Cited by 2,597Autophagy in Disease and TherapyCalcium signaling and nucleotide metabolismCellular transport and secretion

The DOI matches its Crossref record; 20 of the 21 references it cites were found in a registry or an index.

How to Interpret LC3 Immunoblotting

Open access

Mizushima, Noboru, Yoshimori, Tamotsu·2007·Autophagy

DOI 10.4161/auto.4600

Open this paper in CoChat — free account Open PDF

Abstract

Microtubule-associated protein light chain 3 (LC3) is now widely used to monitor autophagy. One approach is to detect LC3 conversion (LC3-I to LC3-II) by immunoblot analysis because the amount of LC3-II is clearly correlated with the number of autophagosomes. However, LC3-II itself is degraded by autophagy, making interpretation of the results of LC3 immunoblotting problematic. Furthermore, the amount of LC3 at a certain time point does not indicate autophagic flux, and therefore, it is important to measure the amount of LC3-II delivered to lysosomes by comparing LC3-II levels in the presence and absence of lysosomal protease inhibitors. Another problem with this method is that LC3-II tends to be much more sensitive to be detected by immunoblotting than LC3-I. Accordingly, simple comparison of LC3-I and LC3-II, or summation of LC3-I and LC3-II for ratio determinations, may not be appropriate, and rather, the amount of LC3-II can be compared between samples.

Integrity signals

Registry

Crossref · 10.4161/auto.4600

Cites

20 of 20 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

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-citation
p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
Bjørkøy, G., Lamark, T., Brech, A., Outzen, H., Perander, M., Øvervatn, A., Stenmark, H., & Johansen, T. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200507002 · Cited by 3,276
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-citation
The role of autophagy in cardiomyocytes in the basal state and in response to hemodynamic stress
Nakai, A., Yamaguchi, O., Takeda, T., Higuchi, Y., Hikoso, S., Taniike, M., Omiya, S., Mizote, I., Matsumura, Y., Asahi, M., et al. (2007) · Nature Medicine · doi:10.1038/nm1574 · Cited by 1,520
Self-citation
LC3, GABARAP and GATE16 localize to autophagosomal membrane depending on form-II formation
Kabeya, Y., Mizushima, N., Yamamoto, A., Oshitani-Okamoto, S., Ohsumi, Y., & Yoshimori, T. (2004) · Journal of Cell Science · doi:10.1242/jcs.01131 · Cited by 1,394
Self-citation
Bafilomycin A1 prevents maturation of autophagic vacuoles by inhibiting fusion between autophagosomes and lysosomes in rat hepatoma cell line, H-4-II-E cells
Yamamoto, 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-citation
Lysosomal 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
The pre‐autophagosomal structure organized by concerted functions of APG genes is essential for autophagosome formation
Suzuki, K., Kirisako, T., Kamada, Y., Mizushima, N., Noda, T., & Ohsumi, Y. (2001) · The EMBO Journal · doi:10.1093/emboj/20.21.5971 · Cited by 1,060
Self-citation
Role of autophagy in temozolomide-induced cytotoxicity for malignant glioma cells
Kanzawa, T., Germano, I. M., Komata, T., Ito, H., Kondo, Y., & Kondo, S. (2004) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401359 · Cited by 995
Methods for monitoring autophagy
Mizushima, N. (2004) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2004.02.005 · Cited by 899
Self-citation

Show all 21 references

Sorted by citations

Items 2,401–2,500 of 2,597

Aptamer-mediated siRNA delivery to target colon cancer stem cells
Shamaileh, H. A. (2016) · Deakin Research Online (Deakin University)
Energy status and ovarian follicular development
Meng, L. (2016) · doi:10.18174/389440
Peer Reviewed Title: The MTORC1/PI3K Inhibitor NVP-BEZ235 Inhibits HIV-1 Infection in Primary Human Cells Through the Induction of Autophagy / Author:
Sue, R. (2014)
Perturbation of PTEN-PI3K/AKT Signalling Impaired Autophagy Modulation in Dystrophin-Deficient MyoblastsPreprint
Yazid, M. D., & Smith, J. D. (2017) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/125476
P120 Catenin Regulates Inflammation In Macrophage
Guan, X. (2017) · Human Biology
Behaviour of endo-lysosomal and mitochondrial compartments in human NCL fibroblasts in vitro
Pezzini, F. (2010)
Estudo dos efeitos da superexpressão da alfa-sinucleína sobre o tráfego mitocondrial e autofagia em leveduras, células SH-SY5Y e neurônios dopaminérgicos derivados de hiPSC de pacientes com doença de Parkinson
Melo, T. Q. (2017) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.5.2017.tde-01032017-131637
Homeostatic role of acid sphingomyelinase in mtor signaling and autophagy
Justice, M. J. (2016) · IUScholarWorks (Indiana University) · doi:10.7912/c2/1797
Autophagy and proinflammatory cytokine expression in the intestinal mucosa and mesenteric fat tissue of patients with Crohn's disease
Leal, R. F., Milanski, M., Coy, C. S. R., Portovedo, M., Rodrigues, V. S., Coope, A., Ayrizono, M. D. L. S., Fagundes, J. J., & Velloso, L. A. (2013) · Journal of Coloproctology · doi:10.1590/s2237-93632013000100003
The Role of the Retinoblastoma Protein Family in Skeletal Myogenesis
Ciavarra, G. (2011) · Library and Archives Canada (Government of Canada)
Interactions of L. monocytogenes with Host Cellular Defenses
Lam, G. Y. (2012) · TSpace (University of Toronto)
AMPK-Mediated Regulation of Protein Degradation Systems in Unloaded Mouse Skeletal Muscle
Egawa, T., Goto, A., Ohno, Y., Yokoyama, S., SUZUKI-TAKUWA, M., IKUTA, A., Hayashi, T., & Goto, K. (2016) · Juntendō Igaku/Juntendo igaku · doi:10.14789/jmj.62.s172
Examining the interplay between oxidative and β-adrenergic regulation of PKARIα and its impact on the mitochondrial fission protein DRP1
Johnston, A. (2017) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-6065
Processo autofágico no reconhecimento de Escherichia coli enteroinvasora: um possível mecanismo da degradação bacteriana por células epiteliais
Santos, H. C. A. S. (2017) · doi:10.11606/t.9.2017.tde-19102016-152507
Avaliação dos mecanismos moleculares das vias de p53/ARF e IFNbeta envolvidos com a resposta de células de melanoma ao tratamento com os transgenes p19Arf e IFNbeta
Ribeiro, A. H. (2016) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.5.2016.tde-04112016-142136
A Dual Role of a Soluble N -Ethylmaleimide Sensitive Factor–Attachment Protein Alpha (αSNAP) in the Regulation of Autophagy
Ivanov, A. I. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-812146-7.00024-x
O papel da autofagia no estresse oncogênico promovido por HRASG12V em queratinócitos humanos imortalizados por E6E7
Lopes, E. C. (2017) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.46.2017.tde-21062017-084659
The effect of short-term heat stress on protein synthesis signaling in isolated rat skeletal muscle
Goto, A., Sekine, K., Oshima, R., Sakon, I., Iwamoto, M., Osaki, T., Haga, K., Hayashi, T., & Egawa, T. (2018) · The Journal of Physical Fitness and Sports Medicine · doi:10.7600/jpfsm.7.87
New Molecular and Innovations in Forensic Pathology
Kondo, T., Ishida, Y., Kimura, A., & Nosaka, M. (2017) · Springer eBooks · doi:10.1007/978-3-319-67092-8_9
Post-translational myristoylation during cell death
Martin, D. D. O. (2011) · ERA: Education and Research Archive (University of Alberta) · doi:10.7939/r36x2s
Myocardial Insulin Signaling and Autophagy
Bartlett, J. J., Trivedi, P. C., Rodrigues, B. B., & Pulinilkunnil, T. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-805253-2.00009-2
Defining the role of progesterone receptor and progestin in luminal breast cancer cells
Bajalović, N. (2018) · doi:10.32657/10220/45830
Identification of novel candidate genes for susceptibility to tuberculosis by identifying disease-causing mutations in individuals with Primary Immunodeficiency disorders
Schlechter, N. (2017) · SUNScholar (Stellenbosch University)
Elucidating the role of metabolic changes in modulating cell fate following treatment with anti-mitotic drugs
Wong, A. X. F. (2018) · doi:10.32657/10220/47517
The role of angiopoietin-like 4 (ANGPTL4) in chemoresistance and autophangy during epithelial-mesenchymal transition (EMT)
Lim, M. M. K. (2019) · doi:10.32657/10220/47586
Proof Delivery Form
Yamakura, M. U. F. (2012)
A protein kináz D szerepének vizsgálata az idegsejtek pusztulását előidéző hatások alatt
Liliom, H. L. (2018) · Eötvös Loránd Tudományegyetem · doi:10.15476/elte.2018.067
Survival Pathways in Breast Cancer Cells During Glucose Deprivation
Walker, A. (2016)
Inhibition of compensatory survival and proliferative pathway activation induced by mTOR inhibition in renal cell carcinoma
Bailey, S. T. (2019) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/nfxr-rg33
Targeting rhabdomyosarcoma with temozolomide: how autophagy regulates TMZ-induced apoptosis in rhabdomyosarcoma cells
Moghadam, A. R. (2018) · Mspace (University of Manitoba) · Cited by 1
Avaliação toxicológica e ecotoxicológica dos principais representantes de éteres de difenilas polibromadas (PBDEs)
Silva, M. P. (2019) · doi:10.11606/t.60.2019.tde-17102018-103418
HIV Tat and Morphine-induced Neurodegeneration in a Beclin 1 Hemizygous Mouse Model
Lapierre, J. (2018) · FIU - Digital Commons (Florida International University) · doi:10.25148/etd.fidc007019
Mechanistic Studies on Arsenic Toxicity in Endothelial Cells
Jia-ni, C. (2018) · KU ScholarWorks (The University of Kansas)
Role of Different Salmonella enterica Serotypes in THP-1 Macrophage Derived Foam Cell Autophagy and Inflammatory Response
Wong, M. Y., Tseng, Y., Huang, T., et al. (2019) · Sains Malaysiana · doi:10.17576/jsm-2019-4810-21
Autophagy: an emerging key regulator of epithelial-mesenchymal transition (EMT) in non-small cell lung cancer (NSCLC) cells
Alizadeh, J. (2017) · Mspace (University of Manitoba)
Autophagic Dysfunction in Neurodegeneration
Kaira, M., Ahlawat, A., Walia, V., & Garg, M. (2020) · Advances in medical diagnosis, treatment, and care (AMDTC) book series · doi:10.4018/978-1-7998-1317-0.ch002
The interplay of hypoxia and autophagy in epithelium-derived ameloblastoma cell survival: a pilot study
AlMuzaini, A. A. A. Y., Boesze‐Battaglia, K., Alawi, F., & Akintoye, S. O. (2021) · Oral Surgery Oral Medicine Oral Pathology and Oral Radiology · doi:10.1016/j.oooo.2020.10.028
Monitoring Autophagy: Not All LC3s Are Created EqualPreprint
Fouad, Y. A., & El‐Naggar, S. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.07.20.211458
γ- and δ-Tocotrienols interfere with senescence leading to decreased viability of cells
Janubova, M., Hatok, J., Koňariková, K., & Žitňanová, I. (2020) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-020-03954-w
Modulating Intra-Nuclear LC3 with Small Molecules Rescues Cells from a Docetaxel-Induced PhenotypePreprint
Rosenberg, D. P., Kolla, L., Heo, D. S., Cassio, E. E., Veenstra, M. J., Vakaki, M. A., Zhang, J., Anyetei‐Anum, C. S., Allison, L. A., & Buchser, W. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.10.28.355826
Der Einfluss von humanem α-Synuclein-Wildtyp und der Mutanten A30P und A53T auf die Autophagie und den Transport synaptischer Vesikel in primären Mittelhirnneuronen der Ratte
Bitow, F. (2020) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-8215
Regulatory Effect of Cordycepin on Autophagy in Rat Glomerular Mesangial Cells
毕, 凌. (2020) · Advances in Clinical Medicine · doi:10.12677/acm.2020.1012490
Role of Inflammatory Cytokine Signaling in Control of Bacterial Infection
Saxena, P. (2020) · uO Research (University of Ottawa) · doi:10.20381/ruor-25300
Multi-Species Phenotypic Screening across Disease Models of Mucolipidosis Type IVPreprint
Hadjikyriacou, A., Iyer, S. V., Mast, J. D., DiPrimio, N., Concannon, J. B., Ketterman, J., Sigoillot, F. D., Rodriguez, T. P., Sam, F. S., Tsang, H., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.05.434120
Connexin32 promotes autophagy of cervical cancer to resistance to chemotherapy-induced apoptosis via AMPK pathwayPreprint
fan, L., Tao, L., Lai, Y., Cai, S., Zhao, Z., Yang, F., Su, R., & Wang, Q. (2021) · Research Square · doi:10.21203/rs.3.rs-337122/v1
Understanding the Role of LRBA in Patients with Inflammatory Bowel Disease
Omary, Z. (2019) · TSpace (University of Toronto)
Cerebrovascular Dysfunction and Degeneration in Alzheimer’s Disease Pathophysiology
Quintana, D. D. (2020) · The Research Repository @ WVU (West Virginia University) · doi:10.33915/etd.7941
Linking proteostasis, aging, and brain ischemia
Yang, W., Li, R., Li, X., & Turner, D. A. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-817990-1.00028-7
The Proteasome Inhibitor Bortezomib Induces Tongue, Pharynx and Salivary Gland Cancer Cells Death in Vitro and Delays Tumor Growth of Salivary Gland Cancer Cells Transplanted in MicePreprint
Benvenuto, M., Ciuffa, S., Focaccetti, C., Sbardella, D., Fazi, S., Tundo, G. R., Barillari, G., Segni, M., Manzari, V., Modesti, A., et al. (2021) · Research Square · doi:10.21203/rs.3.rs-561856/v1
Role of lysosomes in oxidative stress induced regulated cell death
Nagakannan, P. (2020) · Mspace (University of Manitoba)
Effects of physiologic inputs on autophagy
Eisenberg, T., Abdellatif, M., Ljubojević-Holzer, S., & Sedej, S. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-822003-0.00001-2
Emodin Ameliorate High Glucose-induced Podocyte Apoptosis via Regulating AMPK/mTOR- mediated Autophagy Signaling PathwayPreprint
Liu, H. S., Hu, Y., Shi, G., Yang, W., Xiong, F., Hu, T., Wang, H., Zhang, Y., & Chen, W. (2021) · Research Square · doi:10.21203/rs.3.rs-796405/v1
Autophagy in Cardiac Physiology and Pathology
Zaglia, T., & Field, L. J. (2021) · Advances in biochemistry in health and disease · doi:10.1007/978-3-030-78799-8_4
Mecanismes de toxicitat de la dopamina en cèl·lules de neuroblastoma humà SH-SY5Y
Xavier, P. G. (2008) · Dipòsit Digital de la Universitat de Barcelona (Universitat de Barcelona)
The Effects of Aging on Skeletal Muscle AMPK Activation and an Analysis of Chronic AICAR Treatment on the Aging Phenotype
Hardman, S. E. (2014) · ScholarsArchive (Brigham Young University)
Suppression of the Long Non-Coding RNA LINC01279 Triggers Autophagy and Apoptosis in Lung Cancer by Regulating FAK and SIN3APreprint
Su, W., Wu, J., Huang, X., Li, X., Zhou, H., Chen, X., Chen, Y., Huang, J. H., Huang, H., Huang, Z., et al. (2022) · Research Square · doi:10.21203/rs.3.rs-1328827/v1
Faculty Opinions recommendation of Midbody accumulation through evasion of autophagy contributes to cellular reprogramming and tumorigenicity.
Barral, Y., & Saarikangas, J. (2012) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.717948529.793453594
Extracellular vesicles derived from adipose mesenchymal stem cells (AMSCs) reduce autophagic flux via microRNA-25-3p transfer after ischemic stroke
Kuang, Y. (2022) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-9093
Targeting α4 Integrin Containing Complexes in Multiple Myeloma Using Peptidomimetics
Emmons, M. F. (2012) · Digital Commons - University of South Florida (University of South Florida)
Papel da interleucina-6 nas respostas da via da autofagia no coração de camundongos submetidos ao exercício físico agudo exaustivo
Rovina, R. L. (2022) · doi:10.11606/d.109.2022.tde-23032022-093425
The role of hepatocellular eNOS in NAFLD development and hepatic mitochondrial adaptations to exercise
Cunningham, R. P. (2020) · doi:10.32469/10355/81558
Introduction to Autophagy
Hayat, M. A. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-405530-8.00001-7
Perturbation of PI3K/Akt Signalling affected Autophagy Modulation in Dystrophin-Deficient MyoblastsPreprint
Yazid, M. D., & Chen, H.-C. (2020) · Research Square · doi:10.21203/rs.3.rs-41896/v1
Vorinostat, a Histone Deacetylase Inhibitor, as a Candidate Therapy to Treat Liver Pathology in a Niemann-Pick type C Disease Mouse Model
Hammond, N. (2016) · Open Access Victoria University of Wellington | Te Herenga Waka (Figshare) · doi:10.26686/wgtn.17148131
Peer Review #1 of "A comparative in-silico analysis of autophagy proteins in ciliates (v0.1)"
(2017) · PeerJ · doi:10.7287/peerj.2878v0.1/reviews/1
Peer Review #2 of "A comparative in-silico analysis of autophagy proteins in ciliates (v0.1)"
(2017) · PeerJ · doi:10.7287/peerj.2878v0.1/reviews/2
Perturbation of PI3K/Akt Signaling Affected Autophagy Modulation in Dystrophin-deficient MyoblastsPreprint
Yazid, M. D., & Chen, H.-C. (2020) · Research Square · doi:10.21203/rs.3.rs-113469/v1
Discussion
(2013) · Journal of Thoracic and Cardiovascular Surgery · doi:10.1016/j.jtcvs.2013.06.063
Thymoquinone dose-dependently attenuates myocardial injury induced by isoproterenol in rats via integrated modulation of oxidative stress, inflammation, apoptosis, autophagy and fibrosisPreprint
Farag, M. M., Khalifa, A. A., El-Hadidy, W. F., et al. (2021) · Research Square · doi:10.21203/rs.3.rs-169928/v1
Perturbation of PI3K/Akt Signaling affected Autophagy Modulation in Dystrophin-Deficient MyoblastsPreprint
Yazid, M. D., & Chen, H.-C. (2020) · Research Square · doi:10.21203/rs.3.rs-41896/v2
Faculty Opinions recommendation of Network organization of the human autophagy system.
Kiger, A. A., & Aligianni, S. (2010) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.3836990.3571103
Targeting Midbodies in Ovarian Cancer Stem Cells as a Therapeutic Strategy
Doxsey, S. (2014) · Defense Technical Information Center (DTIC) · doi:10.21236/ada614468
Análise dos mecanismos pró-inflamatórios do ácido úrico solúvel: efeito sobre proteínas sensíveis à modulação redox e sobre a polarização de células THP-1
Gomes, C. J. C. (2021) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.46.2021.tde-17012022-123152
AI-guided screen identifies probucol-mediated mitophagy enhancement through modulation of lipid dropletsPreprint
Moskal, N., Visanji, N. P., Gorbenko, O., Narasimhan, V., Tyrrell, H., Nash, J., Lewis, P. N., & McQuibban, G. A. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.05.18.492560
Autophagy activity is inhibited by hnRNP RPreprint
Ji, C. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.06.20.496848
Three consecutive glycolysis enzymes are involved in autophagic flux regulation through monitoring nutrient availabilityPreprint
Lee, D., Choi, I., Park, S. J., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.07.12.499818
Urolithin A reduces amyloid-beta load and improves cognitive deficits uncorrelated with plaque burden in a mouse model of Alzheimer’s diseasePreprint
Ballesteros‐Álvarez, J., Nguyen, W., Sivapatham, R., Rane, A., & Andersen, J. K. (2022) · Research Square · doi:10.21203/rs.3.rs-2046848/v2
Characterization of two novel neutral sphingomyelinase 2 inhibitors in endosomal sorting and Extracellular Vesicle biogenesis
Choezom, D., & Gross, J. C. (2022) · Trillium Extracellular Vesicles · doi:10.47184/tev.2022.01.02
Identification and validation of a novel autophagy modulator that blocks autophagosome-lysosome fusion
Ezazi Erdi, S. (2022) · Publication Server of Goethe University Frankfurt am Main (Goethe University Frankfurt) · doi:10.21248/gups.70950
LncRNA MEG3 regulates ASK1/JNK axis-mediated apoptosis and autophagy via sponging miR-23a in yak granulosa cellsPreprint
Han, X., Pan, Y., Fan, J.-F., et al. (2022) · Research Square · doi:10.21203/rs.3.rs-2348584/v1
Protocol to purify and detect ubiquitinated phospholipids in budding yeast and human cell lines
Sakamaki, J.-I., & Mizushima, N. (2022) · STAR Protocols · doi:10.1016/j.xpro.2022.101935
Self-citation
The effect of metformin on autophagy by LC3 expression in Type 2 Diabetes Mellitus (T2DM) human skeletal muscle cell culture
Prajitno, J. H., Pranoto, A. S., Adiwinoto, R. D., & Soelistijo, S. A. (2022) · Bali Medical Journal · doi:10.15562/bmj.v11i1.3203 · Cited by 1
Supplementary Figure 2 from Oncolytic Reovirus (pelareorep) Induces Autophagy in KRAS-mutated Colorectal Cancer
Jiffry, J., Thavornwatanayong, T., Rao, D., et al. (2023) · doi:10.1158/1078-0432.22479911.v1
Data from Oncolytic Reovirus (pelareorep) Induces Autophagy in KRAS-mutated Colorectal Cancer
Jiffry, J., Thavornwatanayong, T., Rao, D., et al. (2023) · doi:10.1158/1078-0432.c.6530321.v1
Lysosomal trapping of 4-dimethylamino-1-{3-(1-methyl-1H-imidazole-2-yl)propanoyl}piperidine, a hydrophilic and weakly basic amine, in human aortic vascular smooth muscle cells
Takahashi, K., Morita, Y., Udagawa, S., et al. (2023) · Toxicology in Vitro · doi:10.1016/j.tiv.2023.105614
Ethanolic Extract of the Cyperus Rotundus Enhances Chemosensitivity to Docetaxel and Inhibits Autophagic Flux in Her2- Positive Breast CancerPreprint
Bian, X., Liu, X., Li, C., Song, X., Liu, Z., Wang, F., Wang, X., Shao, W., Sun, H., & Yu, Z. (2023) · SSRN Electronic Journal · doi:10.2139/ssrn.4604253
Modes of Chemically Induced Cell Death
Aki, T., Unuma, K., Funakoshi, T., & Uemura, K. (2023) · Elsevier eBooks · doi:10.1016/b978-0-323-95488-4.00013-9 · Cited by 1
p62, the Receptor for Selective Autophagy, Contributes in ATXN3 Aggregate Formation in Spinocerebellar Ataxia Type 3Preprint
Zimmer, A. J., Bahl, C., Schäfer, J. M., Weber, J. J., Rieß, O., & Hübener‐Schmid, J. (2024) · Preprints.org · doi:10.20944/preprints202403.0400.v1
Additional file 1 of Inhibition of ERK downregulates autophagy via mitigating mitochondrial fragmentation to protect SH-SY5Y cells from OGD/R injury
Yuan, Z.-L., Mo, Y.-Z., Li, D.-L., Xie, L., & Chen, M. (2023) · Figshare · doi:10.6084/m9.figshare.23949717
Additional file 2 of Inhibition of ERK downregulates autophagy via mitigating mitochondrial fragmentation to protect SH-SY5Y cells from OGD/R injury
Yuan, Z.-L., Mo, Y.-Z., Li, D.-L., Xie, L., & Chen, M. (2023) · Figshare · doi:10.6084/m9.figshare.23949723
Identification and In Vivo Validation of Unique Anti-Oncogenic Mechanisms Involving Protein Kinase Signaling and Autophagy Mediated by the Investigational Agent PV-10
Tran, S., Sipila, P., Thakur, S. S., et al. (2024) · Cancers · doi:10.3390/cancers16081520
Targeting iron metabolism in cancer to induce ferroptosis: a type of programmed cell death
Beadman, R. (2024) · Cronfa (Swansea University) · doi:10.23889/suthesis.66249
The GTPase-activating protein CG42795 is a potent neuronal regulator of ageing in Drosophila melanogasterPreprint
Falcsik, G., Keresztes, F., Juhász, A., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.06.17.598893
Sertad1 is elevated and plays a necessary role in synaptic loss, neuron death and cognitive impairment in a model of Alzheimer’s diseasePreprint
Ambareen, N., Gharami, K., & Biswas, S. C. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.08.06.606751
Correlating amino acid profiles with improved expression capability of superior CHO based expression platforms
Sharma, V., Guleria, R., & Mukherjee, K. J. (2026) · Indian Journal of Biochemistry and Biophysics · doi:10.56042/ijbb.v63i6.28419
Unravelling a mechanistic link between mitophagy defect, mitochondrial malfunction, and apoptotic neurodegeneration in MPS VIIPreprint
Mandal, N., Das, A., & Datta, R. (2024) · bioRxiv · doi:10.1101/2024.08.23.609363
Bromodomain and extraterminal domain (BET) promote autophagy in buffalo sertoli cells
Yang, Y., Zhang, J., Zhang, Y., Sun, Q., Liu, R., Xu, C., Xu, P., Lu, Y., & Fu, Q. (2024) · Theriogenology · doi:10.1016/j.theriogenology.2024.10.027
A FRET Autophagy Imaging Platform by Macrocyclic Amphiphile
Jiang, Z.-T., Chen, J., Chen, F., Cheng, Y., Yao, S., Ma, R., Li, W., Chen, H., & Guo, D. (2024) · Angewandte Chemie · doi:10.1002/ange.202420793
Soyasaponins alleviate nonalcoholic steatohepatitis by augmenting the DDX5-TSC1/2-mTOR signaling-mediated autophagy
Luo, H., Ding, Y., Lu, J., Wang, J., Chen, J., Zheng, Z., Li, Q., Zheng, X., & Zha, L. (2025) · Food Bioscience · doi:10.1016/j.fbio.2025.106596
Microcystin‐mediated Hepatotoxicity
Call, M. R., Ikumawoyi, V. O., Fotler, R., Dietrich, D. R., & Clarke, J. (2025) · Elsevier eBooks · doi:10.1016/b978-0-323-95488-4.00277-1

Authors: Mizushima, N., & Yoshimori, T.
Affiliations: Tokyo Medical and Dental University (JP)
ORCID: Mizushima, Noboru
Yoshimori, Tamotsu
Venue: Autophagy
Publisher: Informa UK Limited
Published: 2007-11-26
Volume: 3
Issue: 6
Pages: 542-545
ISSN: 1554-8627 (ISSN-L)
1554-8635
DOI: 10.4161/auto.4600
OpenAlex: W1963521777
Semantic Scholar: ab5143ed104a787ff2e14d915df9a12ce5f5871a
Cited by: 2,595
References: 21
Citations by year: 2026: 62 · 2025: 114 · 2024: 152 · 2023: 141 · 2022: 176 · 2021: 164 · 2020: 173 · 2019: 155 · 2018: 177 · 2017: 162 · 2016: 167 · 2015: 179 · 2014: 137 · 2013: 165 · 2012: 120
FWCI: 52.76
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by-nc
Locations: Autophagy (publishedVersion, cc-by-nc)
PubMed (publishedVersion)
Funders: Kato Memorial Bioscience Foundation
Toray Science Foundation
Japan Society for the Promotion of Science
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Keywords: LC3, autophagic flux
MeSH terms: Animals, Autophagy, Humans, Lysosomes, Microtubule-Associated Proteins, Phosphatidylethanolamines, Sensitivity and Specificity, Immunoblotting, PC12 Cells, Cell Line, Tumor, Adaptor Proteins, Signal Transducing, 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

How to Interpret LC3 Immunoblotting

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks