The DOI matches its Crossref record.
Isolation and characterization of autophagy‐defective mutants of Saccharomyces cerevisiae
Open accessAbstract
Autophagy in the yeast is similar to that in mammalian cells. A mutant designated as apg1 (autophagy) defective in accumulation of autophagic bodies in the vacuoles was isolated by selection using a light microscope from a mutagenized proteinase‐deficient strain. In the apg1 strain, which has normal vacuolar proteinases, nitrogen starvation did not induce protein degradation. The apg1 mutant lost its viability faster than wild‐type cells during nitrogen starvation. By using the loss of viability as a first screening test, 75 other apg mutants were selected. These apg mutants including apg1 fell into 15 complementation groups. Genetic analyses of representative apg mutants revealed that they all had single recessive chromosomal mutations. Strains with each apg mutation were defective in protein degradation in the vacuoles induced by nitrogen starvation and homozygous diploids for each apg mutation did not sporulate. These results on the apg mutants suggest that autophagy via autophagic bodies is indispensable for protein degradation in the vacuoles under starvation conditions, and that at least 15 APG genes are involved in autophagy in yeast.
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.
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
Cited by
LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing.
Kabeya, Y., Mizushima, N., Ueno, T., Yamamoto, A., Kirisako, T., Noda, T., Kominami, E., Ohsumi, Y., & Yoshimori, T. (2000) · The EMBO Journal · doi:10.1093/emboj/19.21.5720 · Cited by 6,605
Self-citationSuppression of basal autophagy in neural cells causes neurodegenerative disease in mice
Hara, T., Nakamura, K., Matsui, M., Yamamoto, A., Nakahara, Y., Suzuki-Migishima, R., Yokoyama, M., Mishima, K., Saito, I., Okano, H., et al. (2006) · Nature · doi:10.1038/nature04724 · Cited by 3,882
Loss of autophagy in the central nervous system causes neurodegeneration in mice
Komatsu, M., Waguri, S., Chiba, T., Murata, S., Iwata, J.-I., Tanida, I., Ueno, T., Koike, M., Uchiyama, Y., Kominami, E., et al. (2006) · Nature · doi:10.1038/nature04723 · Cited by 3,500
Induction of autophagy and inhibition of tumorigenesis by beclin 1
Liang, X. H., Jackson, S., Seaman, M., Brown, K., Kempkes, B., Hibshoosh, H., & Levine, B. (1999) · Nature · doi:10.1038/45257 · Cited by 3,347
The role of autophagy during the early neonatal starvation period
Kuma, A., Hatano, M., Matsui, M., Yamamoto, A., Nakaya, H., Yoshimori, T., Ohsumi, Y., Tokuhisa, T., & Mizushima, N. (2004) · Nature · doi:10.1038/nature03029 · Cited by 2,865
Self-citationMechanism and medical implications of mammalian autophagy
Dikic, I., & Elazar, Z. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0003-4 · Cited by 2,771
Impairment of starvation-induced and constitutive autophagy in Atg7 -deficient mice
Komatsu, M., Waguri, S., Ueno, T., Iwata, J., Murata, S., Tanida, I., Ezaki, J., Mizushima, N., Ohsumi, Y., Uchiyama, Y., et al. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200412022 · Cited by 2,331
Self-citationPromotion of tumorigenesis by heterozygous disruption of the beclin 1 autophagy gene
Qu, X., Yu, J., Bhagat, G., Furuya, N., Hibshoosh, H., Troxel, A., Rosen, J., Eskelinen, E.-L., Mizushima, N., Ohsumi, Y., et al. (2003) · Journal of Clinical Investigation · doi:10.1172/jci20039 · Cited by 2,311
Self-citationHomeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice.
Komatsu, M., Waguri, S., Koike, M., Sou, Y.-S., Ueno, T., Hara, T., Mizushima, N., Iwata, J.-I., Ezaki, J., Murata, S., et al. (2007) · Cell · doi:10.1016/j.cell.2007.10.035 · Cited by 2,124
Mizushima, N., Yamamoto, A., Matsui, M., Yoshimori, T., & Ohsumi, Y. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-09-0704 · Cited by 2,105
Self-citationThe machinery of macroautophagy
Feng, Y., He, D., Yao, Z., & Klionsky, D. J. (2014) · Cell Research · doi:10.1038/cr.2013.168 · Cited by 2,083
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
Autophagy in mammalian development and differentiation
Mizushima, N., & Levine, B. (2010) · Nature Cell Biology · doi:10.1038/ncb0910-823 · Cited by 1,555
Growth factor regulation of autophagy and cell survival in the absence of apoptosis
Lum, J. J., Bauer, D. E., Kong, M., Harris, M. H., Li, C., Lindsten, T., & Thompson, C. B. (2005) · Cell · doi:10.1016/j.cell.2004.11.046 · Cited by 1,487
ULK1·ATG13·FIP200 Complex Mediates mTOR Signaling and Is Essential for Autophagy
Ganley, I. G., Lam, D. H., Wang, J., Ding, X., Chen, S., & Jiang, X. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m900573200 · Cited by 1,447
Dissection of Autophagosome Formation Using Apg5-Deficient Mouse Embryonic Stem Cells
Mizushima, N., Yamamoto, A., Hatano, M., Kobayashi, Y., Kabeya, Y., Suzuki, K., Tokuhisa, T., Ohsumi, Y., & Yoshimori, T. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.152.4.657 · Cited by 1,361
Self-citationAutophagy in healthy aging and disease
Aman, Y., Schmauck-Medina, T., Hansen, M., Morimoto, R. I., Simon, A. K., Bjedov, I., Palikaras, K., Simonsen, A., Johansen, T., Tavernarakis, N., et al. (2021) · Nature Aging · doi:10.1038/s43587-021-00098-4 · Cited by 1,313
Autophagy Genes Are Essential for Dauer Development and Life-Span Extension in C. elegans
Meléndez, A., Tallóczy, Z., Seaman, M., Eskelinen, E.-L., Hall, D. H., & Levine, B. (2003) · Science · doi:10.1126/science.1087782 · Cited by 1,270
Molecular dissection of autophagy: two ubiquitin-like systems
Ohsumi, Y. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35056522 · Cited by 1,240
Self-citationCargo recognition and trafficking in selective autophagy
Stolz, A., Ernst, A., & Dikic, I. (2014) · Nature Cell Biology · doi:10.1038/ncb2979 · Cited by 1,207
Tor-Mediated Induction of Autophagy via an Apg1 Protein Kinase Complex
Kamada, Y., Funakoshi, T., Shintani, T., Nagano, K., Ohsumi, M., & Ohsumi, Y. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.150.6.1507 · Cited by 1,145
Self-citationLysosomal turnover, but not a cellular level, of endogenous LC3 is a marker for autophagy
Tanida, I., Minematsu-Ikeguchi, N., Ueno, T., & Kominami, E. (2005) · Autophagy · doi:10.4161/auto.1.2.1697 · Cited by 1,108
Kihara, A., Noda, T., Ishihara, N., & Ohsumi, Y. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.152.3.519 · Cited by 1,004
Self-citationFormation Process of Autophagosome Is Traced with Apg8/Aut7p in Yeast
Kirisako, T., Baba, M., Ishihara, N., Miyazawa, K., Ohsumi, M., Yoshimori, T., Noda, T., & Ohsumi, Y. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.147.2.435 · Cited by 881
“In addition, autophagy deficient mutants are defective in sporulation in yeast, suggesting that it is necessary for the cell differentiation (Tsukada and Ohsumi, 1993).”
BackgroundInfluentialSelf-citationHSV-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
Compromised autophagy and neurodegenerative diseases
Menzies, F. M., Fleming, A., & Rubinsztein, D. C. (2015) · Nature Reviews Neuroscience · doi:10.1038/nrn3961 · Cited by 851
Starvation and ULK1-dependent cycling of mammalian Atg9 between the TGN and endosomes
Young, A. R. J., Chan, E. Y. W., Hu, X. W., Köchl, R., Crawshaw, S. G., High, S., Hailey, D. W., Lippincott-Schwartz, J., & Tooze, S. A. (2006) · Journal of Cell Science · doi:10.1242/jcs.03172 · Cited by 815
Beclin–phosphatidylinositol 3‐kinase complex functions at the trans‐Golgi network
Kihara, A., Kabeya, Y., Ohsumi, Y., & Yoshimori, T. (2001) · The EMBO Reports · doi:10.1093/embo-reports/kve061 · Cited by 813
Self-citationMizushima, N., Kuma, A., Kobayashi, Y., Yamamoto, A., Matsubae, M., Takao, T., Natsume, T., Ohsumi, Y., & Yoshimori, T. (2003) · Journal of Cell Science · doi:10.1242/jcs.00381 · Cited by 791
Self-citationAutophagy-dependent cell death
Denton, D., & Kumar, S. (2019) · Cell Death & Differentiation · doi:10.1038/s41418-018-0252-y · Cited by 777
Atg8 Controls Phagophore Expansion during Autophagosome Formation
Xie, Z., Nair, U., & Klionsky, D. J. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-12-1292 · Cited by 753
A brief history of autophagy from cell biology to physiology and disease
Mizushima, N. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0092-5 · Cited by 696
Small Molecule Inhibition of the Autophagy Kinase ULK1 and Identification of ULK1 Substrates
Egan, D. F., Chun, M. G. H., Vamos, M., Zou, H., Rong, J., Miller, C. J., Lou, H. J., Raveendra-Panickar, D., Yang, C.-C., Sheffler, D. J., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.05.031 · Cited by 715
Methods for Monitoring Autophagy from Yeast to Human
Klionsky, D. J., Cuervo, A. M., & Seglen, P. O. (2007) · Autophagy · doi:10.4161/auto.3678 · Cited by 656
A critical role for the autophagy gene Atg5 in T cell survival and proliferation
Pua, H. H., Dzhagalov, I., Chuck, M., Mizushima, N., & He, Y.-W. (2007) · The Journal of Experimental Medicine · doi:10.1084/jem.20061303 · Cited by 622
“Atg5 was fi rst identifi ed in a screen for yeast incapable of surviving nitrogen starvation (2).”
Receptor-mediated selective autophagy degrades the endoplasmic reticulum and the nucleus
Mochida, K., Oikawa, Y., Kimura, Y., Kirisako, H., Hirano, H., Ohsumi, Y., & Nakatogawa, H. (2015) · Nature · doi:10.1038/nature14506 · Cited by 611
Self-citationYoshimoto, K., Hanaoka, H., Sato, S., Kato, T., Tabata, S., Noda, T., & Ohsumi, Y. (2004) · The Plant Cell · doi:10.1105/tpc.104.025395 · Cited by 603
Self-citationGrowth Arrest and Autophagy Are Required for Salivary Gland Cell Degradation in Drosophila
Berry, D. L., & Baehrecke, E. H. (2007) · Cell · doi:10.1016/j.cell.2007.10.048 · Cited by 602
Guo, J. Y., Karsli-Uzunbas, G., Mathew, R., Aisner, S. C., Kamphorst, J. J., Strohecker, A. M., Chen, G., Price, S., Lu, W., Teng, X., et al. (2013) · Genes & Development · doi:10.1101/gad.219642.113 · Cited by 589
Kuma, A., Matsui, M., & Mizushima, N. (2007) · Autophagy · doi:10.4161/auto.4012 · Cited by 555
Autophagy and aging: keeping that old broom working
Cuervo, A. M. (2008) · Trends in Genetics · doi:10.1016/j.tig.2008.10.002 · Cited by 527
A novel assay to study autophagy: regulation of autophagosome vacuole size by amino acid deprivation
Munafó, D. B., & Colombo, M. I. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.20.3619 · Cited by 516
Autophagy in the liver: functions in health and disease
Ueno, T., & Komatsu, M. (2017) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/nrgastro.2016.185 · Cited by 500
Lipophagy: Connecting Autophagy and Lipid Metabolism
Singh, R., & Cuervo, A. M. (2012) · International Journal of Cell Biology · doi:10.1155/2012/282041 · Cited by 497
The Association of AMPK with ULK1 Regulates Autophagy
Lee, J. W., Park, S., Takahashi, Y., & Wang, H.-G. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015394 · Cited by 482
Biogenesis and Cargo Selectivity of Autophagosomes
Weidberg, H., Shvets, E., & Elazar, Z. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-052709-094552 · Cited by 466
Autophagy Sustains Mitochondrial Glutamine Metabolism and Growth of Braf V600E–Driven Lung Tumors
Strohecker, A. M., Guo, J. Y., Karsli-Uzunbas, G., Price, S. M., Chen, G. J., Mathew, R., McMahon, M., & White, E. (2013) · Cancer Discovery · doi:10.1158/2159-8290.cd-13-0397 · Cited by 435
siRNA Screening of the Kinome Identifies ULK1 as a Multidomain Modulator of Autophagy
Chan, E. Y. W., Kir, S., & Tooze, S. A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703663200 · Cited by 422
Regulation of autophagy by the Rab GTPase network
Ao, X., Zou, L., & Wu, Y. (2014) · Cell Death & Differentiation · doi:10.1038/cdd.2013.187 · Cited by 411
Chan, E. Y. W., Longatti, A., McKnight, N. C., & Tooze, S. A. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01082-08 · Cited by 411
NF-κB Activation Represses Tumor Necrosis Factor-α-induced Autophagy
Djavaheri-Mergny, M., Amelotti, M., Mathieu, J., Besançon, F., Bauvy, C., Souquère, S., Pierron, G., & Codogno, P. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602097200 · Cited by 407
Diverse Cellular Roles of Autophagy
Morishita, H., & Mizushima, N. (2019) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100818-125300 · Cited by 376
Autophagosome Biogenesis in Primary Neurons Follows an Ordered and Spatially Regulated Pathway
Maday, S., & Holzbaur, E. L. F. (2014) · Developmental Cell · doi:10.1016/j.devcel.2014.06.001 · Cited by 372
Autophagy and Alzheimer’s Disease: From Molecular Mechanisms to Therapeutic Implications
Uddin, M. S., Stachowiak, A., Mamun, A. A., Tzvetkov, N. T., Takeda, S., Atanasov, A. G., Bergantin, L. B., Abdel-Daim, M. M., & Stankiewicz, A. M. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00004 · Cited by 395
GSK3-TIP60-ULK1 Signaling Pathway Links Growth Factor Deprivation to Autophagy
Lin, S.-Y., Li, T. Y., Liu, Q., Zhang, C., Li, X., Chen, Y., Zhang, S.-M., Lian, G., Liu, Q., Ruan, K., et al. (2012) · Science · doi:10.1126/science.1217032 · Cited by 365
Targeting autophagy in obesity: from pathophysiology to management
Zhang, Y., Sowers, J. R., & Ren, J. (2018) · Nature Reviews Endocrinology · doi:10.1038/s41574-018-0009-1 · Cited by 338
Yang, Z., Fujii, H., Mohan, S. V., Goronzy, J. J., & Weyand, C. M. (2013) · Journal of Experimental Medicine · doi:10.1084/jem.20130252 · Cited by 334
Lőrincz, P., & Juhász, G. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.10.028 · Cited by 328
Compartment-Specific Regulation of Autophagy in Primary Neurons
Maday, S., & Holzbaur, E. L. F. (2016) · The Journal of Neuroscience · doi:10.1523/jneurosci.4401-15.2016 · Cited by 309
Atg17 Functions in Cooperation with Atg1 and Atg13 in Yeast Autophagy
Kabeya, Y., Kamada, Y., Baba, M., Takikawa, H., Sasaki, M., & Ohsumi, Y. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-08-0669 · Cited by 304
Self-citationDual roles of autophagy in the survival of Caenorhabditis elegans during starvation
Kang, C., You, Y.-J., & Avery, L. (2007) · Genes & Development · doi:10.1101/gad.1573107 · Cited by 294
Two Distinct Pathways for Targeting Proteins from the Cytoplasm to the Vacuole/Lysosome
Baba, M., Osumi, M., Scott, S. V., Klionsky, D. J., & Ohsumi, Y. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.139.7.1687 · Cited by 292
Self-citationFass, E., Shvets, E., Degani, I., Hirschberg, K., & Elazar, Z. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607031200 · Cited by 286
Kim, J., Huang, W.-P., Stromhaug, P. E., & Klionsky, D. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109134200 · Cited by 272
Apg10p, a novel protein‐conjugating enzyme essential for autophagy in yeast
Shintani, T., Mizushima, N., Ogawa, Y., Matsuura, A., Noda, T., & Ohsumi, Y. (1999) · The EMBO Journal · doi:10.1093/emboj/18.19.5234 · Cited by 269
Self-citationMitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging
Leduc-Gaudet, J.-P., Hussain, S. N. A., Barreiro, E., & Gouspillou, G. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22158179 · Cited by 268
“These steps require energy and involve more than 30 autophagy-related (ATG) proteins in yeast, and many of these proteins are highly conserved in mammals [76,77].”
BackgroundRedundancy of human ATG4 protease isoforms in autophagy and LC3/GABARAP processing revealed in cells
Agrotis, A., Pengo, N., Burden, J. J., & Ketteler, R. (2019) · Autophagy · doi:10.1080/15548627.2019.1569925 · Cited by 255
Autophagy in Spinal Cord Motor Neurons in Sporadic Amyotrophic Lateral Sclerosis
Sasaki, S. (2011) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3182160690 · Cited by 249
Huang, W.-P., Scott, S. V., Kim, J., & Klionsky, D. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.8.5845 · Cited by 241
Kuma, A., & Mizushima, N. (2010) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2010.03.002 · Cited by 237
The serine/threonine kinase ULK1 is a target of multiple phosphorylation events
Bach, M., Larance, M., James, D. E., & Ramm, G. (2011) · Biochemical Journal · doi:10.1042/bj20101894 · Cited by 233
Scott, S. V., Nice, D. C., Nau, J. J., Weisman, L. S., Kamada, Y., Keizer-Gunnink, I., Funakoshi, T., Veenhuis, M., Ohsumi, Y., & Klionsky, D. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002813200 · Cited by 227
Self-citationOtto, G. P., Wu, M. Y., Kazgan, N., Anderson, O. R., & Kessin, R. H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212467200 · Cited by 221
Mechanisms of selective autophagy and mitophagy: Implications for neurodegenerative diseases
Chu, C. T. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.07.015 · Cited by 218
Genome-Wide Analyses of Steroid- and Radiation-Triggered Programmed Cell Death in Drosophila
Lee, C.-Y., Clough, E. A., Yellon, P., Teslovich, T. M., Stephan, D. A., & Baehrecke, E. H. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00085-x · Cited by 215
mTORC1 phosphorylates the ULK1-mAtg13-FIP200 autophagy regulatory complex
Chan, E. Y. (2009) · Science Signaling · doi:10.1126/scisignal.284pe51 · Cited by 214
Guan, J., Stromhaug, P. E., George, M. D., Habibzadegah-Tari, P., Bevan, A., Dunn, W. A., & Klionsky, D. J. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.12.3821 · Cited by 204
Qadir, M. A., Kwok, B., Dragowska, W. H., To, K. H., Le, D., Bally, M. B., & Gorski, S. M. (2008) · Breast Cancer Research and Treatment · doi:10.1007/s10549-007-9873-4 · Cited by 201
Hosokawa, N., Hara, Y., & Mizushima, N. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.04.008 · Cited by 194
Inoue, Y., Suzuki, T., Hattori, M., Yoshimoto, K., Ohsumi, Y., & Moriyasu, Y. (2006) · Plant and Cell Physiology · doi:10.1093/pcp/pcl031 · Cited by 189
Self-citationUba1 functions in Atg7- and Atg3-independent autophagy
Chang, T.-K., Shravage, B. V., Hayes, S. D., Powers, C. M., Simin, R. T., Wade Harper, J., & Baehrecke, E. H. (2013) · Nature Cell Biology · doi:10.1038/ncb2804 · Cited by 187
Atg17 Regulates the Magnitude of the Autophagic Response
Cheong, H., Yorimitsu, T., Reggiori, F., Legakis, J. E., Wang, C.-W., & Klionsky, D. J. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-10-0894 · Cited by 187
The requirement of uncoordinated 51-like kinase 1 (ULK1) and ULK2 in the regulation of autophagy
Lee, E.-J., & Tournier, C. (2011) · Autophagy · doi:10.4161/auto.7.7.15450 · Cited by 186
Lysosome: The metabolic signaling hub
Lamming, D. W., & Bar‐Peled, L. (2019) · Traffic · doi:10.1111/tra.12617 · Cited by 173
Rocchi, A., Yamamoto, S., Ting, T., Fan, Y., Sadleir, K., Wang, Y., Zhang, W., Huang, S., Levine, B., Vassar, R., et al. (2017) · PLOS Genetics · doi:10.1371/journal.pgen.1006962 · Cited by 166
Sugawara, K., Suzuki, N. N., Fujioka, Y., Mizushima, N., Ohsumi, Y., & Inagaki, F. (2004) · Genes to Cells · doi:10.1111/j.1356-9597.2004.00750.x · Cited by 158
Self-citationReggiori, F., Monastyrska, I., Shintani, T., & Klionsky, D. J. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-07-0629 · Cited by 155
Structure of the Human Autophagy Initiating Kinase ULK1 in Complex with Potent Inhibitors
Lazarus, M. B., Novotny, C. J., & Shokat, K. M. (2015) · ACS Chemical Biology · doi:10.1021/cb500835z · Cited by 154
Analysis of the Membrane Structures Involved in Autophagy in Yeast by Freeze-Replica Method.
Baba, M., Osumi, M., & Ohsumi, Y. (1995) · Cell Structure and Function · doi:10.1247/csf.20.465 · Cited by 151
Self-citationAutophagy in animal development
Allen, E. A., & Baehrecke, E. H. (2020) · Cell Death & Differentiation · doi:10.1038/s41418-020-0497-0 · Cited by 127
Autophagy in the eye: implications for ocular cell health.
Frost, L. S., Mitchell, C. H., & Boesze-Battaglia, K. (2014) · Experimental Eye Research · doi:10.1016/j.exer.2014.04.010 · Cited by 134
Abeliovich, H., Darsow, T., & Emr, S. D. (1999) · The EMBO Journal · doi:10.1093/emboj/18.21.6005 · Cited by 126
Fengsrud, M., Erichsen, E. S., Berg, T. O., Raiborg, C., & Seglen, P. O. (2000) · European Journal of Cell Biology · doi:10.1078/0171-9335-00125 · Cited by 123
Autophagy and the cytoplasm to vacuole targeting pathway both require Aut10p
Barth, H., Meiling-Wesse, K., Epple, U. D., & Thumm, M. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)03016-2 · Cited by 123
Atg38 is required for autophagy-specific phosphatidylinositol 3-kinase complex integrity
Araki, Y., Ku, W.-C., Akioka, M., May, A. I., Hayashi, Y., Arisaka, F., Ishihama, Y., & Ohsumi, Y. (2013) · Journal of Cell Biology · doi:10.1083/jcb.201304123 · Cited by 119
Self-citationPhysical Exercise: A Novel Tool to Protect Mitochondrial Health
Sorriento, D., Di Vaia, E., & Iaccarino, G. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.660068 · Cited by 118
A conserved mechanism of TOR-dependent RCK-mediated mRNA degradation regulates autophagy
Hu, G., McQuiston, T., Bernard, A., Park, Y.-D., Qiu, J., Vural, A., Zhang, N., Waterman, S. R., Blewett, N. H., Myers, T. G., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3189 · Cited by 116
How and why to study autophagy in Drosophila: It’s more than just a garbage chute
Nagy, P., Varga, Á., Kovács, A. L., Takáts, S., & Juhász, G. (2015) · Methods · doi:10.1016/j.ymeth.2014.11.016 · Cited by 115
Chaperone‐mediated autophagy: Molecular mechanisms, biological functions, and diseases
Yao, R., & Shen, J. (2023) · MedComm · doi:10.1002/mco2.347 · Cited by 111
Membrane scission driven by the PROPPIN Atg18
Gopaldass, N., Fauvet, B., Lashuel, H., Roux, A., & Mayer, A. (2017) · The EMBO Journal · doi:10.15252/embj.201796859 · Cited by 104
Metadata
- Authors
- Tsukada, M., & Ohsumi, Y.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1993-10-25
- Volume
- 333
- Issue
- 1-2
- Pages
- 169-174
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2011580247
- Cited by
- 1,772
- References
- 0
- FWCI
- 4.41
- Type
- journal article
- Language
- en
- Open access
- bronze
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
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
