Autophagy, mitochondria and oxidative stress: cross-talk and redox signalling.

How mitochondria produce reactive oxygen species

Murphy, M. P. (2009) · Biochemical Journal · doi:10.1042/bj20081386 · Cited by 8,207

Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis

Rosen, D. R., Siddique, T., Patterson, D., Figlewicz, D. A., Sapp, P., Hentati, A., Donaldson, D., Goto, J., O'Regan, J. P., Deng, H.-X., et al. (1993) · Nature · doi:10.1038/362059a0 · Cited by 7,062

Apparent hydroxyl radical production by peroxynitrite: Implications for endothelial injury from nitric oxide and superoxide

Beckman, J. S., Beckman, T. W., Chen, J., Marshall, P. A., & Freeman, B. A. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.4.1620 · Cited by 7,029

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

Nitric Oxide and Peroxynitrite in Health and Disease

Pacher, P., Beckman, J. S., & Liaudet, L. (2007) · Physiological Reviews · doi:10.1152/physrev.00029.2006 · Cited by 6,390

p62/SQSTM1 Binds Directly to Atg8/LC3 to Facilitate Degradation of Ubiquitinated Protein Aggregates by Autophagy

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

Motor Neuron Degeneration in Mice that Express a Human Cu,Zn Superoxide Dismutase Mutation

Gurney, M. E., Pu, H., Chiu, A. Y., Dal Canto, M. C., Polchow, C. Y., Alexander, D. D., Caliendo, J., Hentati, A., Kwon, Y. W., Deng, H.-X., et al. (1994) · Science · doi:10.1126/science.8209258 · Cited by 4,143

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

An Nrf2/Small Maf Heterodimer Mediates the Induction of Phase II Detoxifying Enzyme Genes through Antioxidant Response Elements

Itoh, K., Chiba, T., Takahashi, S., Ishii, T., Igarashi, K., Katoh, Y., Oyake, T., Hayashi, N., Satoh, K., Hatayama, I., et al. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.6943 · Cited by 3,999

Guidelines for the use and interpretation of assays for monitoring autophagy

Klionsky, D. J., Abdalla, F. C., Abeliovich, H., Abraham, R. T., Acevedo-Arozena, A., Adeli, K., Agholme, L., Agnello, M., Agostinis, P., Aguirre-Ghiso, J. A., et al. (2012) · Autophagy · doi:10.4161/auto.19496 · Cited by 3,996

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

Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain

Itoh, K., Wakabayashi, N., Katoh, Y., Ishii, T., Igarashi, K., Engel, J. D., & Yamamoto, M. (1999) · Genes & Development · doi:10.1101/gad.13.1.76 · Cited by 3,634

Regulation mechanisms and signaling pathways of autophagy

He, C., & Klionsky, D. J. (2009) · Annual Review of Genetics · doi:10.1146/annurev-genet-102808-114910 · Cited by 3,609

Autophagy and the Integrated Stress Response

Kroemer, G., Mariño, G., & Levine, B. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.023 · Cited by 3,506

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

Hereditary Early-Onset Parkinson's Disease Caused by Mutations in PINK1

Valente, E. M., Abou-Sleiman, P. M., Caputo, V., Muqit, M. M. K., Harvey, K., Gispert, S., Ali, Z., Del Turco, D., Bentivoglio, A. R., Healy, D. G., et al. (2004) · Science · doi:10.1126/science.1096284 · Cited by 3,481

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

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

Fission and selective fusion govern mitochondrial segregation and elimination by autophagy

Twig, G., Elorza, A., Molina, A. J. A., Mohamed, H., Wikstrom, J. D., Walzer, G., Stiles, L., Haigh, S. E., Katz, S., Las, G., et al. (2008) · The EMBO Journal · doi:10.1038/sj.emboj.7601963 · Cited by 3,082

Autophagy proteins regulate innate immune responses by inhibiting the release of mitochondrial DNA mediated by the NALP3 inflammasome

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

Functions of Lysosomes

de Duve, C., & Wattiaux, R. (1966) · Annual Review of Physiology · doi:10.1146/annurev.ph.28.030166.002251 · Cited by 3,033 · cited 1×

PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1

Geisler, S., Holmström, K. M., Skujat, D., Fiesel, F. C., Rothfuss, O. C., Kahle, P. J., & Springer, W. (2010) · Nature Cell Biology · doi:10.1038/ncb2012 · Cited by 2,835

Phosphorylation of ULK1 (hATG1) by AMP-Activated Protein Kinase Connects Energy Sensing to Mitophagy

Egan, D. F., Shackelford, D. B., Mihaylova, M. M., Gelino, S., Kohnz, R. A., Mair, W., Vasquez, D. S., Joshi, A., Gwinn, D. M., Taylor, R., et al. (2011) · Science · doi:10.1126/science.1196371 · Cited by 2,600

Ragulator-Rag Complex Targets mTORC1 to the Lysosomal Surface and Is Necessary for Its Activation by Amino Acids

Sancak, Y., Bar-Peled, L., Zoncu, R., Markhard, A. L., Nada, S., & Sabatini, D. M. (2010) · Cell · doi:10.1016/j.cell.2010.02.024 · Cited by 2,464

Impairment of starvation-induced and constitutive autophagy in Atg7 -deficient mice

Komatsu, M., Waguri, S., Ueno, T., Iwata, J., Murata, S., Tanida, I., Ezaki, J., Mizushima, N., Ohsumi, Y., Uchiyama, Y., et al. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200412022 · Cited by 2,331

Cellular response to oxidative stress: Signaling for suicide and survival*

Martindale, J. L., & Holbrook, N. J. (2002) · Journal of Cellular Physiology · doi:10.1002/jcp.10119 · Cited by 2,314

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

Mitochondrial Complex I Deficiency in Parkinson's Disease

Schapira, A. H. V., Cooper, J. M., Dexter, D., Clark, J. B., Jenner, P., & Marsden, C. D. (1990) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1990.tb02325.x · Cited by 2,283

Dissection of the Autophagosome Maturation Process by a Novel Reporter Protein, Tandem Fluorescent-Tagged LC3

Kimura, S., Noda, T., & Yoshimori, T. (2007) · Autophagy · doi:10.4161/auto.4451 · Cited by 2,278

Guidelines for the use and interpretation of assays for monitoring autophagy in higher eukaryotes

Klionsky, D. J., Abeliovich, H., Agostinis, P., Agrawal, D. K., Aliev, G., Askew, D. S., Baba, M., Baehrecke, E. H., Bahr, B. A., Ballabio, A., et al. (2008) · Autophagy · doi:10.4161/auto.5338 · Cited by 2,230

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

Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4

Scherz‐Shouval, R., Shvets, E., Fass, E., Shorer, H., Gil, L., & Elazar, Z. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601623 · Cited by 2,101

TIGAR, a p53-Inducible Regulator of Glycolysis and Apoptosis

Bensaad, K., Tsuruta, A., Selak, M. A., Vidal, M. N. C., Nakano, K., Bartrons, R., Gottlieb, E., & Vousden, K. H. (2006) · Cell · doi:10.1016/j.cell.2006.05.036 · Cited by 2,019

Mitochondrial DNA damage is more extensive and persists longer than nuclear DNA damage in human cells following oxidative stress

Yakes, F. M., & Van Houten, B. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.2.514 · Cited by 1,854

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., Gélinas, C., et al. (2009) · Cell · doi:10.1016/j.cell.2009.03.048 · Cited by 1,774

MITOCHONDRIAL COMPLEX I DEFICIENCY IN PARKINSON'S DISEASE

Schapira, A. H. V., Cooper, J. A. D., Dexter, D. T., Jenner, P. G., Clark, J. B., & MARSDEN, C. D. (1989) · The Lancet · doi:10.1016/s0140-6736(89)92366-0 · Cited by 1,757

High levels of mitochondrial DNA deletions in substantia nigra neurons in aging and Parkinson disease

Bender, A., Krishnan, K. J., Morris, C. M., Taylor, G. A., Reeve, A. K., Perry, R. H., Jaros, E., Hersheson, J. S., Betts, J., Klopstock, T., et al. (2006) · Nature Genetics · doi:10.1038/ng1769 · Cited by 1,570

Selective degradation of mitochondria by mitophagy

Kim, I., Rodriguez-Enriquez, S., & Lemasters, J. J. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.03.034 · Cited by 1,558

Network organization of the human autophagy system

Behrends, C., Sowa, M. E., Gygi, S. P., & Harper, J. W. (2010) · Nature · doi:10.1038/nature09204 · Cited by 1,554

Termination of autophagy and reformation of lysosomes regulated by mTOR

Yu, L., McPhee, C. K., Zheng, L., Mardones, G. A., Rong, Y., Peng, J., Mi, N., Zhao, Y., Liu, Z., Wan, F., et al. (2010) · Nature · doi:10.1038/nature09076 · Cited by 1,544

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

LC3 conjugation system in mammalian autophagy

Tanida, I., Ueno, T., & Kominami, E. (2004) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2004.05.009 · Cited by 1,512

Hypoxia-Induced Autophagy Is Mediated through Hypoxia-Inducible Factor Induction of BNIP3 and BNIP3L via Their BH3 Domains

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

FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells.

Zhao, J., Brault, J. J., Schild, A., Cao, P., Sandri, M., Schiaffino, S., Lecker, S. H., & Goldberg, A. L. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.11.004 · Cited by 1,489

Amyotrophic Lateral Ssclerosis and Structural Defects in Cu,Zn Superoxide Dismutase

Deng, H., Hentati, A., Tainer, J. A., Iqbal, Z., Cayabyab, A., Hung, W.-Y., Getzoff, E. D., Hu, P., Herzfeldt, B., Roos, R. P., et al. (1993) · Science · doi:10.1126/science.8351519 · Cited by 1,479

Basal Lipid Peroxidation in Substantia Nigra Is Increased in Parkinson's Disease

Dexter, D. T., Carter, C. J., Wells, F. R., Javoy-Agid, F., Agid, Y., Lees, A. J., Jenner, P. G., & MARSDEN, C. D. (1989) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1989.tb09133.x · Cited by 1,397

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

Transition metals, ferritin, glutathione, and ascorbic acid in parkinsonian brains

Riederer, P., Sofic, E., Rausch, W., Schmidt, B., Reynolds, G. P., Jellinger, K., & Youdim, M. B. H. (1989) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1989.tb09150.x · Cited by 1,383

DRAM, a p53-Induced Modulator of Autophagy, Is Critical for Apoptosis

Crighton, D., Wilkinson, S., O'Prey, J., Syed, N., Smith, P., Harrison, P. R., Gasco, M., Garrone, O., Crook, T., & Ryan, K. M. (2006) · Cell · doi:10.1016/j.cell.2006.05.034 · Cited by 1,380

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

Selective Mitochondrial Autophagy, or Mitophagy, as a Targeted Defense Against Oxidative Stress, Mitochondrial Dysfunction, and Aging

Lemasters, J. J. (2005) · Rejuvenation Research · doi:10.1089/rej.2005.8.3 · Cited by 1,342

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

p53 Target Genes Sestrin1 and Sestrin2 Connect Genotoxic Stress and mTOR Signaling

Budanov, A. V., & Karin, M. (2008) · Cell · doi:10.1016/j.cell.2008.06.028 · Cited by 1,326

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

Regulation of autophagy by ROS: physiology and pathology

Scherz-Shouval, R., & Elazar, Z. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.07.007 · Cited by 1,263

Widespread Peroxynitrite-Mediated Damage in Alzheimer’s Disease

Smith, M. A., Richey Harris, P. L., Sayre, L. M., Beckman, J. S., & Perry, G. (1997) · The Journal of Neuroscience · doi:10.1523/jneurosci.17-08-02653.1997 · Cited by 1,239

HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS.

Pandey, U. B., Nie, Z., Batlevi, Y., McCray, B. A., Ritson, G. P., Nedelsky, N. B., Schwartz, S. L., DiProspero, N. A., Knight, M. A., Schuldiner, O., et al. (2007) · Nature · doi:10.1038/nature05853 · Cited by 1,234

Impaired Balance of Mitochondrial Fission and Fusion in Alzheimer's Disease

Wang, X., Su, B., Lee, H.-G., Li, X., Perry, G., Smith, M. A., & Zhu, X. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.1357-09.2009 · Cited by 1,224

Essential role for Nix in autophagic maturation of erythroid cells

Sandoval, H., Thiagarajan, P., Dasgupta, S. K., Schumacher, A., Prchal, J. T., Chen, M., & Wang, J. (2008) · Nature · doi:10.1038/nature07006 · Cited by 1,185

Alterations in glutathione levels in Parkinson's disease and other neurodegenerative disorders affecting basal ganglia

Sian, J., Dexter, D. T., Lees, A. J., Daniel, S., Agid, Y., Javoy‐Agid, F., Jenner, P., & Marsden, C. D. (1994) · Annals of Neurology · doi:10.1002/ana.410360305 · Cited by 1,161

Mitochondrial Import and Accumulation of α-Synuclein Impair Complex I in Human Dopaminergic Neuronal Cultures and Parkinson Disease Brain

Devi, L., Raghavendran, V., Prabhu, B. M., Avadhani, N. G., & Anandatheerthavarada, H. K. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m710012200 · Cited by 1,127

Autophagy mediates the mitotic senescence transition

Young, A. R. J., Narita, M., Ferreira, M., Kirschner, K., Sadaie, M., Darot, J. F. J., Tavaré, S., Arakawa, S., Shimizu, S., Watt, F. M., et al. (2009) · Genes & Development · doi:10.1101/gad.519709 · Cited by 1,078

A Role for NBR1 in Autophagosomal Degradation of Ubiquitinated Substrates

Kirkin, V., Lamark, T., Sou, Y.-S., Bjørkøy, G., Nunn, J. L., Bruun, J.-A., Shvets, E., McEwan, D. G., Clausen, T. H., Wild, P., et al. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.01.020 · Cited by 1,065

Apoptosis and autophagy in nigral neurons of patients with Parkinson's disease.

Anglade, P., Vyas, S., Javoy-Agid, F., Herrero, M. T., Michel, P. P., Marquez, J., Prigent, A., Ruberg, M., Hirsch, É. C., & Agid, Y. (1997) · PubMed · Cited by 1,045

4‐Hydroxynonenal‐Derived Advanced Lipid Peroxidation End Products Are Increased in Alzheimer's Disease

Sayre, L., Zelasko, D. A., Harris, P. L. R., Perry, G., Salomon, R. G., & Smith, M. A. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.68052092.x · Cited by 1,032

Distinct regulation of autophagic activity by Atg14L and Rubicon associated with Beclin 1–phosphatidylinositol-3-kinase complex

Zhong, Y., Wang, Q. J., Li, X., Yan, Y., Backer, J. M., Chait, B. T., Heintz, N., & Yue, Z. (2009) · Nature Cell Biology · doi:10.1038/ncb1854 · Cited by 1,005

Immunohistochemical detection of 4-hydroxynonenal protein adducts in Parkinson disease.

Yoritaka, A., Hattori, N., Uchida, K., Tanaka, M., Stadtman, E. R., & Mizuno, Y. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.7.2696 · Cited by 981

NIX is required for programmed mitochondrial clearance during reticulocyte maturation

Schweers, R. L., Zhang, J., Randall, M. S., Loyd, M. R., Li, W., Dorsey, F. C., Kundu, M., Opferman, J. T., Cleveland, J. L., Miller, J. L., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0708818104 · Cited by 979

Role for Rab7 in maturation of late autophagic vacuoles

Jäger, S., Bucci, C., Tanida, I., Ueno, T., Kominami, E., Säftig, P., & Eskelinen, E. (2004) · Journal of Cell Science · doi:10.1242/jcs.01370 · Cited by 970

Primary LAMP-2 deficiency causes X-linked vacuolar cardiomyopathy and myopathy (Danon disease)

Nishino, I., Fu, J., Tanji, K., Yamada, T., Shimojo, S., Koori, T., Mora, M., Riggs, J. E., Oh, S. J., Koga, Y., et al. (2000) · Nature · doi:10.1038/35022604 · Cited by 959

Loss of PINK1 Function Promotes Mitophagy through Effects on Oxidative Stress and Mitochondrial Fission

Dagda, R. K., Cherra, S. J., Kulich, S. M., Tandon, A., Park, D., & Chu, C. T. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808515200 · Cited by 954

Accumulation of autophagic vacuoles and cardiomyopathy in LAMP-2-deficient mice

Tanaka, Y., Guhde, G., Suter, A., Eskelinen, E.-L., Hartmann, D., Lüllmann-Rauch, R., Janssen, P. M. L., Blanz, J., von Figura, K., & Saftig, P. (2000) · Nature · doi:10.1038/35022595 · Cited by 925

Mitofusin 1 and mitofusin 2 are ubiquitinated in a PINK1/parkin-dependent manner upon induction of mitophagy

Gegg, M. E., Cooper, J. M., Chau, K.-Y., Rojo, M., Schapira, A. H. V., & Taanman, J.-W. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq419 · Cited by 910

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

The TBK1 adaptor and autophagy receptor NDP52 restricts the proliferation of ubiquitin-coated bacteria

Thurston, T. L. M., Ryzhakov, G., Bloor, S., von Muhlinen, N., & Randow, F. (2009) · Nature Immunology · doi:10.1038/ni.1800 · Cited by 901

The PINK1/Parkin pathway regulates mitochondrial morphology

Poole, A. C., Thomas, R. E., Andrews, L. A., McBride, H. M., Whitworth, A. J., & Pallanck, L. J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709336105 · Cited by 885

ALS, SOD and peroxynitrite

Beckman, J. S., Carson, M. A., Smith, C. D. L., & Koppenol, W. H. (1993) · Nature · doi:10.1038/364584a0 · Cited by 876

Oxidant stress evoked by pacemaking in dopaminergic neurons is attenuated by DJ-1

Guzmán, J. N., Sánchez-Padilla, J., Wokosin, D. L., Kondapalli, J., Ilijić, E., Schumacker, P. T., & Surmeier, D. J. (2010) · Nature · doi:10.1038/nature09536 · Cited by 864

Impaired mitochondrial dynamics and abnormal interaction of amyloid beta with mitochondrial protein Drp1 in neurons from patients with Alzheimer's disease: implications for neuronal damage

Mańczak, M., Calkins, M. J., & Reddy, P. H. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr139 · Cited by 847

Oxidative DNA Damage in the Parkinsonian Brain: An Apparent Selective Increase in 8‐Hydroxyguanine Levels in Substantia Nigra

Alam, Z. I., Jenner, A., Daniel, S. E., Lees, A. J., Cairns, N., Marsden, C. D., Jenner, P., & Halliwell, B. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.69031196.x · Cited by 845

Peroxisomes and oxidative stress

Schrader, M., & Fahimi, H. D. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.09.006 · Cited by 838

Degradation of oxidized proteins in mammalian cells

Grune, T., Reinheckel, T., & Davies, K. J. A. (1997) · The FASEB Journal · doi:10.1096/fasebj.11.7.9212076 · Cited by 835

Atg32 Is a Mitochondrial Protein that Confers Selectivity during Mitophagy

Kanki, T., Wang, K., Cao, Y., Baba, M., & Klionsky, D. J. (2009) · Developmental Cell · doi:10.1016/j.devcel.2009.06.014 · Cited by 812

Global mapping of binding sites for Nrf2 identifies novel targets in cell survival response through ChIP-Seq profiling and network analysis

Malhotra, D., Portales-Casamar, É., Singh, A., Srivastava, S., Arenillas, D. J., Happel, C., Shyr, C., Wakabayashi, N., Kensler, T. W., Wasserman, W. W., et al. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq212 · Cited by 812

Superoxide is the major reactive oxygen species regulating autophagy

Chen, Y., Azad, M. B., & Gibson, S. B. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2009.49 · Cited by 806

Mitochondria-Anchored Receptor Atg32 Mediates Degradation of Mitochondria via Selective Autophagy

Okamoto, K., Kondo-Okamoto, N., & Ohsumi, Y. (2009) · Developmental Cell · doi:10.1016/j.devcel.2009.06.013 · Cited by 797

Cardiac autophagy is a maladaptive response to hemodynamic stress

Zhu, H., Tannous, P., Johnstone, J. L., Kong, Y., Shelton, J. M., Richardson, J. A., Le, V., Levine, B., Rothermel, B. A., & Hill, J. A. (2007) · Journal of Clinical Investigation · doi:10.1172/jci27523 · Cited by 775

A 26 S protease subunit that binds ubiquitin conjugates.

Deveraux, Q. L., Ustrell, V., Pickart, C. M., & Rechsteiner, M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37244-7 · Cited by 765

Parkinson's disease

Thomas, B., & Beal, M. F. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm159 · Cited by 748

Toxin-induced models of Parkinson’s disease

Bové, J., Prou, D., Perier, C., & Przedborski, S. (2005) · NeuroRX · doi:10.1602/neurorx.2.3.484 · Cited by 739

Regeneration of peroxiredoxins by p53-regulated sestrins, homologs of bacterial AhpD

Budanov, A. V., Sablina, A. A., Feinstein, E., Koonin, E. V., & Chumakov, P. M. (2004) · Science · doi:10.1126/science.1095569 · Cited by 731

Mammalian Atg18 (WIPI2) localizes to omegasome-anchored phagophores and positively regulates LC3 lipidation

Polson, H. E. J., de Lartigue, J., Rigden, D. J., Reedijk, M., Urbé, S., Clague, M. J., & Tooze, S. A. (2010) · Autophagy · doi:10.4161/auto.6.4.11863 · Cited by 712

Hypersensitivity of DJ-1-deficient mice to 1-methyl-4-phenyl-1,2,3,6-tetrahydropyrindine (MPTP) and oxidative stress

Kim, R. H., Smith, P. D., Aleyasin, H., Hayley, S. P., Mount, M. P., Pownall, S., Wakeham, A. C., You-Ten, A. J., Kalia, S. K., Horne, P., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501282102 · Cited by 711

Functional antioxidant responsive elements

Wasserman, W. W., & Fahl, W. E. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.10.5361 · Cited by 705

Loss of PINK1 causes mitochondrial functional defects and increased sensitivity to oxidative stress

Gautier, C. A., Kitada, T., & Shen, J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802076105 · Cited by 698

Nox enzymes, ROS, and chronic disease: An example of antagonistic pleiotropy

Lambeth, J. D. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.03.027 · Cited by 687

Rab7 is required for the normal progression of the autophagic pathway in mammalian cells

Gutierrez, M. G., Munafó, D. B., Berón, W., & Colombo, M. I. (2004) · Journal of Cell Science · doi:10.1242/jcs.01114 · Cited by 680

Nitric oxide‐induced mitochondrial fission is regulated by dynamin‐related GTPases in neurons

Barsoum, M. J., Yuan, H., Gerencser, A. A., Liot, G., Kushnareva, Y., Gräber, S., Kovács, I., Lee, W. D., Waggoner, J., Cui, J., et al. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601253 · Cited by 677

Anatomic and Disease Specificity of NADH CoQ1 Reductase (Complex I) Deficiency in Parkinson's Disease

Schapira, A. H. V., Mann, V. M., Cooper, J. A. D., Dexter, D. T., Daniel, S. E., Jenner, P. G., Clark, J. B., & MARSDEN, C. D. (1990) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1990.tb05809.x · Cited by 673

The autophagy protein Atg7 is essential for hematopoietic stem cell maintenance

Mortensen, M., Soilleux, E. J., Djordjevic, G., Tripp, R., Lutteropp, M., Sadighi-Akha, E., Stranks, A. J., Glanville, J., Knight, S., W. Jacobsen, S.-E., et al. (2011) · Journal of Experimental Medicine · doi:10.1084/jem.20101145 · Cited by 657

The Mammalian Target of Rapamycin (mTOR) Pathway Regulates Mitochondrial Oxygen Consumption and Oxidative Capacity

Schieke, S. M., Phillips, D., McCoy, J. P., Aponte, A. M., Shen, R.-F., Balaban, R. S., & Finkel, T. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603536200 · Cited by 623

The regulation of autophagy – unanswered questions

Chen, Y., & Klionsky, D. J. (2010) · Journal of Cell Science · doi:10.1242/jcs.064576 · Cited by 617

The mitochondrial permeability transition initiates autophagy in rat hepatocytes

Elmore, S. P., Qian, T., Grissom, S. F., & Lemasters, J. J. (2001) · The FASEB Journal · doi:10.1096/fj.01-0206fje · Cited by 607

Progressive parkinsonism in mice with respiratory-chain-deficient dopamine neurons

Ekstrand, M. I., Terzioglu, M., Galter, D., Zhu, S., Hofstetter, C., Lindqvist, E., Thams, S., Bergstrand, A., Hansson, F. S., Trifunovic, A., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0605208103 · Cited by 605

Reactive oxygen species are downstream mediators of p53-dependent apoptosis.

Johnson, T. M., Yu, Z., Ferrans, V. J., Lowenstein, R. A., & Finkel, T. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.21.11848 · Cited by 597

Identification of a common chemical signal regulating the induction of enzymes that protect against chemical carcinogenesis.

Talalay, P., Long, M. J., & Prochaska, H. J. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.21.8261 · Cited by 595

Absence of autophagy results in reactive oxygen species-dependent amplification of RLR signaling

Tal, M. C., Sasai, M., Lee, H. K., Yordy, B., Shadel, G. S., & Iwasaki, A. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0807694106 · Cited by 595

Reduced and oxidized glutathione in the substantia nigra of patients with Parkinson's disease

Sofic, E., Lange, K. W., Jellinger, K. A., & Riederer, P. (1992) · Neuroscience Letters · doi:10.1016/0304-3940(92)90355-b · Cited by 591

Targeting autophagy potentiates tyrosine kinase inhibitor–induced cell death in Philadelphia chromosome–positive cells, including primary CML stem cells

Bellodi, C., Lidonnici, M. R., Hamilton, A., Helgason, G. V., Soliera, A. R., Ronchetti, M., Galavotti, S., Young, K. W., Selmi, T., Yacobi, R., et al. (2009) · Journal of Clinical Investigation · doi:10.1172/jci35660 · Cited by 589

Chaperone-Mediated Autophagy Markers in Parkinson Disease Brains

Alvarez‐Erviti, L., Rodríguez-Oroz, M. C., Cooper, J. A. D., Caballero, C., Ferrer, I., Obeso, J. A., & Schapira, A. H. V. (2010) · Archives of Neurology · doi:10.1001/archneurol.2010.198 · Cited by 577

Chaperone-Assisted Selective Autophagy Is Essential for Muscle Maintenance

Arndt, V., Dick, N., Tawo, R., Dreiseidler, M., Wenzel, D., Hesse, M., Fürst, D. O., Säftig, P., Saint, R. B., Fleischmann, B. K., et al. (2010) · Current Biology · doi:10.1016/j.cub.2009.11.022 · Cited by 572

Dityrosine Cross-linking Promotes Formation of Stable α-Synuclein Polymers

Souza, J. M., Giasson, B. I., Chen, Q., Lee, V. M. ‐., & Ischiropoulos, H. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000206200 · Cited by 572

Cellular mechanisms of redox cell signalling: role of cysteine modification in controlling antioxidant defences in response to electrophilic lipid oxidation products

Levonen, A., Landar, A. L., Ramachandran, A., CEASER, E. K., Dickinson, D. A., Zanoni, G., Morrow, J. D., & Darley-Usmar, V. M. (2004) · Biochemical Journal · doi:10.1042/bj20031049 · Cited by 569

LC3, an Autophagosome Marker, Can be Incorporated into Protein Aggregates Independent of Autophagy: Caution in the Interpretation of LC3 Localization

Kuma, A., Matsui, M., & Mizushima, N. (2007) · Autophagy · doi:10.4161/auto.4012 · Cited by 555

The ubiquitin system

Varshavsky, A. J. (1997) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(97)01122-5 · Cited by 553

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

Leucine-Rich Repeat Kinase 2 Regulates the Progression of Neuropathology Induced by Parkinson's-Disease-Related Mutant α-synuclein

Lin, X. Z., Parisiadou, L., Gu, X., Wang, L., Shim, H., Sun, L., Xie, C., Long, C.-X., Yang, W.-J., Ding, J., et al. (2009) · Neuron · doi:10.1016/j.neuron.2009.11.006 · Cited by 532

Blocked Autophagy Sensitizes Resistant Carcinoma Cells to Radiation Therapy

Apel, A., Herr, I., Schwarz, H., Rodemann, H. P., & Mayer, A. (2008) · Cancer Research · doi:10.1158/0008-5472.can-07-0562 · Cited by 530

Transcriptional regulation of the rat glutathione S-transferase Ya subunit gene. Characterization of a xenobiotic-responsive element controlling inducible expression by phenolic antioxidants.

Rushmore, T. H., & Pickett, C. B. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)77351-1 · Cited by 522

Protein quality control during aging involves recruitment of the macroautophagy pathway by BAG3

Gamerdinger, M., Hajieva, P., Kaya, A. M., Wolfrum, U., Hartl, F. U., & Behl, C. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.29 · Cited by 522

Loss of leucine-rich repeat kinase 2 causes impairment of protein degradation pathways, accumulation of α-synuclein, and apoptotic cell death in aged mice

Tong, Y., Yamaguchi, H., Giaime, E., Boyle, S., Kopan, R., Kelleher, R. J., & Shen, J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1004676107 · Cited by 521

Nitrosative stress linked to sporadic Parkinson's disease: S-nitrosylation of parkin regulates its E3 ubiquitin ligase activity

Yao, D., Gu, Z., Nakamura, T., Shi, Z., Ma, Y., Gaston, B. M., Palmer, L. A., Rockenstein, E. M., Zhang, Z., Masliah, E., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404161101 · Cited by 520

Role of autophagy in G2019S‐LRRK2‐associated neurite shortening in differentiated SH‐SY5Y cells

Plowey, E. D., Cherra, S. J., Liu, Y., & Chu, C. T. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05217.x · Cited by 517

Role of Protein Aggregation in Mitochondrial Dysfunction and Neurodegeneration in Alzheimer's and Parkinson's Diseases

Hashimoto, M., Rockenstein, E. M., Crews, L. A., & Masliah, E. (2003) · NeuroMolecular Medicine · doi:10.1385/nmm:4:1-2:21 · Cited by 508

Phosphatidylinositol(3)-Phosphate Signaling Mediated by Specific Binding to RING FYVE Domains

Burd, C. G., & Emr, S. D. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80125-2 · Cited by 499

Selective degradation of oxidatively modified protein substrates by the proteasome

Grune, T., Merker, K., Sandig, G., & Davies, K. J. A. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00809-x · Cited by 489

TRAF6 and A20 Regulate Lysine 63–Linked Ubiquitination of Beclin-1 to Control TLR4-Induced Autophagy

Shi, C.-S., & Kehrl, J. H. (2010) · Science Signaling · doi:10.1126/scisignal.2000751 · Cited by 481

DJ-1 gene deletion reveals that DJ-1 is an atypical peroxiredoxin-like peroxidase

Andrés‐Mateos, E., Perier, C., Zhang, L., Blanchard-Fillion, B., Greco, T. M., Thomas, B., Ko, H. S., Sasaki, M., Ischiropoulos, H., Przedborski, S., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0703219104 · Cited by 478

p53 regulates mitochondrial membrane potential through reactive oxygen species and induces cytochrome c‐independent apoptosis blocked by Bcl‐2

Li, P., Dietz, R., & von Harsdorf, R. (1999) · The EMBO Journal · doi:10.1093/emboj/18.21.6027 · Cited by 478

Xenobiotic-inducible expression of murine glutathione S-transferase Ya subunit gene is controlled by an electrophile-responsive element.

Friling, R. S., Bensimon, A., Tichauer, Y., & Daniel, V. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.16.6258 · Cited by 475

Mitochondrial alpha-synuclein accumulation impairs complex I function in dopaminergic neurons and results in increased mitophagy in vivo

Chinta, S. J., Mallajosyula, J. K., Rane, A., & Andersen, J. K. (2010) · Neuroscience Letters · doi:10.1016/j.neulet.2010.09.061 · Cited by 472

DJ-1 acts in parallel to the PINK1/parkin pathway to control mitochondrial function and autophagy

Craig, K. J. T., McCoy, M. K., Blackinton, J. G., Beilina, A. G., van der Brug, M., Matton, A., Miller, D. W., Maric, D., Cedazo-Mı́nguez, Á., & Cookson, M. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq430 · Cited by 467

Biogenesis and Cargo Selectivity of Autophagosomes

Weidberg, H., Shvets, E., & Elazar, Z. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-052709-094552 · Cited by 466

Genetic determinants of p53-induced apoptosis and growth arrest.Preprint

Polyák, K., Waldman, T. A., He, T., Kinzler, K. W., & Vogelstein, B. (1996) · Genes & Development · doi:10.1101/gad.10.15.1945 · Cited by 458

Autophagy requires endoplasmic reticulum targeting of the PI3-kinase complex via Atg14L

Matsunaga, K., Morita, E., Saitoh, T., Akira, S., Ktistakis, N. T., Izumi, T., Noda, T., & Yoshimori, T. (2010) · Journal of Cell Biology · doi:10.1083/jcb.200911141 · Cited by 456

A Selective Increase in Particulate Superoxide Dismutase Activity in Parkinsonian Substantia Nigra

Saggu, H. K., Cooksey, J., Dexter, D. T., Wells, F. R., Lees, A. J., Jenner, P. G., & MARSDEN, C. D. (1989) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1989.tb11759.x · Cited by 454

Increased Oxidative Damage Is Correlated to Altered Mitochondrial Function in Heterozygous Manganese Superoxide Dismutase Knockout Mice

Williams, M. D., Remmen, H. V., Conrad, C. C., Huang, T., Epstein, C. J., & Richardson, A. G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.43.28510 · Cited by 453

Recent Advances in the Genetics of Parkinson's Disease

Martin, I., Dawson, V. L., & Dawson, T. M. (2011) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev-genom-082410-101440 · Cited by 451

The Selective Macroautophagic Degradation of Aggregated Proteins Requires the PI3P-Binding Protein Alfy

Filimonenko, M., Isakson, P., Finley, K. D., Anderson, M. R., Jeong, H., Melia, T. J., Bartlett, B. J., Myers, K. M., Birkeland, H. C. G., Lamark, T., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.04.007 · Cited by 449

Hydrogen Peroxide– and Peroxynitrite-Induced Mitochondrial DNA Damage and Dysfunction in Vascular Endothelial and Smooth Muscle Cells

Ballinger, S. W., Patterson, C., Yan, C.-N., Doan, R., Burow, D. L., Young, C. G., Yakes, F. M., Houten, B. V., Ballinger, C. A., Freeman, B. Α., et al. (2000) · Circulation Research · doi:10.1161/01.res.86.9.960 · Cited by 447

LRRK2 regulates autophagic activity and localizes to specific membrane microdomains in a novel human genomic reporter cellular model

Alegre‐Abarrategui, J., Christian, H., Lufino, M. M., Dafinca, R., Venda, L. L., Ansorge, O., & Wade‐Martins, R. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp346 · Cited by 446

Induction of α-Synuclein Aggregation by Intracellular Nitrative Insult

Paxinou, E., Chen, Q., Weisse, M., Giasson, B. I., Norris, E. H., Rueter, S. M., Trojanowski, J. Q., Lee, V. M. ‐., & Ischiropoulos, H. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-20-08053.2001 · Cited by 440

The Mitochondrial Fusion-Promoting Factor Mitofusin Is a Substrate of the PINK1/Parkin Pathway

Poole, A. C., Thomas, R. E., Yu, S., Vincow, E. S., & Pallanck, L. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010054 · Cited by 440

Autophagy Is Essential for Mitochondrial Clearance in Mature T Lymphocytes

Pua, H. H., Guo, J., Komatsu, M., & He, Y.-W. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0801143 · Cited by 438

Nrf2-induced antioxidant protection: A promising target to counteract ROS-mediated damage in neurodegenerative disease?

de Vries, H. E., Witte, M. E., Hondius, D., Rozemüller, A. J. M., Drukarch, B., Hoozemans, J. J. M., & van Horssen, J. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.09.001 · Cited by 436

Kinase-Inactivated ULK Proteins Inhibit Autophagy via Their Conserved C-Terminal Domains Using an Atg13-Independent Mechanism

Chan, E. Y. W., Longatti, A., McKnight, N. C., & Tooze, S. A. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01082-08 · Cited by 411

NF-κB Activation Represses Tumor Necrosis Factor-α-induced Autophagy

Djavaheri-Mergny, M., Amelotti, M., Mathieu, J., Besançon, F., Bauvy, C., Souquère, S., Pierron, G., & Codogno, P. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602097200 · Cited by 407

Loss of autophagy in erythroid cells leads to defective removal of mitochondria and severe anemia in vivo

Mortensen, M., Ferguson, D. J. P., Edelmann, M. J., Kessler, B. M., Morten, K., Komatsu, M., & Simon, A. K. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0913170107 · Cited by 400

Distinct Autophagosomal-Lysosomal Fusion Mechanism Revealed by Thapsigargin-Induced Autophagy Arrest

Ganley, I. G., Wong, P., Gammoh, N., & Jiang, X. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.04.024 · Cited by 397

Loss of the Parkinson's disease-linked gene DJ-1 perturbs mitochondrial dynamics

Irrcher, I., Aleyasin, H., Seifert, E. L., Hewitt, S. J., Chhabra, S., Phillips, M., Lutz, A. K., Rousseaux, M. W. C., Bevilacqua, L., Jahani‐Asl, A., et al. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq288 · Cited by 394

Complex I deficiency in Parkinson's disease frontal cortex

Parker, W. D., Parks, J. K., & Swerdlow, R. H. (2007) · Brain Research · doi:10.1016/j.brainres.2007.10.061 · Cited by 392

The role of pathogenic DJ‐1 mutations in Parkinson's disease

Abou‐Sleiman, P. M., Healy, D. G., Quinn, N. P., Lees, A. J., & Wood, N. W. (2003) · Annals of Neurology · doi:10.1002/ana.10675 · Cited by 392

The Lysosome

de Duve, C. (1963) · Scientific American · doi:10.1038/scientificamerican0563-64 · Cited by 388

Complex Inhibitory Effects of Nitric Oxide on Autophagy

Sarkar, S., Korolchuk, V. I., Renna, M., Imarisio, S., Fleming, A., Williams, A. J., Garcı́a-Arencibia, M., Rose, C., Luo, S., Underwood, B. R., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.04.029 · Cited by 386

Modulation of intracellular ROS levels by TIGAR controls autophagy

Bensaad, K., Cheung, E. C., & Vousden, K. H. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.242 · Cited by 371

BNIP3 Is an RB/E2F Target Gene Required for Hypoxia-Induced Autophagy

Tracy, K., Dibling, B. C., Spike, B. T., Knabb, J. R., Schumacker, P., & Macleod, K. F. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.02246-06 · Cited by 369

Role and regulation of autophagy in cancer

Chen, N., & Karantza‐Wadsworth, V. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.12.013 · Cited by 368

Rapamycin treatment augments motor neuron degeneration in SOD1G93Amouse model of amyotrophic lateral sclerosis

Zhang, X., Li, L., Chen, S., Yang, D., Wang, Y., Zhang, X., Wang, Z., & Le, W. (2011) · Autophagy · doi:10.4161/auto.7.4.14541 · Cited by 364

Idiopathic Parkinson's disease, progressive supranuclear palsy and glutathione metabolism in the substantia nigra of patients

Perry, T. L., & Yong, V. W. (1986) · Neuroscience Letters · doi:10.1016/0304-3940(86)90320-4 · Cited by 362

HspB8 Chaperone Activity toward Poly(Q)-containing Proteins Depends on Its Association with Bag3, a Stimulator of Macroautophagy

Carra, S., Seguin, S. J., Lambert, H., & Landry, J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706304200 · Cited by 360

Oxidative Stress Stimulates Autophagic Flux During Ischemia/Reperfusion

Hariharan, N., Zhai, P., & Sadoshima, J. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3488 · Cited by 352

Preconditioning Involves Selective Mitophagy Mediated by Parkin and p62/SQSTM1

Huang, C., Andres, A. M., Ratliff, E. P., Hernandez, G., Lee, P. P. W., & Gottlieb, R. A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0020975 · Cited by 347

Mitochondrial function and morphology are impaired in parkin‐mutant fibroblasts

Mortiboys, H., Craig, K. J. T., Koopman, W. J. H., Klaffke, S., Abou‐Sleiman, P. M., Olpin, S. E., Wood, N. W., Willems, P. H. G. M., Smeitink, J. A. M., Cookson, M., et al. (2008) · Annals of Neurology · doi:10.1002/ana.21492 · Cited by 346

Parkin-mediated K63-linked polyubiquitination targets misfolded DJ-1 to aggresomes via binding to HDAC6

Olzmann, J. A., Li, L., Chudaev, M. V., Chen, J., Perez, F. A., Palmiter, R. D., & Chin, L. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200611128 · Cited by 343

Clinical Outcome and Phenotypic Expression in LAMP2 Cardiomyopathy

Maron, B. J. (2009) · JAMA · doi:10.1001/jama.2009.371 · Cited by 343

Mitochondrial association of alpha-synuclein causes oxidative stress

Parihar, M. S., Parihar, A., Fujita, M., Hashimoto, M., & Ghafourifar, P. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-7589-1 · Cited by 340

The Turnover of Mitochondria in a Variety of Tissues of Young Adult and Aged Rats

Menzies, R. A., & Gold, P. H. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62305-1 · Cited by 336

WIPI-1α (WIPI49), a member of the novel 7-bladed WIPI protein family, is aberrantly expressed in human cancer and is linked to starvation-induced autophagy

Proikas-Cezanne, T., Waddell, S., Gaugel, A., Frickey, T., Lupas, A., & Nordheim, A. (2004) · Oncogene · doi:10.1038/sj.onc.1208331 · Cited by 332

Tracker Dyes to Probe Mitochondrial Autophagy (Mitophagy) in Rat Hepatocytes

Rodríguez‐Enríquez, S., Kim, I., Currin, R. T., & Lemasters, J. J. (2006) · Autophagy · doi:10.4161/auto.2229 · Cited by 331

Participation of Autophagy in Storage of Lysosomes in Neurons from Mouse Models of Neuronal Ceroid-Lipofuscinoses (Batten Disease)

Koike, M., Shibata, M., Waguri, S., Yoshimura, K., Tanida, I., Kominami, E., Gotow, T., Peters, C., von Figura, K., Mizushima, N., et al. (2005) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)61253-9 · Cited by 330

p62/SQSTM1 and ALFY interact to facilitate the formation of p62 bodies/ALIS and their degradation by autophagy

Clausen, T. H., Lamark, T., Isakson, P., Finley, K. D., Larsen, K. B., Brech, A., Øvervatn, A., Stenmark, H., Bjørkøy, G., Simonsen, A., et al. (2010) · Autophagy · doi:10.4161/auto.6.3.11226 · Cited by 321

The immunoproteasome, the 20S proteasome and the PA28αβ proteasome regulator are oxidative-stress-adaptive proteolytic complexes

Pickering, A. M., Koop, A. L., Teoh, C., Ermak, G., Grune, T., & Davies, K. J. A. (2010) · Biochemical Journal · doi:10.1042/bj20100878 · Cited by 319

Dissecting the dynamic turnover of GFP-LC3 in the autolysosome

Ni, H.-M., Bockus, A., Wozniak, A. L., Jones, K., Weinman, S., Yin, X.-M., & Ding, W.-X. (2011) · Autophagy · doi:10.4161/auto.7.2.14181 · Cited by 318

Mitochondrial dysfunction and oxidative stress mediate the physiological impairment induced by the disruption of autophagy

Wu, J., Quijano, C., Chen, E., Liu, H., Cao, L., Fergusson, M. M., Rovira, I. I., Gutkind, S., Daniels, M. P., Komatsu, M., et al. (2009) · Aging · doi:10.18632/aging.100038 · Cited by 311

What Part of NO Don't You Understand? Some Answers to the Cardinal Questions in Nitric Oxide Biology

Hill, B. G., Dranka, B. P., Bailey, S. M., Lancaster, J. R., & Darley-Usmar, V. M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.r110.101618 · Cited by 310

Inhibition of ischemic cardiomyocyte apoptosis through targeted ablation of Bnip3 restrains postinfarction remodeling in mice

Diwan, A., Krenz, M., Syed, F. M., Wansapura, J. P., Ren, X., Koesters, A. G., Li, H., Kirshenbaum, L. A., Hahn, H. S., Robbins, J., et al. (2007) · Journal of Clinical Investigation · doi:10.1172/jci32490 · Cited by 305

Regulation of the autophagy protein LC3 by phosphorylation

Cherra, S. J., Kulich, S. M., Uechi, G., Balasubramani, M., Mountzouris, J., Day, B. W., & Chu, C. T. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201002108 · Cited by 304

p62, a Phosphotyrosine-independent Ligand of the SH2 Domain of p56 , Belongs to a New Class of Ubiquitin-binding Proteins

Vadlamudi, R. K., Joung, I., Strominger, J. L., & Shin, J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.34.20235 · Cited by 299

Antioxidant Protective Mechanisms against Reactive Oxygen Species (ROS) Generated by Mitochondrial P450 Systems in Steroidogenic Cells

Hanukoglu, I. (2006) · Drug Metabolism Reviews · doi:10.1080/03602530600570040 · Cited by 293

Alfy, a novel FYVE-domain-containing protein associated with protein granules and autophagic membranes

Simonsen, A., Birkeland, H. C. G., Gillooly, D. J., Mizushima, N., Kuma, A., Yoshimori, T., Slagsvold, T., Brech, A., & Stenmark, H. (2004) · Journal of Cell Science · doi:10.1242/jcs.01287 · Cited by 293

Antagonism of Beclin 1‐dependent autophagy by BCL‐2 at the endoplasmic reticulum requires NAF‐1

Chang, N. C., Nguyen, M., Germain, M., & Shore, G. C. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.369 · Cited by 292

Cathepsin D expression level affects alpha-synuclein processing, aggregation, and toxicity in vivo

Cullen, V., Lindfors, M., Ng, J., Paetau, A. E., Swinton, E., Kolodziej, P., Boston, H., Säftig, P., Woulfe, J., Feany, M. Β., et al. (2009) · Molecular Brain · doi:10.1186/1756-6606-2-5 · Cited by 285

Bnip3 impairs mitochondrial bioenergetics and stimulates mitochondrial turnover

Rikka, S., Quinsay, M. N., Thomas, R. L., Kubli, D. A., Zhang, X., Murphy, A. N., & Gustafsson, Å. B. (2011) · Cell Death & Differentiation · doi:10.1038/cdd.2010.146 · Cited by 277

DJ-1 is critical for mitochondrial function and rescues PINK1 loss of function

Hao, L.-Y., Giasson, B. I., & Bonini, N. M. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911175107 · Cited by 270

Lysosomal enzyme cathepsin D protects against alpha-synuclein aggregation and toxicity

Qiao, L., Hamamichi, S., Caldwell, K. A., Caldwell, G. A., Yacoubian, T. A., Wilson, S. M., Xie, Z., Speake, L. D., Parks, R., Crabtree, D., et al. (2008) · Molecular Brain · doi:10.1186/1756-6606-1-17 · Cited by 264

p65/RelA Modulates BECN1 Transcription and Autophagy

Copetti, T., Bertoli, C., Dalla, E., Demarchi, F., & Schneider, C. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01396-08 · Cited by 262

Localization of α-synuclein to mitochondria within midbrain of mice

Li, W.-W., Yang, R., Guo, J.-C., Ren, H., Zha, X., Cheng, J.-S., & Cai, D. (2007) · Neuroreport · doi:10.1097/wnr.0b013e3282f03db4 · Cited by 261

Caspase cleavage of Atg4D stimulates GABARAP-L1 processing and triggers mitochondrial targeting and apoptosis

Betin, V. M. S., & Lane, J. D. (2009) · Journal of Cell Science · doi:10.1242/jcs.046250 · Cited by 261

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Vázquez‐Martín, A., Oliveras‐Ferraros, C., & Menéndez, J. A. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006251 · Cited by 251

Autophagy in Spinal Cord Motor Neurons in Sporadic Amyotrophic Lateral Sclerosis

Sasaki, S. (2011) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3182160690 · Cited by 249

Association of DJ-1 and parkin mediated by pathogenic DJ-1 mutations and oxidative stress

Moore, D. J., Zhang, L., Troncoso, J. C., Lee, M. K., Hattori, N., Mizuno, Y., Dawson, T. M., & Dawson, V. L. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddi007 · Cited by 248

FIP200 is required for the cell-autonomous maintenance of fetal hematopoietic stem cells

Liu, F., Lee, J., Wei, H., Tanabe, O., Engel, J. D., Morrison, S. J., & Guan, J. (2010) · Blood · doi:10.1182/blood-2010-06-288589 · Cited by 240

Chapter 1 Monitoring Autophagy in Mammalian Cultured Cells through the Dynamics of LC3

Kimura, S., Fujita, N., Noda, T., & Yoshimori, T. (2009) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(08)03601-x · Cited by 236

Mitochondrial clearance is regulated by Atg7-dependent and -independent mechanisms during reticulocyte maturation

Zhang, J., Randall, M. S., Loyd, M. R., Dorsey, F. C., Kundu, M., Cleveland, J. L., & Ney, P. A. (2009) · Blood · doi:10.1182/blood-2008-04-151639 · Cited by 235

LAMP-2: A control step for phagosome and autophagosome maturation

Säftig, P., Beertsen, W., & Eskelinen, E. (2008) · Autophagy · doi:10.4161/auto.5724 · Cited by 233

Nrf2-mediated induction of p62 controls Toll-like receptor-4–driven aggresome-like induced structure formation and autophagic degradation

Fujita, K.-I., Maeda, D., Xiao, Q., & Srinivasula, S. M. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1014156108 · Cited by 232

Autophagy in health and disease. 5. Mitophagy as a way of life

Gottlieb, R. A., & Carreira, R. (2010) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00097.2010 · Cited by 230

Mitochondrial Reactive Oxygen Species (ROS) and ROS-Induced ROS Release

Zorov, D. B., Juhaszova, M., & Sollott, S. J. (2014) · Physiological Reviews · doi:10.1152/physrev.00026.2013 · Cited by 5,383

Anti-Vascular Endothelial Growth Factors Protect Retinal Pigment Epithelium Cells Against Oxidation by Modulating Nitric Oxide Release and Autophagy

Cillà, S. D., Farruggio, S., Vujosevic, S., Raina, G., Filippini, D. A., Gatti, V., Clemente, N., Mary, D., Vezzola, D., Casini, G., et al. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000479441 · Cited by 5,154

An Overview of Autophagy: Morphology, Mechanism, and Regulation

Parzych, K. R., & Klionsky, D. J. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5371 · Cited by 2,521

Hydrogen peroxide as a central redox signaling molecule in physiological oxidative stress: Oxidative eustress

Sies, H. (2017) · Redox Biology · doi:10.1016/j.redox.2016.12.035 · Cited by 2,148

Ageing as a Risk Factor for Disease

Niccoli, T., & Partridge, L. (2012) · Current Biology · doi:10.1016/j.cub.2012.07.024 · Cited by 1,831

REVIEW ARTICLE Autophagy, mitochondria and oxidative stress: cross-talk and redox

Lee, J., Giordano, S. S., & Zhang, J. (2013)

Roles of Autophagy in Oxidative Stress

Yun, H. R., Jo, Y. H., Kim, J., Shin, Y., Kim, S. S., & Choi, T. G. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21093289 · Cited by 413

The Roles of Autophagy in Oxidative Stress.

Mehrdar, M. T., & Rasool, M. (2025) · PubMed · doi:10.32598/ari.80.6.3391

Redox homeostasis, oxidative stress and mitophagy

Garza-Lombó, C., Pappa, A., Panayiotidis, M. I., & Franco, R. (2020) · Mitochondrion · doi:10.1016/j.mito.2020.01.002 · Cited by 168

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Navarro-Yepes, J., Burns, M., Anandhan, A., Khalimonchuk, O., Razo, L. M. D., Quintanilla‐Vega, B., Pappa, A., Panayiotidis, M. I., & Franco, R. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.5837 · Cited by 467