Role of BNIP3 and NIX in cell death, autophagy, and mitophagy

Bcl-2 Antiapoptotic Proteins Inhibit Beclin 1-Dependent Autophagy

Pattingre, S., Tassa, A., Qu, X., Garuti, R., Liang, X. H., Mizushima, N., Packer, M., Schneider, M. D., & Levine, B. (2005) · Cell · doi:10.1016/j.cell.2005.07.002 · Cited by 3,536 · see citing works

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 · see citing works

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 · see citing works

Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death

Baines, C. P., Kaiser, R. A., Purcell, N. H., Blair, N. S., Osinska, H., Hambleton, M. A., Brunskill, E. W., Sayen, M. R., Gottlieb, R. A., Dorn, G. W., et al. (2005) · Nature · doi:10.1038/nature03434 · Cited by 2,280 · see citing works

Beclin 1, an autophagy gene essential for early embryonic development, is a haploinsufficient tumor suppressor

Yue, Z., Jin, S., Yang, C., Levine, A. J., & Heintz, N. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2436255100 · Cited by 2,116 · see citing works

FoxO3 Controls Autophagy in Skeletal Muscle In Vivo

Mammucari, C., Milan, G., Romanello, V., Masiero, E., Rudolf, R., Del Piccolo, P., Burden, S. J., Di Lisi, R., Sandri, C., Zhao, J., et al. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.11.001 · Cited by 1,953 · see citing works

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 · see citing works

Autophagy: molecular machinery for self-eating

Yorimitsu, T., & Klionsky, D. J. (2005) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401765 · Cited by 1,540 · see citing works

BAX and BAK Regulation of Endoplasmic Reticulum Ca 2+ : A Control Point for Apoptosis

Scorrano, L., Oakes, S. A., Opferman, J. T., Cheng, E. H. Y., Sorcinelli, M. D., Pozzan, T., & Korsmeyer, S. J. (2003) · Science · doi:10.1126/science.1081208 · Cited by 1,387 · see citing works

The BH3 mimetic ABT-737 targets selective Bcl-2 proteins and efficiently induces apoptosis via Bak/Bax if Mcl-1 is neutralized

van Delft, M. F., Wei, A. H., Mason, K. D., Vandenberg, C. J., Chen, L., Czabotar, P. E., Willis, S. N., Scott, C. L., Day, C. L., Cory, S., et al. (2006) · Cancer Cell · doi:10.1016/j.ccr.2006.08.027 · Cited by 1,237 · see citing works

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 · see citing works

Bax and Adenine Nucleotide Translocator Cooperate in the Mitochondrial Control of Apoptosis

Marzo, I., Brenner, C., Zamzami, N., Jürgensmeier, J. M., Susin, S. A., Vieira, H. L. A., Prévost, M.-C., Xie, Z., Matsuyama, S., Reed, J. C., et al. (1998) · Science · doi:10.1126/science.281.5385.2027 · Cited by 1,168 · see citing works

Protection against Fatal Sindbis Virus Encephalitis by Beclin, a Novel Bcl-2-Interacting Protein

Liang, X. H., Kleeman, L. K., Jiang, H., Gordon, G. W., Goldman, J. E., Berry, G., Herman, B. A., & Levine, B. (1998) · Journal of Virology · doi:10.1128/jvi.72.11.8586-8596.1998 · Cited by 1,128 · see citing works

Functional and physical interaction between Bcl‐XL and a BH3‐like domain in Beclin‐1

Maiuri, M. C., Toumelin-Braizat, G. L., Criollo, A., Rain, J., Gautier, F., Juin, P. P., Tasdemir, E., Pierron, G., Troulinaki, K., Tavernarakis, N., et al. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601689 · Cited by 1,107 · see citing works

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 939 · see citing works

Hierarchical regulation of mitochondrion-dependent apoptosis by BCL-2 subfamilies

Kim, H., Rafiuddin-Shah, M., Tu, H.-C., Jeffers, J. R., Zambetti, G. P., Hsieh, J. J.-D., & Cheng, E. H.-Y. (2006) · Nature Cell Biology · doi:10.1038/ncb1499 · Cited by 874 · see citing works

CYTOPLASMIC COMPONENTS IN HEPATIC CELL LYSOSOMES

Ashford, T. P., & Porter, K. R. (1962) · The Journal of Cell Biology · doi:10.1083/jcb.12.1.198 · Cited by 849 · see citing works

Expression of the gene encoding the proapoptotic Nip3 protein is induced by hypoxia

Bruick, R. K. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.16.9082 · Cited by 767 · see citing works

HIF-1-dependent regulation of hypoxic induction of the cell death factors BNIP3 and NIX in human tumors.

Sowter, H., Ratcliffe, P. J., Watson, P. H., Greenberg, A. H., & Harris, A. L. (2001) · PubMed · Cited by 711 · see citing works

The adenovirus E1A proteins induce apoptosis, which is inhibited by the E1B 19-kDa and Bcl-2 proteins.

Rao, L., Debbas, M. E., Sabbatini, P., Hockenbery, D. M., Korsmeyer, S. J., & White, E. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.16.7742 · Cited by 660 · see citing works

Bcl-2-family proteins: the role of the BH3 domain in apoptosis

Kelekar, A., & Thompson, C. B. (1998) · Trends in Cell Biology · doi:10.1016/s0962-8924(98)01321-x · Cited by 654 · see citing works

BNIP3 and Genetic Control of Necrosis-Like Cell Death through the Mitochondrial Permeability Transition Pore

Velde, C. V., Cizeau, J., Dubik, D., Alimonti, J. B., Brown, T., Israels, S. J., Hakem, R., & Greenberg, A. H. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.15.5454-5468.2000 · Cited by 619 · see citing works

Response to myocardial ischemia/reperfusion injury involves Bnip3 and autophagy

Hamacher-Brady, A., Brady, N. R., Logue, S. E., Sayen, M. R., Jinno, M., Kirshenbaum, L. A., Gottlieb, R. A., & Gustafsson, Å. B. (2007) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401936 · Cited by 609 · see citing works

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 · see citing works

Ulk1 plays a critical role in the autophagic clearance of mitochondria and ribosomes during reticulocyte maturation

Kundu, M., Lindsten, T., Yang, C.-Y., Wu, J., Zhao, F., Zhang, J., Selak, M. A., Ney, P. A., & Thompson, C. B. (2008) · Blood · doi:10.1182/blood-2008-02-137398 · Cited by 571 · see citing works

Crystal Structure of the Bcl-XL-Beclin 1 Peptide Complex

Oberstein, A., Jeffrey, P. D., & Shi, Y. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700492200 · Cited by 567 · see citing works

The Role of Autophagy in Mammalian Development: Cell Makeover Rather than Cell Death

Cecconi, F., & Levine, B. (2008) · Developmental Cell · doi:10.1016/j.devcel.2008.08.012 · Cited by 518 · see citing works

Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set of cellular proteins

Boyd, J. M., Malstrom, S. E., Subramanian, T., Venkatesh, L., Schaeper, U., Elangovan, B., D’Sa-Eipper, C., & Chinnadurai, G. (1994) · Cell · doi:10.1016/0092-8674(94)90202-x · Cited by 476 · see citing works

Hypoxia and acidosis activate cardiac myocyte death through the Bcl-2 family protein BNIP3

Kubasiak, L. A., Hernandez, O. M., Bishopric, N. H., & Webster, K. A. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.202474099 · Cited by 438 · see citing works

Control of autophagy by oncogenes and tumor suppressor genes

Maiuri, M. C., Tasdemir, E., Criollo, A., Morselli, E., Vicencio, J. M., Carnuccio, R., & Kroemer, G. (2008) · Cell Death and Differentiation · doi:10.1038/cdd.2008.131 · Cited by 433 · see citing works

Bcl-2 decreases the free Ca 2+ concentration within the endoplasmic reticulum

Foyouzi-Youssefi, R., Arnaudeau, S., Borner, C., Kelley, W. L., Tschopp, J., Lew, D. P., Demaurex, N., & Krause, K. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.11.5723 · Cited by 432 · see citing works

CELLULAR DIFFERENTIATION IN THE KIDNEYS OF NEWBORN MICE STUDIED WITH THE ELECTRON MICROSCOPE

Clark, S. L. (1957) · The Journal of Cell Biology · doi:10.1083/jcb.3.3.349 · Cited by 418 · see citing works

Pivotal Role of the Cell Death Factor BNIP3 in Ceramide-Induced Autophagic Cell Death in Malignant Glioma Cells

Daido, S., Kanzawa, T., Yamamoto, A., Takeuchi, H., Kondo, Y., & Kondo, S. (2004) · Cancer Research · doi:10.1158/0008-5472.can-03-3084 · Cited by 411 · see citing works

Arsenic trioxide induces autophagic cell death in malignant glioma cells by upregulation of mitochondrial cell death protein BNIP3

Kanzawa, T., Zhang, L., Xiao, L., Germano, I. M., Kondo, Y., & Kondo, S. (2004) · Oncogene · doi:10.1038/sj.onc.1208095 · Cited by 407 · see citing works

<i>BNIP3</i> 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 · see citing works

Hypoxia induces the expression of the pro-apoptotic gene BNIP3

Guo, K., Searfoss, G. H., Krolikowski, D., Pagnoni, M., Franks, C. F., Clark, K. L., Yu, K. T., Jaye, M., & Ivashchenko, Y. (2001) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400810 · Cited by 353 · see citing works

BNIP3 Heterodimerizes with Bcl-2/Bcl-XL and Induces Cell Death Independent of a Bcl-2 Homology 3 (BH3) Domain at Both Mitochondrial and Nonmitochondrial Sites

Ray, R., Chen, G., Velde, C. V., Cizeau, J., Park, J. H., Reed, J. C., Gietz, R. D., & Greenberg, A. H. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.2.1439 · Cited by 349 · see citing works

The E1B 19K/Bcl-2–binding Protein Nip3 is a Dimeric Mitochondrial Protein that Activates Apoptosis

Chen, G., Ray, R., Dubik, D., Shi, L. F., Cizeau, J., Bleackley, R. C., Saxena, S. P., Gietz, R. D., & Greenberg, A. H. (1997) · The Journal of Experimental Medicine · doi:10.1084/jem.186.12.1975 · Cited by 332 · see citing works

Bax and Bak Promote Apoptosis by Modulating Endoplasmic Reticular and Mitochondrial Ca2+ Stores

Nutt, L. K., Pataer, A., Pahler, J. C., Fang, B., Roth, J. A., McConkey, D. J., & Swisher, S. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m106817200 · Cited by 320 · see citing works

Foxo3 is required for the regulation of oxidative stress in erythropoiesis

Marinković, D., Zhang, X., Yalcin, S., Luciano, J. P., Brugnara, C., Huber, T. L., & Ghaffari, S. (2007) · Journal of Clinical Investigation · doi:10.1172/jci31807 · Cited by 320 · see citing works

Inducible Expression of BNIP3 Provokes Mitochondrial Defects and Hypoxia-Mediated Cell Death of Ventricular Myocytes

Regula, K. M., Ens, K., & Kirshenbaum, L. A. (2002) · Circulation Research · doi:10.1161/01.res.0000029232.42227.16 · Cited by 318 · see citing works

Nix and Nip3 Form a Subfamily of Pro-apoptotic Mitochondrial Proteins

Chen, G., Cizeau, J., Velde, C. V., Park, J. H., Bozek, G., Bolton, J. M., Shi, L. F., Dubik, D., & Greenberg, A. H. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.1.7 · Cited by 310 · see citing works

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

Diwan, A., Krenz, M., Syed, F. M., Wansapura, J., Ren, X.-P., Koesters, A., Li, H.-R., Kirshenbaum, L., Hahn, H., Robbins, J., et al. (2007) · Journal of Clinical Investigation · doi:10.1172/jci32490 · Cited by 302 · see citing works

Mitochondrial death protein Nix is induced in cardiac hypertrophy and triggers apoptotic cardiomyopathy

Yussman, M. G., Toyokawa, T., Odley, A. M., Lynch, R. A., Wu, G., Colbert, M. C., Aronow, B. J., Lorenz, J. N., & Dorn, G. W. (2002) · Nature Medicine · doi:10.1038/nm719 · Cited by 296 · see citing works

Transmembrane glycine zippers: Physiological and pathological roles in membrane proteins

Kim, S., Jeon, T., Oberai, A., Yang, D., Schmidt, J. J., & Bowie, J. U. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501234102 · Cited by 279 · see citing works

Proapoptotic BH3-only Bcl-2 family members induce cytochrome c release, but not mitochondrial membrane potential loss, and do not directly modulate voltage-dependent anion channel activity

Shimizu, S., & Tsujimoto, Y. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.2.577 · Cited by 273 · see citing works

Silencing of the Hypoxia-Inducible Cell Death Protein BNIP3 in Pancreatic Cancer

Okami, J., Simeone, D. M., & Logsdon, C. D. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-0089 · Cited by 238 · see citing works

Bnip3L is induced by p53 under hypoxia, and its knockdown promotes tumor growth

Fei, P., Wang, W., Kim, S.-H., Wang, S., Burns, T. F., Sax, J. K., Buzzai, M., Dicker, D. T., McKenna, W. G., Bernhard, E. J., et al. (2004) · Cancer Cell · doi:10.1016/j.ccr.2004.10.012 · Cited by 231 · see citing works

Macroautophagy Is Required for Multicellular Development of the Social Amoeba Dictyostelium discoideum

Otto, G. P., Wu, M. Y., Kazgan, N., Anderson, O. R., & Kessin, R. H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212467200 · Cited by 221 · see citing works

The role of Bcl-2 family member BNIP3 in cell death and disease: NIPping at the heels of cell death

Burton, T. R., & Gibson, S. B. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2008.185 · Cited by 218 · see citing works

Adenovirus E1B-19K/BCL-2 Interacting Protein BNIP3 Contains a BH3 Domain and a Mitochondrial Targeting Sequence

Yasuda, M., Theodorakis, P., Subramanian, T., & Chinnadurai, G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.20.12415 · Cited by 218 · see citing works

Bnip3 mediates mitochondrial dysfunction and cell death through Bax and Bak

Kubli, D. A., Ycaza, J. E., & Gustafsson, Å. B. (2007) · Biochemical Journal · doi:10.1042/bj20070319 · Cited by 208 · see citing works

Bcl-2/E1B 19 kDa-interacting protein 3-like protein (Bnip3L) interacts with Bcl-2/Bcl-xL and induces apoptosis by altering mitochondrial membrane permeability

Imazu, T., Shimizu, S., Tagami, S., Matsushima, M., Nakamura, Y., Miki, T., Okuyama, Ä., & Tsujimoto, Y. (1999) · Oncogene · doi:10.1038/sj.onc.1202722 · Cited by 187 · see citing works

Bnip3 functions as a mitochondrial sensor of oxidative stress during myocardial ischemia and reperfusion

Kubli, D. A., Quinsay, M. N., Huang, C., Lee, Y., & Gustafsson, Å. B. (2008) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00552.2008 · Cited by 187 · see citing works

FoxO3a regulates erythroid differentiation and induces BTG1, an activator of protein arginine methyl transferase 1

Bakker, W. J., Blázquez-Domingo, M., Kolbus, A., Besooyen, J., Steinlein, P., Beug, H., Coffer, P. J., Löwenberg, B., Lindern, M. V., & van Dijk, T. B. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200307056 · Cited by 182 · see citing works

Membrane assembly and remodeling during reticulocyte maturation

Chasis, J. A., Prenant, M., Leung, A., et al. (1989) · Blood · doi:10.1182/blood.v74.3.1112.1112 · Cited by 177 · see citing works

Molecular Basis of Bcl-xL’s Target Recognition Versatility Revealed by the Structure of Bcl-xL in Complex with the BH3 Domain of Beclin-1

Feng, W., Huang, S., Wu, H., & Zhang, M. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.06.069 · Cited by 175 · see citing works

Nix-Mediated Apoptosis Links Myocardial Fibrosis, Cardiac Remodeling, and Hypertrophy Decompensation

Diwan, A., Wansapura, J. P., Syed, F. M., Matkovich, S. J., Lorenz, J. N., & Dorn, G. W. (2008) · Circulation · doi:10.1161/circulationaha.107.727073 · Cited by 168 · see citing works

Unrestrained erythroblast development in Nix −/− mice reveals a mechanism for apoptotic modulation of erythropoiesis

Diwan, A., Koesters, A. G., Odley, A. M., Pushkaran, S., Baines, C. P., Spike, B. T., Daria, D., Jegga, A. G., Geiger, H., Aronow, B. J., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0610666104 · Cited by 159 · see citing works

Endoplasmic reticulum–mitochondria crosstalk in NIX-mediated murine cell death

Diwan, A., Matkovich, S. J., Yuan, Q., Zhao, W. H., Yatani, A., Brown, J. H., Molkentin, J. D., Kranias, E. G., & Dorn, G. W. (2008) · Journal of Clinical Investigation · doi:10.1172/jci36445 · Cited by 139 · see citing works

Distinct Pathways Regulate Proapoptotic Nix and BNip3 in Cardiac Stress

Galvez, A. S., Brunskill, E. W., Marreez, Y., Benner, B. J., Regula, K. M., Kirshenbaum, L. A., & Dorn, G. W. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509056200 · Cited by 129 · see citing works

Unique Dimeric Structure of BNip3 Transmembrane Domain Suggests Membrane Permeabilization as a Cell Death Trigger

Bocharov, E. V., Pustovalova, Y. E., Pavlov, K. V., Volynsky, P. E., Goncharuk, M. V., Ermolyuk, Y. S., Karpunin, D. V., Schulga, A. A., Kirpichnikov, M. P., Efremov, R. G., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701745200 · Cited by 128 · see citing works

Maturation of the reticulocyte in vitro

Gronowicz, G., Swift, H., & Steck, T. L. (1984) · Journal of Cell Science · doi:10.1242/jcs.71.1.177 · Cited by 128 · see citing works

Phylogenomics of Life-Or-Death Switches in Multicellular Animals: Bcl-2, BH3-Only, and BNip Families of Apoptotic Regulators

Aouacheria, A., Brunet, F., & Gouy, M. (2005) · Molecular Biology and Evolution · doi:10.1093/molbev/msi234 · Cited by 125 · see citing works

In vitro maturation of nascent reticulocytes to erythrocytes

Koury, M. J., Koury, S. T., Kopsombut, P., et al. (2004) · Blood · doi:10.1182/blood-2004-02-0616 · Cited by 123 · see citing works

The proapoptotic factor Nix is coexpressed with Bcl-xL during terminal erythroid differentiation

Aerbajinai, W., Giattina, M., Lee, Y. T., Raffeld, M. A., & Miller, J. L. (2003) · Blood · doi:10.1182/blood-2002-11-3324 · Cited by 116 · see citing works

Genetic studies with tumorigenic adenoviruses

TAKEMORI, N., Riggs, J. L., & Aldrich, C. E. (1968) · Virology · doi:10.1016/0042-6822(68)90189-x · Cited by 109 · see citing works

Sequence-specific Dimerization of the Transmembrane Domain of the “BH3-only” Protein BNIP3 in Membranes and Detergent

Sulistijo, E. S., Jaszewski, T. M., & MacKenzie, K. R. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308429200 · Cited by 100 · see citing works

NIX induces mitochondrial autophagy in reticulocytes

Zhang, J., & Ney, P. A. (2008) · Autophagy · doi:10.4161/auto.5552 · Cited by 92 · see citing works

cyt gene of adenoviruses 2 and 5 is an oncogene for transforming function in early region E1B and encodes the E1B 19,000-molecular-weight polypeptide

TAKEMORI, N., Cladaras, C., Bhat, B., Conley, A. J., & Wold, W. S. M. (1984) · Journal of Virology · doi:10.1128/jvi.52.3.793-805.1984 · Cited by 79 · see citing works

The Carboxy Terminal C-Tail of BNip3 Is Crucial in Induction of Mitochondrial Permeability Transition in Isolated Mitochondria

Kim, J.-Y., Cho, J.-J., Ha, J., & Park, J. (2002) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2001.2673 · Cited by 68 · see citing works

Sequence Dependence of BNIP3 Transmembrane Domain Dimerization Implicates Side-chain Hydrogen Bonding and a Tandem GxxxG Motif in Specific Helix–Helix Interactions

Sulistijo, E. S., & MacKenzie, K. R. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.09.065 · Cited by 67 · see citing works

Surface area and volume changes during maturation of reticulocytes in the circulation of the baboon

Waugh, R. E., McKenney, J. B., Bauserman, R. G., et al. (1997) · Journal of Laboratory and Clinical Medicine · doi:10.1016/s0022-2143(97)90007-x · Cited by 64 · see citing works

Autophagy of mitochondria in rat bone marrow erythroid cells Relation to nuclear extrusion

Heynen, M. J., Tricot, G. J. K., & Verwilghen, R. L. (1985) · Cell and Tissue Research · doi:10.1007/bf00214924 · Cited by 57 · see citing works

A novel adenovirus E1B19K-binding protein B5 inhibits apoptosis induced by Nip3 by forming a heterodimer through the C-terminal hydrophobic region

Ohi, N., Tokunaga, A., Tsunoda, H., et al. (1999) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400493 · Cited by 46 · see citing works

Analysis of the candidate 8p21 tumour suppressor, BNIP3L, in breast and ovarian cancer

Lai, J., Flanagan, J. M., Phillips, W. A., Chenevix‐Trench, G., & Arnold, J. M. (2003) · British Journal of Cancer · doi:10.1038/sj.bjc.6600674 · Cited by 45 · see citing works

The C. elegans orthologue ceBNIP3 interacts with CED-9 and CED-3 but kills through a BH3- and caspase-independent mechanism

Cizeau, J., Ray, R., Chen, G., Gietz, R. D., & Greenberg, A. H. (2000) · Oncogene · doi:10.1038/sj.onc.1203929 · Cited by 45 · see citing works

Functional substitution identifies a cell survival promoting domain common to adenovirus E1B 19 kDa and Bcl-2 proteins.

Subramanian, T., Boyd, J. M., & Chinnadurai, G. (1995) · PubMed · Cited by 37 · see citing works

Acidosis Regulates the Stability, Hydrophobicity, and Activity of the BH3-Only Protein Bnip3

Frazier, D. P., Wilson, A., Graham, R. M., Thompson, J. W., Bishopric, N. H., & Webster, K. A. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1625 · Cited by 36 · see citing works

Regulation of apoptosis by a Caenorhabditis elegans BNIP3 homolog

Yasuda, M., D’Sa-Eipper, C., Gong, X.-L., et al. (1998) · Oncogene · doi:10.1038/sj.onc.1202467 · Cited by 30 · see citing works

Bilateral multiple renal oncocytomas and cysts associated with a constitutional translocation (8;9)(q24.1;q34.3) and a rare constitutional VHL missense substitution

Teh, B. T., Blennow, E., Giraud, S., Sahlén, S., Hii, S.-I., Brookwell, R., Brauch, H. B., Nordenskjöld, M., Larsson, C., & Nicol, D. L. (1998) · Genes Chromosomes and Cancer · doi:10.1002/(sici)1098-2264(199803)21:3 · Cited by 25 · see citing works

Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) ¹

Klionsky, D. J., Abdel-Aziz, A. K., Abdelfatah, S., Abdellatif, M., Abdoli, A., Abel, S., Abeliovich, H., Abildgaard, M. H., Abudu, Y. P., Acevedo-Arozena, A., et al. (2021) · Autophagy · doi:10.1080/15548627.2020.1797280 · Cited by 2,622 · see citing works

Oxidative stress and autophagy: The clash between damage and metabolic needs

Filomeni, G., De Zio, D., & Cecconi, F. (2015) · Cell Death &amp; Differentiation · doi:10.1038/cdd.2014.150 · Cited by 2,195 · see citing works

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 · see citing works

Cargo recognition and trafficking in selective autophagy

Stolz, A., Ernst, A., & Dikic, I. (2014) · Nature Cell Biology · doi:10.1038/ncb2979 · Cited by 1,207 · see citing works

Interplay between ROS and autophagy in cancer cells, from tumor initiation to cancer therapy

Poillet-Perez, L., Despouy, G., Delage-Mourroux, R., & Boyer-Guittaut, M. (2015) · Redox Biology · doi:10.1016/j.redox.2014.12.003 · Cited by 503 · see citing works

Autophagy is required for exercise training‐induced skeletal muscle adaptation and improvement of physical performance

Lira, V. A., Okutsu, M., Zhang, M., Greene, N. P., Laker, R. C., Breen, D. S., Hoehn, K. L., & Yan, Z. (2013) · The FASEB Journal · doi:10.1096/fj.13-228486 · Cited by 432 · see citing works

Autophagy in acute kidney injury

Kaushal, G. P., & Shah, S. V. (2016) · Kidney International · doi:10.1016/j.kint.2015.11.021 · Cited by 389 · see citing works

Mitophagy: An Emerging Role in Aging and Age-Associated Diseases

Chen, G., Kroemer, G., & Kepp, O. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00200 · Cited by 359 · see citing works

Single-cell multiregion dissection of Alzheimer’s disease

Mathys, H., Boix, C. A., Akay, L. A., Xia, Z., Davila-Velderrain, J., Ng, A. P., Jiang, X., Abdelhady, G., Galani, K., Mantero, J., et al. (2024) · Nature · doi:10.1038/s41586-024-07606-7 · Cited by 343 · see citing works

Potential function for the Huntingtin protein as a scaffold for selective autophagy

Ochaba, J., Lukacsovich, T., Csikos, G., Zheng, S., Margulis, J., Salazar, L., Mao, K., Lau, A. L., Yeung, S. Y., Humbert, S., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1420103111 · Cited by 308 · see citing works

Mitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging

Leduc-Gaudet, J.-P., Hussain, S. N. A., Barreiro, E., & Gouspillou, G. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22158179 · Cited by 268 · see citing works

Mitochondrial Pruning by Nix and BNip3: An Essential Function for Cardiac-Expressed Death Factors

Dorn, G. W. (2010) · Journal of Cardiovascular Translational Research · doi:10.1007/s12265-010-9174-x · Cited by 215 · see citing works

Peroxisome Proliferator-activated Receptor γ Coactivator 1α or 1β Overexpression Inhibits Muscle Protein Degradation, Induction of Ubiquitin Ligases, and Disuse Atrophy

Brault, J. J., Jespersen, J. G., & Goldberg, A. L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.113092 · Cited by 217 · see citing works

Hypoxia and Selective Autophagy in Cancer Development and Therapy

Daskalaki, I., Gkikas, I., & Tavernarakis, N. (2018) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2018.00104 · Cited by 188 · see citing works

Modulation of autophagy and ubiquitin-proteasome pathways during ultra-endurance running

Jamart, C., Francaux, M., Millet, G. Y., Deldicque, L., Frère, D., & Féasson, L. (2012) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00952.2011 · Cited by 157 · see citing works

Intensified mitophagy in skeletal muscle with aging is downregulated by PGC-1alpha overexpression in vivo

Yeo, D., Kang, C., Gomez-Cabrera, M. C., Vina, J., & Ji, L. L. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.10.456 · Cited by 137 · see citing works

Mitophagy in Acute Kidney Injury and Kidney Repair

Wang, Y., Cai, J., Tang, C., & Dong, Z. (2020) · Cells · doi:10.3390/cells9020338 · Cited by 130 · see citing works

Mitochondrial maintenance via autophagy contributes to functional skeletal muscle regeneration and remodeling

Nichenko, A. S., Southern, W. M., Atuan, M., Luan, J., Peissig, K. B., Foltz, S. J., Beedle, A. M., Warren, G. L., & Call, J. A. (2016) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00066.2016 · Cited by 80 · see citing works

In mammalian skeletal muscle, phosphorylation of TOMM22 by protein kinase CSNK2/CK2 controls mitophagy

Kravic, B., Harbauer, A. B., Romanello, V., Simeone, L., Vögtle, F.-N., Kaiser, T., Straubinger, M., Huraskin, D., Böttcher, M., Cerqua, C., et al. (2018) · Autophagy · doi:10.1080/15548627.2017.1403716 · Cited by 75 · see citing works

Selective Autophagy Receptors in Neuronal Health and Disease

Conway, O., Akpinar, H. A., Rogov, V. V., & Kirkin, V. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.10.013 · Cited by 75 · see citing works

HIF1α-dependent mitophagy facilitates cardiomyoblast differentiation

Zhao, J.-F., Rodger, C. E., Allen, G. F. G., Weidlich, S., & Ganley, I. G. (2020) · Cell Stress · doi:10.15698/cst2020.05.220 · Cited by 61 · see citing works

Inhibition of Isoprenylcysteine Carboxylmethyltransferase Induces Cell-Cycle Arrest and Apoptosis through p21 and p21-Regulated BNIP3 Induction in Pancreatic Cancer

Manu, K. A., Chai, T. F., Teh, J. T., Zhu, W. L., Casey, P. J., & Wang, M. (2017) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-16-0703 · Cited by 55 · see citing works

PAHSAs reduce cellular senescence and protect pancreatic beta cells from metabolic stress through regulation of Mdm2/p53

Rubin de Celis, M. F., Garcia-Martin, R., Syed, I., Lee, J., Aguayo-Mazzucato, C., Bonner-Weir, S., & Kahn, B. B. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2206923119 · Cited by 39 · see citing works

The Dual Roles for Autophagy in Cell Death and Survival

Debnath, J., & Fung, C. (2006) · doi:10.1002/352760880x.ch5

Autophagy functions in programmed cell death

Berry, D. L., & Baehrecke, E. H. (2008) · Autophagy · doi:10.4161/auto.5575 · Cited by 67 · see citing works

Presequence protease reverses mitochondria‐specific amyloid‐β‐induced mitophagy to protect mitochondria

Dou, Y., & Tan, Y. (2023) · The FASEB Journal · doi:10.1096/fj.202200216rrrr · Cited by 16 · see citing works

Mitophagy Plays an Essential Role in Reducing Mitochondrial Production of Reactive Oxygen Species and Mutation of Mitochondrial DNA by Maintaining Mitochondrial Quantity and Quality in Yeast

Kurihara, Y., Kanki, T., Aoki, Y., Hirota, Y., Saigusa, T., Uchiumi, T., & Kang, D. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.280156 · Cited by 279 · see citing works

Autophagy: Executor and Manager of Programmed Cell Death

Ji, Z. (2010) · Medical Recapitulate · Cited by 1 · see citing works