino 111, 80131 Naples, Italy.
- Cambridge Institute for Medical Research, Wellcome Trust–Medical Research Council Building, Addenbrooke’s Hospital, Hills Road, Cambridge CB2 0XY, UK.
- Telethon Institute Of Genetics And Medicine (IT)
- Addenbrooke's Hospital (GB)
- Corresponding author
- Ballabio, Andrea
- ORCID
- Venue
- Science
- Published
- 2011-06-17
- Volume
- 332
- Issue
- 6036
- Pages
- 1429-1433
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC3638014
- OpenAlex
- W1975200363
- Cited by
- 3,365
- References
- 33
- Citations by year
- 2026: 283 · 2025: 275 · 2024: 287 · 2023: 270 · 2022: 328 · 2021: 290 · 2020: 317 · 2019: 251 · 2018: 227 · 2017: 192 · 2016: 184 · 2015: 152 · 2014: 116 · 2013: 96 · 2012: 66
- FWCI
- 73.01
- Type
- journal article
- Language
- en
- Update notices
- correction (2025-12-18)
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Acceda (Universidad de Las Palmas de Gran Canaria) (submittedVersion)
- Funders
- Wellcome Trust
- National Institute of Neurological Disorders and Stroke (R01NS078072)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (P30HD024064)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- TFEB, autophagy, lysosomal biogenesis, starvation, autophagosome-lysosome fusion, autophagosome formation, substrate degradation, serine phosphorylation, ERK2, mitogen-activated protein kinase, nutrient sensing, transcriptional regulation, nuclear localization
- MeSH terms
- Animals, Autophagy, Cell Nucleus, Cells, Cultured, Chlorocebus aethiops, Cytoplasm, Gene Expression Regulation, HeLa Cells, Humans, Liver, Lysosomes, Mice, Transgenic, Microtubule-Associated Proteins, Phagosomes, Phosphorylation, Transcription, Genetic, Up-Regulation, COS Cells, Mitogen-Activated Protein Kinase 1, MAP Kinase Signaling System, Active Transport, Cell Nucleus, RNA Interference, Mice, Basic Helix-Loop-Helix Leucine Zipper Transcription Factors
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