Generation and Characterization of Endonuclease G Null Mice
Open accessAbstract
Endonuclease G (endo G) is one of the most abundant nucleases in eukaryotic cells. It is encoded in the nucleus and imported to the mitochondrial intermembrane space. This nuclease is active on single- and double-stranded DNA. We genetically disrupted the endo G gene in mice without disturbing a conserved, overlapping gene of unknown function that is oriented tail to tail with the endo G gene. In these mice, the production of endo G protein is not detected, and the disruption abolishes the nuclease activity of endo G. The absence of endo G has no effect on mitochondrial DNA copy number, structure, or mutation rate over the first five generations. There is also no obvious effect on nuclear DNA degradation in standard apoptosis assays. The endo G null mice are viable and show no age-related or generational abnormalities anatomically or histologically. We infer that this highly conserved protein has no mitochondrial or apoptosis function that can discerned by the assays described here and that it may have a function yet to be determined. The early embryonic lethality of endo G null mice recently reported by others may be due to the disruption of the gene that overlaps the endo G gene.
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The actual contribution of ENDOG to RCD in mammals has been questioned by generation of Endog−/− mice, whose cells display normal sensitivity to multiple lethal triggers.
“the actual contribution of ENDOG to RCD in mammals [675] has been questioned by the generation of Endog−/− mice, whose cells display normal sensitivity to multiple lethal triggers [676, 677].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [677]
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Endonuclease G is an apoptotic DNase when released from mitochondria
Li, L. Y., Luo, X., & Wang, X. (2001) · Nature · doi:10.1038/35083620 · Cited by 1,787 · see citing works
Sequence and gene organization of mouse mitochondrial DNA.
Bibb, M., Etten, R. V., Wright, C. T., Walberg, M. W., & Clayton, D. A. (1981) · Cell · doi:10.1016/0092-8674(81)90300-7 · Cited by 1,619 · see citing works
R-loops at immunoglobulin class switch regions in the chromosomes of stimulated B cells
Yu, K.-F., Chédin, F., Hsieh, C.-L., Wilson, T. E., & Lieber, M. (2003) · Nature Immunology · doi:10.1038/ni919 · Cited by 767 · see citing works
Self-citationAn abundance of bidirectional promoters in the human genome.Preprint
Trinklein, N., Aldred, S. F., Hartman, S. J., Schroeder, D. I., Otillar, R., & Myers, R. (2003) · Genome Research · doi:10.1101/gr.1982804 · Cited by 641 · see citing works
Replication and Transcription of Vertebrate Mitochondrial DNA
Clayton, D. A. (1991) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.07.110191.002321 · Cited by 639 · see citing works
The harlequin mouse mutation downregulates apoptosis-inducing factor
Klein, J. A., Longo-Guess, C. M., Rossmann, M. P., Seburn, K. L., Hurd, R. E., Frankel, W. N., Bronson, R. T., & Ackerman, S. L. (2002) · Nature · doi:10.1038/nature01034 · Cited by 605 · see citing works
Mitochondrial endonuclease G is important for apoptosis in C. elegans
Parrish, J., Li, L., Klotz, K., Ledwich, D., Wang, X., & Xue, D. (2001) · Nature · doi:10.1038/35083608 · Cited by 427 · see citing works
Transcription and Replication of Animal Mitochondrial DNAs
Clayton, D. A. (1992) · International review of cytology · doi:10.1016/s0074-7696(08)62067-7 · Cited by 360 · see citing works
Failure to produce mitochondrial DNA results in embryonic lethality in Rnaseh1 null mice
Cerritelli, S. M., Frolova, E. G., Feng, C., Grinberg, A., Love, P. E., & Crouch, R. J. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00088-1 · Cited by 358 · see citing works
Bidirectional Gene Organization
Adachi, N., & Lieber, M. R. (2002) · Cell · doi:10.1016/s0092-8674(02)00758-4 · Cited by 346 · see citing works
Self-citationDependence of transcriptional repression on CpG methylation density
Hsieh, C.-L. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.8.5487-5494.1994 · Cited by 321 · see citing works
Self-citationDependence of Transcriptional Repression on CpG Methylation Density
Hsieh, C. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.8.5487 · Cited by 300 · see citing works
Self-citationPrimers for Mitochondrial DNA Replication Generated by Endonuclease G
Côté, J., & Ruiz-Carrillo, A. (1993) · Science · doi:10.1126/science.7688144 · Cited by 240 · see citing works
Daniels, G. A., & Lieber, M. R. (1995) · Nucleic Acids Research · doi:10.1093/nar/23.24.5006 · Cited by 214 · see citing works
Self-citationChang, D. D., Hauswirth, W. W., & Clayton, D. A. (1985) · The EMBO Journal · doi:10.1002/j.1460-2075.1985.tb03817.x · Cited by 209 · see citing works
Xu, B., & Clayton, D. A. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00676.x · Cited by 190 · see citing works
Zhang, J., Liu, X., Scherer, D. C., Kaer, L. V., Wang, X., & Xu, M. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.21.12480 · Cited by 183 · see citing works
Initiation of Mitochondrial DNA Replication by Transcription and R-loop Processing
Lee, D. Y., & Clayton, D. A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.46.30614 · Cited by 164 · see citing works
Xu, B., & Clayton, D. A. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.1.580 · Cited by 142 · see citing works
Schäfer, P., Scholz, S., Gimadutdinow, O., Cymerman, I. A., Bujnicki, J. M., Ruiz-Carrillo, A., Pingoud, A. M., & Meiß, G. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.02.069 · Cited by 106 · see citing works
Endonuclease G is required for early embryogenesis and normal apoptosis in mice
Zhang, J., Dong, M., Li, L. Y., Fan, Y., Pathre, P., Dong, J., Lou, D., Wells, J. M., Olivares–Villagómez, D., Kaer, L. V., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2636393100 · Cited by 100 · see citing works
Nucleic acid structures and enzymes in the immunoglobulin class switch recombination mechanism
Yu, K., & Lieber, M. R. (2003) · DNA repair · doi:10.1016/j.dnarep.2003.08.010 · Cited by 96 · see citing works
Self-citationMammalian mitochondrial endonuclease G
Ohsato, T., Ishihara, N., Muta, T., Umeda, S., Ikeda, S., Mihara, K., Hamasaki, N., & Kang, D. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2002.03238.x · Cited by 91 · see citing works
Takai, D. (2003) · Molecular Biology and Evolution · doi:10.1093/molbev/msh040 · Cited by 83 · see citing works
Lee, D. Y., & Clayton, D. A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.39.24262 · Cited by 76 · see citing works
Recognition of (dG) .(dC) Sequences by Endonuclease G
Côté, J., Renaud, J., & Ruiz-Carrillo, A. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)94066-4 · Cited by 61 · see citing works
Analysis of the role of the NUC1 endo/exonuclease in yeast mitochondrial DNA recombination
Zassenhaus, H. P., & Denniger, G. (1994) · Current Genetics · doi:10.1007/bf00309540 · Cited by 60 · see citing works
Endonuclease G from mammalian nuclei is identical to the major endonuclease of mitochondria
Gerschenson, M., Houmiel, K. L., & Low, R. L. (1995) · Nucleic Acids Research · doi:10.1093/nar/23.1.88 · Cited by 51 · see citing works
Huang, K.-J., Zemelman, B. V., & Lehman, I. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201785200 · Cited by 33 · see citing works
Characterization and Expression of the Mouse Endonuclease G Gene
Prats, E., Noël, M., LÉTOURNEAU, J., Tiranti, V., Vaqué, J., Debón, R. M., Zeviani, M., Cornudella, L., & Ruiz-Carrillo, A. (1997) · DNA and Cell Biology · doi:10.1089/dna.1997.16.1111 · Cited by 31 · see citing works
Screening for Aging-Dependent Point Mutations in mtDNA
Michikawa, Y., & Attardi, G. M. (2003) · Mitochondrial DNA · doi:10.1385/1-59259-284-8:075 · Cited by 7 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Galluzzi, L., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Agostinis, P., Alnemri, E. S., Altucci, L., Amelio, I., Andrews, D. W., et al. (2018) · Cell Death & Differentiation · doi:10.1038/s41418-017-0012-4 · Cited by 6,680 · see citing works
Mitochondrial membrane permeabilization in cell death
Kroemer, G., Galluzzi, L., & Brenner, C. (2007) · Physiological Reviews · doi:10.1152/physrev.00013.2006 · Cited by 3,598 · see citing works
Mitochondria and cell death: outer membrane permeabilization and beyond
Tait, S. W. G., & Green, D. R. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2952 · Cited by 2,593 · see citing works
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 · see citing works
A nuclease that mediates cell death induced by DNA damage and poly(ADP-ribose) polymerase-1
Wang, Y., An, R., Umanah, G. K., Park, H., Nambiar, K., Eacker, S. M., Kim, B., Bao, L., Harraz, M. M., Chang, C., et al. (2016) · Science · doi:10.1126/science.aad6872 · Cited by 421 · see citing works
Heart mitochondria: gates of life and death
Gustafsson, Å. B., & Gottlieb, R. A. (2007) · Cardiovascular Research · doi:10.1093/cvr/cvm005 · Cited by 420 · see citing works
Poly(ADP-ribose) signals to mitochondrial AIF: A key event in parthanatos
Wang, Y., Dawson, V. L., & Dawson, T. M. (2009) · Experimental Neurology · doi:10.1016/j.expneurol.2009.03.020 · Cited by 405 · see citing works
Endonuclease G Regulates Budding Yeast Life and Death
Büttner, S., Eisenberg, T., Carmona-Gutierrez, D., Ruli, D., Knauer, H., Ruckenstuhl, C., Sigrist, C., Wissing, S., Kollroser, M., Fröhlich, K.-U., et al. (2007) · Molecular Cell · doi:10.1016/j.molcel.2006.12.021 · Cited by 331 · see citing works
Trashing the genome: the role of nucleases during apoptosis
Samejima, K., & Earnshaw, W. C. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1715 · Cited by 312 · see citing works
Mitochondrial control of caspase-dependent and -independent cell death
Pradelli, L. A., Bénéteau, M., & Ricci, J. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0285-y · Cited by 284 · see citing works
The mitochondrial death pathway: a promising therapeutic target in diseases
Gupta, S., Kass, G. E. N., Szegezdi, É., & Joseph, B. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2009.00697.x · Cited by 278 · see citing works
Mitochondrial membrane permeabilization: the sine qua non for cell death
Armstrong, J. S. (2006) · BioEssays · doi:10.1002/bies.20370 · Cited by 243 · see citing works
Mitochondria: a target for cancer therapy
Armstrong, J. S. (2005) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0706556 · Cited by 231 · see citing works
Apoptosis-inducing factor: A matter of neuron life and death
Krantic, S. M., Mechawar, N., Reix, S., & Quirion, R. (2007) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2006.12.002 · Cited by 189 · see citing works
Cheung, E. C., Joza, N. A., Steenaart, N. A. E., McClellan, K. A., Neuspiel, M., McNamara, S., MacLaurin, J. G., Rippstein, P. U., Park, D. S., Shore, G. C., et al. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601276 · Cited by 191 · see citing works
Apoptotic-like regulation of programmed cell death in plants
Reape, T. J., & McCabe, P. F. (2010) · APOPTOSIS · doi:10.1007/s10495-009-0447-2 · Cited by 181 · see citing works
Endonuclease G is a novel determinant of cardiac hypertrophy and mitochondrial function
McDermott‐Roe, C., Ye, J., Ahmed, R., Sun, X.-M., Serafin, A. M., Ware, J. S., Bottolo, L., Muckett, P. J., Cañas, X., Zhang, J., et al. (2011) · Nature · doi:10.1038/nature10490 · Cited by 157 · see citing works
Mitochondria and Programmed Cell Death in Parkinson's Disease: Apoptosis and Beyond
Perier, C., Bové, J., & Vila, M. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4074 · Cited by 159 · see citing works
DNA repair in mammalian mitochondria: Much more than we thought?
Liu, P., & Demple, B. (2010) · Environmental and Molecular Mutagenesis · doi:10.1002/em.20576 · Cited by 159 · see citing works
Keyel, P. A. (2017) · Developmental Biology · doi:10.1016/j.ydbio.2017.06.028 · Cited by 154 · see citing works
Apoptosis in Cardiovascular Diseases: Mechanism and Clinical Implications
Kim, N.-H., & Kang, P. M. (2010) · Korean Circulation Journal · doi:10.4070/kcj.2010.40.7.299 · Cited by 134 · see citing works
Cellular and nuclear degradation during apoptosis
He, B., Lü, N., & Zhou, Z. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.08.008 · Cited by 129 · see citing works
The mitochondrial death squad: hardened killers or innocent bystanders?
Ekert, P. G., & Vaux, D. L. (2005) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2005.09.001 · Cited by 120 · see citing works
Apoptogenic factors released from mitochondria
Vaux, D. L. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.08.002 · Cited by 119 · see citing works
Role of the nucleus in apoptosis: signaling and execution
Prokhorova, E. A., Zamaraev, A. V., Kopeina, G. S., Zhivotovsky, B., & Lavrik, I. N. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2031-y · Cited by 115 · see citing works
BUB1 mediation of caspase-independent mitotic death determines cell fate
Niikura, Y., Dixit, A., Scott, R. T., Perkins, G. A., & Kitagawa, K. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200702134 · Cited by 105 · see citing works
Switch from Caspase-dependent to Caspase-independent Death during Heart Development
Bahí, N., Zhang, J., Llovera, M., Ballester, M., Comella, J. X., & Sanchı́s, D. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601025200 · Cited by 100 · see citing works
EndoG is dispensable in embryogenesis and apoptosis
David, K. K., Sasaki, M., Yu, S.-W., Dawson, T. M., & Dawson, V. L. (2006) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401787 · Cited by 96 · see citing works
Gannavaram, S., Vedvyas, C., & Debrabant, A. (2007) · Journal of Cell Science · doi:10.1242/jcs.014050 · Cited by 91 · see citing works
Developmentally Programmed Nuclear Destruction during Yeast Gametogenesis
Eastwood, M. D., Cheung, S. W. T., Lee, K. Y., Moffat, J., & Meneghini, M. D. (2012) · Developmental Cell · doi:10.1016/j.devcel.2012.05.005 · Cited by 81 · see citing works
Nagata, S. (2007) · Immunological Reviews · doi:10.1111/j.1600-065x.2007.00571.x · Cited by 77 · see citing works
EXOG, a novel paralog of Endonuclease G in higher eukaryotes
Cymerman, I. A., Chung, I., Beckmann, B. M., Bujnicki, J. M., & Meiß, G. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkm1169 · Cited by 71 · see citing works
Endonuclease G: A role for the enzyme in recombination and cellular proliferation
Huang, K.-J., Ku, C., & Lehman, I. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603445103 · Cited by 65 · see citing works
Kiang, J. G., & Tsen, K. (2006) · PubMed · Cited by 65 · see citing works
“Simple but not simpler”: toward a unified picture of energy requirements in cell death
Chiarugi, A. (2005) · The FASEB Journal · doi:10.1096/fj.05-4200rev · Cited by 63 · see citing works
DNase γ Is the Effector Endonuclease for Internucleosomal DNA Fragmentation in Necrosis
Mizuta, R., Araki, S., Furukawa, M., Furukawa, Y., Ebara, S., Shiokawa, D., Hayashi, K., Tanuma, S.-I., & Kitamura, D. (2013) · PLoS ONE · doi:10.1371/journal.pone.0080223 · Cited by 60 · see citing works
Does apoptosis‐inducing factor (AIF) have both life and death functions in cells?
Porter, A. G., & Urbano, A. (2006) · BioEssays · doi:10.1002/bies.20444 · Cited by 58 · see citing works
Induction of Renal Endonuclease G by Cisplatin Is Reduced in DNase I-Deficient Mice
Yin, X., Apostolov, E. O., Shah, S. V., Wang, X., Bogdanov, K. V., Buzder, T., Stewart, A. G., & Basnakian, A. G. (2007) · Journal of the American Society of Nephrology · doi:10.1681/asn.2006080896 · Cited by 55 · see citing works
Caspase-independent apoptosis in yeast
Liang, Q., Li, W., & Zhou, B. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.02.018 · Cited by 55 · see citing works
AIF and endoG translocation in noise exposure induced hair cell death
Han, W., Shi, X., & Nuttall, A. L. (2005) · Hearing Research · doi:10.1016/j.heares.2005.10.004 · Cited by 54 · see citing works
Endonuclease G promotes cell death of non-invasive human breast cancer cells
Basnakian, A. G., Apostolov, E. O., Yin, X., Abiri, S. O., Stewart, A. G., Singh, A. B., & Shah, S. V. (2006) · Experimental Cell Research · doi:10.1016/j.yexcr.2006.09.012 · Cited by 53 · see citing works
Inserte, J., Cardona, M., Poncelas, M., Hernando, V., Vilardosa, Ú., Aluja, D., Parra, V. M., Sanchı́s, D., & David Garcia-dorado, A. (2016) · Basic Research in Cardiology · doi:10.1007/s00395-016-0537-6 · Cited by 52 · see citing works
Critical factors in the adoption of emotionally disturbed youths.
Kagan, R. M., & Reid, W. J. (1986) · PubMed · Cited by 49 · see citing works
Cuts can kill: the roles of apoptotic nucleases in cell death and animal development
Parrish, J. Z., & Xue, D. (2006) · Chromosoma · doi:10.1007/s00412-005-0038-0 · Cited by 48 · see citing works
Higgins, G. C., Beart, P. M., & Nagley, P. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0079-2 · Cited by 45 · see citing works
Endonuclease G promotes mitochondrial genome cleavage and replication
Wiehe, R. S., Gole, B., Châtre, L., Walther, P., Calzia, E., Ricchetti, M., & Wiesmüller, L. (2018) · Oncotarget · doi:10.18632/oncotarget.24822 · Cited by 44 · see citing works
The Drosophila melanogaster Gene cg4930 Encodes a High Affinity Inhibitor for Endonuclease G
Temme, C., Weißbach, R., Lilie, H., WILSON, C. G., Meinhart, A., Meyer, S., Golbik, R. P., Schierhorn, A., & Wahle, E. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808319200 · Cited by 41 · see citing works
Rescuing yeast mutants with human genes
Osborn, M. J., & Miller, J. (2007) · Briefings in Functional Genomics and Proteomics · doi:10.1093/bfgp/elm017 · Cited by 39 · see citing works
Crystal structure of the EndoG/EndoGI complex: mechanism of EndoG inhibition
Loll, B., Gebhardt, M., Wahle, E., & Meinhart, A. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp770 · Cited by 37 · see citing works
Zhang, J., Ye, J., Altafaj, A., Cardona, M., Bahi, N., Llovera, M., Cañas, X., Cook, S., Comella, J., & Sanchís, D. (2011) · PLoS ONE · doi:10.1371/journal.pone.0017998 · Cited by 39 · see citing works
Lee, J., Seo, T. W., Yi, J. H., Shin, K. S., & Yoo, S. J. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.181 · Cited by 36 · see citing works
Endonuclease G mediates endothelial cell death induced by carbamylated LDL
Apostolov, E. O., Ray, D., Alobuia, W. M., Mikhailova, M. V., Wang, X., Basnakian, A. G., & Shah, S. V. (2011) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01311.2010 · Cited by 35 · see citing works
Autoinflammation by Endogenous DNA
Nagata, S., & Kawane, K. (2011) · Advances in immunology · doi:10.1016/b978-0-12-387663-8.00004-1 · Cited by 32 · see citing works
Wang, X., Tryndyak, V., Apostolov, E. O., Yin, X., Shah, S. V., Pogribny, I. P., & Basnakian, A. G. (2008) · Cancer Letters · doi:10.1016/j.canlet.2008.04.053 · Cited by 29 · see citing works
Role of caspase-independent apoptosis in cardiovascular diseases
Bae, S. (2007) · Frontiers in bioscience · doi:10.2741/2861 · Cited by 28 · see citing works
Zan, H., Zhang, J., Al-Qahtani, A., Pone, E. J., White, C. A., Lee, D., Yel, L., Mai, T., & Casali, P. (2010) · Molecular Immunology · doi:10.1016/j.molimm.2010.10.023 · Cited by 26 · see citing works
Zan, H., & Casali, P. (2008) · Molecular Immunology · doi:10.1016/j.molimm.2008.07.003 · Cited by 26 · see citing works
Yeast Endonuclease G: Complex Matters of Death, and of Life
Burhans, W. C., & Weinberger, M. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.01.030 · Cited by 26 · see citing works
Role of EndoG in development and cell injury
Apostolov, E. O., Wang, X., Shah, S. V., & Basnakian, A. G. (2007) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402217 · Cited by 26 · see citing works
Role of endonuclease G in senescence-associated cell death of human endothelial cells
Diener, T., Neuhaus, M., Kozieł, R., Mičutková, L., & Jansen‐Dürr, P. (2010) · Experimental Gerontology · doi:10.1016/j.exger.2010.03.002 · Cited by 24 · see citing works
Robertson, A. B., Robertson, J., Fußer, M., & Klungland, A. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku1032 · Cited by 23 · see citing works
Multifaceted promotion of apoptosis by acetylcholinesterase
Knorr, D. Y., Demirbas, D., & Heinrich, R. (2023) · Frontiers in Cell Death · doi:10.3389/fceld.2023.1169966 · Cited by 22 · see citing works
Xu, Z., Zhang, J., David, K. K., Yang, Z.-J., Li, X., Dawson, T. M., Dawson, V. L., & Koehler, R. C. (2010) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00747.2009 · Cited by 20 · see citing works
Fismen, S., Mortensen, E., & Rekvig, O. P. (2010) · Immunology and Cell Biology · doi:10.1038/icb.2010.75 · Cited by 21 · see citing works
Blasco, N., Beà, A., Barés, G., Girón, C., Navaridas, R., Irazoki, A., López‐Lluch, G., Zorzano, A., Dolcet, X., Llovera, M., et al. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101736 · Cited by 19 · see citing works
Witte, F., Ruiz‐Orera, J., Mattioli, C. C., Blachut, S., Adami, E., Schulz, J. F., Schneider-Lunitz, V., Hummel, O., Patone, G., Mücke, M. B., et al. (2021) · Genome biology · doi:10.1186/s13059-021-02397-w · Cited by 16 · see citing works
Pardo, R., Blasco, N., Vilà, M., Beiroa, D., Nogueiras, R., Cañas, X., Simó, R., Sanchı́s, D., & Villena, J. A. (2016) · Endocrinology · doi:10.1210/en.2015-1334 · Cited by 19 · see citing works
Apoptosis and autoimmune diseases
Nagata, S. (2006) · IUBMB Life · doi:10.1080/15216540600746401 · Cited by 19 · see citing works
Buzder, T., Yin, X., Wang, X., Bánfalvi, G., & Basnakian, A. G. (2009) · DNA and Cell Biology · doi:10.1089/dna.2008.0850 · Cited by 17 · see citing works
Lin, J. L. J., Nakagawa, A., Lin, C., Hsiao, Y.-Y., Yang, W., Wang, Y.-T., Doudeva, L. G., Skeen-Gaar, R. R., Xue, D., & Yuan, H. S. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.316075 · Cited by 14 · see citing works
Endonucleases and apoptosis in animals
Aleksandrushkina, N. I., & Vanyushin, B. F. (2012) · Biochemistry (Moscow) · doi:10.1134/s0006297912130032 · Cited by 14 · see citing works
Cell death in normal and abnormal development
Mirkes, P. E. (2008) · Congenital Anomalies · doi:10.1111/j.1741-4520.2007.00175.x · Cited by 13 · see citing works
Ageichik, A. V., Samejima, K., Kaufmann, S. H., & Earnshaw, W. C. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704307200 · Cited by 13 · see citing works
Handbook of Mitochondrial Dysfunction
Ahmad, S. I. (2019) · CRC Press eBooks · doi:10.1201/9780429443336 · Cited by 12 · see citing works
Oda, K., Kawasaki, N., Fukuyama, M., & Ikeda, S. (2007) · BMB Reports · doi:10.5483/bmbrep.2007.40.6.1095 · Cited by 12 · see citing works
Czarny, P. L., Ziółkowska, S., Kołodziej, Ł., Watała, C. W., Wigner, P., Bliźniewska-Kowalska, K. M., Wachowska, K., Gałecka, M., Synowiec, E., Gałecki, P., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241914752 · Cited by 11 · see citing works
DNase I Induces Other Endonucleases in Kidney Tubular Epithelial Cells by Its DNA-Degrading Activity
Fahmi, T., Wang, X., Zhdanov, D. D., Islam, I., Apostolov, E. O., Savenka, A. V., & Basnakian, A. G. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21228665 · Cited by 10 · see citing works
Barés, G., Beà, A., Hernández, L., Navaridas, R., Felip, I., Megino‐Luque, C., Blasco, N., Nadeu, F., Campo, E., Llovera, M., et al. (2021) · Cancers · doi:10.3390/cancers13153803 · Cited by 9 · see citing works
The Intrinsic Pathway of Apoptosis
Kaufmann, S. H. (2007) · Humana Press eBooks · doi:10.1007/978-1-59745-221-2_1 · Cited by 9 · see citing works
Biallelic Variants in ENDOG Associated with Mitochondrial Myopathy and Multiple mtDNA Deletions
Nasca, A., Legati, A., Meneri, M., Ermert, M. E., Frascarelli, C., Zanetti, N., Garbellini, M., Comi, G. P., Catania, A., Lamperti, C., et al. (2022) · Cells · doi:10.3390/cells11060974 · Cited by 8 · see citing works
CHCHD10 mutations induce tissue-specific mitochondrial DNA deletions with a distinct signature
Shammas, M. K., Nie, Y., Gilsrud, A. J., Huang, X., Narendra, D. P., & Chinnery, P. F. (2023) · Human Molecular Genetics · doi:10.1093/hmg/ddad161 · Cited by 7 · see citing works
Giralt, A., Sanchı́s, D., Cherubini, M., Ginés, S., Cañas, X., Comella, J. X., & Alberch, J. (2013) · Experimental Neurology · doi:10.1016/j.expneurol.2013.03.028 · Cited by 7 · see citing works
Xu, X., Penjweini, R., Székvölgyi, L., Karányi, Z., Heckel, A., Gurusamy, D., Varga, D., Yang, S., Brown, A. L., Cui, W., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2411298122 · Cited by 6 · see citing works
Seo, T. W., Lee, J. S., & Yoo, S. J. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.08.047 · Cited by 6 · see citing works
Misic, V., El-Mogy, M. M., Geng, S., & Haj-Ahmad, Y. (2016) · Molecular Biology · doi:10.1134/s0026893316020175 · Cited by 4 · see citing works
EndoGI modulates Notch signaling and axon guidance in Drosophila
O’Keefe, D. D., Edgar, B. A., & Saucedo, L. J. (2010) · Mechanisms of Development · doi:10.1016/j.mod.2010.10.001 · Cited by 4 · see citing works
Sarah, A. T. (2011) · InTech eBooks · doi:10.5772/23358 · Cited by 4 · see citing works
Apoptosis, senescence and cancer (cancer drug discovery and development)
Young, A. R. J. (2009) · British Journal of Cancer · doi:10.1038/sj.bjc.6604944 · Cited by 4 · see citing works
Endonuclease G: The Link Between Mitochondria and Cardiac Hypertrophy?
Bugger, H., & Abel, E. D. (2012) · Circulation Research · doi:10.1161/res.0b013e318249dcc8 · Cited by 3 · see citing works
Cupo, R. R., Domínguez‐Martín, E., & Youle, R. (2026) · Current Biology · doi:10.1016/j.cub.2026.01.006 · Cited by 2 · see citing works
Human Endonuclease G Preferentially Cleaves Oxidatively Damaged DNA
Lu, W.-T., Chen, Y.-P., Yang, W., Yuan, H. S., & Lin, J. L. J. (2026) · Biochemistry · doi:10.1021/acs.biochem.5c00669 · Cited by 1 · see citing works
Cytotoxic Endonucleases: New Targets for Prostate Cancer Chemotherapy
Wang, X., Marina, V., & Alexei, G. (2011) · InTech eBooks · doi:10.5772/25585 · Cited by 1 · see citing works
Yang, N., & Goping, I. S. (2013) · Colloquium Series on Building Blocks of the Cell Cell Structure and Function · doi:10.4199/c00080ed1v01y201303bbc003 · Cited by 1 · see citing works
Endonuclease G is dispensable for sperm mitochondrial DNA elimination during spermatogenesis in mice
Xie, X., Li, J., Zhang, X., Mo, S., Li, A., Sun, T., Xie, F.-Y., Luo, S., Wang, G., Ou, X., et al. (2024) · Biology Open · doi:10.1242/bio.061730 · Cited by 1 · see citing works
Fatokun, A. A. (2012) · TSpace (University of Toronto) · Cited by 1 · see citing works
Zhang, J. (2009) · Repositori ObertUDL (University of Lleida) · Cited by 1 · see citing works
Misic, V. (2013) · Brock University Digital Repository (Brock University) · Cited by 1 · see citing works
Role of Mitochondrial Proteins in Apoptosis
Saelens, X., Festjens, N., Walle, L. V., & Vandenabeele, P. (2006) · doi:10.1002/9783527619665.ch6
The role of cardiolipin in the regulation of mitochondria-dependent apoptosis
Gonzalvez, F. (2008) · Enlighten: Theses (The University of Glasgow)
Identification of novel signaling pathways for cardiomyocyte differentiation and growth
Ye, J. (2012) · LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas)
- Authors
- Irvine, R. A., Adachi, N., Shibata, D. K., Cassell, G. D., Yu, K., Karanjawala, Z. E., Hsieh, C.-L., & Lieber, M. R.
- Affiliations
- University of Southern California (US)
- Departments of Pathology, of Biochemistry & Molecular Biology, of Molecular Microbiology & Immunology, and of Biological Sciences
- Corresponding author
- Lieber, Michael R.
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2005-01
- Volume
- 25
- Issue
- 1
- Pages
- 294-302
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- PMC
- PMC538798
- OpenAlex
- W2125483893
- Cited by
- 111
- References
- 30
- Citations by year
- 2026: 2 · 2025: 1 · 2024: 3 · 2023: 4 · 2022: 1 · 2021: 4 · 2020: 2 · 2019: 1 · 2018: 2 · 2017: 1 · 2016: 5 · 2015: 3 · 2014: 2 · 2013: 7 · 2012: 6
- FWCI
- 3.67
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Molecular and Cellular Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute of General Medical Sciences (R01GM056984)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Keywords
- endonuclease G, gene knockout, mitochondrial DNA, mitochondrial intermembrane space, nuclease activity, mitochondrial DNA copy number, apoptosis, nuclear DNA degradation, embryonic lethality
- MeSH terms
- Animals, Cell Nucleus, Cell Survival, Chromatin, DNA, DNA, Mitochondrial, Endodeoxyribonucleases, Enzyme-Linked Immunosorbent Assay, Immunoglobulin G, Immunoglobulin M, Mice, Inbred C57BL, Mice, Mutant Strains, Mice, Transgenic, Mitochondria, Models, Genetic, Mutation, Plasmids, Spleen, Blotting, Southern, Blotting, Western, Apoptosis, Transgenes, Mice, DNA Fragmentation
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