Lack of p53 Affects the Expression of Several Brain Mitochondrial Proteins: Insights from Proteomics into Important Pathways Regulated by p53
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The tumor suppressor protein p53 has been described "as the guardian of the genome" for its crucial role in regulating the transcription of numerous genes responsible for cells cycle arrest, senescence, or apoptosis in response to various stress signals. Although p53 promotes longevity by decreasing the risk of cancer through activation of apoptosis or cellular senescence, several findings suggest that an increase of its activity may have deleterious effects leading to selected aspects of the aging phenotype and neurodegenerative diseases. There is the link between p53 and oxidative stress, the latter a crucial factor that contributes to neurodegenerative processes like Alzheimer disease (AD). In the present study, using a proteomics approach, we analyzed the impact of lack of p53 on the expression of several brain mitochondrial proteins involved in different pathways, and how lack of p53 may present a target to restore neuronal impairments. Our investigation on isolated brain mitochondria from p53((-/-)) mice also provides a better understanding of the p53-mitochondria relationship and its involvement in the development of many diseases.
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Protein expression of MnSOD was significantly increased in mitochondria isolated from the brain of p53 knockout mice.
“Protein expression of MnSOD was significantly increased in mitochondria isolated from the brain of p53 knockout mice [89]”
From Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease (2020) · cites this paper as [89]
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Cites
Mutations in the p53 tumor suppressor gene: clues to cancer etiology and molecular pathogenesis.
Greenblatt, M. S., Bennett, W. P., Hollstein, M., & Harris, C. C. (1994) · PubMed · Cited by 3,463 · see citing works
Live or let die: the cell's response to p53
Vousden, K. H., & Lü, X. (2002) · Nature reviews. Cancer · doi:10.1038/nrc864 · Cited by 3,177 · see citing works
Calcium, ATP, and ROS: a mitochondrial love-hate triangle
Brookes, P. S., Yoon, Y., Robotham, J. L., Anders, M. W., & Sheu, S.-S. (2004) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00139.2004 · Cited by 2,575 · see citing works
A model for p53-induced apoptosis
Polyak, K., Xia, Y., Zweier, J. L., Kinzler, K. W., & Vogelstein, B. (1997) · Nature · doi:10.1038/38525 · Cited by 2,500 · see citing works
Cellular response to oxidative stress: Signaling for suicide and survival *
Martindale, J., & Holbrook, N. (2002) · Journal of Cellular Physiology · doi:10.1002/jcp.10119 · Cited by 2,392 · see citing works
Oxidative stress hypothesis in Alzheimer’s disease
Markesbery, W. R. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(96)00629-6 · Cited by 2,383 · see citing works
p53 mutant mice that display early ageing-associated phenotypes
Tyner, S. D., Venkatachalam, S., Choi, J., Jones, S., Ghebranious, N., Igelmann, H., Lu, X., Soron, G., Cooper, B., Brayton, C., et al. (2002) · Nature · doi:10.1038/415045a · Cited by 1,459 · see citing works
Evidence of oxidative damage in Alzheimer's disease brain: central role for amyloid β-peptide
Butterfield, D. A., Drake, J., Pocernich, C., & Castegna, A. (2001) · Trends in Molecular Medicine · doi:10.1016/s1471-4914(01)02173-6 · Cited by 1,114 · see citing works
Self-citationThe antioxidant function of the p53 tumor suppressor
Sablina, A. A., Budanov, A. V., Ilyinskaya, G. V., Agapova, L. S., Kravchenko, J. E., & Chumakov, P. M. (2005) · Nature Medicine · doi:10.1038/nm1320 · Cited by 1,110 · see citing works
Mitochondria, oxygen free radicals, disease and ageing
Raha, S., & Robinson, B. H. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01674-1 · Cited by 1,066 · cited 14× · see citing works
“High levels of p53 increase intracellular ROS by transactivation of genes encoding pro-oxidant proteins such as NQO1 (quinone oxidoreductase) [11] and proline oxidase (POX) [11], and for proapoptotic proteins, which include BAX and PUMA [11].”
BackgroundInfluentialDecision making by p53: life, death and cancer
Oren, M. (2003) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401183 · Cited by 1,063 · see citing works
VDAC2 Inhibits BAK Activation and Mitochondrial Apoptosis
Cheng, E. H.-Y., Sheiko, T. V., Fisher, J. K., Craigen, W. J., & Korsmeyer, S. J. (2003) · Science · doi:10.1126/science.1083995 · Cited by 852 · see citing works
ROS and p53: A versatile partnership
Liu, B., Chen, Y., & Clair, D. K. S. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.01.011 · Cited by 829 · see citing works
The Chaperone Function of hsp70 Is Required for Protection against Stress-Induced Apoptosis
Mosser, D., Caron, A., Bourget, L., Meriin, A. B., Sherman, M., Morimoto, R., & Massie, B. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.19.7146-7159.2000 · Cited by 768 · see citing works
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 · see citing works
MDM2 — master regulator of the p53 tumor suppressor protein
Momand, J., Wu, H.-H., & Dasgupta, G. (2000) · Gene · doi:10.1016/s0378-1119(99)00487-4 · Cited by 641 · see citing works
The cellular response to p53: the decision between life and death
Sionov, R. V., & Haupt, Y. (1999) · Oncogene · doi:10.1038/sj.onc.1203130 · Cited by 600 · see citing works
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 596 · see citing works
Modulation of mammalian life span by the short isoform of p53
Maier, B., Gluba, W., Bernier, B., Turner, T., Mohammad, K., Guise, T., Sutherland, A., Thorner, M., & Scrable, H. (2004) · Genes & Development · doi:10.1101/gad.1162404 · Cited by 586 · see citing works
Castegna, A., Aksenov, M. Y., Thongboonkerd, V., Klein, J. B., Pierce, W. M. J., Booze, R. M., Markesbery, W. R., & Butterfield, D. A. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01103.x · Cited by 581 · see citing works
Self-citationButterfield, D. A., Reed, T., Newman, S. F., & Sultana, R. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.05.037 · Cited by 564 · see citing works
Self-citationProteomic identification of nitrated proteins in Alzheimer's disease brain
Castegna, A., Thongboonkerd, V., Klein, J. B., Lynn, B. C., Markesbery, W. R., & Butterfield, D. A. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01786.x · Cited by 535 · see citing works
Self-citationCoping with stress: multiple ways to activate p53
Horn, H. F., & Vousden, K. H. (2007) · Oncogene · doi:10.1038/sj.onc.1210263 · Cited by 522 · see citing works
Sultana, R., Perluigi, M., & Butterfield, D. A. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.09.027 · Cited by 478 · see citing works
Self-citationAldehyde Dehydrogenases and Their Role in Carcinogenesis
Lindahl, R. G. (1992) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409239209082565 · Cited by 402 · see citing works
Sims, N. (1990) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1990.tb04189.x · Cited by 388 · see citing works
Butterfield, D. A., Poon, H. F., St. Clair, D., Keller, J. N., Pierce, W. M., Klein, J. B., & Markesbery, W. R. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2005.11.002 · Cited by 377 · see citing works
Self-citationIdentification of a novel stress-responsive gene Hi95 involved in regulation of cell viability
Budanov, A. V., Shoshani, T., Faerman, A., Zelin, E., Kamer, I., Kalinski, H., Gorodin, S., Fishman, A., Chajut, A., Einat, P., et al. (2002) · Oncogene · doi:10.1038/sj.onc.1205877 · Cited by 363 · see citing works
Maddocks, O. D. K., & Vousden, K. H. (2011) · Journal of Molecular Medicine · doi:10.1007/s00109-011-0735-5 · Cited by 359 · see citing works
Shoshan‐Barmatz, V., Israelson, A., Brdiczka, D. G., & Sheu, S. (2006) · Current Pharmaceutical Design · doi:10.2174/138161206777585111 · Cited by 307 · see citing works
Butterfield, D. A., Lange, M. L. B., & Rukhsana Sultana, A. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2010.02.005 · Cited by 298 · see citing works
Self-citationRegulation of the Human hsp70 Promoter by p53
Agoff, S. N., Hou, J., Linzer, D. I., & Wu, B. (1993) · Science · doi:10.1126/science.8418500 · Cited by 292 · see citing works
The Role of p53 in Metabolic Regulation
Puzio-Kuter, A. M. (2011) · Genes & Cancer · doi:10.1177/1947601911409738 · Cited by 273 · see citing works
Structure and expression of a human gene coding for a 71 kd heat shock ‘cognate’ protein
Dwornczak, B., & Mirault, M.-É. (1987) · Nucleic Acids Research · doi:10.1093/nar/15.13.5181 · Cited by 255 · see citing works
Velasco-Miguel, S., Buckbinder, L., Jean, P., Gelbert, L., Talbott, R. L., Laidlaw, J. L., Seizinger, B. R., & Kley, N. (1999) · Oncogene · doi:10.1038/sj.onc.1202274 · Cited by 249 · see citing works
Identification of ALDH4 as a p53-inducible gene and its protective role in cellular stresses
Yoon, K., Nakamura, Y., & Arakawa, H. (2004) · Journal of Human Genetics · doi:10.1007/s10038-003-0122-3 · Cited by 236 · see citing works
Nonn, L., Berggren, M. M., & Powis, G. (2003) · PubMed · Cited by 216 · see citing works
Outcomes of p53 activation - spoilt for choice
Vousden, K. H. (2006) · Journal of Cell Science · doi:10.1242/jcs.03293 · Cited by 188 · see citing works
Reddy, P. H. (2009) · CNS Spectrums · doi:10.1017/s1092852900024901 · Cited by 186 · see citing works
Proteomic Analysis of Protein Expression and Oxidative Modification in R6/2 Transgenic Mice
Marzia Perluigi, A., Poon, H. F., Maragos, W. F., Pierce, W. M. J., Klein, J. B., Calabrese, V., Cini, C., Marco, C. M. D., & Butterfield, D. A. (2005) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m500090-mcp200 · Cited by 184 · see citing works
Self-citationReciprocal down-regulation of p53 and SOD2 gene expression-implication in p53 mediated apoptosis
Drane, P., Bravard, A., Bouvard, V., & May, E. (2001) · Oncogene · doi:10.1038/sj.onc.1204101 · Cited by 180 · see citing works
A family of novel peroxidases, peroxiredoxins
Rhee, S. G., Kang, S. W., Netto, L. E. S., Seo, M. S., & Stadtman, E. R. (1999) · BioFactors · doi:10.1002/biof.5520100218 · Cited by 170 · see citing works
Olovnikov, I. A., Kravchenko, J. E., & Chumakov, P. M. (2008) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2008.11.005 · Cited by 151 · see citing works
Reduction of mitochondrial H2O2 by overexpressing peroxiredoxin 3 improves glucose tolerance in mice
Chen, L., Na, R., Gu, M., Salmon, A. B., Liu, Y., Liang, H., Qi, W., Remmen, H. V., Richardson, A. G., & Ran, Q. (2008) · Aging Cell · doi:10.1111/j.1474-9726.2008.00432.x · Cited by 148 · see citing works
Kim, S. H., Fountoulakis, M., Cairns, N. J., & Lübec, G. (2001) · Springer eBooks · doi:10.1007/978-3-7091-6262-0_18 · Cited by 142 · see citing works
Debra Boyd-kimball, A., Castegna, A., Rukhsana Sultana, A., Poon, H. F., Petroze, R. T., Lynn, B. C., Klein, J. B., & Butterfield, D. A. (2005) · Brain Research · doi:10.1016/j.brainres.2005.02.086 · Cited by 142 · see citing works
Self-citationDeranged Expression of Molecular Chaperones in Brains of Patients with Alzheimer's Disease
Yoo, B. C., Kim, S. H., Cairns, N. J., Fountoulakis, M., & Lübec, G. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.4109 · Cited by 137 · see citing works
MEKK1 suppresses oxidative stress-induced apoptosis of embryonic stem cell-derived cardiac myocytes
Minamino, T., Yujiri, T., Papst, P. J., Chan, E. D., Johnson, G. L., & Terada, N. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.26.15127 · Cited by 135 · see citing works
Pani, G., Bedogni, B., Anzevino, R., Colavitti, R., Palazzotti, B., Borrello, S., & Galeotti, T. (2000) · PubMed · Cited by 134 · see citing works
Sompol, P. M., Ittarat, W., Tangpong, J., Chen, Y., Doubinskaia, I. E., Batinic-Haberle, I., Abdul, H. M., Butterfield, D. A., & Clair, D. K. S. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2008.01.044 · Cited by 134 · see citing works
Self-citationSchägger, H., & Ohm, T. G. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.tb20219.x · Cited by 117 · see citing works
Cenini, G., Sultana, R., Memo, M., & Butterfield, D. A. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00163.x · Cited by 117 · see citing works
Self-citationDhar, S. K., Xu, Y., Chen, Y., & Clair, D. K. S. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601083200 · Cited by 111 · see citing works
Marzia Perluigi, A., Domenico, F. D., Giorgi, A., Schininà, M. E., Coccia, R., Cini, C., Bellia, F., Cambria, M. T., Cornelius, C., Butterfield, D. A., et al. (2010) · Journal of Neuroscience Research · doi:10.1002/jnr.22500 · Cited by 109 · see citing works
Self-citationBoyd-Kimball, D., Poon, H. F., Lynn, B. C., Cai, J., Pierce Jr., W. M., Klein, J. B., Ferguson, J., Link, C. D., & Butterfield, D. A. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.07.001 · Cited by 98 · see citing works
Conformational Altered p53 as an Early Marker of Oxidative Stress in Alzheimer's Disease
Buizza, L., Cenini, G., Lanni, C., Ferrari‐Toninelli, G., Prandelli, C., Govoni, S. M., Buoso, E., Racchi, M., Barcikowska, M., Styczyńska, M., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0029789 · Cited by 81 · see citing works
Self-citationCenini, G., Sultana, R., Memo, M., & Butterfield, D. A. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.03.015 · Cited by 79 · see citing works
Self-citationDomenico, F. D., Cenini, G., Rukhsana Sultana, A., Marzia Perluigi, A., Uberti, D. L., Memo, M., & Butterfield, D. A. (2009) · Neurochemical Research · doi:10.1007/s11064-009-9924-9 · Cited by 77 · see citing works
Self-citationWatching the watcher: Regulation of p53 by mitochondria
Holley, A. K., & St Clair, D. K. (2009) · Future Oncology · doi:10.2217/14796694.5.1.117 · Cited by 75 · see citing works
Self-citationp53: at the crossroad between cancer and ageing
Papazoglu, C., & Mills, A. (2007) · The Journal of Pathology · doi:10.1002/path.2086 · Cited by 73 · see citing works
Oxidation of 4‐hydroxy‐2‐nonenal by succinic semialdehyde dehydrogenase (ALDH5A)
Murphy, T. C., Amarnath, V., Gibson, K. M., & Picklo, M. J. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01839.x · Cited by 72 · see citing works
Manganese superoxide dismutase versus p53: the mitochondrial center
Holley, A. K., Dhar, S. K., & Clair, D. K. S. (2010) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2010.05612.x · Cited by 49 · see citing works
Human Diseases with Defects in Oxidative Phosphorylation
Bentlage, H., de Coo, I. F. M., Laak, H. T., Sengers, R. C. A., Trijbels, F. J. M., Ruitenbeek, W., Schlote, W., Pfeiffer, K., Gencic, S., von JAGOW, G., et al. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.0909p.x · Cited by 48 · see citing works
The p53 knowledgebase: an integrated information resource for p53 research
Lim, Y.-P., Lim, T. T., Chan, Y. L., Song, A. C. M., Yeo, B. H., Vojtĕsek, B., Coomber, D., Rajagopal, G., & Lane, D. P. (2006) · Oncogene · doi:10.1038/sj.onc.1209952 · Cited by 47 · see citing works
Proteasome Inhibitors Induce the Association of Alzheimer's Amyloid Precursor Protein with Hsc73
Kouchi, Z., Sorimachi, H., Suzuki, K., & Ishiura, S. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.9977 · Cited by 44 · see citing works
Mitochondrial localization of the low level p53 protein in proliferative cells
Ferecatu, I., Bergeaud, M., Rodriguez-Enfedaque, A., et al. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.07.111 · Cited by 43 · see citing works
Identification of a 71-Kilodalton Surface-Associated Hsp70 Homologue in Coxiella burnetii
Macellaro, A., Tujulin, E., Hjalmarsson, K., et al. (1998) · Infection and Immunity · doi:10.1128/iai.66.12.5882-5888.1998 · Cited by 40 · see citing works
Mitochondrial oxidation of 4‐hydroxy‐2‐nonenal in rat cerebral cortex
Murphy, T. C., Amarnath, V., & Picklo, M. J. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01628.x · Cited by 38 · see citing works
Barone, E., Cenini, G., Rukhsana Sultana, A., Domenico, F. D., Fiorini, A., Marzia Perluigi, A., Noel, T. J., Wang, C., Mancuso, C., Clair, D. K. S., et al. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4124 · Cited by 30 · see citing works
Self-citationHuman Diseases with Defects in Oxidative Phosphorylation
Schägger, H., & Ohm, T. G. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.0916p.x · Cited by 21 · see citing works
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- [51]Holley AK, St Clair DK (2009) Watching the watcher: regulation of p53 by mitochondria. Future Oncology 5: 117– 130. 19243304 PMC2710969
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Lee, J., Kim, Y., Liu, T., Hwang, Y. J., Hyeon, S. J., Im, H., Lee, K., Alvarez, V. E., McKee, A. C., Um, S., et al. (2018) · Aging Cell · doi:10.1111/acel.12679 · Cited by 213 · see citing works
p53 and mitochondrial dysfunction: novel insight of neurodegenerative diseases
Dai, C.-Q., Luo, T.-T., Luo, S.-C., Wang, J.-Q., Wang, S.-M., Bai, Y.-H., Yang, Y.-L., & Wang, Y.-Y. (2016) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-016-9669-5 · Cited by 93 · see citing works
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“Protein expression of MnSOD was significantly increased in mitochondria isolated from the brain of p53 knockout mice [89], which is consistent with the p53 transcriptional repression of MnSOD [90,91].”
BackgroundSelf-citationTramutola, A., Pupo, G., Di Domenico, F., Barone, E., Arena, A., Lanzillotta, C., Broekaart, D., Blarzino, C., Head, E., Butterfield, D. A., et al. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-151105 · Cited by 40 · see citing works
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- Authors
- Fiorini, A., Sultana, R., Barone, E., Cenini, G., Perluigi, M., Mancuso, C., Cai, J., Klein, J. B., St. Clair, D., & Butterfield, D. A.
- Affiliations
- University of Kentucky (US)
- Sapienza University of Rome (IT)
- University of Louisville (US)
- Corresponding author
- Butterfield, D. Allan
- Venue
- PLoS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2012-11-27
- Volume
- 7
- Issue
- 11
- Pages
- e49846
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC3507874
- OpenAlex
- W2135607483
- Cited by
- 16
- References
- 70
- Citations by year
- 2021: 1 · 2020: 3 · 2019: 1 · 2018: 1 · 2017: 3 · 2016: 4 · 2015: 1 · 2014: 1 · 2013: 1
- FWCI
- 0.39
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- PLoS ONE (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- UKnowledge (University of Kentucky) (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- IRIS Research product catalog (Sapienza University of Rome) (submittedVersion)
- PubliCatt (Università Cattolica del Sacro Cuore) (submittedVersion, other-oa)
- Funders
- National Institutes of Health
- National Institute on Aging (P01AG005119, AG0 5119)
- National Cancer Institute (R01CA139843, CA139843)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Keywords
- p53, p53 knockout mice, brain mitochondria, mitochondrial proteins, oxidative stress, neurodegeneration, Alzheimer's disease, aging, tumor suppressor, proteomics
- MeSH terms
- Animals, Brain, Gene Expression Regulation, Male, Mitochondria, Models, Biological, Signal Transduction, Tumor Suppressor Protein p53, Mice, Knockout, Mitochondrial Proteins, Proteomics, Mice
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