The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
Distinct regulation of autophagic activity by Atg14L and Rubicon associated with Beclin 1–phosphatidylinositol-3-kinase complex
Open accessAbstract
Beclin 1, a mammalian autophagy protein that has been implicated in development, tumour suppression, neurodegeneration and cell death, exists in a complex with Vps34, the class III phosphatidylinositol-3-kinase (PI(3)K) that mediates multiple vesicle-trafficking processes including endocytosis and autophagy. However, the precise role of the Beclin 1-Vps34 complex in autophagy regulation remains to be elucidated. Combining mouse genetics and biochemistry, we have identified a large in vivo Beclin 1 complex containing the known proteins Vps34, p150/Vps15 and UVRAG, as well as two newly identified proteins, Atg14L (yeast Atg14-like) and Rubicon (RUN domain and cysteine-rich domain containing, Beclin 1-interacting protein). Characterization of the new proteins revealed that Atg14L enhances Vps34 lipid kinase activity and upregulates autophagy, whereas Rubicon reduces Vps34 activity and downregulates autophagy. We show that Beclin 1 and Atg14L synergistically promote the formation of double-membraned organelles that are associated with Atg5 and Atg12, whereas forced expression of Rubicon results in aberrant late endosomal/lysosomal structures and impaired autophagosome maturation. We hypothesize that by forming distinct protein complexes, Beclin 1 and its binding proteins orchestrate the precise function of the class III PI(3)K in regulating autophagy at multiple steps.
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
“Yeast Atg14 is the autophagy-specific subunit of the Vps34 complex I, 404 and a human homolog, named ATG14 (ATG14L/BARKOR), has been identified.[405][406][407][408]”
From Guidelines for the use and interpretation of assays for monitoring autophagy (2012) · cites this paper as [406]
Experimental — accuracy not yet measuredIn the citing paper
“the class III phosphoinositide 3-kinase (PI3K) complex regulates vesicle nucleation and phagophore formation”
From Autophagy in kidney homeostasis and disease (2020) · cites this paper as [10]
In the citing paper
“Defects in induction, maturation, or lysosomal clearance impair protein degradation (Zhong et al. 2009), (Pickford et al. 2008), (Ravikumar et al. 2005), (Webb et al. 2004), (Iwata et al. 2005), (Kimura et al. 2008), (Wong and Cuervo 2010), (Lee et al. 2010), and is assessable via LC3-II turnover or p62 degradation (Mizushima et al. 2010), (Ju et al. 2010), (Klionsky et al. 2008b), (Tanida et al.”
From TMEM55B downregulation promotes neurodegeneration in Alzheimer’s disease models (2026) · cites this paper as Zhong et al. 2009
In the citing paper
“Detection of endogenous phospho-ATG16L1 [823] has been demonstrated as a novel method to monitor autophagy induction.”
From Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1 (2021) · cites this paper as [823]
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
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
Pankiv, S., Clausen, T. H., Lamark, T., Brech, A., Bruun, J.-A., Outzen, H., Øvervatn, A., Bjørkøy, G., & Johansen, T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702824200 · Cited by 4,578
Suppression 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
Promotion 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
A ubiquitin-like system mediates protein lipidation
Ichimura, Y., Kirisako, T., Takao, T., Satomi, Y., Shimonishi, Y., Ishihara, N., Mizushima, N., Tanida, I., Kominami, E., Ohsumi, M., et al. (2000) · Nature · doi:10.1038/35044114 · Cited by 2,139
Homeostatic 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
Self-citationYue, Z., Jin, S., Yang, C., Levine, A. J., & Heintz, N. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2436255100 · Cited by 2,116
Self-citationLC3, 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
Flagged first, then by citations
Cited by
Sorted by citations
Items 801–900 of 1,001
Recent Advances in Single-Particle Electron Microscopic Analysis of Autophagy Degradation Machinery
Cheung, Y. W. S., Nam, S.-E., & Yip, C. K. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218051 · Cited by 4
Jordan, T. X., & Randall, G. C. (2014) · Wiley eBooks · doi:10.1002/9781118677551.ch6 · Cited by 4
Kumar, S., Sarma, M., Khan, E., & Dubey, V. K. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.145847 · Cited by 3
Herpes simplex virus 1 ICP34.5 acts to maintain latency in human and mouse neurons
Canova, P. N., Katzenell, S., Cerón, S., Charron, A. J., Pesola, J. M., Oh, H. S., Coen, D. M., Knipe, D. M., & Leib, D. A. (2025) · Virology · doi:10.1016/j.virol.2025.110652 · Cited by 5
A lipid transfer-dependent feedback loop activates ATG9A compartments in autophagy initiation
Holzer, E., Sawa-Makarska, J. Z., Bernklau, D., Romanov, J., Schuschnig, M., & Martens, S. (2026) · Nature Communications · doi:10.1038/s41467-026-77368-5 · Cited by 3
Burján, T., Aslam, M., Keresztes, F., Sigmond, T., Billes, V., Bencsik, N., Schlett, K., Vellai, T., & Kovács, A. L. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262110443 · Cited by 3
Tellez-Quijorna, C., Juan-Lopez, A., Eritja, N., Llobet‐Navàs, D., & Devis, L. (2025) · Reproductive Biology and Endocrinology · doi:10.1186/s12958-025-01494-w · Cited by 3
The advances in acetylation modification in senescence and aging-related diseases
Xu, M., Wang, W., Lu, S., Xiong, M., Zhao, T., Yu, Y., Song, C., Yang, J., Zhang, N., Cao, L., et al. (2025) · Frontiers in Physiology · doi:10.3389/fphys.2025.1553646 · Cited by 5
Molecular Cross-Talk between the Autophagy and Apoptotic Networks in Cancer
Driscoll, J. J., & Malek, M. A. Y. A. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-801033-4.00002-3 · Cited by 4
Zhu, H., Chen, H., Chen, G., Liu, M., Chu, L., Gu, Y., Chen, Y., Zhang, C., Qin, Q., Chen, Y., et al. (2022) · Annals of Translational Medicine · doi:10.21037/atm-21-3630 · Cited by 2
Beth Levine’s Legacy: From the Discovery of BECN1 to Therapies. A Mentees’ Perspective
An, Z., Chiang, W., Fernández, Á. F., Franco, L. H., He, C., Huang, S., Lee, E., Liu, Y., Sebti, S., Shoji-Kawata, S., et al. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.891332 · Cited by 4
Jian, J.-T., Zhang, H.-Y., Liu, L.-K., & Liu, H.-P. (2024) · Aquaculture · doi:10.1016/j.aquaculture.2024.741689 · Cited by 3
Xia, J., Bajpai, A. K., Liu, Y., Yu, L., Dong, Y., Li, F., Chen, F., Lu, L., & Feng, S. (2025) · Genes · doi:10.3390/genes16050605 · Cited by 3
THE CELLULAR PROCESS OF AUTOPHAGY AND CONTROL OF AUTOPHAGY IN NEURONS
McKnight, N. C., Mizushima, N., & Yue, Z. (2012) · WORLD SCIENTIFIC eBooks · doi:10.1142/9789814350457_0001 · Cited by 3
Self-citationThe Delicate Balance of Autophagy in Neurodegeneration
Nassif, M., Woehlbier, U., & Manque, P. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-812146-7.00019-6 · Cited by 3
Oxidative Stress and Dysfunction of the Intracellular Proteolytic Machinery
Homma, T., & Fujii, J. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-814466-4.00005-7 · Cited by 3
Chaperone‐Mediated Autophagy and Parkinson's Disease
Martínez‐Vicente, M., & Wong, E. (2011) · Wiley eBooks · doi:10.1002/9781118063903.ch3 · Cited by 3
ULK1-Mediated Metabolic Reprogramming Regulates Vps34 Lipid Kinase Activity by Its LactylationPreprint
Yue, X., Zhou, Q., Jia, M., Chang, C., Gong, W., Feng, J., Sun, W., Li, X., Wang, A., Zou, Y., et al. (2022) · SSRN Electronic Journal · doi:10.2139/ssrn.4047255 · Cited by 3
Self-citationLu, H., Hu, H., Yang, Z., & Li, S. (2023) · Medicine · doi:10.1097/md.0000000000033515 · Cited by 2
Coculo, L., Wits, M., Mariani, I., Fianco, G., Cappato, S., Bocciardi, R., Pedemonte, N., Volpe, E., Ciolfi, S., Sessa, R. L., et al. (2025) · Cell Death Discovery · doi:10.1038/s41420-025-02393-0 · Cited by 2
A new role of RAB21 and VARP in autophagy and autophagic exocytosis of ATP
Barbosa, M. C., Reta, P. M., Nola, S., Aguilera, M. O., Galli, T., Colombo, M. I., & Fader, C. M. (2025) · Autophagy Reports · doi:10.1080/27694127.2025.2501365 · Cited by 2
Rubicon modulates neuroimmune responses following traumatic brain injury
Thapa, S., Mehrabani-Tabari, A. A., Pettyjohn-Robin, O., Nguyen, D. P., Weldemariam, M. M., Sarkar, C., Khan, M., Kane, M. A., & Lipinski, M. M. (2026) · Cell Death and Disease · doi:10.1038/s41419-026-09083-4 · Cited by 3
Autophagy and LC3-associated phagocytosis: similarities and differences
Рафисович, И. Б., Skibo, Y. V., & Abramova, Z. I. (2023) · Medical Immunology (Russia) · doi:10.15789/10.15789/1563-0625-aal-2569 · Cited by 2
Kaur, S., Vashistt, J., & Changotra, H. (2023) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2023.2252097 · Cited by 2
Zhu, Z., Li, L., Ye, Y., & Zhong, Q. (2024) · Cellular Oncology · doi:10.1007/s13402-024-00996-w · Cited by 3
Hirota, Y., Fujimoto, K., & Tanak, Y. (2013) · InTech eBooks · doi:10.5772/54578 · Cited by 3
Nayvelt, I., John, S., Hsu, H., Yang, P., Liu, W., Das, G. M., Hyvönen, M. T., Alhonen, L. I., Keinänen, T. A., Shirahata, A., et al. (2011) · Amino Acids · doi:10.1007/s00726-011-1005-0 · Cited by 2
Powis, K., & MacDougall, L. K. (2011) · Cellular Signalling · doi:10.1016/j.cellsig.2011.02.010 · Cited by 2
Molecular Machines Involved in Pexophagy
Nazarko, T. Y., & Farré, J. (2014) · Springer eBooks · doi:10.1007/978-3-7091-1788-0_22 · Cited by 2
Ji, Y., Okuno, M. N., Shogren, K. L., Fritchie, K., Okuno, S. H., Yaszemski, M. J., & Maran, A. (2020) · Annals of Joint · doi:10.21037/aoj.2020.02.07 · Cited by 2
Skibo, Y. V., Tikhomirova, M. V., Abramov, S. N., Биктагирова, Э. М., Решетникова, И. Д., Акберова, Н. И., & Abramova, Z. I. (2019) · Učënye zapiski Kazanskogo universiteta. Seriâ Estestvennye nauki/Učënye zapiski Kazanskogo universiteta. Seriâ Estestvennye nauki/Učenye zapiski Kazanskogo gosudarstvennogo universiteta. Seriâ Estestvennye nauki · doi:10.26907/2542-064x.2019.4.505-520 · Cited by 1
The Fusion Between Autophagic Vesicles and Lysosomes
Liu, X., & Zhong, Q. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-981-16-2830-6_4 · Cited by 3
Nedelsky, N. B., Kuballa, P., Castoreno, A. B., & Xavier, R. J. (2019) · Springer eBooks · doi:10.1007/978-3-030-28703-0_14 · Cited by 3
Marukawa, D., Gotoh, K., Kobayashi, S., Sasaki, K., Iwagami, Y., Yamada, D., Tomimaru, Y., Akita, H., Asaoka, T., Noda, T., et al. (2023) · International Journal of Clinical Oncology · doi:10.1007/s10147-023-02306-0 · Cited by 2
Karanasios, E., & Ktistakis, N. T. (2016) · Springer eBooks · doi:10.1007/978-3-319-33145-4_4 · Cited by 2
Rab7a in Endocytosis and Signaling
BasuRay, S., Agola, J. O., Jim, P. A., Seaman, M. N. J., & Wandinger‐Ness, A. (2017) · Springer eBooks · doi:10.1007/978-3-319-67199-4_623 · Cited by 2
Zhou, X., Lee, Y.-K., Li, X., Kim, H., Sánchez-Priego, C., Han, X., Tan, H., Zhou, S., Fu, Y., Purtell, K., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.12.04.519029 · Cited by 2
Self-citationPhosphatidylserine clustering by membrane receptors triggers LC3-associated phagocytosisPreprint
Boada-Romero, E., Guy, C. S., Palacios, G., Mari, L., Li, Z., & Green, D. R. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.09.06.556449 · Cited by 2
Filho, E. G. F., Zaidan, I., Fortes-Rocha, M., Alzamora-Terrel, D. L., Bifano, C., de Castro, P. A., Piraine, R. E. A., Pinzan, C. F., Rezende, C. P., Boada-Romero, E., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.03.25.645097 · Cited by 2
The Role of Transglutaminase Type 2 in the Regulation of Autophagy
D’Eletto, M., Rossin, F., Farrace, M. G., & Piacentini, M. (2015) · Springer eBooks · doi:10.1007/978-4-431-55825-5_8 · Cited by 1
Autophagy and Intracellular Membrane Dynamics in Aging and Age-Related Diseases
Minami, S., Nakamura, S., & Yoshimori, T. (2025) · Learning materials in biosciences · doi:10.1007/978-3-031-88121-3_7 · Cited by 1
High-fat diet impairs intermediate-term memory by autophagic-lysosomal dysfunction in Drosophila
Tong, Y. A., Jiang, M., Onuki, K., Itoh, M., & Tonoki, A. (2025) · PLoS Genetics · doi:10.1371/journal.pgen.1011818 · Cited by 1
Sharma, B., Lal, N., Dixit, K., Niharika, N., Singh, L. R., & Luthra, P. M. (2025) · Molecular Biology Reports · doi:10.1007/s11033-025-10987-1 · Cited by 1
Role of Rubicon in platelets: a promoter of thrombosis but not an autophagy repressor
Alfar, H. R., Driehaus, E. R., Smith, A. N., Coenen, D. M., Mahmood, D. F. D., Wood, J. P., & Whiteheart, S. W. (2025) · Blood Advances · doi:10.1182/bloodadvances.2025017486 · Cited by 1
Chen, X., Li, J., Liu, Y., Li, L., Deng, X., Sheng, Y., Zhu, X., Jiang, X., Li, W., Cai, X., et al. (2026) · Advanced Science · doi:10.1002/advs.202507509 · Cited by 1
Brivio, F., Guarato, G., Panzeri, E., Manganelli, F., Filosto, M., Vantaggiato, C., & Bassi, M. T. (2026) · Pharmacological Research · doi:10.1016/j.phrs.2026.108115 · Cited by 1
Autophagy in kidney physiology: from cellular quality control to organ metabolism
Yamamoto, T., Minami, S., & Isaka, Y. (2026) · Autophagy Reports · doi:10.1080/27694127.2026.2622228 · Cited by 1
Gao, X., Yu, Y., Sun, J., Zhao, H., You, Y., Shi, X., Wang, K., Hong, S., Xiong, X., Huang, C., et al. (2026) · PLoS Biology · doi:10.1371/journal.pbio.3003647 · Cited by 1
Exclusion of Notch from the contact site during efferocytosis restricts anticancer immunity
Li, Z., Xu, B., Sharma, P., Guy, C. S., Boada-Romero, E., Verbist, K., Guo, A., Mari, L., Poudel, S., Yang, M., et al. (2026) · Nature Immunology · doi:10.1038/s41590-026-02452-3 · Cited by 2
Fangchinoline restores TFEB-driven lysosomal biogenesis and blocks H1N1 infection
Cheng, C., Xie, F., Liu, Z., Li, J., Qiao, Y., Kong, L., Li, Q., Ma, K., Liu, F., Song, L.-D., et al. (2026) · Acta Pharmacologica Sinica · doi:10.1038/s41401-026-01776-y · Cited by 3
The ATG14: multi-layer autophagy control and an emerging therapeutic target in cancer
Wang, W., Yu, C., Sun, F., Wang, R., Xia, W., Song, Q., Zhang, H., Jia, Z., Zhang, M., Wang, H. Y., et al. (2026) · APOPTOSIS · doi:10.1007/s10495-026-02302-5 · Cited by 1
Autophagy in MASLD : A Metabolic and Precision Medicine Perspective
Cazzaniga, A., Frigo, S., Cherubini, A., Rrapaj, E., & Valenti, L. V. C. (2026) · Liver International · doi:10.1111/liv.70816 · Cited by 1
Roles of autophagy in brain homeostasis and disease
Kim, H., Wickstead, E. S., Zhou, X., Choi, I., & Yue, Z. (2026) · Nature Neuroscience · doi:10.1038/s41593-026-02426-6 · Cited by 1
Self-citationRole of Autophagy in Tumorigenesis
Tao, H., Taylor, R., Zeng, X., & Jin, S. (2013) · Springer eBooks · doi:10.1007/978-1-4614-6561-4_5 · Cited by 1
MAINTAINING AUTOPHAGIC BALANCE: A ROLE FOR BRAKES
Cherra, S. J., & Chu, C. T. (2012) · WORLD SCIENTIFIC eBooks · doi:10.1142/9789814350457_0005 · Cited by 1
AUTOPHAGOSOME MATURATION, ENDOCYTOSIS AND NEURODEGENERATIVE DISEASE
Yamamoto, A., & Simonsen, A. (2012) · WORLD SCIENTIFIC eBooks · doi:10.1142/9789814350457_0002 · Cited by 1
Endoplasmic Reticulum Stress and Autophagy in Cancer
Tan, M., Tan, H. K., & Muhammad, T. S. T. (2020) · Springer eBooks · doi:10.1007/978-3-030-30845-2_18 · Cited by 1
Noncanonical use of the autophagy machinery in antigen presentation
Münz, C. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-820538-9.00006-5 · Cited by 1
Rubicon deficiency exacerbates fasting-induced hepatic steatosis
Dong, F., Hu, X., Zhang, S., He, F., Naz, A., He, L., & Zhu, H. (2021) · Journal of Bio-X Research · doi:10.1097/jbr.0000000000000111 · Cited by 1
Does Autophagy have a Role in the Pathogenesis of Pediatric Hepatic Steatosis?
Ehsan, N., Kandil, M. A. E.-H., Holah, N. S., Sobhy, G. A., Ahmed, M., El-Gammal, S., & Gadallah, M. (2024) · Asian Pacific Journal of Cancer Prevention · doi:10.31557/apjcp.2024.25.5.1753 · Cited by 1
Рафисович, И. Б., Skibo, Y. V., Решетникова, И. Д., Abramov, S. N., Daminova, A. G., Evtyugin, V. G., & Abramova, Z. I. (2023) · Medical Immunology (Russia) · doi:10.15789/1563-0625-eot-2868 · Cited by 2
Nedelsky, N. B., Kuballa, P., Castoreno, A. B., & Xavier, R. J. (2013) · Springer eBooks · doi:10.1007/978-1-4614-8256-7_12 · Cited by 1
Silva, L. M., & Jung, J. U. (2013) · Springer eBooks · doi:10.1007/978-1-4614-6561-4_8 · Cited by 1
Host Autophagy in Antifungal Immunity
Nicola, A. M., Fabricant, S. A., Albuquerque, P., Felipe, M. S. S., & Casadevall, A. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802936-7.00019-2 · Cited by 1
Reductive regulation of BECN1 gene in adult Egyptian patients with do novo AML
Ghozlan, M. F., Farweez, B. A. T., Safwat, N. A., Hassan, N. B., & Elsalakawy, W. A. (2020) · Egyptian Journal of Medical Human Genetics · doi:10.1186/s43042-020-00087-z · Cited by 1
The role of assaying recombinant Beclin1 by in vitro and in vivo tests
Prizad, H., Sheikholeslami, F., Mahmoudi, M., Fazeli, M., & Fadajan, Z. (2021) · Gene Reports · doi:10.1016/j.genrep.2021.101221 · Cited by 1
Oxidative Stress-Induced Autophagy
Sethi, J., & Sethi, U. (2022) · Handbook of Oxidative Stress in Cancer: Therapeutic Aspects · doi:10.1007/978-981-16-5422-0_180 · Cited by 1
Molecular Mechanism of AGC Kinases in Human Malignant
Shu, S. (2010) · Digital Commons - University of South Florida (University of South Florida) · Cited by 1
Crystal Structure and Characterization of the SCOC Coiled Coil Domain
Behrens, C. (2014) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-4638 · Cited by 1
Rab7a in Endocytosis and Signaling
BasuRay, S., Agola, J. O., Jim, P. A., Seaman, M. N. J., & Wandinger‐Ness, A. (2012) · Springer eBooks · doi:10.1007/978-1-4419-0461-4_623 · Cited by 1
Small cytosolic dsDNAs repress cGAS activation and induce autophagyPreprint
Liu, Y., Chen, X., Zhao, Y., Wang, X., Chen, L., Wang, W., Zhong, S., Hu, M., Dai, Z., Jiang, J., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.06.30.498186 · Cited by 1
Canova, P. N., Katzenell, S., Cerón, S., Charron, A. J., Pesola, J. M., Oh, H. S., Coen, D. M., Knipe, D. M., & Leib, D. A. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.04.04.647253 · Cited by 1
Regulation of ULK1 in autophagy
Loska, S. (2012) · Research Explorer (The University of Manchester) · Cited by 1
Molecular aspects of antiestrogen resistance and autophagy in breast cancer cells
Nayvelt, I. (2009) · Rutgers University Community Repository (Rutgers University) · doi:10.7282/t32n52g8
Selective Autophagy and Cancer
Ichimura, Y., & Komatsu, M. (2013) · Springer eBooks · doi:10.1007/978-1-4614-6561-4_6
Cell-Death Pathways and Mitochondria
Marı́n-Garcı́a, J. (2012) · Springer eBooks · doi:10.1007/978-1-4614-4599-9_11
Modulation of Autophagy as a Novel Cancer Therapeutic Strategy
Cui, J., & Shen, H. (2013) · Humana Press eBooks · doi:10.1007/978-1-62703-456-2_10
Characterization of FHL2 expression and function in breast cancer cell lines
Phan, L. D. (2012) · Summit (Simon Fraser University) · Cited by 1
Regulation of autophagy and mTOR during Semliki Forest virus infection
Eng, K. E. (2012) · Figshare
Navas, R. M. G. (2014) · Gredos (University of Salamanca) · doi:10.14201/gredos.124153
Tamoxifen Resistant Breast Cancer and Autophagy
Grey, A. A., Adam, N., & Kim, S.-W. (2011) · InTech eBooks · doi:10.5772/22977
Development of a cell motility characterization system for industrial biotechnological applications
Villella, V. R. (2010) · Università degli Studi di Napoli Federico II · doi:10.6092/unina/fedoa/8186
Determining the Role of Autophagy in HER2/neu-Induced Mammary Tumor Dormancy and Recurrence
Dwyer, S. (2013) · Scholarly Commons (University of Pennsylvania)
Targeting Protein Quality Control Pathways in Spinal and Bulbar Muscular Atrophy
Wang, A. M. (2012) · Deep Blue (University of Michigan)
Hale, A. N. (2014) · UKnowledge (University of Kentucky)
The Functions of Autophagy Genes in Lymphocytes and Osteoclasts
Miller, B. C. (2011) · Open Scholarship Institutional Repository (Washington University in St. Louis) · doi:10.7936/k7m043dz
Zhong, Y., Morris, D. H., Jin, L., Patel, M. S., Karunakaran, S. K., Fu, Y., Matuszak, E. A., Weiss, H. L., Chait, B. T., & Wang, Q. J. (2014)
Self-citationA new Rab7 effector protein sheds light on membrane trafficking pathways
Lin, M. G., & Zhong, Q. (2011)
RAB24 ja GOSR1-proteiinien vuorovaikutus ja rooli autofagiassa
Viljanen, S. (2015) · Työväentutkimus Vuosikirja
Kyöstilä, K. (2015) · Työväentutkimus Vuosikirja
Sim, J. P. L. (2014) · DR-NTU (Nanyang Technological University) · doi:10.32657/10356/64797
Yang, Z. (2010) · Deep Blue (University of Michigan)
Advances in Relationship Between Class Ⅲ PI3K Complex and Autophagy*
Wu, P., & Xu, C. (2012) · PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS · doi:10.3724/sp.j.1206.2011.00387
Regulation of autophagy and cell death in breast carcinoma cells
Koterba, K. L. (2010) · OhioLink ETD Center (Ohio Library and Information Network)
The role of autophagy in clearance of protein aggregates
Isakson, P. (2011) · NORA - Norwegian Open Research Archives
Mammalian Autophagy Can Occur Through an Atg5/Atg7-Independent Pathway
Shimizu, S., Arakawa, S., Nishida, Y., Yamaguchi, H., & Yoshida, T. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-405877-4.00003-2
Targeting PI3-Kinases in Modulating Autophagy and Anti-cancer Therapy
Dou, Z., & Zong, W. (2016) · Current cancer research · doi:10.1007/978-3-319-42740-9_5
Metadata
- Authors
- Zhong, Y., Wang, Q. J., Li, X., Yan, Y., Backer, J. M., Chait, B. T., Heintz, N., & Yue, Z.
- Affiliations
- Howard Hughes Medical Institute (US)
- Rockefeller University (US)
- Icahn School of Medicine at Mount Sinai (US)
- Albert Einstein College of Medicine (US)
- Corresponding author
- Yue, Zhenyu
- ORCID
- Venue
- Nature Cell Biology
- Published
- 2009-03-08
- Volume
- 11
- Issue
- 4
- Pages
- 468-476
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- PMC
- PMC2664389
- OpenAlex
- W1983831622
- Cited by
- 1,005
- References
- 35
- Citations by year
- 2026: 29 · 2025: 43 · 2024: 38 · 2023: 48 · 2022: 63 · 2021: 62 · 2020: 69 · 2019: 51 · 2018: 57 · 2017: 58 · 2016: 72 · 2015: 56 · 2014: 64 · 2013: 77 · 2012: 64
- FWCI
- 49.02
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- U.S. Public Health Service (RNS055683A)
- National Institute of Neurological Disorders and Stroke (R21NS055683, R01NS060123)
- National Center for Research Resources (RR00862, P41RR000862, RR 022220, U54RR022220)
- 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 › Physiology › Calcium signaling and nucleotide metabolism
- Keywords
- autophagy regulation, Beclin-1, ATG14L, Rubicon, Vps34, class III phosphatidylinositol 3-kinase, UVRAG, autophagosome maturation, late endosomes, lysosomes, ATG5, ATG12, lipid kinase activity
- MeSH terms
- Beclin-1, Amino Acid Sequence, Animals, Autophagy, Cell Membrane, HeLa Cells, Humans, Lysosomes, Molecular Sequence Data, Protein Binding, Proteins, Endosomes, Phosphatidylinositol Phosphates, Phosphatidylinositol 3-Kinases, NIH 3T3 Cells, Adaptor Proteins, Signal Transducing, Green Fluorescent Proteins, Apoptosis Regulatory Proteins, Mice
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
