The DOI matches its Crossref record; 196 of the 196 references it cites were found in a registry or an index.
Autophagy and organelle homeostasis in cancer
Open accessAbstract
Beginning with the earliest studies of autophagy in cancer, there have been indications that autophagy can both promote and inhibit cancer growth and progression. Autophagy regulation of organelle homeostasis is similarly complicated. In this review, we discuss pro- and anti-tumor effects of organelle-targeted autophagy and how this contributes to several hallmarks of cancer, such as evading cell death, genomic instability, and altered metabolism. Typically, the removal of damaged or dysfunctional organelles prevents tumor development but can also aid in proliferation or drug resistance in established tumors. By better understanding how organelle-specific autophagy takes place and can be manipulated, it may be possible to go beyond the brute force approach of trying to manipulate all autophagy in order to improve therapeutic targeting of this process in cancer.
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
Cites
3 retracted
Mitochondrial Autophagy Is an HIF-1-dependent Adaptive Metabolic Response to Hypoxia
Zhang, H., Bosch-Marce, M., Shimoda, L. A., Tan, Y. S., Baek, J. H., Wesley, J. B., Gonzalez, F. J., & Semenza, G. L. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800102200 · Cited by 1,601
RetractedRETRACTED ARTICLE: Parkin and PINK1 mitigate STING-induced inflammation
Sliter, D. A., Martinez, J., Hao, L., Chen, X., Sun, N., Fischer, T. D., Burman, J. L., Li, Y., Zhang, Z., Narendra, D. P., et al. (2018) · Nature · doi:10.1038/s41586-018-0448-9 · Cited by 1,287
RetractedWei, R., Cao, J., & Yao, S. (2018) · Cell Stress and Chaperones · doi:10.1007/s12192-018-0937-7 · Cited by 90
RetractedRepertoires of Autophagy in the Pathogenesis of Ocular Diseases
Li, Y.-J., Jiang, Q., Cao, G.-F., Yao, J., & Yan, B. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000373980 · Cited by 16,304
Warburg, O. (1956) · Science · doi:10.1126/science.123.3191.309 · Cited by 13,425
Down-Regulation of Na+/K+ATPase Activity by Human Parvovirus B19 Capsid Protein VP1
Almilaji, A., Szteyn, K., Fein, E., Pakladok, T., Munoz, C., Elvira, B., Towhid, S. T., Alesutan, I., Shumilina, E., Bock, C.-T., et al. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000350083 · Cited by 8,675
The versatility and universality of calcium signalling
Berridge, M. J., Lipp, P., & Bootman, M. D. (2000) · Nature Reviews Molecular Cell Biology · doi:10.1038/35036035 · Cited by 5,701
The metabolism of tumors in the body
Warburg, O., Wind, F., & Negelein, E. (1927) · Journal of General Physiology · doi:10.1085/jgp.8.6.519 · Cited by 4,416
Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
Narendra, D., Tanaka, A., Suen, D.-F., & Youle, R. J. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200809125 · Cited by 4,026
Autophagy regulates lipid metabolism
Singh, R., Kaushik, S., Wang, Y., Xiang, Y., Novak, I., Komatsu, M., Tanaka, K., Cuervo, A. M., & Czaja, M. J. (2009) · Nature · doi:10.1038/nature07976 · Cited by 3,975
The Pathophysiology of Mitochondrial Cell Death
Green, D. R., & Kroemer, G. (2004) · Science · doi:10.1126/science.1099320 · Cited by 3,418
Nakahira, K., Haspel, J. A., Rathinam, V. A. K., Lee, S.-J., Dolinay, T., Lam, H. C., Englert, J. A., Rabinovitch, M., Cernadas, M., Kim, H. P., et al. (2011) · Nature Immunology · doi:10.1038/ni.1980 · Cited by 3,049
PINK1 Is Selectively Stabilized on Impaired Mitochondria to Activate Parkin
Narendra, D. P., Jin, S. M., Tanaka, A., Suen, D.-F., Gautier, C. A., Shen, J., Cookson, M. R., & Youle, R. J. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000298 · Cited by 2,944
Biological Functions of Autophagy Genes: A Disease Perspective
Levine, B., & Kroemer, G. (2019) · Cell · doi:10.1016/j.cell.2018.09.048 · Cited by 2,832
The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy
Lazarou, M., Sliter, D. A., Kane, L. A., Sarraf, S. A., Wang, C., Burman, J. L., Sideris, D. P., Fogel, A. I., & Youle, R. J. (2015) · Nature · doi:10.1038/nature14893 · Cited by 2,774
Mechanism 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
The Role of Mitochondria in Apoptosis
Wang, C., & Youle, R. J. (2009) · Annual Review of Genetics · doi:10.1146/annurev-genet-102108-134850 · Cited by 1,987
Identification of the molecular basis of doxorubicin-induced cardiotoxicity
Zhang, S., Liu, X., Bawa-Khalfe, T., Lu, L.-S., Lyu, Y. L., Liu, L. F., & Yeh, E. T. H. (2012) · Nature Medicine · doi:10.1038/nm.2919 · Cited by 1,948
Mitochondrial metabolism and ROS generation are essential for Kras-mediated tumorigenicity
Weinberg, F., Hamanaka, R., Wheaton, W. W., Weinberg, S., Joseph, J., Lopez, M., Kalyanaraman, B., Mutlu, G. M., Budinger, G. R. S., & Chandel, N. S. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1003428107 · Cited by 1,742
Autophagy Suppresses Tumorigenesis through Elimination of p62
Mathew, R., Karp, C. M., Beaudoin, B., Vuong, N., Chen, G., Chen, H.-Y., Bray, K., Reddy, A., Bhanot, G., Gelinas, C., et al. (2009) · Cell · doi:10.1016/j.cell.2009.03.048 · Cited by 1,719
Signals from the lysosome: a control centre for cellular clearance and energy metabolism
Settembre, C., Fraldi, A., Medina, D. L., & Ballabio, A. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3565 · Cited by 1,697
Macropinocytosis of protein is an amino acid supply route in Ras-transformed cells
Commisso, C., Davidson, S. M., Soydaner-Azeloglu, R. G., Parker, S. J., Kamphorst, J. J., Hackett, S., Grabocka, E., Nofal, M., Drebin, J. A., Thompson, C. B., et al. (2013) · Nature · doi:10.1038/nature12138 · Cited by 1,683
Peroxisomes (microbodies and related particles).
De Duve, C., & Baudhuin, P. (1966) · Physiological Reviews · doi:10.1152/physrev.1966.46.2.323 · Cited by 1,666
Bellot, G., Garcia-Medina, R., Gounon, P., Chiche, J., Roux, D., Pouysségur, J., & Mazure, N. M. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00166-09 · Cited by 1,501
Pancreatic cancers require autophagy for tumor growth
Yang, S., Wang, X., Contino, G., Liesa, M., Sahin, E., Ying, H., Bause, A., Li, Y., Stommel, J. M., Dell'Antonio, G., et al. (2011) · Genes & Development · doi:10.1101/gad.2016111 · Cited by 1,498
Ubiquitin is phosphorylated by PINK1 to activate parkin
Koyano, F., Okatsu, K., Kosako, H., Tamura, Y., Go, E., Kimura, M., Kimura, Y., Tsuchiya, H., Yoshihara, H., Hirokawa, T., et al. (2014) · Nature · doi:10.1038/nature13392 · Cited by 1,477
The coming of age of chaperone-mediated autophagy
Kaushik, S., & Cuervo, A. M. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0001-6 · Cited by 1,407
Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL
Jin, S. M., Lazarou, M., Wang, C., Kane, L. A., Narendra, D. P., & Youle, R. J. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201008084 · Cited by 1,375
Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin
Tanaka, A., Cleland, M. M., Xu, S., Narendra, D. P., Suen, D.-F., Karbowski, M., & Youle, R. J. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201007013 · Cited by 1,369
Autophagy-deficient mice develop multiple liver tumors
Takamura, A., Komatsu, M., Hara, T., Sakamoto, A., Kishi, C., Waguri, S., Eishi, Y., Hino, O., Tanaka, K., & Mizushima, N. (2011) · Genes & Development · doi:10.1101/gad.2016211 · Cited by 1,342
Lemasters, J. J. (2005) · Rejuvenation Research · doi:10.1089/rej.2005.8.3 · Cited by 1,340
Santos, C. R., & Schulze, A. (2012) · The FEBS Journal · doi:10.1111/j.1742-4658.2012.08644.x · Cited by 1,335
The role for autophagy in cancer
White, E. (2015) · Journal of Clinical Investigation · doi:10.1172/jci73941 · Cited by 1,332
Cancer metabolism: fatty acid oxidation in the limelight
Carracedo, A., Cantley, L. C., & Pandolfi, P. P. (2013) · Nature Reviews Cancer · doi:10.1038/nrc3483 · Cited by 1,324
Activated Ras requires autophagy to maintain oxidative metabolism and tumorigenesis
Guo, J. Y., Chen, H.-Y., Mathew, R., Fan, J., Strohecker, A. M., Karsli-Uzunbas, G., Kamphorst, J. J., Chen, G., Lemons, J. M. S., Karantza, V., et al. (2011) · Genes & Development · doi:10.1101/gad.2016311 · Cited by 1,323
Nix is a selective autophagy receptor for mitochondrial clearance
Novak, I., Kirkin, V., McEwan, D. G., Zhang, J., Wild, P., Rozenknop, A., Rogov, V., Löhr, F., Popovic, D., Occhipinti, A., et al. (2010) · The EMBO Reports · doi:10.1038/embor.2009.256 · Cited by 1,309
Autophagy in malignant transformation and cancer progression
Galluzzi, L., Pietrocola, F., Bravo‐San Pedro, J. M., Amaravadi, R. K., Baehrecke, E. H., Cecconi, F., Codogno, P., Debnath, J., Gewirtz, D. A., Karantza, V., et al. (2015) · The EMBO Journal · doi:10.15252/embj.201490784 · Cited by 1,182
Self-citationA Class of Membrane Proteins Shaping the Tubular Endoplasmic Reticulum
Voeltz, G. K., Prinz, W. A., Shibata, Y., Rist, J. M., & Rapoport, T. A. (2006) · Cell · doi:10.1016/j.cell.2005.11.047 · Cited by 1,152
The impact of the endoplasmic reticulum protein-folding environment on cancer development
Wang, M., & Kaufman, R. J. (2014) · Nature Reviews Cancer · doi:10.1038/nrc3800 · Cited by 1,112
Galectin 8 targets damaged vesicles for autophagy to defend cells against bacterial invasion
Thurston, T. L. M., Wandel, M. P., von Muhlinen, N., Foeglein, Á., & Randow, F. (2012) · Nature · doi:10.1038/nature10744 · Cited by 1,034
Suzuki, K. (2001) · The EMBO Journal · doi:10.1093/emboj/20.21.5971 · Cited by 1,033
Rogov, V., Dötsch, V., Johansen, T., & Kirkin, V. (2014) · Molecular Cell · doi:10.1016/j.molcel.2013.12.014 · Cited by 992
Heat shock proteins in cancer: chaperones of tumorigenesis
Calderwood, S. K., Khaleque, M. A., Sawyer, D. B., & Ciocca, D. R. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.01.006 · Cited by 957
Regulation of endoplasmic reticulum turnover by selective autophagy
Khaminets, A., Heinrich, T., Mari, M., Grumati, P., Huebner, A. K., Akutsu, M., Liebmann, L., Stolz, A., Nietzsche, S., Koch, N., et al. (2015) · Nature · doi:10.1038/nature14498 · Cited by 956
Targeting Autophagy in Cancer: Recent Advances and Future Directions
Amaravadi, R. K., Kimmelman, A. C., & Debnath, J. (2019) · Cancer Discovery · doi:10.1158/2159-8290.cd-19-0292 · Cited by 928
Heo, J.-M., Ordureau, A., Paulo, J. A., Rinehart, J., & Harper, J. W. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.08.016 · Cited by 906
Microautophagy of Cytosolic Proteins by Late Endosomes
Sahu, R., Kaushik, S., Clement, C. C., Cannizzo, E. S., Scharf, B., Follenzi, A., Potolicchio, I., Nieves, E., Cuervo, A. M., & Santambrogio, L. (2011) · Developmental Cell · doi:10.1016/j.devcel.2010.12.003 · Cited by 902
Kamphorst, J. J., Nofal, M., Commisso, C., Hackett, S. R., Lu, W., Grabocka, E., Vander Heiden, M. G., Miller, G., Drebin, J. A., Bar-Sagi, D., et al. (2015) · Cancer Research · doi:10.1158/0008-5472.can-14-2211 · Cited by 893
Mitochondrial DNA in inflammation and immunity
Riley, J. S., & Tait, S. W. (2020) · EMBO reports · doi:10.15252/embr.201949799 · Cited by 865
Autophagy-Independent Functions of the Autophagy Machinery
Galluzzi, L., & Green, D. R. (2019) · Cell · doi:10.1016/j.cell.2019.05.026 · Cited by 863
Hanna, R. A., Quinsay, M. N., Orogo, A. M., Giang, K., Rikka, S., & Gustafsson, Å. B. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.322933 · Cited by 762
p53 status determines the role of autophagy in pancreatic tumour development
Rosenfeldt, M. T., O’Prey, J., Morton, J. P., Nixon, C., MacKay, G., Mrowinska, A., Au, A., Rai, T. S., Zheng, L., Ridgway, R., et al. (2013) · Nature · doi:10.1038/nature12865 · Cited by 713
Lysosomal cell death at a glance
Aits, S., & Jäättelä, M. (2013) · Journal of Cell Science · doi:10.1242/jcs.091181 · Cited by 667
Autophagy mediates degradation of nuclear lamina
Dou, Z., Xu, C., Donahue, G., Shimi, T., Pan, J.-A., Zhu, J., Ivanov, A., Capell, B. C., Drake, A. M., Shah, P. P., et al. (2015) · Nature · doi:10.1038/nature15548 · Cited by 655
Role of peroxisomes in ros/rns-metabolism: Implications for human disease
Fransen, M., Nordgren, M., Wang, B., & Apanasets, O. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.12.001 · Cited by 644
Autophagy sequesters damaged lysosomes to control lysosomal biogenesis and kidney injury
Maejima, I., Takahashi, A., Omori, H., Kimura, T., Takabatake, Y., Saitoh, T., Yamamoto, A., Hamasaki, M., Noda, T., Isaka, Y., et al. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.171 · Cited by 642
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
Mitophagy receptor FUNDC1 regulates mitochondrial dynamics and mitophagy
Chen, M., Chen, Z., Wang, Y., Tan, Z., Zhu, C., Li, Y., Han, Z., Chen, L., Gao, R., Liu, L., et al. (2016) · Autophagy · doi:10.1080/15548627.2016.1151580 · Cited by 588
Shiba-Fukushima, K., Imai, Y., Yoshida, S., Ishihama, Y., Kanao, T., Sato, S., & Hattori, N. (2012) · Scientific Reports · doi:10.1038/srep01002 · Cited by 577
Cleaning house: selective autophagy of organelles
Anding, A. L., & Baehrecke, E. H. (2017) · Developmental Cell · doi:10.1016/j.devcel.2017.02.016 · Cited by 576
Distinct roles for cysteine cathepsin genes in multistage tumorigenesis
Gocheva, V., Zeng, W., Ke, D., Klimstra, D., Reinheckel, T., Peters, C., Hanahan, D., & Joyce, J. A. (2006) · Genes & Development · doi:10.1101/gad.1407406 · Cited by 570
Cytosolic lipolysis and lipophagy: two sides of the same coin
Zechner, R., Madeo, F., & Kratky, D. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.76 · Cited by 550
Microautophagy in mammalian cells: Revisiting a 40-year-old conundrum
Mijaljica, D., Prescott, M., & Devenish, R. J. (2011) · Autophagy · doi:10.4161/auto.7.7.14733 · Cited by 547
Ubiquitin signals autophagic degradation of cytosolic proteins and peroxisomes
Kim, P. K., Hailey, D. W., Mullen, R. T., & Lippincott-Schwartz, J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0810611105 · Cited by 532
Colell, A., Ricci, J.-E., Tait, S., Milasta, S., Maurer, U., Bouchier-Hayes, L., Fitzgerald, P., Guio-Carrion, A., Waterhouse, N. J., Li, C. W., et al. (2007) · Cell · doi:10.1016/j.cell.2007.03.045 · Cited by 516
Peroxisomal β-oxidation—A metabolic pathway with multiple functions
Poirier, Y., Antonenkov, V. D., Glumoff, T., & Hiltunen, J. K. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.08.034 · Cited by 499
Autophagy is critical for pancreatic tumor growth and progression in tumors with p53 alterations
Yang, A., Rajeshkumar, N. V., Wang, X., Yabuuchi, S., Alexander, B. M., Chu, G. C., Von Hoff, D. D., Maitra, A., & Kimmelman, A. C. (2014) · Cancer Discovery · doi:10.1158/2159-8290.cd-14-0362 · Cited by 486
Lysosomes as mediators of drug resistance in cancer
Zhitomirsky, B., & Assaraf, Y. G. (2016) · Drug Resistance Updates · doi:10.1016/j.drup.2015.11.004 · Cited by 482
Chauhan, S., Kumar, S., Jain, A., Ponpuak, M., Mudd, M. H., Kimura, T., Choi, S. W., Peters, R., Mandell, M., Bruun, J.-A., et al. (2016) · Developmental Cell · doi:10.1016/j.devcel.2016.08.003 · Cited by 480
Mitophagy is triggered by mild oxidative stress in a mitochondrial fission dependent manner
Frank, M., Duvezin-Caubet, S., Koob, S., Occhipinti, A., Jagasia, R., Petcherski, A., Ruonala, M. O., Priault, M., Salin, B., & Reichert, A. S. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.08.007 · Cited by 468
Translocon component Sec62 acts in endoplasmic reticulum turnover during stress recovery
Fumagalli, F., Noack, J., Bergmann, T. J., Cebollero, E., Pisoni, G. B., Fasana, E., Fregno, I., Galli, C., Loi, M., Soldà, T., et al. (2016) · Nature Cell Biology · doi:10.1038/ncb3423 · Cited by 464
Nixon-Abell, J., Obara, C. J., Weigel, A. V., Li, D., Legant, W. R., Xu, C. S., Pasolli, H. A., Harvey, K., Hess, H. F., Betzig, E., et al. (2016) · Science · doi:10.1126/science.aaf3928 · Cited by 455
Smith, M. D., Harley, M. E., Kemp, A. J., Wills, J., Lee, M., Arends, M., von Kriegsheim, A., Behrends, C., & Wilkinson, S. (2018) · Developmental Cell · doi:10.1016/j.devcel.2017.11.024 · Cited by 444
A dual role for autophagy in a murine model of lung cancer
Rao, S., Tortola, L., Perlot, T., Wirnsberger, G., Novatchkova, M., Nitsch, R., Sykacek, P., Frank, L., Schramek, D., Komnenovic, V., et al. (2014) · Nature Communications · doi:10.1038/ncomms4056 · Cited by 442
Full length RTN3 regulates turnover of tubular endoplasmic reticulum via selective autophagy
Grumati, P., Morozzi, G., Hölper, S., Mari, M., Harwardt, M.-L. I., Yan, R., Müller, S., Reggiori, F., Heilemann, M., & Dikic, I. (2017) · eLife · doi:10.7554/elife.25555 · Cited by 442
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
Parkin, a p53 target gene, mediates the role of p53 in glucose metabolism and the Warburg effect
Zhang, C., Lin, M., Wu, R., Wang, X., Yang, B., Levine, A. J., Hu, W., & Feng, Z. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1113884108 · Cited by 431
ATM functions at the peroxisome to induce pexophagy in response to ROS
Zhang, J., Tripathi, D. N., Jing, J., Alexander, A., Kim, J., Powell, R. T., Dere, R., Tait-Mulder, J., Lee, J.-H., Paull, T. T., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3230 · Cited by 426
Plasma cells require autophagy for sustainable immunoglobulin production
Pengo, N., Scolari, M., Oliva, L., Milan, E., Mainoldi, F., Raimondi, A., Fagioli, C., Merlini, A., Mariani, E., Pasqualetto, E., et al. (2013) · Nature Immunology · doi:10.1038/ni.2524 · Cited by 425
Autophagy in cancer: moving from understanding mechanism to improving therapy responses in patients
Mulcahy Levy, J. M., & Thorburn, A. (2020) · Cell Death & Differentiation · doi:10.1038/s41418-019-0474-7 · Cited by 416
Self-citationAMBRA1 is able to induce mitophagy via LC3 binding, regardless of PARKIN and p62/SQSTM1
Strappazzon, F., Nazio, F., Corrado, M., Cianfanelli, V, Romagnoli, A., Fimia, G. M., Campello, S., Nardacci, R., Piacentini, M., Campanella, M., et al. (2015) · Cell Death & Differentiation · doi:10.1038/cdd.2014.139 · Cited by 399
Targeting lipid metabolism of cancer cells: A promising therapeutic strategy for cancer
Liu, Q., Luo, Q., Halim, A., & Song, G. (2017) · Cancer Letters · doi:10.1016/j.canlet.2017.05.002 · Cited by 379
Intrinsically Disordered Protein TEX264 Mediates ER-phagy
Chino, H., Hatta, T., Natsume, T., & Mizushima, N. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.03.033 · Cited by 364
Mitochondrial DNA drives abscopal responses to radiation that are inhibited by autophagy
Yamazaki, T., Kirchmair, A., Sato, A., Buqué, A., Rybstein, M., Petroni, G., Bloy, N., Finotello, F., Stafford, L., Navarro Manzano, E., et al. (2020) · Nature Immunology · doi:10.1038/s41590-020-0751-0 · Cited by 359
Yang, A., Herter-Sprie, G., Zhang, H., Lin, E. Y., Biancur, D., Wang, X., Deng, J., Hai, J., Yang, S., Wong, K.-K., et al. (2018) · Cancer Discovery · doi:10.1158/2159-8290.cd-17-0952 · Cited by 349
Papadopoulos, C., Kirchner, P., Bug, M., Grum, D., Koerver, L., Schulze, N., Poehler, R., Dressler, A., Fengler, S., Arhzaouy, K., et al. (2017) · The EMBO Journal · doi:10.15252/embj.201695148 · Cited by 347
Mitochondria as therapeutic targets for cancer chemotherapy
Galluzzi, L., Larochette, N., Zamzami, N., & Kroemer, G. (2006) · Oncogene · doi:10.1038/sj.onc.1209598 · Cited by 337
Mitophagy defects arising from BNip3 loss promote mammary tumor progression to metastasis
Chourasia, A. H., Tracy, K., Frankenberger, C., Boland, M. L., Sharifi, M. N., Drake, L. E., Sachleben, J. R., Asara, J. M., Locasale, J. W., Karczmar, G. S., et al. (2015) · EMBO reports · doi:10.15252/embr.201540759 · Cited by 331
TRIM Proteins Regulate Autophagy and Can Target Autophagic Substrates by Direct Recognition
Mandell, M. A., Jain, A., Arko-Mensah, J., Chauhan, S., Kimura, T., Dinkins, C., Silvestri, G., Münch, J., Kirchhoff, F., Simonsen, A., et al. (2014) · Developmental Cell · doi:10.1016/j.devcel.2014.06.013 · Cited by 329
Role of autophagy in suppression of inflammation and cancer
White, E., Karp, C., Strohecker, A. M., Guo, Y., & Mathew, R. (2010) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.12.008 · Cited by 328
Parkin-Independent Mitophagy Controls Chemotherapeutic Response in Cancer Cells
Villa, E., Proïcs, E., Rubio-Patiño, C., Obba, S., Zunino, B., Bossowski, J. P., Rozier, R. M., Chiche, J., Mondragón, L., Riley, J. S., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.08.087 · Cited by 313
ATL3 Is a Tubular ER-Phagy Receptor for GABARAP-Mediated Selective Autophagy
Chen, Q., Xiao, Y., Chai, P., Zheng, P., Teng, J., & Chen, J. (2019) · Current Biology · doi:10.1016/j.cub.2019.01.041 · Cited by 304
The ER in 3D: a multifunctional dynamic membrane network
Friedman, J. R., & Voeltz, G. K. (2011) · Trends in Cell Biology · doi:10.1016/j.tcb.2011.07.004 · Cited by 300
An, H., Ordureau, A., Paulo, J. A., Shoemaker, C. J., Denic, V., & Harper, J. W. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.03.034 · Cited by 292
HUWE1 E3 ligase promotes PINK1/PARKIN-independent mitophagy by regulating AMBRA1 activation via IKKα
Di Rita, A., Peschiaroli, A., D′Acunzo, P., Strobbe, D., Hu, Z., Gruber, J., Nygaard, M., Lambrughi, M., Melino, G., Papaleo, E., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-05722-3 · Cited by 284
Molecular Principles of the Interactions of Disordered Proteins
Mészáros, B., Tompa, P., Simon, I., & Dosztányi, Z. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.07.004 · Cited by 278
Spatiotemporally controlled induction of autophagy-mediated lysosome turnover
Hung, Y.-H., Chen, L. M.-W., Yang, J.-Y., & Yuan Yang, W. (2013) · Nature Communications · doi:10.1038/ncomms3111 · Cited by 268
Role of tumor and host autophagy in cancer metabolism
Poillet-Perez, L., & White, E. (2019) · Genes & Development · doi:10.1101/gad.325514.119 · Cited by 266
Phosphorylated ubiquitin chain is the genuine Parkin receptor
Okatsu, K., Koyano, F., Kimura, M., Kosako, H., Saeki, Y., Tanaka, K., & Matsuda, N. (2015) · Journal of Cell Biology · doi:10.1083/jcb.201410050 · Cited by 263
Li, C., Zhang, Y., Cheng, X., Yuan, H., Zhu, S., Liu, J., Wen, Q., Xie, Y., Liu, J., Kroemer, G., et al. (2018) · Developmental Cell · doi:10.1016/j.devcel.2018.07.012 · Cited by 258
Antonucci, L., Fagman, J. B., Kim, J. Y., Todoric, J., Gukovsky, I., Mackey, M., Ellisman, M. H., & Karin, M. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1519384112 · Cited by 257
Stephani, M., Picchianti, L., Gajic, A., Beveridge, R., Skarwan, E., Sanchez de Medina Hernandez, V., Mohseni, A., Clavel, M., Zeng, Y., Naumann, C., et al. (2020) · eLife · doi:10.7554/elife.58396 · Cited by 253
Ostenfeld, M. S., Fehrenbacher, N., Høyer-Hansen, M., Thomsen, C., Farkas, T., & Jäättelä, M. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-0269 · Cited by 248
Lipid Droplets: A New Player in Colorectal Cancer Stem Cells Unveiled by Spectroscopic Imaging
Tirinato, L., Liberale, C., Di Franco, S., Candeloro, P., Benfante, A., La Rocca, R., Potze, L., Marotta, R., Ruffilli, R., Rajamanickam, V. P., et al. (2015) · Stem Cells · doi:10.1002/stem.1837 · Cited by 245
Mandic, A., Viktorsson, K., Strandberg, L., Heiden, T., Hansson, J., Linder, S., & Shoshan, M. C. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.9.3003-3013.2002 · Cited by 245
Davenport, E. L., Moore, H. E., Dunlop, A. S., Sharp, S. Y., Workman, P., Morgan, G. J., & Davies, F. E. (2007) · Blood · doi:10.1182/blood-2006-11-053728 · Cited by 238
PPT1 Promotes Tumor Growth and Is the Molecular Target of Chloroquine Derivatives in Cancer
Rebecca, V. W., Nicastri, M. C., Fennelly, C., Chude, C. I., Barber-Rotenberg, J. S., Ronghe, A., McAfee, Q., McLaughlin, N. P., Zhang, G., Goldman, A. R., et al. (2019) · Cancer Discovery · doi:10.1158/2159-8290.cd-18-0706 · Cited by 238
Hydrogen peroxide generation in peroxisome proliferator-induced oncogenesis
Yeldandi, A. V., Rao, M. S., & Reddy, J. K. (2000) · Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis · doi:10.1016/s0027-5107(99)00234-1 · Cited by 225
Wu, J., Chen, S., Liu, H., Zhang, Z., Ni, Z., Chen, J., Yang, Z., Nie, Y., & Fan, D. (2018) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-018-0935-8 · Cited by 223
No Parkin Zone: Mitophagy without Parkin
Villa, E., Marchetti, S., & Ricci, J.-E. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.07.004 · Cited by 221
Denmeade, S. R., Mhaka, A. M., Rosen, D. M., Brennen, W. N., Dalrymple, S., Dach, I., Olesen, C., Gurel, B., DeMarzo, A. M., Wilding, G., et al. (2012) · Science Translational Medicine · doi:10.1126/scitranslmed.3003886 · Cited by 220
Erdal, H., Berndtsson, M., Castro, J., Brunk, U., Shoshan, M. C., & Linder, S. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408592102 · Cited by 218
Parkin as a tumor suppressor gene for hepatocellular carcinoma
Fujiwara, M., Marusawa, H., Wang, H.-Q., Iwai, A., Ikeuchi, K., Imai, Y., Kataoka, A., Nukina, N., Takahashi, R., & Chiba, T. (2008) · Oncogene · doi:10.1038/onc.2008.199 · Cited by 218
Groth-Pedersen, L., Ostenfeld, M. S., Høyer-Hansen, M., Nylandsted, J., & Jäättelä, M. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-3520 · Cited by 215
Bröker, L. E., Huisman, C., Span, S. W., Rodriguez, J. A., Kruyt, F. A. E., & Giaccone, G. (2004) · Cancer Research · doi:10.1158/0008-5472.can-03-3060 · Cited by 206
Autophagy Inhibition Mediates Apoptosis Sensitization in Cancer Therapy by Relieving FOXO3a Turnover
Fitzwalter, B. E., Towers, C. G., Sullivan, K. D., Andrysik, Z., Hoh, M., Ludwig, M., O'Prey, J., Ryan, K. M., Espinosa, J. M., Morgan, M. J., et al. (2018) · Developmental Cell · doi:10.1016/j.devcel.2018.02.014 · Cited by 206
Self-citationCombating apoptosis and multidrug resistant cancers by targeting lysosomes
Groth-Pedersen, L., & Jäättelä, M. (2013) · Cancer Letters · doi:10.1016/j.canlet.2010.05.021 · Cited by 193
Expanding perspectives on the significance of mitophagy in cancer
Drake, L. E., Springer, M. Z., Poole, L. P., Kim, C. J., & Macleod, K. F. (2017) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2017.04.008 · Cited by 184
Autophagy as a therapeutic target in pancreatic cancer
Piffoux, M., Eriau, E., & Cassier, P. A. (2021) · British Journal of Cancer · doi:10.1038/s41416-020-01039-5 · Cited by 181
PEX2 is the E3 ubiquitin ligase required for pexophagy during starvation
Sargent, G., van Zutphen, T., Shatseva, T., Zhang, L., Di Giovanni, V., Bandsma, R., & Kim, P. K. (2016) · Journal of Cell Biology · doi:10.1083/jcb.201511034 · Cited by 180
Autophagy inhibition overcomes multiple mechanisms of resistance to BRAF inhibition in brain tumors
Mulcahy Levy, J. M., Zahedi, S., Griesinger, A. M., Morin, A., Davies, K. D., Aisner, D. L., Kleinschmidt-DeMasters, B., Fitzwalter, B. E., Goodall, M. L., Thorburn, J., et al. (2017) · eLife · doi:10.7554/elife.19671 · Cited by 175
Self-citationRegulation of inflammasomes by autophagy
Saitoh, T., & Akira, S. (2016) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2016.05.009 · Cited by 173
Mitochondria: gatekeepers of response to chemotherapy
Sarosiek, K. A., Ni Chonghaile, T., & Letai, A. (2013) · Trends in Cell Biology · doi:10.1016/j.tcb.2013.08.003 · Cited by 171
Pexophagy: The Selective Degradation of Peroxisomes
Till, A., Lakhani, R., Burnett, S. F., & Subramani, S. E. (2012) · International Journal of Cell Biology · doi:10.1155/2012/512721 · Cited by 169
Yan, C., Luo, L., Guo, C.-Y., Goto, S., Urata, Y., Shao, J.-H., & Li, T.-S. (2017) · Cancer Letters · doi:10.1016/j.canlet.2016.11.018 · Cited by 169
ESCRT-III-driven piecemeal micro-ER-phagy remodels the ER during recovery from ER stress
Loi, M., Raimondi, A., Morone, D., & Molinari, M. (2019) · Nature Communications · doi:10.1038/s41467-019-12991-z · Cited by 168
Differential Expression of Lipid Metabolism-Related Proteins in Different Breast Cancer Subtypes
Kim, S., Lee, Y., & Koo, J. S. (2015) · PLOS ONE · doi:10.1371/journal.pone.0119473 · Cited by 161
The Genomic Landscape of Renal Oncocytoma Identifies a Metabolic Barrier to Tumorigenesis
Joshi, S., Tolkunov, D., Aviv, H., Hakimi, A. A., Yao, M., Hsieh, J. J., Ganesan, S., Chan, C. S., & White, E. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.10.059 · Cited by 161
FAM 134B oligomerization drives endoplasmic reticulum membrane scission for ER ‐phagy
Jiang, X., Wang, X., Ding, X., Du, M., Li, B., Weng, X., Zhang, J., Li, L., Tian, R., Zhu, Q., et al. (2020) · The EMBO Journal · doi:10.15252/embj.2019102608 · Cited by 161
Lysosomal disruption preferentially targets acute myeloid leukemia cells and progenitors
Sukhai, M. A., Prabha, S., Hurren, R., Rutledge, A. C., Lee, A. Y., Sriskanthadevan, S., Sun, H., Wang, X., Škrtić, M., Seneviratne, A. K., et al. (2012) · Journal of Clinical Investigation · doi:10.1172/jci64180 · Cited by 155
Mahalingam, D., Wilding, G., Denmeade, S. R., Sarantopoulas, J., Cosgrove, D., Cetnar, J. P., Azad, N. S., Bruce, J. Y., Kurman, M. R., Allgood, V., et al. (2016) · British Journal of Cancer · doi:10.1038/bjc.2016.72 · Cited by 155
Yao, N., Wang, C., Hu, N., Li, Y., Liu, M., Lei, Y., Chen, M., Chen, L., Chen, C., Lan, P., et al. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1470-z · Cited by 154
CALCOCO1 acts with VAMP‐associated proteins to mediate ER‐phagy
Nthiga, T. M., Shrestha, B. K., Sjøttem, E., Bruun, J., Larsen, K. B., Bhujabal, Z., Lamark, T., & Johansen, T. (2020) · The EMBO Journal · doi:10.15252/embj.2019103649 · Cited by 152
Mitochondria and the hallmarks of cancer
Giampazolias, E., & Tait, S. W. G. (2015) · FEBS Journal · doi:10.1111/febs.13603 · Cited by 145
Sensitization to the Lysosomal Cell Death Pathway upon Immortalization and Transformation
Fehrenbacher, N., Gyrd‐Hansen, M., Poulsen, B., Felbor, U., Kallunki, T., Boes, M. L., Weber, E., Leist, M., & Jäättelä, M. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-1427 · Cited by 144
Dynamic nanoscale morphology of the ER surveyed by STED microscopy
Schroeder, L. K., Barentine, A. E. S., Merta, H., Schweighofer, S., Zhang, Y., Baddeley, D., Bewersdorf, J., & Bahmanyar, S. (2018) · The Journal of Cell Biology · doi:10.1083/jcb.201809107 · Cited by 140
Cross-cancer profiling of molecular alterations within the human autophagy interaction network
Lebovitz, C. B., Robertson, A. G., Goya, R., Jones, S. J. M., Morin, R. D., Marra, M. A., & Gorski, S. M. (2015) · Autophagy · doi:10.1080/15548627.2015.1067362 · Cited by 139
Nieva, C., Marro, M., Santana-Codina, N., Rao, S. K., Petrov, D. V., & Sierra, À. (2012) · PLoS ONE · doi:10.1371/journal.pone.0046456 · Cited by 137
Vorinostat Induces Reactive Oxygen Species and DNA Damage in Acute Myeloid Leukemia Cells
Petruccelli, L. A., Dupéré-Richer, D., Pettersson, F., Retrouvey, H., Skoulikas, S., & Miller, W. H. (2011) · PLoS ONE · doi:10.1371/journal.pone.0020987 · Cited by 133
The ubiquitin‐conjugating enzyme UBE2QL1 coordinates lysophagy in response to endolysosomal damage
Koerver, L., Papadopoulos, C., Liu, B., Kravić, B., Rota, G., Brecht, L., Veenendaal, T., Polajnar, M., Bluemke, A., Ehrmann, M., et al. (2019) · EMBO Reports · doi:10.15252/embr.201948014 · Cited by 132
Werneburg, N. W., Guicciardi, M. E., Bronk, S. F., Kaufmann, S. H., & Gores, G. J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705671200 · Cited by 127
Jang, Y. M., Kendaiah, S., Drew, B., Phillips, T., Selman, C., Julian, D. A., & Leeuwenburgh, C. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.10.053 · Cited by 126
Autophagic Degradation of NBR1 Restricts Metastatic Outgrowth during Mammary Tumor Progression
Marsh, T., Kenific, C. M., Suresh, D., Velozo, H. G., Shamir, E. R., Mei, W., Tankka, A. T., Leidal, A. M., Kalavacherla, S., Woo, K., et al. (2020) · Developmental Cell · doi:10.1016/j.devcel.2020.01.025 · Cited by 124
p62/SQSTM1 synergizes with autophagy for tumor growth in vivoPreprint
Wei, H., Wang, C., Croce, C. M., & Guan, J. (2014) · Genes & Development · doi:10.1101/gad.237354.113 · Cited by 120
Dysregulation of mitophagy in carcinogenesis and tumor progression
Chang, J. Y., Yi, H., Kim, H.-W., & Shong, M. (2016) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2016.12.008 · Cited by 119
Menard, J. A., Christianson, H. C., Kucharzewska, P., Bourseau-Guilmain, E., Svensson, K. J., Lindqvist, E., Chandran, V. I., Kjellén, L., Welinder, C., Bengzon, J., et al. (2016) · Cancer Research · doi:10.1158/0008-5472.can-15-2831 · Cited by 115
α‐Methylacyl‐CoA racemase – an ‘obscure’ metabolic enzyme takes centre stage
Lloyd, M. D., Darley, D. J., Wierzbicki, A. S., & Threadgill, M. D. (2008) · FEBS Journal · doi:10.1111/j.1742-4658.2008.06290.x · Cited by 114
Kim, J.-H., Kim, H. Y., Lee, Y., Yoon, Y.-S., Xu, W. G., Yoon, J., Choi, S., Ko, Y., Kim, M. J., Lee, S., et al. (2011) · Autophagy · doi:10.4161/auto.7.10.16643 · Cited by 112
Wnt canonical pathway activates macropinocytosis and lysosomal degradation of extracellular proteins
Tejeda‐Muñoz, N., Albrecht, L. V., Bui, M. H., & Robertis, E. M. D. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1903506116 · Cited by 108
Hostetler, H. A., Kier, A. B., & Schroeder, F. (2006) · Biochemistry · doi:10.1021/bi060198l · Cited by 103
Cancer Cells Upregulate NRF2 Signaling to Adapt to Autophagy Inhibition
Towers, C. G., Fitzwalter, B. E., Regan, D. P., Goodspeed, A. E., Morgan, M. J., Liu, C., Gustafson, D. L., & Thorburn, A. M. (2019) · Developmental Cell · doi:10.1016/j.devcel.2019.07.010 · Cited by 101
Self-citationWeng, L., Du, J., Zhou, Q.-H., Cheng, B., Li, J., Zhang, D., & Ling, C. (2012) · Molecular Cancer · doi:10.1186/1476-4598-11-39 · Cited by 86
Mukhopadhyay, S., Schlaepfer, I. R., Bergman, B. C., Panda, P. K., Praharaj, P. P., Naik, P. P., Agarwal, R., & Bhutia, S. K. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.01.007 · Cited by 85
Catalase inhibition induces pexophagy through ROS accumulation
Lee, J. N., Dutta, R. K., Maharjan, Y., Liu, Z., Lim, J.-Y., Kim, S.-J., Cho, D., So, H., Choe, S., & Park, R. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.05.050 · Cited by 77
A dietary enzyme: α-methylacyl-CoA racemase/P504S is overexpressed in colon carcinoma
Jiang, Z., Fanger, G. R., Banner, B. F., Woda, B. A., Algate, P. A., Dresser, K., Xu, J., Reed, S. G., Rock, K. L., & Chu, P. G. (2003) · Cancer Detection and Prevention · doi:10.1016/j.cdp.2003.07.003 · Cited by 74
Apoptosis and Cancer: Force Awakens, Phantom Menace, or Both?
Cao, K., & Tait, S. W. G. (2018) · International review of cytology · doi:10.1016/bs.ircmb.2017.12.003 · Cited by 74
Sec62 Bridges the Gap from 3q Amplification to Molecular Cell Biology in Non–Small Cell Lung Cancer
Linxweiler, M., Linxweiler, J., Barth, M., Benedix, J., Jung, V., Kim, Y.-J., Bohle, R. M., Zimmermann, R., & Greiner, M. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2011.10.039 · Cited by 73
Misra, P., & Reddy, J. K. (2013) · Biochimie · doi:10.1016/j.biochi.2013.11.011 · Cited by 70
Wible, D. J., Chao, H., Tang, D. G., & Bratton, S. B. (2019) · Cell Discovery · doi:10.1038/s41421-019-0110-1 · Cited by 70
Zhao, T., Du, H., Ding, X., Walls, K., & Yan, C. (2014) · Oncogene · doi:10.1038/onc.2014.143 · Cited by 69
Kaini, R. R., Sillerud, L. O., Zhaorigetu, S., & Hu, C. A. (2012) · The Prostate · doi:10.1002/pros.22489 · Cited by 68
RETREG1 ( FAM134B ): A new player in human diseases: 15 years after the discovery in cancer
Islam, F., Gopalan, V., & Lam, A. K.-Y. (2017) · Journal of Cellular Physiology · doi:10.1002/jcp.26384 · Cited by 66
Silencing of the SEC62 gene inhibits migratory and invasive potential of various tumor cells
Greiner, M., Kreutzer, B., Jung, V., Grobholz, R., Hasenfus, A., Stöhr, R., Tornillo, L., Dudek, J., Stöckle, M., Unteregger, G., et al. (2010) · International Journal of Cancer · doi:10.1002/ijc.25580 · Cited by 63
Yu, S., & Kim, S. J. (2010) · Experimental & Molecular Medicine · doi:10.3858/emm.2010.42.11.079 · Cited by 62
Induction of endoplasmic reticulum stress by ellipticine plant alkaloids
Hägg, M., Berndtsson, M., Mandic, A., Zhou, R., Shoshan, M. C., & Linder, S. T. (2004) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.489.3.4 · Cited by 61
Repurposing Brigatinib for the Treatment of Colorectal Cancer Based on Inhibition of ER-phagy
Zhang, Z., Gao, W. Q., Zhou, L., Chen, Y., Qin, S., Zhang, L., Liu, J., He, Y., Lei, Y., Chen, H., et al. (2019) · Theranostics · doi:10.7150/thno.36254 · Cited by 61
Jung, V., Kindich, R., Kamradt, J., Jung, M., Müller, M., Schulz, W. A., Engers, R., Unteregger, G., Stöckle, M., Zimmermann, R., et al. (2006) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-05-0165 · Cited by 60
Regulation of Apoptosis by Autophagy to Enhance Cancer Therapy.
Tompkins, K. D., & Thorburn, A. M. (2019) · PubMed Central · Cited by 59
Self-citationCritical Roles of Lysosomal Acid Lipase in T Cell Development and Function
Qu, P., Du, H., Wilkes, D. S., et al. (2009) · American Journal Of Pathology · doi:10.2353/ajpath.2009.080562 · Cited by 58
Tang, W. C., Chui, C. H., Fatima, S., Kok, S., Pak, K. C., Ou, T., Hui, K., Wong, M., Wong, J., Law, S. Y.-K., et al. (2007) · International Journal of Molecular Medicine · doi:10.3892/ijmm.19.6.915 · Cited by 57
Rak, S., Zan, T. D., Štefulj, J., Kosović, M., Gamulin, O., & Osmak, M. (2014) · The Analyst · doi:10.1039/c4an00412d · Cited by 56
Increased transport of acetyl‐CoA into the endoplasmic reticulum causes a progeria‐like phenotype
Peng, Y., Shapiro, S. L., Banduseela, V. C., Dieterich, I. A., Hewitt, K. J., Bresnick, E. H., Kong, G., Zhang, J., Schueler, K. L., Keller, M. P., et al. (2018) · Aging Cell · doi:10.1111/acel.12820 · Cited by 56
Witkiewicz, A. K., Varambally, S., Shen, R., Mehra, R., Sabel, M. S., Ghosh, D., Chinnaiyan, A. M., Rubin, M. A., & Kleer, C. G. (2005) · Cancer Epidemiology Biomarkers & Prevention · doi:10.1158/1055-9965.epi-04-0607 · Cited by 55
Microtargeting cancer metabolism: opening new therapeutic windows based on lipid metabolism
de Cedrón, M. G., & de Molina, A. R. (2016) · Journal of Lipid Research · doi:10.1194/jlr.r061812 · Cited by 50
Degradation of excess peroxisomes in mammalian liver cells by autophagy and other mechanisms
Yokota, S., & Fahimi, H. D. (2009) · Histochemistry and Cell Biology · doi:10.1007/s00418-009-0564-6 · Cited by 48
Zhang, Z., Wang, N., Ma, Q., Chen, Y., Li, Y., Zhang, L., Li, Q., Shi, M., Wang, H., & Ying, Z. (2019) · Acta Pharmacologica Sinica · doi:10.1038/s41401-019-0260-6 · Cited by 48
Panda, P. K., Patra, S., Naik, P. P., Praharaj, P. P., Mukhopadhyay, S., Meher, B. R., Gupta, P. K., Verma, R. S., Maiti, T. K., & Bhutia, S. K. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.29182 · Cited by 46
The roles of JK-1 (FAM134B) expressions in colorectal cancer
Kasem, K., Gopalan, V., Salajegheh, A., Lu, C., Smith, R. A., & Lam, A. K.-Y. (2014) · Experimental Cell Research · doi:10.1016/j.yexcr.2014.06.013 · Cited by 44
Du, H., Zhao, T., Ding, X., & Yan, C. (2015) · American Journal Of Pathology · doi:10.1016/j.ajpath.2015.05.021 · Cited by 44
Initial evidence for Sec62 as a prognostic marker in advanced head and neck squamous cell carcinoma
Wemmert, S., LINDNER, Y., Linxweiler, J., Wagenpfeil, S., Bohle, R. M., Niewald, M., & Schick, B. (2016) · Oncology Letters · doi:10.3892/ol.2016.4135 · Cited by 39
Involvement of mitophagy in cisplatin-induced cell death regulation
Abdrakhmanov, A., Kulikov, A. V., Luchkina, E. A., Zhivotovsky, B., & Gogvadze, V. G. (2018) · Biological Chemistry · doi:10.1515/hsz-2018-0210 · Cited by 38
Nishimura, Y., Sameni, M., & Sloane, B. F. (1998) · Pathology & Oncology Research · doi:10.1007/bf02905219 · Cited by 37
Li, C., Fang, F.-M., Lan, J., Wang, J., Kung, H.-J., Chen, L., Chen, T.-J., Li, S.-H., Wang, Y.-H., Tai, H.-C., et al. (2014) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-1182 · Cited by 37
Linxweiler, M., Bochen, F., Schick, B., Wemmert, S., Kadah, B. A., Greiner, M., Hasenfus, A., Bohle, R.-M., Juhasz‐Böss, I., Solomayer, E., et al. (2016) · BMC Cancer · doi:10.1186/s12885-016-2739-6 · Cited by 33
Kasem, K., Gopalan, V., Salajegheh, A., Lu, C., Smith, R. A., & Lam, A. K.-Y. (2014) · Experimental and Molecular Pathology · doi:10.1016/j.yexmp.2014.05.001 · Cited by 32
Effects of antilipolytic agents on rat liver peroxisomes and peroxisomal oxidative activities
Cubeddu, T., Masiello, P., Pollera, M., & Bergamini, E. (1985) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(85)90186-2 · Cited by 31
Regulation of lysosome integrity and lysophagy by the ubiquitin-conjugating enzyme UBE2QL1
Kravić, B., Behrends, C., & Meyer, H. H. (2019) · Autophagy · doi:10.1080/15548627.2019.1687217 · Cited by 31
Erythroleukemia cells acquire an alternative mitophagy capability
Wang, J., Fang, Y., Yan, L., Yuan, N., Zhang, S., Li, X., Nie, M., Zhang, X., & Wang, J. (2016) · Scientific Reports · doi:10.1038/srep24641 · Cited by 30
Zhao, T., Ding, X., Du, H., & Yan, C. (2016) · American Journal Of Pathology · doi:10.1016/j.ajpath.2016.04.014 · Cited by 28
High content screening for nonclassical peroxisome proliferators
Sexton, J. Z., He, Q., Forsberg, L. J., & Brenman, J. E. (2010) · International Journal of High Throughput Screening · doi:10.2147/ijhts.s10547 · Cited by 26
Box, A. H., Alshalalfa, M., Hegazy, S. A., et al. (2016) · Tumor Biology · doi:10.1007/s13277-016-5075-1 · Cited by 25
Zhang, N., Sheng, M., Wu, M., Zhang, X., Ding, Y., Lin, Y., Yu, W., Wang, S., & Du, H. (2019) · Experimental Biology and Medicine · doi:10.1177/1535370219878651 · Cited by 20
Kostenko, E. V., Olabisi, O. O., Sahay, S., Rodriguez, P. L., & Whitehead, I. P. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00670-06 · Cited by 18
Jindal, Y. (2016) · JOURNAL OF CLINICAL AND DIAGNOSTIC RESEARCH · doi:10.7860/jcdr/2016/19539.8721 · Cited by 16
Removing the waste bags: how p97 drives autophagy of lysosomes
Seczyńska, M., & Đikić, I. (2016) · The EMBO Journal · doi:10.15252/embj.201695950 · Cited by 9
Circumventing autophagy inhibition
Towers, C. G., & Thorburn, A. M. (2019) · Cell Cycle · doi:10.1080/15384101.2019.1692483 · Cited by 7
Self-citation
Cited by
Autophagy in major human diseases
Klionsky, D. J., Petroni, G., Amaravadi, R. K., Baehrecke, E. H., Ballabio, A., Boya, P., Bravo‐San Pedro, J. M., Cadwell, K., Cecconi, F., Choi, A. M. K., et al. (2021) · The EMBO Journal · doi:10.15252/embj.2021108863 · Cited by 1,585
Metadata
- Authors
- Miller, D. R., & Thorburn, A.
- Venue
- Developmental Cell
- Publisher
- Elsevier BV
- Published
- 2021-04
- Volume
- 56
- Issue
- 7
- Pages
- 906-918
- ISSN
- 1534-5807 (ISSN-L)
- OpenAlex
- W3134787367
- Cited by
- 258
- References
- 196
- FWCI
- 20.37
- 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.