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
Cited by
Sorted by citations
Items 501–600 of 1,018
The Pathways Underlying the Multiple Roles of p62 in Inflammation and Cancer
Hennig, P., Fenini, G., Filippo, M. D., Karakaya, T., & Beer, H. (2021) · Biomedicines · doi:10.3390/biomedicines9070707 · Cited by 121
Gao, L., Li, X., Meng, S., Ma, T., Wan, L., & Xu, S. (2020) · Drug Design Development and Therapy · doi:10.2147/dddt.s235969 · Cited by 115
Lysosomes: Signaling Hubs for Metabolic Sensing and Longevity
Savini, M., Zhao, Q., & Wang, M. C. (2019) · Trends in Cell Biology · doi:10.1016/j.tcb.2019.08.008 · Cited by 116
Chloroquine and bafilomycin A mimic lysosomal storage disorders and impair mTORC1 signalling
Fedele, A. O., & Proud, C. G. (2020) · Bioscience Reports · doi:10.1042/bsr20200905 · Cited by 118
Autophagy induction promoted by m6A reader YTHDF3 through translation upregulation of FOXO3 mRNA
Hao, W.-C., Dian, M., Zhou, Y., Zhong, Q., Pang, W., Li, Z., Zhao, Y., Ma, J., Lin, X., Luo, R., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-32963-0 · Cited by 115
p62/SQSTM1 synergizes with autophagy for tumor growth in vivoPreprint
Wei, H., Wang, C., Croce, C. M., & Guan, J. (2014) · Genes & Development · doi:10.1101/gad.237354.113 · Cited by 120
Annunziata, I., van de Vlekkert, D., Wolf, E., Finkelstein, D., Neale, G. A. M., Machado, E., Mosca, R., Campos, Y., Sheppard, H., Roussel, M. F., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-11568-0 · Cited by 114
Life-long oligodendrocyte development and plasticity
Nishiyama, A., Shimizu, T., Sherafat, A., & Richardson, W. D. (2021) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2021.02.004 · Cited by 126
Lü, H., Jia, C., Wu, D., Jin, H., Zeng, L., Pan, J., Li, X., & Wang, W. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-04157-x · Cited by 118
Autophagy and cell growth – the yin and yang of nutrient responses
Neufeld, T. P. (2012) · Journal of Cell Science · doi:10.1242/jcs.103333 · Cited by 114
Kim, S., Choi, K. J., Cho, S., Yun, S., Jeon, J., Koh, Y. H., Song, J., Johnson, G. V. W., & Jo, C. (2016) · Scientific Reports · doi:10.1038/srep24933 · Cited by 116
Zheng, K., Li, Y., Wang, S., Wang, X., Liao, C., Hu, X., Fan, L., Kang, Q., Zeng, Y., Wu, X., et al. (2016) · Autophagy · doi:10.1080/15548627.2016.1192751 · Cited by 114
Sha, Z., Schnell, H. M., Ruoff, K., & Goldberg, A. L. (2018) · The Journal of Cell Biology · doi:10.1083/jcb.201708168 · Cited by 118
Zhang, J., Wang, J., Zhou, Z., Park, J.-E., Wang, L., Wu, S., Sun, X., Lu, L., Wang, T., Lin, Q., et al. (2018) · Autophagy · doi:10.1080/15548627.2018.1447290 · Cited by 44
An mTORC1-to-CDK1 Switch Maintains Autophagy Suppression during Mitosis
Odle, R., Walker, S. A., Oxley, D., Kidger, A. M., Balmanno, K., Gilley, R., Okkenhaug, H., Florey, O., Ktistakis, N. T., & Cook, S. J. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.10.016 · Cited by 113
Jiang, S., & Bhaskar, K. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.586731 · Cited by 119
Xu, Y., Wang, Q., Wang, J., Qian, C., Wang, Y., Lu, S., Song, L., He, Z., Liu, W., & Wan, W. (2024) · Immunity · doi:10.1016/j.immuni.2024.11.017 · Cited by 120
ACAT1/SOAT1 as a Therapeutic Target for Alzheimer's Disease
Shibuya, Y., Chang, C. C., & Chang, T.-Y. (2015) · Future Medicinal Chemistry · doi:10.4155/fmc.15.161 · Cited by 113
Wang, H., Wang, N., Xu, D., Ma, Q., Chen, Y., Xu, S., Qin, X., Zhang, Y., Prehn, J. H. M., Wang, G., et al. (2019) · Autophagy · doi:10.1080/15548627.2019.1704104 · Cited by 114
The Lysosome at the Intersection of Cellular Growth and Destruction
Shin, H. R., & Zoncu, R. (2020) · Developmental Cell · doi:10.1016/j.devcel.2020.06.010 · Cited by 121
Yang, C., Su, C.-F., Iyaswamy, A., Krishnamoorthi, S. K., Zhu, Z., Yang, S., Tong, B. C., Liu, J., Sreenivasmurthy, S. G., Guan, X., et al. (2022) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2022.01.017 · Cited by 117
Porter, K. M., Jeyabalan, N., Lin, Y., & Liton, P. B. (2013) · Autophagy · doi:10.4161/auto.23568 · Cited by 113
Autophagy Function and Regulation in Kidney Disease
Kaushal, G. P., Chandrashekar, K., Juncos, L. A., & Shah, S. V. (2020) · Biomolecules · doi:10.3390/biom10010100 · Cited by 112
The antibiotic bedaquiline activates host macrophage innate immune resistance to bacterial infection
Giraud-Gatineau, A., Coya, J. M., Maure, A., Biton, A., Thomson, M., Bernard, E. M., Marrec, J., Gutierrez, M. G., Larrouy-Maumus, G. J., Brosch, R., et al. (2020) · eLife · doi:10.7554/elife.55692 · Cited by 113
Feng, T., Lacrampe, A., & Hu, F. (2021) · Acta Neuropathologica · doi:10.1007/s00401-020-02246-3 · Cited by 110
Self-eating in the plaque: what macrophage autophagy reveals about atherosclerosis
Sergin, I., & Razani, B. (2014) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2014.03.010 · Cited by 111
Alonso‐Curbelo, D., Riveiro‐Falkenbach, E., Pérez‐Guijarro, E., Cifdaloz, M., Karras, P., Osterloh, L., Megı́as, D., Cañón, E., Calvo, T. G., Olmeda, D., et al. (2014) · Cancer Cell · doi:10.1016/j.ccr.2014.04.030 · Cited by 114
Nutrient-sensing mTORC1: Integration of metabolic and autophagic signals
Tan, V. P., & Miyamoto, S. (2016) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2016.01.005 · Cited by 113
Exercise induces TFEB expression and activity in skeletal muscle in a PGC-1α-dependent manner
Erlich, A. T., Brownlee, D., Beyfuss, K. A., & Hood, D. A. (2017) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00162.2017 · Cited by 112
gene2drug: a computational tool for pathway-based rational drug repositioning
Napolitano, F., Carrella, D., Mandriani, B., Pisonero‐Vaquero, S., Sirci, F., Medina, D. L., Brunetti‐Pierri, N., & di Bernardo, D. (2017) · Bioinformatics · doi:10.1093/bioinformatics/btx800 · Cited by 110
Self-citationA lysosome-targeted DNA nanodevice selectively targets macrophages to attenuate tumours
Cui, C., Chakraborty, K., Tang, X. A., Schoenfelt, K. Q., Hoffman, A., Blank, A., McBeth, B., Pulliam, N., Reardon, C. A., Kulkarni, S., et al. (2021) · Nature Nanotechnology · doi:10.1038/s41565-021-00988-z · Cited by 113
Self-citationIershov, A., Nemazanyy, I., Alkhoury, C., Girard, M., Barth, E., Cagnard, N., Montagner, A., Chretien, D., Rugarli, E. I., Guillou, H., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-09598-9 · Cited by 109
Asparaginase induces apoptosis and cytoprotective autophagy in chronic myeloid leukemia cells
Song, P., Ye, L., Fan, J., Li, Y., Zeng, X. L., Wang, Z., Wang, S., Zhang, G., Yang, P., Cao, Z., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.2869 · Cited by 109
2-Hydroxypropyl-β-cyclodextrin Promotes Transcription Factor EB-mediated Activation of Autophagy
Song, W., Wang, F., Lotfi, P., Sardiello, M., & Segatori, L. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.506246 · Cited by 115
Self-citationRotenone impairs autophagic flux and lysosomal functions in Parkinson’s disease
Wu, F., Xu, H., Guan, J.-J., Hou, Y., Gu, J., Zhen, X., & Qin, Z. (2014) · Neuroscience · doi:10.1016/j.neuroscience.2014.11.004 · Cited by 112
Sphingolipids and lysosomal pathologies
Schulze, H., & Sandhoff, K. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2013.10.015 · Cited by 114
Autophagy in neurodegenerative diseases: From pathogenic dysfunction to therapeutic modulation
Martínez‐Vicente, M. (2015) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2015.03.005 · Cited by 114
Neuronal Tsc1/2 complex controls autophagy through AMPK-dependent regulation of ULK1
Nardo, A. D., Wertz, M. H., Kwiatkowski, E. R., Tsai, P. T., Leech, J. D., Greene-Colozzi, E. A., Goto, J., Dilsiz, P., Talos, D. M., Clish, C. B., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu101 · Cited by 112
Settembre, C., & Medina, D. L. (2015) · Methods in cell biology · doi:10.1016/bs.mcb.2014.11.011 · Cited by 109
Self-citationChoi, H., Merceron, C., Mangiavini, L., Seifert, E. L., Schipani, E., Shapiro, I. M., & Risbud, M. V. (2016) · Autophagy · doi:10.1080/15548627.2016.1192753 · Cited by 111
Enhanced lysosomal degradation maintains the quiescent state of neural stem cells
Kobayashi, T., Piao, W., Takamura, T., Kori, H., Miyachi, H., Kitano, S., Iwamoto, Y., Yamada, M., Imayoshi, I., Shioda, S., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-13203-4 · Cited by 111
Self-citationNatural compounds modulate the autophagy with potential implication of stroke
Ahsan, A., Liu, M., Zheng, Y., Yan, W., Pan, L., Li, Y., Ma, S., Zhang, X., Cao, M., Wu, Z., et al. (2020) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2020.10.018 · Cited by 109
Kao, C., Chao, A., Tsai, C.-L., Chuang, W.-C., Huang, W.-P., Chen, G., Lin, C.-Y., Th, W., Wang, H., & Lai, C. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.468 · Cited by 111
Shibuya, Y., Chang, C. C. Y., Huang, L.-H., Bryleva, E. Y., & Chang, T.-Y. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.2567-14.2014 · Cited by 108
Fine-Tuning Cardiac Insulin-Like Growth Factor 1 Receptor Signaling to Promote Health and Longevity
Abdellatif, M., Trummer-Herbst, V., Heberle, A. M., Humnig, A., Pendl, T., Durand, S., Cerrato, G., Hofer, S. J., Islam, M., Voglhuber, J., et al. (2022) · Circulation · doi:10.1161/circulationaha.122.059863 · Cited by 108
Parkin is required for exercise-induced mitophagy in muscle: Impact of aging
Chen, C. C. W., Erlich, A. T., Crilly, M. J., & Hood, D. A. (2018) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00391.2017 · Cited by 108
Holler, C. J., Taylor, G., McEachin, Z. T., Deng, Q., Watkins, W. J., Hudson, K. F., Easley, C. A., Hu, W. T., Hales, C. M., Rossoll, W., et al. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0114-3 · Cited by 109
Mizunoe, Y., Sudo, Y., Okita, N., Hiraoka, H., Mikami, K., Narahara, T., Negishi, A., Yoshida, M., Higashibata, R., Watanabe, S., et al. (2017) · Autophagy · doi:10.1080/15548627.2016.1274850 · Cited by 111
Regulation of TFEB activity and its potential as a therapeutic target against kidney diseases
Zhang, W., Li, X., Wang, S., Chen, Y., & Liu, H. (2020) · Cell Death Discovery · doi:10.1038/s41420-020-0265-4 · Cited by 112
CDK4/6 regulate lysosome biogenesis through TFEB/TFE3
Yin, Q., Jian, Y., Xu, M., Huang, X., Wang, N., Liu, Z., Li, Q., Li, J., Zhou, H., Xu, L., et al. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.201911036 · Cited by 109
Ma, W., Sun, X., Zhu, Y., & Liu, N. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-03162-w · Cited by 112
Wang, Z., Liu, J., Zhu, Z., Su, C.-F., Sreenivasmurthy, S. G., Iyaswamy, A., Lu, J., Chen, G., Song, J., & Li, M. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110968 · Cited by 109
TFEB induces mitochondrial itaconate synthesis to suppress bacterial growth in macrophages
Schuster, E.-M., Epple, M. W., Glaser, K. M., Mihlan, M., Lucht, K., Zimmermann, J. A., Bremser, A., Polyzou, A., Obier, N., Cabezas‐Wallscheid, N., et al. (2022) · Nature Metabolism · doi:10.1038/s42255-022-00605-w · Cited by 108
Self-citationDrosophilaMitf regulates the V-ATPase and the lysosomal-autophagic pathway
Bouchè, V., Perez, A. M., Leone, L., Sardiello, M., Ballabio, A., & Botas, J. (2016) · Autophagy · doi:10.1080/15548627.2015.1134081 · Cited by 116
Self-citationRole of Autophagy in Parkinson’s Disease
Cerri, S., & Blandini, F. (2018) · Current Medicinal Chemistry · doi:10.2174/0929867325666180226094351 · Cited by 107
Rapamycin directly activates lysosomal mucolipin TRP channels independent of mTOR
Zhang, X., Chen, W., Gao, Q., Yang, J., Yan, X., Zhao, H., Su, L., Yang, M., Gao, C., Yao, Y., et al. (2019) · PLoS Biology · doi:10.1371/journal.pbio.3000252 · Cited by 110
Niemann–Pick type C disease: cellular pathology and pharmacotherapy
Wheeler, S., & Sillence, D. J. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14895 · Cited by 111
Lotfi, P., Tse, D. Y., Di Ronza, A., Seymour, M. L., Martano, G., Cooper, J. D., Pereira, F. A., Passafaro, M., Wu, S. M., & Sardiello, M. (2018) · Autophagy · doi:10.1080/15548627.2018.1474313 · Cited by 106
Self-citationCellular and molecular effects of the mTOR inhibitor everolimus
Saran, U., Foti, M., & Dufour, J. (2015) · Clinical Science · doi:10.1042/cs20150149 · Cited by 111
Neurodegeneration: From cellular concepts to clinical applications
Katsnelson, A., Strooper, B. D., & Zoghbi, H. Y. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aal2074 · Cited by 109
MAP4K3 mediates amino acid-dependent regulation of autophagy via phosphorylation of TFEB
Hsu, C. L., Lee, E. X., Gordon, K. L., Paz, E. A., Shen, W.-C., Ohnishi, K., Meisenhelder, J., Hunter, T. R., & Spada, A. R. L. (2018) · Nature Communications · doi:10.1038/s41467-018-03340-7 · Cited by 110
TFEB–vacuolar ATPase signaling regulates lysosomal function and microglial activation in tauopathy
Wang, B., Martini‐Stoica, H., Qi, C., Lu, T., Wang, S., Xiong, W., Qi, Y., Xu, Y., Sardiello, M., Li, H., et al. (2023) · Nature Neuroscience · doi:10.1038/s41593-023-01494-2 · Cited by 107
Self-citationThomes, P. G., Trambly, C. S., Fox, H. S., Tuma, D. J., & Donohue, T. M. (2015) · Alcoholism Clinical and Experimental Research · doi:10.1111/acer.12904 · Cited by 106
Autophagy in non-alcoholic fatty liver disease and alcoholic liver disease
Khambu, B., Yan, S., Huda, N., Liu, G., & Yin, X. (2018) · Liver Research · doi:10.1016/j.livres.2018.09.004 · Cited by 107
Balan, E., Schwalm, C., Naslain, D., Nielens, H., Francaux, M., & Deldicque, L. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.01088 · Cited by 104
Precision autophagy directed by receptor regulators – emerging examples within the TRIM family
Kimura, T., Mandell, M. A., & Deretic, V. P. (2016) · Journal of Cell Science · doi:10.1242/jcs.163758 · Cited by 106
Nuclear Export Inhibition Enhances HLH-30/TFEB Activity, Autophagy, and Lifespan
Silvestrini, M. J., Johnson, J. R., Kumar, A. V., Thakurta, T. G., Blais, K., Neill, Z. A., Marion, S. W., St. Amand, V., Reenan, R. A., & Lapierre, L. R. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.04.063 · Cited by 101
MITF has a central role in regulating starvation-induced autophagy in melanoma
Möller, K., Sigurbjörnsdóttir, S., Arnthorsson, A. O., Pogenberg, V., Dilshat, R., Fock, V., Brynjólfsdóttir, S. H., Bindesbøll, C., Bessadóttir, M., Ogmundsdottir, H. M., et al. (2019) · Scientific Reports · doi:10.1038/s41598-018-37522-6 · Cited by 109
MiT/TFE factors control ER‐phagy via transcriptional regulation of FAM134B
Cinque, L., Leonibus, C. D., Iavazzo, M., Krahmer, N., Intartaglia, D., Salierno, F. G., Cegli, R. D., Malta, C. D., Svelto, M., Lanzara, C., et al. (2020) · The EMBO Journal · doi:10.15252/embj.2020105696 · Cited by 106
Self-citationAutophagic lysosome reformation in health and disease
Nanayakkara, R., Gurung, R., Rodgers, S. J., Eramo, M. J., Ramm, G., Mitchell, C. A., & McGrath, M. J. (2022) · Autophagy · doi:10.1080/15548627.2022.2128019 · Cited by 110
Giatromanolaki, A. N., Kalamida, D., Sivridis, E., Karagounis, I. V., Gatter, K. C., Harris, A. L., & Koukourakis, M. I. (2015) · Lung Cancer · doi:10.1016/j.lungcan.2015.07.008 · Cited by 103
Calcineurin signaling in the heart: The importance of time and place
Parra, V., & Rothermel, B. A. (2016) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2016.12.006 · Cited by 109
NUPR1 maintains autolysosomal efflux by activatingSNAP25transcription in cancer cells
Mu, Y., Yan, X., Li, D., Zhao, D., Wang, L., Wang, X., Gao, D., Yang, J., Zhang, H., Li, Y., et al. (2017) · Autophagy · doi:10.1080/15548627.2017.1338556 · Cited by 105
Sirtuins' control of autophagy and mitophagy in cancer
Aventaggiato, M., Vernucci, E., Barreca, F., Russo, M. A., & Tafani, M. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107748 · Cited by 103
Rakshe, P. S., Dutta, B. J., Chib, S., Maurya, N., & Singh, S. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102255 · Cited by 107
Circadian autophagy rhythm: a link between clock and metabolism?
Ma, D., Li, S., Molusky, M. M., & Lin, J. D. (2012) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2012.03.004 · Cited by 106
Eaten alive: novel insights into autophagy from multicellular model systems
Zhang, H., & Baehrecke, E. H. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.03.001 · Cited by 102
Fennelly, C., & Amaravadi, R. K. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-6934-0_19 · Cited by 107
Interleukin 6 protects pancreatic β cells from apoptosis by stimulation of autophagy
Linnemann, A. K., Blumer, J. T., Marasco, M. R., Battiola, T. J., Umhoefer, H. M., Han, J. Y., Lamming, D. W., & Davis, D. B. (2017) · The FASEB Journal · doi:10.1096/fj.201700061rr · Cited by 103
β-cell autophagy: Mechanism and role in β-cell dysfunction
Lee, Y., Kim, J., Park, K., & Lee, M. (2019) · Molecular Metabolism · doi:10.1016/j.molmet.2019.06.014 · Cited by 106
Gao, L., Dou, Z., Ren, W., Li, S., Liang, K. X., & Zhi, K. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1971-9 · Cited by 102
Mechanisms and Therapeutic Implications of GSK-3 in Treating Neurodegeneration
Rippin, I., & Eldar-Finkelman, H. (2021) · Cells · doi:10.3390/cells10020262 · Cited by 102
TSC2 regulates lysosome biogenesis via a non-canonical RAGC and TFEB-dependent mechanism
Alesi, N., Akl, E. W., Khabibullin, D., Liu, H.-J., Nidhiry, A. S., Garner, E. R., Filippakis, H., Lam, H. C., Shi, W., Viswanathan, S. R., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24499-6 · Cited by 106
Key genes and convergent pathogenic mechanisms in Parkinson disease
Coukos, R., & Krainc, D. (2024) · Nature reviews. Neuroscience · doi:10.1038/s41583-024-00812-2 · Cited by 116
Dissection of autophagy in human platelets
Feng, W., Chang, C., Luo, D., Su, H., Yu, S., Hua, W., Chen, Z., Hu, H., & Liu, W. (2014) · Autophagy · doi:10.4161/auto.27832 · Cited by 102
Tomuleasa, C., Şoriţău, O., Orza, A. I., Dudea, M., Petrushev, B., Moșteanu, O., Șușman, S., Florea, A., Páll, E., Aldea, M. D., et al. (2012) · PubMed · Cited by 102
The IAP family member BRUCE regulates autophagosome–lysosome fusion
Ebner, P., Poetsch, I., Deszcz, L., Hoffmann, T., Zuber, J. A., & Ikeda, F. (2018) · Nature Communications · doi:10.1038/s41467-018-02823-x · Cited by 104
Huang, M., Modeste, E. S., Dammer, E. B., Merino, P., Taylor, G., Duong, D. M., Deng, Q., Holler, C. J., Gearing, M., Dickson, D. W., et al. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-01037-x · Cited by 102
Stress granules and mTOR are regulated by membrane atg8ylation during lysosomal damage
Jia, J., Wang, F., Bhujabal, Z., Peters, R. S., Mudd, M. H., Duque, T. L. A., Allers, L., Javed, R., Salemi, M., Behrends, C., et al. (2022) · The Journal of Cell Biology · doi:10.1083/jcb.202207091 · Cited by 104
Autophagy and lysosomal related protein expression patterns in human glioblastoma
Giatromanolaki, A. N., Sivridis, E., Mitrakas, A. G., Kalamida, D., Zois, C. E., Haider, S. A., Piperidou, C., Pappa, A., Gatter, K. C., Harris, A. L., et al. (2014) · Cancer Biology & Therapy · doi:10.4161/15384047.2014.955719 · Cited by 99
Nàger, M., Sallan, M. C., Visa, A., Pushparaj, C., Santacana, M., Macià, A., Yeramian, A., Cantı́, C., & Herreros, J. (2018) · Autophagy · doi:10.1080/15548627.2017.1423439 · Cited by 99
Revisiting Rab7 Functions in Mammalian Autophagy: Rab7 Knockout Studies
Kuchitsu, Y., & Fukuda, M. (2018) · Cells · doi:10.3390/cells7110215 · Cited by 99
An FGF15/19-TFEB regulatory loop controls hepatic cholesterol and bile acid homeostasis
Wang, Y., Gunewardena, S., Li, F., Matye, D. J., Chen, C., Chao, X., Jung, T., Zhang, Y., Czerwiński, M., Ni, H., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-17363-6 · Cited by 100
The aldolase inhibitor aldometanib mimics glucose starvation to activate lysosomal AMPK
Zhang, C., Li, M., Wang, Y., Li, X., Zong, Y., Long, S., Zhang, M., Feng, J.-W., Wei, X., Liu, Y., et al. (2022) · Nature Metabolism · doi:10.1038/s42255-022-00640-7 · Cited by 104
Cathepsin B modulates lysosomal biogenesis and host defense against Francisella novicida infection
Qi, X., Man, S. M., Malireddi, R. K. S., Karki, R., Lupfer, C. R., Gurung, P., Neale, G. A. M., Guy, C. S., Lamkanfi, M., & Kanneganti, T. (2016) · The Journal of Experimental Medicine · doi:10.1084/jem.20151938 · Cited by 99
Lysosomes and Cancer Progression: A Malignant Liaison
Machado, E., Annunziata, I., van de Vlekkert, D., Grosveld, G. C., & d’Azzo, A. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.642494 · Cited by 102
Lu, H., Sun, J., Liang, W., Chang, Z., Rom, O., Zhao, Y., Zhao, G., Xiong, W., Wang, H., Zhu, T., et al. (2020) · Circulation · doi:10.1161/circulationaha.119.044803 · Cited by 98
Age-dependent loss of adipose Rubicon promotes metabolic disorders via excess autophagy
Yamamuro, T., Kawabata, T., Fukuhara, A., Saita, S., Nakamura, S., Takeshita, H., Fujiwara, M., Enokidani, Y., Yoshida, G., Tabata, K., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-17985-w · Cited by 97
Johansson, I., Monsen, V. T., Pettersen, K., Mildenberger, J., Misund, K., Kaarniranta, K., Schønberg, S., & Bjørkøy, G. (2015) · Autophagy · doi:10.1080/15548627.2015.1061170 · Cited by 100
Pallichankandy, S., Rahman, A. U., Thayyullathil, F., & Galadari, S. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.10.404 · Cited by 98
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
