The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.
LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing.
Open accessAbstract
Little is known about the protein constituents of autophagosome membranes in mammalian cells. Here we demonstrate that the rat microtubule-associated protein 1 light chain 3 (LC3), a homologue of Apg8p essential for autophagy in yeast, is associated to the autophagosome membranes after processing. Two forms of LC3, called LC3-I and -II, were produced post-translationally in various cells. LC3-I is cytosolic, whereas LC3-II is membrane bound. The autophagic vacuole fraction prepared from starved rat liver was enriched with LC3-II. Immunoelectron microscopy on LC3 revealed specific labelling of autophagosome membranes in addition to the cytoplasmic labelling. LC3-II was present both inside and outside of autophagosomes. Mutational analyses suggest that LC3-I is formed by the removal of the C-terminal 22 amino acids from newly synthesized LC3, followed by the conversion of a fraction of LC3-I into LC3-II. The amount of LC3-II is correlated with the extent of autophagosome formation. LC3-II is the first mammalian protein identified that specifically associates with autophagosome membranes.
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
“As LC3II is a lipidated form of LC3 (Kabeya et al., 2000), these results indicated an increase in autophagosome formation.”
From Inducible Rpt3, a Proteasome Component, Knockout in Adult Skeletal Muscle Results in Muscle Atrophy (2020) · cites this paper as Kabeya et al., 2000
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
“The cytosolic form of LC3 (designated LC3-I) is conjugated to phosphatidylethanolamine (PE) and in this form (designated LC3-II) it is recruited to the growing autophagosome membrane [26].”
From LC3-Associated Phagocytosis (LAP): Connections with Host Autophagy (2012) · cites this paper as [26]
Experimental — accuracy not yet measuredThe check wasn’t confident either way, so it gives no verdict — never disputed.
In the citing paper
“Another alternative to mRFP or mCherry is to use the Venus variant of YFP, which is brighter than mRFP and less sensitive to pH than GFP.186”
From Guidelines for the use and interpretation of assays for monitoring autophagy (2012) · cites this paper as [186]
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.
Citations
Cites
Smith, D. B., & Johnson, K. S. (1988) · Gene · doi:10.1016/0378-1119(88)90005-4 · Cited by 5,844
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
Isolation and characterization of autophagy‐defective mutants of Saccharomyces cerevisiae
Tsukada, M., & Ohsumi, Y. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80398-e · Cited by 1,837
Self-citationA protein conjugation system essential for autophagy
Mizushima, N., Noda, T., Yoshimori, T., Tanaka, Y., Ishii, T., George, M. D., Klionsky, D. J., Ohsumi, M., & Ohsumi, Y. (1998) · Nature · doi:10.1038/26506 · Cited by 1,758
Self-citationYamamoto, A., Tagawa, Y., Yoshimori, T., Moriyama, Y., Masaki, R., & Tashiro, Y. (1998) · Cell Structure and Function · doi:10.1247/csf.23.33 · Cited by 1,312
Self-citationKirisako, T., Ichimura, Y., Okada, H., Kabeya, Y., Mizushima, N., Yoshimori, T., Ohsumi, M., Takao, T., Noda, T., & Ohsumi, Y. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.2.263 · Cited by 1,024
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
Self-citationGABAA-receptor-associated protein links GABAA receptors and the cytoskeleton
Wang, H.-B., Bedford, F., Brandon, N., Moss, S., & Olsen, R. (1999) · Nature · doi:10.1038/16264 · Cited by 754
Autophagy and related mechanisms of lysosome-mediated protein degradation
Dunn, W. A. (1994) · Trends in Cell Biology · doi:10.1016/0962-8924(94)90069-8 · Cited by 534
A New Protein Conjugation System in Human
Mizushima, N., Sugita, H., Yoshimori, T., & Ohsumi, Y. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.51.33889 · Cited by 521
Self-citation
Cited by
Sorted by citations
Items 701–800 of 1,091
The Parkinson’s disease-associated genes ATP13A2 and SYT11 regulate autophagy via a common pathway
Bento, C. F., Ashkenazi, A., Jiménez-Sánchez, M., & Rubinsztein, D. C. (2016) · Nature Communications · doi:10.1038/ncomms11803 · Cited by 196
Autophagy in Yeast: A Review of the Molecular Machinery.
Huang, W., & Klionsky, D. J. (2002) · Cell Structure and Function · doi:10.1247/csf.27.409 · Cited by 194
Mitophagy Selectively Degrades Individual Damaged Mitochondria After Photoirradiation
Kim, I., & Lemasters, J. J. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3768 · Cited by 198
Autophagy inhibition promotes paclitaxel-induced apoptosis in cancer cells
Xi, G., Hu, X., Wu, B., Jiang, H., Young, C. Y. F., Pang, Y., & Yuan, H. (2011) · Cancer Letters · doi:10.1016/j.canlet.2011.03.026 · Cited by 192
Autophagy and p62 in Cardiac Proteinopathy
Zheng, Q., Su, H., Ranek, M. J., & Wang, X. (2011) · Circulation Research · doi:10.1161/circresaha.111.244707 · Cited by 188
Peng, H., Yang, J., Li, G., You, Q., Han, W., Li, T., Gao, D., Xie, X., Lee, B., Du, J., et al. (2017) · Cell Research · doi:10.1038/cr.2017.40 · Cited by 195
Role and regulation of autophagy in cancer
Rakesh, R., Dharshini, L. C. P., Sakthivel, K. M., & Rasmi, R. R. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2022.166400 · Cited by 198
Tubastatin A/ACY-1215 Improves Cognition in Alzheimer's Disease Transgenic Mice
Zhang, L., Liu, C., Wu, J., Tao, J.-J., Sui, X., Yao, Z., Xu, Y., Huang, L., Zhu, H., Sheng, S., et al. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-140066 · Cited by 193
eIF4GI links nutrient sensing by mTOR to cell proliferation and inhibition of autophagy
Ramírez‐Valle, F., Braunstein, S. E., Zavadil, J., Formenti, S. C., & Schneider, R. J. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200710215 · Cited by 198
LC3, an autophagosome marker, is highly expressed in gastrointestinal cancers
Yoshioka (1992) · International Journal of Oncology · doi:10.3892/ijo_00000028 · Cited by 192
Methods for Assessing Autophagy and Autophagic Cell Death
Tasdemir, E., Galluzzi, L., Maiuri, M. C., Criollo, A., Vitale, I., Hangen, E., Modjtahedi, N., & Kroemer, G. (2008) · Methods in molecular biology · doi:10.1007/978-1-59745-157-4_3 · Cited by 200
Sulzer, D., Mosharov, E. V., Tallóczy, Z., Zucca, F. A., Simon, J. D., & Zecca, L. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05385.x · Cited by 195
Autophagy is essential for mouse sense of balance
Mariño, G., Fernández, Á. F., Cabrera, S., Lundberg, Y. W., Cabanillas, R., Rodríguez, F. J., Salvador-Montoliu, N., Vega, J. A., Germanà, A., Fueyo, A., et al. (2010) · Journal of Clinical Investigation · doi:10.1172/jci42601 · Cited by 196
Suh, Y., Afaq, F., Khan, N., Johnson, J. J., Khusro, F. H., & Mukhtar, H. (2010) · Carcinogenesis · doi:10.1093/carcin/bgq115 · Cited by 196
Ruan, S., Xie, R., Qin, L., Yu, M., Xiao, W., Hu, C., Yu, W., Qian, Z., Ouyang, L., He, Q., et al. (2019) · Nano Letters · doi:10.1021/acs.nanolett.9b03968 · Cited by 192
STING orchestrates the neuronal inflammatory stress response in multiple sclerosis
Woo, M. S., Mayer, C., Binkle-Ladisch, L., Sonner, J. K., Rosenkranz, S. C., Shaposhnykov, A., Rothammer, N., Tsvilovskyy, V., Lorenz, S., Raich, L., et al. (2024) · Cell · doi:10.1016/j.cell.2024.05.031 · Cited by 197
Autophagy-regulating protease Atg4: structure, function, regulation and inhibition
Maruyama, T., & Noda, N. N. (2018) · The Journal of Antibiotics · doi:10.1038/ja.2017.104 · Cited by 190
WASH inhibits autophagy through suppression of Beclin 1 ubiquitination
Xia, P., Wang, S., Du, Y., Zhao, Z., Shi, L., Sun, L., Huang, G., Ye, B., Li, C., Dai, Z., et al. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.189 · Cited by 194
Ku, B., Woo, J., Liang, C., Lee, K.-H., Hong, H.-S., Xiaofei, E., Kim, K.-S., Jung, J. U., & Oh, B. (2008) · PLoS Pathogens · doi:10.1371/journal.ppat.0040025 · Cited by 194
Mutant LRRK2 Elicits Calcium Imbalance and Depletion of Dendritic Mitochondria in Neurons
Cherra, S. J., Steer, E. K., Gusdon, A. M., Kiselyov, K. I., & Chu, C. T. (2012) · American Journal Of Pathology · doi:10.1016/j.ajpath.2012.10.027 · Cited by 190
Liu, H., Javaheri, A., Godar, R. J., Murphy, J., Ma, X., Rohatgi, N., Mahadevan, J., Hyrc, K. L., Säftig, P., Marshall, C. A., et al. (2017) · Autophagy · doi:10.1080/15548627.2017.1368596 · Cited by 194
Glucocorticoid induced autophagy in osteocytes
Xia, X., Kar, R., Gluhak-Heinrich, J., Yao, W., Lane, N. E., Bonewald, L. F., Biswas, S. K., Lo, W.-K., & Jiang, J. X. (2010) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.160 · Cited by 193
Starvation‐induced expression of autophagy‐related genes in Arabidopsis
Rose, T. L., Bonneau, L., Der, C., Marty‐Mazars, D., & Marty, F. (2005) · Biology of the Cell · doi:10.1042/bc20040516 · Cited by 189
Lin, X. Z., Parisiadou, L., Sgobio, C., Liu, G., Yu, J. H., Sun, L., Shim, H., Gu, X., Luo, J., Long, C., et al. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.1731-12.2012 · Cited by 192
Tumorigenesis in tuberous sclerosis complex is autophagy and p62/sequestosome 1 (SQSTM1)-dependent
Parkhitko, A. A., Myachina, F., Morrison, T. A., Hindi, K. M., Auricchio, N., Karbowniczek, M., Wu, J. J., Finkel, T., Kwiatkowski, D. J., Yu, J. J., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1104361108 · Cited by 193
Samaddar, J. S., Gaddy, V. T., Duplantier, J., Thandavan, S. P., Shah, M. A., Smith, M. J., Browning, D. D., Rawson, J., Smith, S. B., Barrett, J. T., et al. (2008) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-08-0447 · Cited by 190
Association Between Autophagy and Neurodegenerative Diseases
Fujikake, N., Shin, M., & Shimizu, S. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00255 · Cited by 197
Inhibition of autophagy, lysosome and VCP function impairs stress granule assembly
Seguin, S. J., Morelli, F. F., Vinet, J., Amore, D., Biasi, S. D., Poletti, A., Rubinsztein, D. C., & Carra, S. (2014) · Cell Death and Differentiation · doi:10.1038/cdd.2014.103 · Cited by 196
Gorbea, C. M., Makar, K. A., Pauschinger, M., Pratt, G. W., Bersola, J., Varela, J. J., David, R. M., Banks, L. D., Huang, C., Li, H., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.047464 · Cited by 192
Curcumin promotes differentiation of glioma‐initiating cells by inducing autophagy
Zhuang, W., Long, L., Zheng, B., Ji, W., Yang, N., Zhang, Q., & Liang, Z. (2011) · Cancer Science · doi:10.1111/j.1349-7006.2011.02198.x · Cited by 188
Li, H., Gao, A., Feng, D., Wang, Y., Zhang, L., Cui, Y., Лі, Б., Wang, Z., & Chen, G. (2014) · Translational Stroke Research · doi:10.1007/s12975-014-0354-x · Cited by 187
Russo, R., Berliocchi, L., Adornetto, A., Varano, G. P., Cavaliere, F., Nucci, C., Rotiroti, D., Morrone, L. A., Bagetta, G., & Corasaniti, M. T. (2011) · Cell Death and Disease · doi:10.1038/cddis.2011.29 · Cited by 186
Asanuma, K., Tanida, I., Shirato, I., Ueno, T., Takahara, H., Nishitani, T., Kominami, E., & Tomino, Y. (2003) · The FASEB Journal · doi:10.1096/fj.02-0580fje · Cited by 186
Self-citationA comprehensive glossary of autophagy-related molecules and processes
Klionsky, D. J., Codogno, P., Cuervo, A. M., Deretic, V. P., Elazar, Z., Fueyo-Margareto, J., Gewirtz, D. A., Kroemer, G., Levine, B., Mizushima, N., et al. (2010) · Autophagy · doi:10.4161/auto.6.4.12244 · Cited by 185
Self-citationCopper Oxide Nanoparticles Induce Autophagic Cell Death in A549 Cells
Sun, T., Yan, Y., Zhao, Y., Guo, F., & Jiang, C. (2012) · PLoS ONE · doi:10.1371/journal.pone.0043442 · Cited by 189
The Pan-Bcl-2 Inhibitor (−)-Gossypol Triggers Autophagic Cell Death in Malignant Glioma
Voss, V., Senft, C., Lang, V., Ronellenfitsch, M. W., Steinbach, J. P., Seifert, V., & Kögel, D. (2010) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-09-0562 · Cited by 189
Jung, S., Choe, S., Woo, H., Jeong, H., An, H.-K., Moon, H., Ryu, H. Y., Yeo, B. K., Lee, Y. W., Choi, H., et al. (2020) · Autophagy · doi:10.1080/15548627.2019.1630222 · Cited by 183
Liu, H., Zhang, Y., Yang, N., Yx, Z., Liu, X. J., Cg, L., Zhao, Y., Wang, Y.-G., Zhang, G.-G., Yang, P., et al. (2011) · Cell Death and Disease · doi:10.1038/cddis.2011.27 · Cited by 188
Negative Regulation of Vps34 by Cdk Mediated Phosphorylation
Furuya, T., Kim, M., Lipinski, M. M., Li, J., Kim, D., Lu, T., Shen, Y., Rameh, L. E., Yankner, B. A., Tsai, L., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.05.009 · Cited by 191
Inflammasome-Independent Modulation of Cytokine Response by Autophagy in Human Cells
Crișan, T. O., Plantinga, T. S., van de Veerdonk, F. L., Farcas, M. F., Stoffels, M., Kullberg, B. J., van der Meer, J. W. M., Joosten, L. A. B., & Netea, M. G. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018666 · Cited by 193
Fan, X., Wang, J., Hou, J., Lin, C.-R., Bensoussan, A., Chang, D., Liu, J., & Wang, B. (2015) · Journal of Translational Medicine · doi:10.1186/s12967-015-0450-z · Cited by 185
Bacterial interactions with the autophagic pathway
Dorn, B. R., Dunn, W. A., & Progulske‐Fox, A. (2002) · Cellular Microbiology · doi:10.1046/j.1462-5822.2002.00164.x · Cited by 184
The interplay between autophagy and ROS in tumorigenesis
Kongara, S., & Karantza, V. (2012) · Frontiers in Oncology · doi:10.3389/fonc.2012.00171 · Cited by 186
Hepatitis B virus X protein inhibits autophagic degradation by impairing lysosomal maturation
Liu, B., Fang, M., Hu, Y., Huang, B., Li, N., Chang, C., Huang, R., Xu, X., Yang, Z., Chen, Z., et al. (2013) · Autophagy · doi:10.4161/auto.27286 · Cited by 189
Laforin, the most common protein mutated in Lafora disease, regulates autophagy
Aguado, C., Sarkar, S., Korolchuk, V. I., Criado‐García, O., Vernia, S., Boya, P., Sanz, P., de Córdoba, S. R., Knecht, E., & Rubinsztein, D. C. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq190 · Cited by 188
Corcelle–Termeau, E., Nebout, M., Bekri, S., Gauthier, N. C., Hofman, P. M., Poujeol, P., Fénichel, P., & Mograbi, B. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-3557 · Cited by 185
Yanai, H., Matsuda, A., An, J., Koshiba, R., Nishio, J., Negishi, H., Ikushima, H., Onoe, T., Ohdan, H., Yoshida, N., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1320808110 · Cited by 184
Heiseke, A., Aguib, Y., Riemer, C., Baier, M., & Schätzl, H. M. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.05906.x · Cited by 189
Autophagy in Yeast: Mechanistic Insights and Physiological Function
Abeliovich, H., & Klionsky, D. J. (2001) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.65.3.463-479.2001 · Cited by 183
Deletion of the Huntingtin Polyglutamine Stretch Enhances Neuronal Autophagy and Longevity in Mice
Zheng, S., Clabough, E. B. D., Sarkar, S., Futter, M., Rubinsztein, D. C., & Zeitlin, S. O. (2010) · PLoS Genetics · doi:10.1371/journal.pgen.1000838 · Cited by 192
The role of autophagy in follicular development and atresia in rat granulosa cells
Choi, J. Y., Jo, M., Lee, E. Y., Yoon, B.-K., & Choi, D. S. (2010) · Fertility and Sterility · doi:10.1016/j.fertnstert.2009.11.021 · Cited by 183
Chen, J., Wang, L., Wu, C., Hu, Q., Gu, C., Yan, F., Li, J., Yan, W. X., & Chen, G. (2013) · Journal of Pineal Research · doi:10.1111/jpi.12086 · Cited by 183
Mammalian macroautophagy at a glance
Ravikumar, B., Futter, M., Jahreiss, L., Korolchuk, V. I., Lichtenberg, M., Luo, S., Massey, D. C. O., Menzies, F. M., Narayanan, U., Renna, M., et al. (2009) · Journal of Cell Science · doi:10.1242/jcs.031773 · Cited by 196
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
Aurora kinase A inhibition-induced autophagy triggers drug resistance in breast cancer cells
Zou, Z., Yuan, Z., Zhang, Q., Long, Z., Chen, J., Tang, Z., Zhu, Y., Chen, S., Xu, J., Yan, M., et al. (2012) · Autophagy · doi:10.4161/auto.22110 · Cited by 184
Induction of Autophagy Causes Dramatic Changes in the Subcellular Distribution of GFP‐Rab24
Munafó, D. B., & Colombo, M. I. (2002) · Traffic · doi:10.1034/j.1600-0854.2002.30704.x · Cited by 182
Autophagy–physiology and pathophysiology
Uchiyama, Y., Shibata, M., Koike, M., Yoshimura, K., & Sasaki, M. (2008) · Histochemistry and Cell Biology · doi:10.1007/s00418-008-0406-y · Cited by 188
Current knowledge of the pre‐autophagosomal structure (PAS)
Suzuki, K., & Ohsumi, Y. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.02.001 · Cited by 184
Self-citationKoukourakis, M. I., Kalamida, D., Giatromanolaki, A., Zois, C. E., Sivridis, E., Pouliliou, S., Mitrakas, A., Gatter, K. C., & Harris, A. L. (2015) · PLoS ONE · doi:10.1371/journal.pone.0137675 · Cited by 183
Assaying autophagic activity in transgenic GFP-Lc3 and GFP-Gabarap zebrafish embryos
He, C., Bartholomew, C. R., Zhou, W., & Klionsky, D. J. (2009) · Autophagy · doi:10.4161/auto.5.4.7768 · Cited by 186
Filippi‐Chiela, E. C., Villodre, E. S., Zamin, L. L., & Lenz, G. (2011) · PLoS ONE · doi:10.1371/journal.pone.0020849 · Cited by 181
Wei, K., Wang, P., & Miao, C. (2012) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.12005 · Cited by 183
Unsaturated lipid peroxidation-derived aldehydes activate autophagy in vascular smooth-muscle cells
Hill, B. G., Haberzettl, P., Ahmed, Y., Srivastava, S., & Bhatnagar, A. (2008) · Biochemical Journal · doi:10.1042/bj20071063 · Cited by 187
Autophagy protects neuron from Aβ-induced cytotoxicity
Hung, S., Huang, W., Liou, H., & Fu, W. (2009) · Autophagy · doi:10.4161/auto.5.4.8096 · Cited by 183
Pathological apoptosis in the developing brain
Blomgren, K., Leist, M., & Groc, L. (2007) · APOPTOSIS · doi:10.1007/s10495-007-0754-4 · Cited by 183
Stern, S. T., Zolnik, B. S., McLeland, C. B., Clogston, J. D., Zheng, J., & McNeil, S. E. (2008) · Toxicological Sciences · doi:10.1093/toxsci/kfn137 · Cited by 184
Gao, W., Shen, Z., Shang, L., & Wang, X. (2011) · Cell Death & Differentiation · doi:10.1038/cdd.2011.33 · Cited by 178
Li, X., & Fan, Z. (2010) · Cancer Research · doi:10.1158/0008-5472.can-10-0157 · Cited by 179
Kim, K. W., Mutter, R. W., Cao, C., Albert, J. M., Freeman, M. L., Hallahan, D. E., & Lu, J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607094200 · Cited by 179
Autophagy is required for necrotic cell death in Caenorhabditis elegans
Samara, C., Syntichaki, P., & Tavernarakis, N. (2007) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402231 · Cited by 181
Regulation of Autophagy By Signaling Through the Atg1/ULK1 Complex
Papinski, D., & Kraft, C. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.03.030 · Cited by 186
Accumulation of autophagosomes confers cytotoxicity
Button, R. W., Roberts, S. L., Willis, T. L., Hanemann, C. O., & Luo, S. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.782276 · Cited by 186
Ding, L., Zhu, X., Wang, Y., Shi, B., Ling, X., Chen, H., Nan, W., Barrett, A., Guo, Z., Tao, W., et al. (2017) · Nano Letters · doi:10.1021/acs.nanolett.7b03021 · Cited by 180
Emerging role of mitophagy in cardiovascular physiology and pathology
Morales, P. E., Arias-Durán, C., Ávalos-Guajardo, Y., Aedo, G., Verdejo, H., Parra, V., & Lavandero, S. (2019) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2019.09.006 · Cited by 179
The late stages of autophagy: how does the end begin?
Noda, T., Fujita, N., & Yoshimori, T. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2009.54 · Cited by 190
Self-citationMetabolic Profiling of Hypoxic Cells Revealed a Catabolic Signature Required for Cell Survival
Frezza, C., Zheng, L., Tennant, D. A., Papkovsky, D. B., Hedley, B. A., Kalna, G., Watson, D. G., & Gottlieb, E. (2011) · PLoS ONE · doi:10.1371/journal.pone.0024411 · Cited by 177
Membrane remodeling by the PX-BAR protein SNX18 promotes autophagosome formation
Knævelsrud, H., Søreng, K., Raiborg, C., Håberg, K., Rasmuson, F., Brech, A., Liestøl, K., Rusten, T. E., Stenmark, H., Neufeld, T. P., et al. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201205129 · Cited by 177
DAP1, a Novel Substrate of mTOR, Negatively Regulates Autophagy
Koren, I., Reem, E., & Kimchi, A. (2010) · Current Biology · doi:10.1016/j.cub.2010.04.041 · Cited by 188
Gassen, N. C., Hartmann, J., Zschocke, J., Stepan, J., Hafner, K., Zellner, A., Kirmeier, T., Kollmannsberger, L. K., Wagner, K. V., Dedic, N., et al. (2014) · PLoS Medicine · doi:10.1371/journal.pmed.1001755 · Cited by 180
Levine, B., & Klionsky, D. J. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1619876114 · Cited by 184
Autophagic Stress in Neuronal Injury and Disease
Chu, C. T. (2006) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/01.jnen.0000229233.75253.be · Cited by 211
Xiao, D., Powolny, A. A., de Moura, M. B., Kelley, E. E., Bommareddy, A., Kim, S., Hahm, E., Normolle, D. P., Houten, B. V., & Singh, S. V. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.063255 · Cited by 176
Dysregulation of autophagy as a common mechanism in lysosomal storage diseases
Seranova, E., Connolly, K. J., Zatyka, M., Rosenstock, T. R., Barrett, T. G., Tuxworth, R. I., & Sarkar, S. (2017) · Essays in Biochemistry · doi:10.1042/ebc20170055 · Cited by 183
Kageyama, S., Omori, H., Saitoh, T., Sone, T., Guan, J.-L., Akira, S., Imamoto, F., Noda, T., & Yoshimori, T. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-11-0893 · Cited by 175
Self-citationYang, N., Tan, S.-H., Ng, S., Shi, Y. P., Zhou, J., Tan, K. S. W., Wong, W. S. F., & Shen, H. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.564567 · Cited by 175
Wong, M., Gertz, B., Chestnut, B. A., & Martin, L. J. (2013) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2013.00279 · Cited by 179
OATL1, a novel autophagosome-resident Rab33B-GAP, regulates autophagosomal maturation
Itoh, T., Kanno, E., Uemura, T., Waguri, S., & Fukuda, M. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201008107 · Cited by 181
Crosstalk between cGAS–STING signaling and cell death
Murthy, A. M. V., Robinson, N., & Kumar, S. (2020) · Cell Death and Differentiation · doi:10.1038/s41418-020-00624-8 · Cited by 178
Daido, S., Yamamoto, A., Fujiwara, K., Sawaya, R. A., Kondo, S., & Kondo, Y. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-4202 · Cited by 175
Self-citationAutophagic dysfunction in mucolipidosis type IV patients
Vergarajauregui, S., Connelly, P. S., Daniels, M. P., & Puertollano, R. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn174 · Cited by 182
Gutierrez, M. G., Saka, H. A., Chinen, I., Zoppino, F. C. M., Yoshimori, T., Bocco, J. L., & Colombo, M. I. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0601437104 · Cited by 174
Self-citationCaccamo, A., Majumder, S., Deng, J. J., Bai, Y., Thornton, F. B., & Oddo, S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.031278 · Cited by 169
Molecular cloning and characterization of rat LC3A and LC3B—Two novel markers of autophagosome
Wu, J., Dang, Y., Su, W., Liu, C., Ma, H., Shan, Y., Pei, Y., Wan, B., Guo, J., & Yu, L. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.10.211 · Cited by 180
Lefort, S., Joffre, C., Kieffer, Y., Givel, A.-M., Bourachot, B., Zago, G., Bieche, I., Dubois, T., Meseure, D., Vincent-Salomon, A., et al. (2014) · Autophagy · doi:10.4161/15548627.2014.981788 · Cited by 173
Remodeling of ER‐exit sites initiates a membrane supply pathway for autophagosome biogenesis
Ge, L., Zhang, M., Kenny, S. J., Liu, D., Maeda, M., Saito, K., Mathur, A., Xu, K., & Schekman, R. W. (2017) · EMBO Reports · doi:10.15252/embr.201744559 · Cited by 174
The VMP1-Beclin 1 interaction regulates autophagy induction
Molejon, M. I., Ropolo, A., Ré, A. L., Boggio, V., & Vaccaro, M. I. (2013) · Scientific Reports · doi:10.1038/srep01055 · Cited by 181
Camnasio, S., Carri, A. D., Lombardo, A., Grad, I., Mariotti, C., Castucci, A., Rozell, B., Riso, P. L., Castiglioni, V., Zuccato, C., et al. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.12.042 · Cited by 175
Involvement of JNK in the regulation of autophagic cell death
Shimizu, S., Konishi, A., Nishida, Y., Mizuta, T., Nishina, H., Yamamoto, A., & Tsujimoto, Y. (2010) · Oncogene · doi:10.1038/onc.2009.487 · Cited by 180
Self-citationGABAA receptor associated proteins: a key factor regulating GABAA receptor function
Chen, Z., & Olsen, R. W. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04206.x · Cited by 173
MicroRNA-221 inhibits autophagy and promotes heart failure by modulating the p27/CDK2/mTOR axis
Su, M., Wang, J., Wang, C.-X., Wang, X., Dong, W., Qiu, W., Wang, Y., Zhao, X., Zou, Y., Song, L., et al. (2014) · Cell Death and Differentiation · doi:10.1038/cdd.2014.187 · Cited by 170
Metadata
- Authors
- Kabeya, Y., Mizushima, N., Ueno, T., Yamamoto, A., Kirisako, T., Noda, T., Kominami, E., Ohsumi, Y., & Yoshimori, T.
- Affiliations
- National Institute for Basic Biology (JP)
- Juntendo University (JP)
- Kansai Medical University (JP)
- Corresponding author
- Yoshimori, Tamotsu
- ORCID
- Mizushima, Noboru
- Venue
- The EMBO Journal
- Published
- 2000-11-01
- Volume
- 19
- Issue
- 21
- Pages
- 5720-5728
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC305793
- OpenAlex
- W1977767269
- Cited by
- 6,605
- References
- 31
- Citations by year
- 2026: 135 · 2025: 173 · 2024: 226 · 2023: 272 · 2022: 287 · 2021: 342 · 2020: 344 · 2019: 380 · 2018: 377 · 2017: 387 · 2016: 381 · 2015: 426 · 2014: 389 · 2013: 447 · 2012: 386
- FWCI
- 18.08
- Type
- journal article
- Language
- en
- Update notices
- erratum (2003-09-01)
- Open access
- bronze
- doi.org
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Tokyo Tech Research Repository (Tokyo Institute of Technology) (submittedVersion)
- Funders
- National Institute for Basic Biology
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- LC3, autophagy, LC3-II, post-translational processing, C-terminal truncation, autophagosomes, yeast homologue
- MeSH terms
- Amino Acid Sequence, Animals, Base Sequence, Fungal Proteins, HeLa Cells, Humans, Intracellular Membranes, Microtubule-Associated Proteins, Molecular Sequence Data, Phagosomes, Protein Processing, Post-Translational, Subcellular Fractions, Transfection, Microscopy, Immunoelectron, Sequence Homology, Amino Acid, DNA Primers, Rats
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