TFEB Transcriptional Responses Reveal Negative Feedback by BHLHE40 and BHLHE41
Open accessAbstract
Transcription factor EB (TFEB) activates lysosomal biogenesis genes in response to environmental cues. Given implications of impaired TFEB signaling and lysosomal dysfunction in metabolic, neurological, and infectious diseases, we aim to systematically identify TFEB-directed circuits by examining transcriptional responses to TFEB subcellular localization and stimulation. We reveal that steady-state nuclear TFEB is sufficient to activate transcription of lysosomal, autophagy, and innate immunity genes, whereas other targets require higher thresholds of stimulation. Furthermore, we identify shared and distinct transcriptional signatures between mTOR inhibition and bacterial autophagy. Using a genome-wide CRISPR library, we find TFEB targets that protect cells from or sensitize cells to lysosomal cell death. BHLHE40 and BHLHE41, genes responsive to high, sustained levels of nuclear TFEB, act in opposition to TFEB upon lysosomal cell death induction. Further investigation identifies genes counter-regulated by TFEB and BHLHE40/41, adding this negative feedback to the current understanding of TFEB regulatory mechanisms.
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?
The transcription factor EB (TFEB), a key regulator of lysosomal and autophagy, is negatively regulated by BHLHE40/41.
“Furthermore, a recent study shown that the transcription factor EB (TFEB), a key regulator of lysosomal and autophagy, is negatively regulated by BHLHE40/41 [54].”
From Targeting Microglial Transcriptional Reprogramming as a Therapy Strategy for Alzheimer's Disease (2026) · cites this paper as [54]
The Introduction identifies TFEB as a regulator of lysosomal biogenesis and autophagy. The Results and Discussion describe BHLHE40/41 as part of a negative feedback loop that represses select TFEB target genes. They do not establish that BHLHE40/41 negatively regulate TFEB itself or all of its activity, as the citing sentence could imply. (LLM, conf=0.84)
Experimental — accuracy not yet measuredBHLHE40/41 bind to open chromatin at promoters and enhancers of LXR:RXR and MiT/TFE family transcriptional factors, acting as transcriptional repressors and modulating cholesterol/lipid efflux genes and lysosomal genes, thereby influencing cellular clearance functions.
“BHLHE40/41 bind to open chromatin at promoters and enhancers of LXR:RXR and MiT/TFE family transcriptional factors, acting as transcriptional repressors and modulating cholesterol/lipid efflux genes and lysosomal genes, thereby influencing cellular clearance functions (Figure 1 and Table 2) [53, 54].”
From Targeting Microglial Transcriptional Reprogramming as a Therapy Strategy for Alzheimer's Disease (2026) · cites this paper as [54]
Split into 2 atoms — 0 confirmed, 2 partially supported, 0 disputed, 0 misattributed, 0 unverifiable. Expand the claim to see per-atom verdicts.
Experimental — accuracy not yet measuredPU.1, IRF8, and BHLHE40/41 regulate multiple downstream targets that orchestrate microglial immune response functions, including phagocytosis, cytokine production, and inflammatory signaling.
“PU.1, IRF8, and BHLHE40/41 regulates multiple downstream targets that orchestrate microglial immune response functions, including phagocytosis, cytokine production, and inflammatory signaling”
From Targeting Microglial Transcriptional Reprogramming as a Therapy Strategy for Alzheimer's Disease (2026) · cites this paper as [54]
The Results section on BHLHE40/41 negative feedback (page not available in our copy) reports that BHLHE40/41 reduce expression of several TFEB-responsive genes, including IFI30 and GPNMB. The Results also identify innate-immune-response genes among TFEB targets. These passages do not establish the claimed roles for PU.1 or IRF8, or show that these regulators orchestrate microglial phagocytosis, cytokine production, and inflammatory signaling. (LLM, conf=0.85)
Experimental — accuracy not yet measuredMEF2C functions as a counterbalance by suppressing excessive pro-inflammatory responses.
“MEF2C functions as a counterbalance by suppressing excessive pro‐inflammatory responses”
From Targeting Microglial Transcriptional Reprogramming as a Therapy Strategy for Alzheimer's Disease (2026) · cites this paper as [54]
The Results passages discuss TFEB-dependent innate immune gene expression, but do not address MEF2C or its effect on pro-inflammatory responses. Searches for “MEF2C” and its proposed suppression of pro-inflammatory responses found no supporting passage in our copy. The indexed passages provide section labels but no page numbers. (LLM, conf=0.73)
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
Robinson, M. D., McCarthy, D. J., & Smyth, G. K. (2010) · Bioinformatics · doi:10.1093/bioinformatics/btp616 · Cited by 41,364 · see citing works
HTSeq—a Python framework to work with high-throughput sequencing data
Anders, S., Pyl, P. T., & Huber, W. (2015) · Bioinformatics · doi:10.1093/bioinformatics/btu638 · Cited by 21,464 · see citing works
An integrated encyclopedia of DNA elements in the human genome
The ENCODE Project Consortium (2012) · Nature · doi:10.1038/nature11247 · Cited by 18,072 · see citing works
Self-citationHeinz, S., Benner, C., Spann, N., Bertolino, E., Lin, Y. C., Laslo, P., Cheng, J. X., Murre, C., Singh, H., & Glass, C. K. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.05.004 · Cited by 13,382 · see citing works
Kim, D., Pertea, G., Trapnell, C., Pimentel, H., Kelley, R., & Salzberg, S. L. (2013) · Genome Biology · doi:10.1186/gb-2013-14-4-r36 · Cited by 12,668 · see citing works
Genome engineering using the CRISPR-Cas9 system
Ran, F. A., Hsu, P. D., Wright, J., Agarwala, V., Scott, D. A., & Zhang, F. (2013) · Nature Protocols · doi:10.1038/nprot.2013.143 · Cited by 11,133 · see citing works
Improved vectors and genome-wide libraries for CRISPR screening
Sanjana, N. E., Shalem, O., & Zhang, F. (2014) · Nature Methods · doi:10.1038/nmeth.3047 · Cited by 5,239 · see citing works
CellProfiler: image analysis software for identifying and quantifying cell phenotypes
Carpenter, A. E., Jones, T. R., Lamprecht, M. R., Clarke, C., Kang, I. H., Friman, O., Guertin, D. A., Chang, J. H., Lindquist, R. A., Moffat, J., et al. (2006) · Genome biology · doi:10.1186/gb-2006-7-10-r100 · Cited by 5,077 · see citing works
Optimized sgRNA design to maximize activity and minimize off-target effects of CRISPR-Cas9
Doench, J. G., Fusi, N., Sullender, M., Hegde, M., Vaimberg, E. W., Donovan, K. F., Smith, I., Tothova, Z., Wilen, C., Orchard, R., et al. (2016) · Nature Biotechnology · doi:10.1038/nbt.3437 · Cited by 4,637 · see citing works
Self-citationTFEB Links Autophagy to Lysosomal Biogenesis
Settembre, C., Di Malta, C., Polito, V. A., Arencibia, M. G., Vetrini, F., Erdin, S., Erdin, S. U., Huynh, T., Medina, D., Colella, P., et al. (2011) · Science · doi:10.1126/science.1204592 · Cited by 3,365 · see citing works
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 · see citing works
Smart-seq2 for sensitive full-length transcriptome profiling in single cells
Picelli, S., Björklund, Å. K., Faridani, O. R., Sagasser, S., Winberg, G., & Sandberg, R. (2013) · Nature Methods · doi:10.1038/nmeth.2639 · Cited by 2,358 · see citing works
Rabinowitz, J. D., & White, E. (2010) · Science · doi:10.1126/science.1193497 · Cited by 1,982 · see citing works
A lysosome‐to‐nucleus signalling mechanism senses and regulates the lysosome via mTOR and TFEB
Settembre, C., Zoncu, R., Medina, D. L., Vetrini, F., Erdin, S., Erdin, S. U., Huynh, T., Ferron, M., Karsenty, G., Vellard, M. C., et al. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.32 · Cited by 1,932 · see citing works
Rioux, J. D., Xavier, R. J., Taylor, K. D., Silverberg, M. S., Goyette, P., Huett, A., Green, T., Kuballa, P., Barmada, M. M., Datta, L. W., et al. (2007) · Nature Genetics · doi:10.1038/ng2032 · Cited by 1,769 · see citing works
Self-citationMTORC1 functions as a transcriptional regulator of autophagy by preventing nuclear transport of TFEB
Martina, J. A., Chen, Y., Guček, M., & Puertollano, R. (2012) · Autophagy · doi:10.4161/auto.19653 · Cited by 1,360 · see citing works
Roczniak-Ferguson, A., Petit, C. S. V., Froehlich, F., Qian, S., Ky, J., Angarola, B. L., Walther, T. C., & Ferguson, S. M. (2012) · Science Signaling · doi:10.1126/scisignal.2002790 · Cited by 1,358 · see citing works
GOATOOLS: A Python library for Gene Ontology analyses
Klopfenstein, D. V., Zhang, L., Pedersen, B. S., Ramírez, F., Vesztrocy, A. W., Naldi, A., Mungall, C., Yunes, J. M., Botvinnik, O. B., Weigel, M., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-28948-z · Cited by 1,307 · see citing works
Bray, M.-A., Singh, S., Han, H., Davis, C. T., Borgeson, B., Hartland, C., Kost-Alimova, M., Gustafsdottir, S. M., Gibson, C. C., & Carpenter, A. E. (2016) · Nature Protocols · doi:10.1038/nprot.2016.105 · Cited by 1,090 · see citing works
Self-citationTFEB controls cellular lipid metabolism through a starvation-induced autoregulatory loop
Settembre, C., De Cegli, R., Mansueto, G., Saha, P. K., Vetrini, F., Visvikis, O., Huynh, T., Carissimo, A., Palmer, D., Jürgen Klisch, T., et al. (2013) · Nature Cell Biology · doi:10.1038/ncb2718 · Cited by 1,022 · see citing works
Characterization of the CLEAR network reveals an integrated control of cellular clearance pathways
Palmieri, M., Impey, S., Kang, H., di Ronza, A., Pelz, C., Sardiello, M., & Ballabio, A. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr306 · Cited by 1,022 · see citing works
The lysosome as a cellular centre for signalling, metabolism and quality control
Lawrence, R. E., & Zoncu, R. (2019) · Nature Cell Biology · doi:10.1038/s41556-018-0244-7 · Cited by 920 · see citing works
Autophagy in the Cellular Energetic Balance
Singh, R., & Cuervo, A. M. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.04.004 · Cited by 788 · see citing works
Abu-Remaileh, M., Wyant, G. A., Kim, C., Laqtom, N. N., Abbasi, M., Chan, S. H., Freinkman, E., & Sabatini, D. M. (2017) · Science · doi:10.1126/science.aan6298 · Cited by 665 · see citing works
The Lysosome as a Regulatory Hub
Perera, R. M., & Zoncu, R. (2016) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-111315-125125 · Cited by 664 · see citing works
Puertollano, R., Ferguson, S. M., Brugarolas, J., & Ballabio, A. (2018) · The EMBO Journal · doi:10.15252/embj.201798804 · Cited by 519 · see citing works
Rusmini, P., Cortese, K., Crippa, V., Cristofani, R., Cicardi, M. E., Ferrari, V., Vezzoli, G., Tedesco, B., Meroni, M., Messi, E., et al. (2019) · Autophagy · doi:10.1080/15548627.2018.1535292 · Cited by 436 · see citing works
mTOR-dependent phosphorylation controls TFEB nuclear export
Napolitano, G., Esposito, A., Choi, H., Matarese, M., Benedetti, V., Malta, C. D., Monfregola, J., Medina, D. L., Lippincott‐Schwartz, J., & Ballabio, A. (2018) · Nature Communications · doi:10.1038/s41467-018-05862-6 · Cited by 408 · see citing works
Innate 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 330 · see citing works
The biogenesis of lysosomes and lysosome-related organelles
Luzio, J. P., Hackmann, Y., Dieckmann, N. M. G., & Griffiths, G. M. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a016840 · Cited by 330 · see citing works
Mitochondrial Respiration Controls Lysosomal Function during Inflammatory T Cell Responses
Baixauli, F., Acín‐Pérez, R., Villarroya‐Beltri, C., Mazzeo, C., Núñez‐Andrade, N., Gabandé‐Rodríguez, E., Ledesma, M. D., Blázquez, A., Martín, M. A., Falcón‐Pérez, J. M., et al. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.07.020 · Cited by 327 · see citing works
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 · see citing works
Ravenhill, B. J., Boyle, K. B., von Muhlinen, N., Ellison, C. J., Masson, G. R., Otten, E. G., Foeglein, Á., Williams, R., & Randow, F. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.01.041 · Cited by 298 · see citing works
Macedo, A. C. L., & Isaac, L. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2016.00055 · Cited by 293 · see citing works
Mitochondria–Lysosome Crosstalk: From Physiology to Neurodegeneration
Deus, C. M., Yambire, K. F., Oliveira, P. J., & Raimundo, N. (2019) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2019.10.009 · Cited by 291 · see citing works
Discovery of a proteinaceous cellular receptor for a norovirus
Orchard, R. C., Wilen, C. B., Doench, J. G., Baldridge, M. T., McCune, B. T., Lee, Y.-C. J., Lee, S., Pruett‐Miller, S. M., Nelson, C. A., Fremont, D. H., et al. (2016) · Science · doi:10.1126/science.aaf1220 · Cited by 279 · see citing works
Self-citationThiele, D. L., & Lipsky, P. E. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.1.83 · Cited by 264 · see citing works
Autophagy, lipophagy and lysosomal lipid storage disorders
Ward, C., Martínez-López, N., Otten, E. G., Carroll, B., Maetzel, D., Singh, R., Sarkar, S., & Korolchuk, V. I. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2016.01.006 · Cited by 243 · see citing works
Conway, K. L., Kuballa, P., Song, J., Patel, K., Castoreno, A. B., Yilmaz, Ö. H., Jijon, H. B., Zhang, M., Aldrich, L. N., Villablanca, E. J., et al. (2013) · Gastroenterology · doi:10.1053/j.gastro.2013.08.035 · Cited by 233 · see citing works
Self-citationHigh-performance web services for querying gene and variant annotation
Xin, J., Mark, A., Afrasiabi, C., Tsueng, G., Juchler, M., Gopal, N., Stupp, G. S., Putman, T., Ainscough, B. J., Griffith, O. L., et al. (2016) · Genome biology · doi:10.1186/s13059-016-0953-9 · Cited by 226 · see citing works
Eisenreich, W., Rudel, T., Heesemann, J., & Goebel, W. (2019) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2019.00042 · Cited by 218 · see citing works
Low-Affinity Binding Sites and the Transcription Factor Specificity Paradox in Eukaryotes
Kribelbauer, J. F., Rastogi, C., Bussemaker, H. J., & Mann, R. S. (2019) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100617-062719 · Cited by 216 · see citing works
Wibowo, A. S., Singh, M., Reeder, K. M., Carter, J. J., Kovach, A. R., Meng, W., Ratnam, M., Zhang, F. P. Y., & Dann, C. E. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1308827110 · Cited by 213 · see citing works
Lintner, K. E., Wu, Y. L., Yang, Y., Spencer, C. H., Hauptmann, G., Hebert, L. A., Atkinson, J. P., & Yu, C. Y. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2016.00036 · Cited by 210 · see citing works
Prosaposin facilitates sortilin-independent lysosomal trafficking of progranulin
Zhou, X., Sun, L., de Oliveira, F. M. B., Qi, X., Brown, W. J., Smolka, M. B., Sun, Y., & Hu, F. (2015) · The Journal of Cell Biology · doi:10.1083/jcb.201502029 · Cited by 201 · see citing works
Willett, R. A., Martina, J. A., Zewe, J. P., Wills, R. C., Hammond, G. R. V., & Puertollano, R. (2017) · Nature Communications · doi:10.1038/s41467-017-01871-z · Cited by 196 · see citing works
Eichner, L. J., Brun, S. N., Herzig, S., Young, N. P., Curtis, S. D., Shackelford, D. B., Shokhirev, M. N., Leblanc, M., Vera, L. I., Hutchins, A., et al. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.10.005 · Cited by 190 · see citing works
Median Absolute Deviation to Improve Hit Selection for Genome-Scale RNAi Screens
Chung, N., Zhang, X. D., Kreamer, A., Locco, L., Kuan, P. F., Bartz, S. R., Linsley, P. S., Ferrer, M., & Strulovici, B. (2008) · SLAS DISCOVERY · doi:10.1177/1087057107312035 · Cited by 184 · see citing works
A Critical Role of Autophagy in Regulating Microglia Polarization in Neurodegeneration
Jin, M.-M., Wang, F., Qi, D., Liu, W.-W., Gu, C., Mao, C.-J., Yang, Y.-P., Zhao, Z., Hu, L.-F., & Liu, C.-F. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00378 · Cited by 180 · see citing works
The glycoprotein GPNMB attenuates astrocyte inflammatory responses through the CD44 receptor
Neal, M. P., Boyle, A. M., Budge, K. M., Safadi, F. F., & Richardson, J. R. (2018) · Journal of Neuroinflammation · doi:10.1186/s12974-018-1100-1 · Cited by 179 · see citing works
Martina, J. A., & Puertollano, R. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.003471 · Cited by 167 · see citing works
DEC1 Modulates the Circadian Phase of Clock Gene Expression
Nakashima, A., Kawamoto, T., Honda, K. K., Ueshima, T., Noshiro, M., Iwata, T., Fujimoto, K., Kubo, H., Honma, S., Yorioka, N., et al. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.02168-07 · Cited by 163 · see citing works
Emerging roles for TFEB in the immune response and inflammation
Brady, O. A., Martina, J. A., & Puertollano, R. (2017) · Autophagy · doi:10.1080/15548627.2017.1313943 · Cited by 162 · see citing works
Autophagy and innate immunity: Insights from invertebrate model organisms
Kuo, C., Hansen, M., & Troemel, E. R. (2017) · Autophagy · doi:10.1080/15548627.2017.1389824 · Cited by 160 · see citing works
Martina, J. A., Diab, H. I., Li, H., & Puertollano, R. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1565-8 · Cited by 155 · see citing works
Tanaka, Y., Matsuwaki, T., Yamanouchi, K., & Nishihara, M. (2013) · Neuroscience · doi:10.1016/j.neuroscience.2013.06.049 · Cited by 153 · see citing works
Spatiotemporal compartmentalization of hepatic NADH and NADPH metabolism
Goodman, R. P., Calvo, S. E., & Mootha, V. K. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.tm117.000258 · Cited by 148 · see citing works
GILT is a critical host factor for Listeria monocytogenes infection
Singh, R., Jamieson, A. M., & Cresswell, P. (2008) · Nature · doi:10.1038/nature07344 · Cited by 144 · see citing works
Complement C3 Drives Autophagy-Dependent Restriction of Cyto-invasive Bacteria
Sorbara, M. T., Foerster, E. G., Tsalikis, J., Abdel‐Nour, M., Mangiapane, J., Sirluck-Schroeder, I., Tattoli, I., van Dalen, R., Isenman, D. E., Rohde, J. R., et al. (2018) · Cell Host & Microbe · doi:10.1016/j.chom.2018.04.008 · Cited by 136 · see citing works
A TFEB nuclear export signal integrates amino acid supply and glucose availability
Li, L., Friedrichsen, H. J., Andrews, S., Picaud, S., Volpon, L., Ngeow, K. C., Berridge, G., Fischer, R., Borden, K. L. B., Filippakopoulos, P., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-04849-7 · Cited by 121 · see citing works
HIF-1α induction suppresses excessive lipid accumulation in alcoholic fatty liver in mice
Nishiyama, Y., Goda, N., Kanai, M., Niwa, D., Osanai, K., Yamamoto, Y., Senoo‐Matsuda, N., Johnson, R. S., Miura, S., Kabe, Y., et al. (2011) · Journal of Hepatology · doi:10.1016/j.jhep.2011.07.024 · Cited by 119 · see citing works
Kreslavsky, T., Vilagos, B., Tagoh, H., Kostanova‐Poliakova, D., Schwickert, T. A., Wöhner, M., Jaritz, M., Weiß, S., Taneja, R., Rossner, M. J., et al. (2017) · Nature Immunology · doi:10.1038/ni.3694 · Cited by 119 · see citing works
El–Houjeiri, L., Possik, E., Vijayaraghavan, T., Paquette, M., Martina, J. A., Kazan, J. M., Ma, E. H., Jones, R. G., Blanchette, P., Puertollano, R., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.02.102 · Cited by 117 · see citing works
Workflow and Metrics for Image Quality Control in Large-Scale High-Content Screens
Bray, M., Fraser, A. N., Hasaka, T. P., & Carpenter, A. E. (2011) · SLAS DISCOVERY · doi:10.1177/1087057111420292 · Cited by 116 · see citing works
Hastings, K. T., & Cresswell, P. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3684 · Cited by 105 · see citing works
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., Amand, V. S., Reenan, R. A., & Lapierre, L. R. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.04.063 · Cited by 104 · see citing works
Repnik, U., Distefano, M. B., Speth, M. T., Ng, M. Y. W., Progida, C., Hoflack, B., Gruenberg, J. E., & Griffiths, G. (2017) · Journal of Cell Science · doi:10.1242/jcs.204529 · Cited by 103 · see citing works
Marques, A. R. A., Spiezio, A. D., Thießen, N., Schmidt, L., Grötzinger, J., Lüllmann‐Rauch, R., Daμμe, M., Storck, S. E., Pietrzik, C. U., Fogh, J. M., et al. (2019) · Autophagy · doi:10.1080/15548627.2019.1637200 · Cited by 103 · see citing works
Fernández-Mosquera, L., Diogo, C. V., Yambire, K. F., Santos, G. L., Luna‐Sánchez, M., Bénit, P., Rustin, P., López, L. C., Milošević, I., & Raimundo, N. (2017) · Scientific Reports · doi:10.1038/srep45076 · Cited by 96 · see citing works
G0S2: A small giant controller of lipolysis and adipose-liver fatty acid flux
Zhang, X., Heckmann, B. L., Campbell, L. E., & Liu, J. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2017.06.007 · Cited by 93 · see citing works
Xu, Y., Ren, J., He, X., Chen, H., Wei, T., & Feng, W. (2019) · Autophagy · doi:10.1080/15548627.2019.1569928 · Cited by 87 · see citing works
Van der Lienden, M. J. C., Gaspar, P., Boot, R., Aerts, J. M. F. G., & Van Eijk, M. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms20010066 · Cited by 84 · see citing works
Murine Cathepsin F Deficiency Causes Neuronal Lipofuscinosis and Late-Onset Neurological Disease
Tang, C., Lee, J., Galvez, M. G., Robillard, L., Mole, S., & Chapman, H. A. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.6.2309-2316.2006 · Cited by 80 · see citing works
TFEB controls vascular development by regulating the proliferation of endothelial cells
Doronzo, G., Astanina, E., Corà, D., Chiabotto, G., Comunanza, V., Noghero, A., Neri, F., Puliafito, A., Primo, L., Spampanato, C., et al. (2018) · The EMBO Journal · doi:10.15252/embj.201798250 · Cited by 78 · see citing works
Nguyen, A. D., Nguyen, T. A., Zhang, J., Devireddy, S., Zhou, P., Karydas, A. M., Xu, X., Miller, B. L., Rigo, F., Ferguson, S. M., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1722344115 · Cited by 75 · see citing works
Progranulin Stimulates the In Vitro Maturation of Pro-Cathepsin D at Acidic pH
Butler, V. J., Cortopassi, W. A., Argouarch, A. R., Ivry, S. L., Craik, C. S., Jacobson, M. P., & Kao, A. W. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.01.027 · Cited by 75 · see citing works
Jacobson, L. S., Lima, H., Goldberg, M. F., Gocheva, V., Tsiperson, V., Sutterwala, F. S., Joyce, J. A., Gapp, B. V., Blomen, V. A., Chandran, K., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.400655 · Cited by 74 · see citing works
How to rewire the host cell: A home improvement guide for intracellular bacteria
Taylor-Cornejo, E., Schlaermann, P., & Mukherjee, S. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201701095 · Cited by 73 · see citing works
Assembly and Architecture of Biogenesis of Lysosome-related Organelles Complex-1 (BLOC-1)
Lee, H. H., Němeček, D., Schindler, C., Smith, W. J., Ghirlando, R., Steven, A. C., Bonifacino, J. S., & Hurley, J. H. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.325746 · Cited by 70 · see citing works
Autophagy and Ubiquitination in Salmonella Infection and the Related Inflammatory Responses
Wang, L., Yan, J. Y., Niu, H., Huang, R., & Wu, S. (2018) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2018.00078 · Cited by 69 · see citing works
Self-citationAn Evolutionarily Conserved PLC-PKD-TFEB Pathway for Host Defense
Najibi, M., Labed, S. A., Visvikis, O., & Irazoqui, J. E. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.04.052 · Cited by 64 · see citing works
TFEB-driven lysosomal biogenesis is pivotal for PGC1α-dependent renal stress resistance
Lynch, M. R., Tran, M. T., Ralto, K. M., Zsengellér, Z. K., Raman, V., Bhasin, S. S., Sun, N., Chen, X., Brown, D., Rovira, I. I., et al. (2019) · JCI Insight · doi:10.1172/jci.insight.126749 · Cited by 61 · see citing works
TFEB-driven lysosomal biogenesis is pivotal for PGC1α-dependent renal stress resistance
Lynch, M. R., Tran, M. T., Ralto, K. M., Zsengellér, Z. K., Raman, V., Bhasin, S. S., Sun, N., Chen, X., Brown, D., Rovira, I. I., et al. (2020) · JCI Insight · doi:10.1172/jci.insight.142898 · Cited by 55 · see citing works
The Transcription Factor EB Links Cellular Stress to the Immune Response .
Nabar, N. R., & Kehrl, J. H. (2017) · Europe PMC (PubMed Central) · Cited by 50 · see citing works
Brojatsch, J., Lima, H., Palliser, D., Jacobson, L. S., Muehlbauer, S. M., Furtado, R., Goldman, D. L., Lisanti, M. P., & Chandran, K. (2015) · Cell Cycle · doi:10.4161/15384101.2014.991194 · Cited by 50 · see citing works
Kanda, M., Yamanaka, H., Kojo, S., Usui, Y., Honda, H., Sotomaru, Y., Harada, M., Taniguchi, M., Suzuki, N., Atsumi, T., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1604178113 · Cited by 48 · see citing works
Glycoprotein NMB: an Emerging Role in Neurodegenerative Disease
Budge, K. M., Neal, M. P., Richardson, J. R., & Safadi, F. F. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0707-z · Cited by 46 · see citing works
Meireles, A. M., Shen, K., Zoupi, L., Iyer, H., Bouchard, E. L., Williams, A. C., & Talbot, W. (2018) · Developmental Cell · doi:10.1016/j.devcel.2018.10.003 · Cited by 43 · see citing works
Tan, H. W. S., Anjum, B., Shen, H., Ghosh, S., Yen, P. M., & Sinha, R. A. (2019) · Autophagy · doi:10.1080/15548627.2019.1609847 · Cited by 39 · see citing works
Orvedahl, A., McAllaster, M. R., Sansone, A., Dunlap, B. F., Desai, C., Wang, Y., Balce, D. R., Luke, C. J., Lee, S., Orchard, R. C., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1822157116 · Cited by 39 · see citing works
Self-citationMurano, T., Najibi, M., Paulus, G. L. C., Adiliaghdam, F., Valencia-Guerrero, A. L., Selig, M. K., Wang, X., Jeffrey, K. L., Xavier, R. J., Lassen, K. G., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-14370-4 · Cited by 37 · see citing works
Self-citationClinical utility of whole-exome sequencing in rare diseases: Galactosialidosis
Prada, C. E., Gonzaga-Jauregui, C., Tannenbaum, R., Penney, S., Lupski, J. R., Hopkin, R. J., & Sutton, V. R. (2014) · European Journal of Medical Genetics · doi:10.1016/j.ejmg.2014.04.005 · Cited by 29 · see citing works
Bhlhe40 Represses PGC-1α Activity on Metabolic Gene Promoters in Myogenic Cells
Chung, S. Y., Kao, C. H., Villarroya, F., Chang, H. Y., Chang, H. C., Hsiao, S. P., Liou, G., & Chen, S. L. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.00387-15 · Cited by 23 · see citing works
A new heterozygous compound mutation in the CTSA gene in galactosialidosis
Nakajima, H., Ueno, M., Adachi, K., Nanba, E., Narita, A., Tsukimoto, J., Itoh, K., & Kawakami, A. (2019) · Human Genome Variation · doi:10.1038/s41439-019-0054-x · Cited by 19 · see citing works
Handcuffs for bacteria - NDP52 orchestrates xenophagy of intracellular Salmonella
Verlhac, P., Viret, C., & Faure, M. (2015) · Microbial Cell · doi:10.15698/mic2015.06.208 · Cited by 4 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Tan, A., Prasad, R., Lee, C., & Jho, E. (2022) · Cell Death and Differentiation · doi:10.1038/s41418-022-01028-6 · Cited by 258 · see citing works
Cell Painting: a decade of discovery and innovation in cellular imaging
Seal, S., Trapotsi, M., Spjuth, O., Singh, S., Puigvert, J. C., Greene, N., Bender, A., & Carpenter, A. E. (2024) · Nature Methods · doi:10.1038/s41592-024-02528-8 · Cited by 120 · see citing works
Self-citationLysosomal membrane homeostasis and its importance in physiology and disease
Radulovic, M., Yang, C., & Stenmark, H. (2025) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-025-00873-w · Cited by 86 · see citing works
Sex‐specific transcriptome of spinal microglia in neuropathic pain due to peripheral nerve injury
Fiore, N. T., Yin, Z., Güneykaya, D., Gauthier, C. D., Hayes, J. P., D’Hary, A., Butovsky, O., & Moalem‐Taylor, G. (2022) · Glia · doi:10.1002/glia.24133 · Cited by 72 · see citing works
Activation of PPARα enhances astroglial uptake and degradation of β-amyloid
Raha, S., Ghosh, A., Dutta, D., Patel, D. R., & Pahan, K. (2021) · Science Signaling · doi:10.1126/scisignal.abg4747 · Cited by 63 · see citing works
Podleśny-Drabiniok, A., Novikova, G., Liu, Y., Dunst, J., Temizer, R., Giannarelli, C., Marro, S., Kreslavsky, T., Marcora, E., & Goate, A. M. (2024) · Nature Communications · doi:10.1038/s41467-024-46315-7 · Cited by 52 · see citing works
Rapalogs downmodulate intrinsic immunity and promote cell entry of SARS-CoV-2
Shi, G., Chiramel, A. I., Li, T., Lai, K. K., Kenney, A. D., Zani, A., Eddy, A. C., Majdoul, S., Zhang, L., Dempsey, T., et al. (2022) · Journal of Clinical Investigation · doi:10.1172/jci160766 · Cited by 47 · see citing works
Role of TFEB in Autophagy and the Pathogenesis of Liver Diseases
Yan, S. (2022) · Biomolecules · doi:10.3390/biom12050672 · Cited by 44 · see citing works
MiT Family Transcriptional Factors in Immune Cell Functions
Kim, S., Song, H.-S., Yu, J., & Kim, Y. (2021) · Molecules and Cells · doi:10.14348/molcells.2021.0067 · Cited by 42 · see citing works
Tang, Z., Xing, C., Araszkiewicz, A. M., Yang, K., Huai, W., Jeltema, D., Dobbs, N., Zhang, Y., Sun, L. O., & Yan, N. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.03.008 · Cited by 40 · see citing works
Jin, Y. H., Pan, Y., Zheng, S., Liu, Y., Xu, J., Peng, Y., Zhang, Z., Wang, Y., Xiong, Y., Xu, L., et al. (2022) · Oncogene · doi:10.1038/s41388-022-02203-2 · Cited by 39 · see citing works
Apilimod dimesylate in C9orf72 amyotrophic lateral sclerosis: a randomized phase 2a clinical trial
Babu, S., Nicholson, K. A., Rothstein, J. D., Swenson, A., Sampognaro, P. J., Pant, P., Macklin, E. A., Spruill, S. E., Paganoni, S., Gendron, T. F., et al. (2024) · Brain · doi:10.1093/brain/awae109 · Cited by 31 · see citing works
Lysosomal damage due to cholesterol accumulation triggers immunogenic cell death
Alvarez-Valadez, K., Sauvat, A., Diharce, J., Leduc, M., Stoll, G., Guittat, L., Lambertucci, F., Paillet, J., Motiño, O., Ferret, L., et al. (2024) · Autophagy · doi:10.1080/15548627.2024.2440842 · Cited by 29 · see citing works
Cobo, I., Murillo‐Saich, J., Alishala, M., Calderon, S., Coras, R., Hemming, B., Inkum, F., Rosas, F., Takei, R., Spann, N. J., et al. (2025) · Immunity · doi:10.1016/j.immuni.2025.02.023 · Cited by 29 · see citing works
Veremeichik, G. N., Shkryl, Y., Rusapetova, T. V., Silantieva, S. A., Grigorchuk, V. P., Velansky, P. V., Brodovskaya, E. V., Konnova, Y. A., Khopta, A. A., Bulgakov, D. V., et al. (2022) · Planta · doi:10.1007/s00425-022-03927-x · Cited by 28 · see citing works
TFEB safeguards trophoblast syncytialization in humans and mice
Zheng, W., Zhang, Y., Xu, P., Wang, Z., Shao, X., Chen, C., Cai, H., Wang, Y., Sun, M.-A., Deng, W., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2404062121 · Cited by 26 · see citing works
DMXL1 promotes recruitment of V1-ATPase to lysosomes upon TRPML1 activation
Lee, C., Eldridge, M. J. G., Gonzalez‐Lozano, M. A., Bresnahan, T., Niday, Z., del Camino, D., Fu, T., Paulo, J. A., Moran, M. M., Hélaine, S., et al. (2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-025-01581-x · Cited by 23 · see citing works
Bogacki, E. C., Parfitt, G. M., Cunha, A., Longmore, G., Wray, S., Lewis, P. A., & Herbst, S. (2025) · Science Advances · doi:10.1126/sciadv.adv1434 · Cited by 24 · see citing works
Rodriguez‐Gil, J. L., Baxter, L. L., Watkins‐Chow, D. E., Johnson, N. L., Davidson, C. D., Carlson, S. R., Incao, A. A., Program, N. C. S., Wallom, K., Farhat, N. Y., et al. (2021) · Human Molecular Genetics · doi:10.1093/hmg/ddab194 · Cited by 22 · see citing works
BORC-ARL8-HOPS ensemble is required for lysosomal cholesterol egress through NPC2
Anderson, J. R., Walker, G., & Pu, J. (2022) · Molecular Biology of the Cell · doi:10.1091/mbc.e21-11-0595-t · Cited by 20 · see citing works
A Decade in a Systematic Review: The Evolution and Impact of Cell PaintingPreprint
Seal, S., Trapotsi, M., Spjuth, O., Singh, S., Puigvert, J. C., Greene, N., Bender, A., & Carpenter, A. E. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.05.04.592531 · Cited by 20 · see citing works
Self-citationLee, Y. Y., Ha, J., Kim, Y. S., Ramani, S., Sung, S., Gil, E. S., Choo, O., Jang, J. H., & Choung, Y. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242417513 · Cited by 19 · see citing works
TFEB and TFE3 regulate STING1-dependent immune responses by controlling type I interferon signaling
Tapía, P., Martina, J. A., Contreras, P. S., Prashar, A., Jeong, E., Nardo, D. D., & Puertollano, R. (2025) · Autophagy · doi:10.1080/15548627.2025.2487036 · Cited by 19 · see citing works
TFEB and TFE3 control glucose homeostasis by regulating insulin gene expression
Pasquier, A., Pastore, N., D'Orsi, L., Colonna, R., Esposito, A., Maffia, V., Cegli, R. D., Mutarelli, M., Ambrosio, S., Tufano, G., et al. (2023) · EMBO Journal · doi:10.15252/embj.2023113928 · Cited by 11 · see citing works
Transcription factor EB as a key molecular factor in human health and its implication in diseases
Gebrie, A. (2023) · SAGE Open Medicine · doi:10.1177/20503121231157209 · Cited by 14 · see citing works
Liu, L., Lei, I., Tian, S., Gao, W., Guo, Y., Li, Z., Sabry, Z., Tang, P. C. Y., Chen, Y. E., & Wang, Z. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114054 · Cited by 14 · see citing works
Balboa, E., Marín, T., Oyarzún, J. E., Contreras, P. S., Hardt, R., van den Bosch, T., Alvarez, A. R., Rebolledo‐Jaramillo, B., Klein, A. D., Winter, D., et al. (2021) · Cells · doi:10.3390/cells10082159 · Cited by 12 · see citing works
von Coburg, E., Wedler, M., Muiño, J. M., Wolff, C., Körber, N., Dunst, S., & Liu, S. (2025) · Nature Communications · doi:10.1038/s41467-025-58765-8 · Cited by 12 · see citing works
SLIT2/ROBO1 signaling suppresses mTORC1 for organelle control and bacterial killing
Bhosle, V. K., Tan, J. M. J., Li, T., Hua, R., Kwon, H., Li, Z., Patel, S., Tessier‐Lavigne, M., Robinson, L. A., Kim, P. K., et al. (2023) · Life Science Alliance · doi:10.26508/lsa.202301964 · Cited by 11 · see citing works
Kim, Y., Ha, T.-Y., Kondaurova, O., Lee, M.-S., & Chang, K. (2026) · Journal of Neuroinflammation · doi:10.1186/s12974-026-03728-z · Cited by 10 · see citing works
Lear, T., Larsen, M. B., Lin, B., Treat, B. R., Cao, Q. N., Boudreau, Á. N., Lockwood, K. C., Alfaras, I., Kennerdell, J. R., Salminen, L., et al. (2025) · Science Advances · doi:10.1126/sciadv.adv4033 · Cited by 10 · see citing works
Autophagy activator AA-20 improves proteostasis and extends Caenorhabditis elegans lifespan
Tan, E. P., Lyang, N., Doroodian, S., Sanz-Martinez, P., Xu, J., Zaretski, S., Nieto-Torres, J. L., Ebata, H., Lim, S. H. Y., Hou, W. C., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2423455122 · Cited by 9 · see citing works
Cabral-Fernandes, L., Goyal, S., Farahvash, A., Tsalikis, J., Philpott, D., & Girardin, S. (2022) · Molecular and Cellular Biology · doi:10.1128/mcb.00241-22 · Cited by 5 · see citing works
Podleśny-Drabiniok, A., Novikova, G., Liu, Y.-Y., Dunst, J., Temizer, R., Giannarelli, C., Marro, S. G., Kreslavsky, T., Marcora, E., & Goate, A. (2023) · bioRxiv · doi:10.1101/2023.02.13.528372 · Cited by 5 · see citing works
Tejwani, L., Heffner, C. M., Balak, C. D., Skuja, L. L., Tatarakis, D., Rana, A., Yu, S. B., Fitzgerald, G. A., Ha, C., de Melo, G. L., et al. (2026) · Immunity · doi:10.1016/j.immuni.2026.07.009 · Cited by 7 · see citing works
Romanò, R., Cordella, P., & Bucci, C. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26020549 · Cited by 4 · see citing works
Alternate dyes for image-based profiling assays
Sivagurunathan, S., Byrne, P. J., Muñoz, A. F., Arévalo, J., Carpenter, A. E., Singh, S., Kost‐Alimova, M., & Cimini, B. A. (2025) · SLAS DISCOVERY · doi:10.1016/j.slasd.2025.100268 · Cited by 5 · see citing works
Self-citationHonwad, H. H., Najibi, M., Shen, J., Watts, S., Fu, A., Koscsó, B., Bogunovic, M., & Irazoqui, J. E. (2025) · Journal of Leukocyte Biology · doi:10.1093/jleuko/qiaf077 · Cited by 4 · see citing works
Lysosomes cell autonomously regulate myeloid cell states and immune responses
Tejwani, L., Balak, C., Skuja, L. L., Tatarakis, D., Rana, A., Fitzgerald, G. A., Ha, C., Lunkes de Melo, G., Sun, E. W., Heffner, C. M., et al. (2024) · doi:10.1101/2024.11.11.623074 · Cited by 4 · see citing works
Memari, A., Shahrbabaki, P. M., Zakeri, M. A., & Ahmadinejad, M. (2023) · Frontiers in Psychiatry · doi:10.3389/fpsyt.2023.1269402 · Cited by 3 · see citing works
Cancer cell phagocytosis induces an anti-inflammatory gene regulatory program in macrophagesPreprint
Zhang, C. R., Xiong, L., Gu, M., Yeh, C. Y., Jerby‐Arnon, L., Kundaje, A. B., Greenleaf, W. J., & Bassik, M. C. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.08.18.670953 · Cited by 3 · see citing works
Li, Y., Yang, E., Geng, Y., Li, M., Wang, X., & Zhang, D. (2024) · Archives of Oral Biology · doi:10.1016/j.archoralbio.2024.105909 · Cited by 2 · see citing works
Wu, Z., Zhao, Y., Hao, S., An, M., Song, C., & Li, J. (2025) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-24-01371 · Cited by 4 · see citing works
Dysregulation of cellular iron predisposes chemotherapy resistant cancer cells to ferroptosisPreprint
Loftus, L. V., Rolle, L. T. A., Cherry, C., Patatanian, M., Orzolek, L. D., Wang, B., Pienta, K. J., & Amend, S. R. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.12.05.626685 · Cited by 2 · see citing works
Kövér, B., Willis, T. L., Sherwin, O., Kaufman-Cook, J., Kemkem, Y., Segoviano, M. V., Lodge, E. J., Zamojski, M., Mendelev, N., Zhang, Z., et al. (2026) · Cell Reports · doi:10.1016/j.celrep.2026.117407 · Cited by 1 · see citing works
Distéfano‐Gagné, F., Belhamiti, N., Saxon, W., Bitarafan, S., Xavier, A. M., Fiola, S., Rivest, S., & Gosselin, D. (2026) · Cell Reports · doi:10.1016/j.celrep.2026.117569 · Cited by 1 · see citing works
Bogacki, E. C., Lewis, P. A., & Herbst, S. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.12.19.572409 · Cited by 1 · see citing works
Targeting Microglial Transcriptional Reprogramming as a Therapy Strategy for Alzheimer's Disease
Kim, B., Wang, S. S., Kim, J. R., & Kim, J. (2026) · BioEssays · doi:10.1002/bies.70186
“IRF8 reciprocally stabilizes PU.1 expression via enhancer interactions, forming a positive feedback 1 and Table 2) [53, 54].”
Optimizing the Cell Painting assay for image-based profiling
Cimini, B. A., Chandrasekaran, S. N., Kost-Alimova, M., Miller, L., Goodale, A., Fritchman, B., Byrne, P., Garg, S., Jamali, N., Logan, D. J., et al. (2023) · Nature Protocols · doi:10.1038/s41596-023-00840-9 · Cited by 177 · see citing works
Self-citationKövér, B., Willis, T. L., Sherwin, O., Kaufman-Cook, J., Kemkem, Y., Segoviano, M. V., Lodge, E. J., Zamojski, M., Mendelev, N., Zhang, Z., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.28.685060
New Insights into TFEB SUMOylation and Its Role in Lipid Metabolism and Cardiovascular Disease
Meng, Q., Li, C. G., Chen, X., Cao, R., Zhang, H. Q., Wang, P., & Jin, J. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms27010347
Gontier, G., Kim, G., Wang, C., Zhu, K., Gau, R., Zhang, N., Naphade, S. B., Stewart, A. J., Schmidt, M. J., Galemmo, R., et al. (2026) · Clinical and Translational Science · doi:10.1111/cts.70489
Lysosomal function and homeostasis: From cellular adaptation to disease pathogenesis
Minami, S., & Hamasaki, M. (2026) · International review of cytology · doi:10.1016/bs.ircmb.2026.04.002
Yuan, C., Wang, J., Wang, Z., Mao, P., Dong, P., Dong, J., Guo, L., Liu, K., Cui, L., Li, J., et al. (2026) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2026.05.293
McDougal, M. B., Sandoval, A., Kinter, M., Jain, A., Lee, S., Jung, S. Y., & Yoon, W. H. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.09.23.753918
- Authors
- Carey, K. L., Paulus, G. L. C., Wang, L., Balce, D. R., Luo, J. W., Bergman, P., Ferder, I. C., Kong, L., Renaud, N., Singh, S., Kost-Alimova, M., Nyfeler, B., Lassen, K. G., Virgin, H. W., & Xavier, R. J.
- Affiliations
- Broad Institute (US)
- Harvard University (US)
- Washington University in St. Louis (US)
- Novartis Institutes for BioMedical Research (CH)
- Corresponding author
- Xavier, Ramnik J.
- ORCID
- Venue
- Cell Reports
- Publisher
- Elsevier BV
- Published
- 2020-11
- Volume
- 33
- Issue
- 6
- Pages
- 108371
- ISSN
- 2211-1247 (ISSN-L)
- PMC
- PMC7686957
- OpenAlex
- W3100411033
- Cited by
- 55
- References
- 95
- Citations by year
- 2026: 9 · 2025: 16 · 2024: 10 · 2023: 8 · 2022: 8 · 2021: 4
- FWCI
- 3.59
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Cell Reports (publishedVersion, cc-by)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Digital Commons@Becker (Washington University School of Medicine) (submittedVersion, cc-by)
- The Novartis Repository (Novartis) (submittedVersion, cc-by)
- CONICET Digital (CONICET) (submittedVersion, cc-by-nc-sa)
- Funders
- National Institutes of Health
- Topics
- Health Sciences › Medicine › Epidemiology › 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 › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Keywords
- TFEB, BHLHE40, BHLHE41, lysosomal biogenesis, autophagy, lysosomal cell death, negative feedback regulation, transcriptional regulation, mTOR inhibition, innate immunity, lysosomal dysfunction, CRISPR screen
- MeSH terms
- Cell Nucleus, HeLa Cells, Humans, Lysosomes, Mitochondria, Transcription, Genetic, Homeodomain Proteins, Basic Helix-Loop-Helix Leucine Zipper Transcription Factors, Basic Helix-Loop-Helix Transcription Factors, Basic Helix-Loop-Helix Proteins, Gene Knockout Techniques
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
