The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Image-based genome-wide siRNA screen identifies selective autophagy factors
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 SQSTM1 protein serves as a link between LC3 and ubiquitinated substrates.
“The SQSTM1 protein serves as a link between LC3 and ubiquitinated substrates [121].”
From Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1 (2021) · cites this paper as [121]
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
Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
Narendra, D., Tanaka, A., Suen, D.-F., & Youle, R. J. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200809125 · Cited by 4,026
Autophagy regulates lipid metabolism
Singh, R., Kaushik, S., Wang, Y., Xiang, Y., Novak, I., Komatsu, M., Tanaka, K., Cuervo, A. M., & Czaja, M. J. (2009) · Nature · doi:10.1038/nature07976 · Cited by 3,975
Autophagy in immunity and inflammation
Levine, B., Mizushima, N., & Virgin, H. W. (2011) · Nature · doi:10.1038/nature09782 · Cited by 3,289
Self-citationPINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1
Geisler, S., Holmström, K. M., Skujat, D., Fiesel, F. C., Rothfuss, O. C., Kahle, P. J., & Springer, W. (2010) · Nature Cell Biology · doi:10.1038/ncb2012 · Cited by 2,835
Autophagy in mammalian development and differentiation
Mizushima, N., & Levine, B. (2010) · Nature Cell Biology · doi:10.1038/ncb0910-823 · Cited by 1,555
Self-citationThe role of the Atg1/ULK1 complex in autophagy regulation
Mizushima, N. (2010) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.12.004 · Cited by 1,062
HSV-1 ICP34.5 Confers Neurovirulence by Targeting the Beclin 1 Autophagy Protein
Orvedahl, A., Alexander, D., Tallóczy, Z., Sun, Q., Wei, Y., Zhang, W., Burns, D., Leib, D. A., & Levine, B. (2007) · Cell Host & Microbe · doi:10.1016/j.chom.2006.12.001 · Cited by 857
Self-citationHDAC6 controls autophagosome maturation essential for ubiquitin‐selective quality‐control autophagy
Lee, J., Koga, H., Kawaguchi, Y., Tang, W., Wong, E., Gao, Y., Pandey, U. B., Kaushik, S., Tresse, E., Lu, J., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2009.405 · Cited by 756
Autophagy Protects against Sindbis Virus Infection of the Central Nervous System
Orvedahl, A., MacPherson, S., Sumpter, R., Tallóczy, Z., Zou, Z., & Levine, B. (2010) · Cell Host & Microbe · doi:10.1016/j.chom.2010.01.007 · Cited by 558
Self-citation
Flagged first, then by citations
Research works printed but not linked: 16
- Noda, N. N., Ohsumi, Y. & Inagaki, F. Atg8-family interacting motif crucial for selective autophagy. FEBS Lett. 584, 1379–1385 (2010) · DOI
- Wild, P. et al. Phosphorylation of the autophagy receptor optineurin restricts Salmonella growth. Science 333, 228–233 (2011) · DOI · Paper page
- Komatsu, M. & Ichimura, Y. Selective autophagy regulates various cellular functions. Genes Cells 15, 923–933 (2010) · DOI
- Lipinski, M. M. et al. A genome-wide siRNA screen reveals multiple mTORC1 independent signaling pathways regulating autophagy under normal nutritional conditions. Dev. Cell 18, 1041–1052 (2010) · DOI
- Monastyrska, I., Rieter, E., Klionsky, D. J. & Reggiori, F. Multiple roles of the cytoskeleton in autophagy. Biol. Rev. Camb. Philos. Soc. 84, 431–448 (2009) · DOI
- Longatti, A. & Tooze, S. A. Vesicular trafficking and autophagosome formation. Cell Death Differ. 16, 956–965 (2009) · DOI
- Nair, U. et al. SNARE proteins are required for macroautophagy. Cell 146, 290–302 (2011) · DOI
- Behrends, C., Sowa, M. E., Gygi, S. P. & Harper, J. W. Network organization of the human autophagy system. Nature 466, 68–76 (2010) · DOI · Paper page
- Pagliarini, D. J. et al. A mitochondrial protein compendium elucidates complex I disease biology. Cell 134, 112–123 (2008) · DOI · Paper page
- Xing, L., Zhang, M. & Chen, D. Smurf control in bone cells. J. Cell. Biochem. 110, 554–563 (2010) · DOI
- Talloczy, Z. et al. Regulation of starvation- and virus-induced autophagy by the eIF2α kinase signaling pathway. Proc. Natl Acad. Sci. USA 99, 190–195 (2002) · DOI
- Talloczy, Z., Virgin, H. W. I. V. & Levine, B. PKR-dependent xenophagic degradation of herpes simplex virus type 1. Autophagy 2, 24–29 (2006) · DOI · Paper page
- Narendra, D., Kane, L. A., Hauser, D. N., Fearnley, I. M. & Youle, R. J. p62/SQSTM1 is required for Parkin-induced mitochondrial clustering but not mitophagy; VDAC1 is dispensable for both. Autophagy 6, 1090–1106 (2010) · DOI
- Yamashita, M. et al. Ubiquitin ligase Smurf1 controls osteoblast activity and bone homeostasis by targeting MEKK2 for degradation. Cell 121, 101–113 (2005) · DOI
- Cho, W. & Stahelin, R. V. Membrane binding and subcellular targeting of C2 domains. Biochim. Biophys. Acta 1761, 838–849 (2006) · DOI
- Lu, K. et al. Pivotal role of the C2 domain of the Smurf1 ubiquitin ligase in substrate selection. J. Biol. Chem. 286, 16861–16870 (2011) · DOI
Cited by
Sorted by citations
Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition).
Klionsky, D. J., Abdelmohsen, K., Abe, A., Abedin, M. J., Abeliovich, H., Acevedo Arozena, A., Adachi, H., Adams, C. M., Adams, P. D., Adeli, K., et al. (2016) · Autophagy · doi:10.1080/15548627.2015.1100356 · Cited by 5,894
Self-citationGuidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1
Klionsky, D. J., Abdel-Aziz, A. K., Abdelfatah, S., Abdellatif, M., Abdoli, A., Abel, S., Abeliovich, H., Abildgaard, M. H., Abudu, Y. P., Acevedo-Arozena, A., et al. (2021) · Autophagy · doi:10.1080/15548627.2020.1797280 · Cited by 2,897
Self-citationAutophagy in Human Health and Disease
Choi, A. M. K., Ryter, S. W., & Levine, B. (2013) · New England Journal of Medicine · doi:10.1056/nejmra1205406 · Cited by 2,583
Self-citationThe Roles of PINK1, Parkin, and Mitochondrial Fidelity in Parkinson’s Disease
Pickrell, A. M., & Youle, R. J. (2015) · Neuron · doi:10.1016/j.neuron.2014.12.007 · Cited by 2,310
Autophagy in infection, inflammation and immunity
Deretic, V., Saitoh, T., & Akira, S. (2013) · Nature Reviews Immunology · doi:10.1038/nri3532 · Cited by 1,919
The pathways of mitophagy for quality control and clearance of mitochondria
Ashrafi, G., & Schwarz, T. L. (2013) · Cell Death & Differentiation · doi:10.1038/cdd.2012.81 · Cited by 1,900
Molecular definitions of autophagy and related processes
Galluzzi, L., Baehrecke, E. H., Ballabio, A., Boya, P., Bravo‐San Pedro, J. M., Cecconi, F., Choi, A. M., Chu, C. T., Codogno, P., Colombo, M. I., et al. (2017) · The EMBO Journal · doi:10.15252/embj.201796697 · Cited by 1,646
Self-citationEmerging regulation and functions of autophagy
Boya, P., Reggiori, F., & Codogno, P. (2013) · Nature Cell Biology · doi:10.1038/ncb2788 · Cited by 1,216
Mitophagy: mechanisms, pathophysiological roles, and analysis
Ding, W.-X., & Yin, X.-M. (2012) · bchm · doi:10.1515/hsz-2012-0119 · Cited by 1,032
Autophagy during viral infection — a double-edged sword
Choi, Y., Bowman, J. W., & Jung, J. U. (2018) · Nature Reviews Microbiology · doi:10.1038/s41579-018-0003-6 · Cited by 838
Pharmacological modulation of autophagy: therapeutic potential and persisting obstacles
Galluzzi, L., Bravo-San Pedro, J. M., Levine, B., Green, D. R., & Kroemer, G. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2017.22 · Cited by 842
Self-citationUbiquitination and selective autophagy
Shaid, S., Brandts, C. H., Serve, H., & Dikic, I. (2013) · Cell Death & Differentiation · doi:10.1038/cdd.2012.72 · Cited by 800
Mitophagy-dependent necroptosis contributes to the pathogenesis of COPD
Mizumura, K., Cloonan, S. M., Nakahira, K., Bhashyam, A. R., Cervo, M., Kitada, T., Glass, K., Owen, C. A., Mahmood, A., Washko, G. R., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci74985 · Cited by 611
Autophagy balances inflammation in innate immunity
Deretic, V., & Levine, B. (2018) · Autophagy · doi:10.1080/15548627.2017.1402992 · Cited by 563
Self-citationAutophagy and cellular immune responses
Ma, Y., Galluzzi, L., Zitvogel, L., & Kroemer, G. (2013) · Immunity · doi:10.1016/j.immuni.2013.07.017 · Cited by 447
Autophagy promotes primary ciliogenesis by removing OFD1 from centriolar satellites
Tang, Z., Lin, M. G., Stowe, T. R., Chen, S., Zhu, M., Stearns, T., Franco, B., & Zhong, Q. (2013) · Nature · doi:10.1038/nature12606 · Cited by 414
Lassen, K. G., Kuballa, P., Conway, K. L., Patel, K. K., Becker, C. E., Peloquin, J. M., Villablanca, E. J., Norman, J. M., Liu, T.-C., Heath, R. J., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1407001111 · Cited by 373
Self-citationAutophagy in Antimicrobial Immunity
Gomes, L. C., & Dikic, I. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.03.009 · Cited by 350
Optical Pooled Screens in Human Cells
Feldman, D., Singh, A., Schmid-Burgk, J. L., Carlson, R. J., Mezger, A., Garrity, A. J., Zhang, F., & Blainey, P. C. (2019) · Cell · doi:10.1016/j.cell.2019.09.016 · Cited by 321
Fanconi Anemia Proteins Function in Mitophagy and Immunity
Sumpter, R., Sirasanagandla, S., Fernández, Á. F., Wei, Y., Dong, X., Franco, L., Zou, Z., Marchal, C., Lee, M. Y., Clapp, D. W., et al. (2016) · Cell · doi:10.1016/j.cell.2016.04.006 · Cited by 250
“In contrast, in Fancc−/− MEFs (similar to virophagy-deficient Pkr−/− and Smurf1−/− MEFs (Orvedahl et al., 2011; Talloczy et al., 2006)), there were fewer HSV-1-containing autophagosomes/autolysosomes and more free nucleocapsids and assembled virions inside in the cytoplasm.”
InfluentialSelf-citationMechanisms of Selective Autophagy in Normal Physiology and Cancer
Mancias, J. D., & Kimmelman, A. C. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.02.027 · Cited by 196
RNF166 determines recruitment of adaptor proteins during antibacterial autophagy
Heath, R. J., Goel, G., Baxt, L. A., Rush, J. S., Mohanan, V., Paulus, G. L. C., Jani, V., Lassen, K. G., & Xavier, R. J. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.11.005 · Cited by 108
“From this core contingent, we focused on RNF166, which has multiple protein-protein interactions in known autophagy networks (Figure 1; Orvedahl et al., 2011; Sorbara and Girardin, 2015).”
BackgroundSelf-citationThe transition zone protein Rpgrip1l regulates proteasomal activity at the primary cilium
Gerhardt, C., Lier, J. M., Burmühl, S., Struchtrup, A., Deutschmann, K., Vetter, M., Leu, T., Reeg, S., Grune, T., & Rüther, U. (2015) · Journal of Cell Biology · doi:10.1083/jcb.201408060 · Cited by 88
Mitochondrial function and mitochondrial DNA maintenance with advancing age
Gaziev, A. I., Abdullaev, S., & Podlutsky, A. (2014) · Biogerontology · doi:10.1007/s10522-014-9515-2 · Cited by 77
Mitophagy is required for brown adipose tissue mitochondrial homeostasis during cold challenge
Lu, Y., Fujioka, H., Joshi, D., Li, Q., Sangwung, P., Hsieh, P., Zhu, J., Torio, J., Sweet, D., Wang, L., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-26394-5 · Cited by 76
Pooled genetic perturbation screens with image-based phenotypes
Feldman, D., Funk, L., Le, A., Carlson, R. J., Leiken, M. D., Tsai, F., Soong, B., Singh, A., & Blainey, P. C. (2022) · Nature Protocols · doi:10.1038/s41596-021-00653-8 · Cited by 59
TMEM39A and Human Diseases: A Brief Review
Tran, Q., Park, J., Lee, H., Hong, Y., Hong, S., Park, S., Park, J., & Kim, S.-H. (2017) · Toxicological Research · doi:10.5487/tr.2017.33.3.205 · Cited by 25
Manipulation of selective macroautophagy by pathogens at a glance
Cong, Y., Dinesh Kumar, N., Mauthe, M., Verlhac, P., & Reggiori, F. (2020) · Journal of Cell Science · doi:10.1242/jcs.240440 · Cited by 23
Metadata
- Authors
- Orvedahl, A., Sumpter, R., Xiao, G., Ng, A., Zou, Z., Tang, Y., Narimatsu, M., Gilpin, C., Sun, Q., Roth, M., Forst, C. V., Wrana, J. L., Zhang, Y. E., Luby-Phelps, K., Xavier, R. J., Xie, Y., & Levine, B.
- Venue
- Nature
- Published
- 2011-12-01
- Volume
- 480
- Issue
- 7375
- Pages
- 113-117
- ISSN
- 0028-0836
- 1476-4687
- PMC
- PMC3229641
- Cited by
- 474
- References
- 9
- Language
- en
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