The DOI matches its Crossref record; 56 of the 56 references it cites were found in a registry or an index.
SIRT4 Has Tumor-Suppressive Activity and Regulates the Cellular Metabolic Response to DNA Damage by Inhibiting Mitochondrial Glutamine Metabolism
Open accessAbstract
DNA damage elicits a cellular signaling response that initiates cell cycle arrest and DNA repair. Here, we find that DNA damage triggers a critical block in glutamine metabolism, which is required for proper DNA damage responses. This block requires the mitochondrial SIRT4, which is induced by numerous genotoxic agents and represses the metabolism of glutamine into tricarboxylic acid cycle. SIRT4 loss leads to both increased glutamine-dependent proliferation and stress-induced genomic instability, resulting in tumorigenic phenotypes. Moreover, SIRT4 knockout mice spontaneously develop lung tumors. Our data uncover SIRT4 as an important component of the DNA damage response pathway that orchestrates a metabolic block in glutamine metabolism, cell cycle arrest, and tumor suppression.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Moreover, evidence has shown that during the DNA damage response, normal cells show a decrease in glutaminolysis controlled by SIRT4 protein suppressing GLUD1. In the absence of SIRT4, a failure to undergo cell cycle arrest induced by DNA damage causes a delay in DNA repair and increased chromosomal instability, suggesting a tumor suppressor effect of SIRT4151.”
From Glutamine reliance in cell metabolism (2020) · cites this paper as [151]
In the citing paper
“Accordingly, loss of SIRT4 enhances glutamine-dependent proliferation and genomic instability, which simultaneously contribute to tumorigenesis151.”
From Glutamine reliance in cell metabolism (2020) · cites this paper as [151]
In the citing paper
“Similarly, SIRT4 is upregulated as part of the DNA damage response via ATF4 (Jeong et al. 2013).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Jeong et al. 2013
In the citing paper
“SIRT4 likewise appears to control tumorigenesis ((Jeong et al. 2013), (Csibi et al. 2013)) by inhibiting the high rate of glutamine metabolism associated with cancer growth;”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Jeong et al. 2013
In the citing paper
“DHODH activity is also elevated in response to DNA damage and upon genotoxic chemotherapy treatment to increase nucleotide synthesis for DNA repair.76,77”
From The multifaceted contributions of mitochondria to cellular metabolism (2018) · cites this paper as [76]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139
Rogakou, E. P., Pilch, D. R., Orr, A. H., Ivanova, V. S., & Bonner, W. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.10.5858 · Cited by 5,438
The DNA Damage Response: Making It Safe to Play with Knives
Ciccia, A., & Elledge, S. J. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.019 · Cited by 4,368
Otto Warburg's contributions to current concepts of cancer metabolism
Koppenol, W. H., Bounds, P. L., & Dang, C. V. (2011) · Nature Reviews Cancer · doi:10.1038/nrc3038 · Cited by 3,427
p21 in cancer: Intricate networks and multiple activities
Abbas, T., & Dutta, A. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2657 · Cited by 2,712
hSIR2SIRT1 Functions as an NAD-Dependent p53 Deacetylase
Vaziri, H., Dessain, S. K., Eaton, E. N., Imai, S., Frye, R. A., Pandita, T. K., Guarente, L., & Weinberg, R. A. (2001) · Cell · doi:10.1016/s0092-8674(01)00527-x · Cited by 2,690
DeBerardinis, R. J., Mancuso, A., Daikhin, E., Nissim, I., Yudkoff, M., Wehrli, S., & Thompson, C. B. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709747104 · Cited by 2,622
Genomic instability — an evolving hallmark of cancer
Negrini, S., Gorgoulis, V. G., & Halazonetis, T. D. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2858 · Cited by 2,397
Regulation of glutathione synthesis
Lu, S. C.-L. (2008) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2008.05.005 · Cited by 2,131
Sirtuins as regulators of metabolism and healthspan
Houtkooper, R. H., Pirinen, E., & Auwerx, J. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3293 · Cited by 2,008
Cell cycle checkpoint signaling through the ATM and ATR kinases
Abraham, R. T. (2001) · Genes & Development · doi:10.1101/gad.914401 · Cited by 1,966
Flagged first, then by citations
Cited by
Sorted by citations
From Krebs to clinic: glutamine metabolism to cancer therapy
Altman, B. J., Stine, Z. E., & Dang, C. V. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2016.71 · Cited by 2,119
The multifaceted contributions of mitochondria to cellular metabolism
Spinelli, J. B., & Haigis, M. C. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0124-1 · Cited by 1,935
Self-citationSIRT1 and other sirtuins in metabolism
Chang, H.-C., & Guarente, L. (2014) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2013.12.001 · Cited by 1,157
Mitochondrial dysfunction in cell senescence and aging
Miwa, S., Kashyap, S., Chini, E., & von Zglinicki, T. (2022) · Journal of Clinical Investigation · doi:10.1172/jci158447 · Cited by 1,061
Glutamine reliance in cell metabolism
Yoo, H. C., Yu, Y. C., Sung, Y., & Han, J. M. (2020) · Experimental & Molecular Medicine · doi:10.1038/s12276-020-00504-8 · Cited by 1,021
Glutaminolysis: A Hallmark of Cancer Metabolism
Yang, L., Venneti, S., & Nagrath, D. (2017) · Annual Review of Biomedical Engineering · doi:10.1146/annurev-bioeng-071516-044546 · Cited by 859
Metabolites and the Tumour Microenvironment: From Cellular Mechanisms to Systemic Metabolism
Elia, I., & Haigis, M. C. (2021) · Nature Metabolism · doi:10.1038/s42255-020-00317-z · Cited by 651
Self-citationAgeing, age-related diseases and oxidative stress: What to do next?
Luo, J., Mills, K., le Cessie, S., Noordam, R., & van Heemst, D. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2019.100982 · Cited by 581
NAD+ metabolism, stemness, the immune response, and cancer
Navas, L. E., & Carnero, A. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00354-w · Cited by 551
The aging lung: Physiology, disease, and immunity
Schneider, J. L., Rowe, J. H., Garcia-de-Alba, C., Kim, C. F., Sharpe, A. H., & Haigis, M. C. (2021) · Cell · doi:10.1016/j.cell.2021.03.005 · Cited by 500
Self-citationThe multifaceted functions of sirtuins in cancer
Chalkiadaki, A., & Guarente, L. (2015) · Nature reviews. Cancer · doi:10.1038/nrc3985 · Cited by 513
Sirtuins, a promising target in slowing down the ageing process
Grabowska, W., Sikora, E., & Bielak-Zmijewska, A. (2017) · Biogerontology · doi:10.1007/s10522-017-9685-9 · Cited by 470
Calorie restriction and sirtuins revisited
Guarente, L. (2013) · Genes & Development · doi:10.1101/gad.227439.113 · Cited by 464
Sirtuin 4 is a lipoamidase regulating pyruvate dehydrogenase complex activity
Mathias, R. A., Greco, T. M., Oberstein, A., Budayeva, H. G., Chakrabarti, R., Rowland, E. A., Kang, Y., Shenk, T., & Cristea, I. M. (2014) · Cell · doi:10.1016/j.cell.2014.11.046 · Cited by 430
Sirtuin signaling in cellular senescence and aging
Lee, S.-H., Lee, J.-H., Lee, H., & Min, K. (2019) · BMB Reports · doi:10.5483/bmbrep.2019.52.1.290 · Cited by 449
Self-citationNuclear DNA damage signalling to mitochondria in ageing
Fang, E. F., Scheibye-Knudsen, M., Chua, K. F., Mattson, M. P., Croteau, D. L., & Bohr, V. A. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.14 · Cited by 387
Tafani, M., Sansone, L., Limana, F., Arcangeli, T., Santis, E. D., Polese, M., Fini, M., & Russo, M. A. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/3907147 · Cited by 379
Emerging roles of SIRT1 in fatty liver diseases
Ding, R., Bao, J., & Deng, C. (2017) · International Journal of Biological Sciences · doi:10.7150/ijbs.19370 · Cited by 364
Self-citationThe Roles of Histone Deacetylases and Their Inhibitors in Cancer Therapy
Guo, L., Tian, Y., & Zhu, W. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.576946 · Cited by 364
Sirtuins in Renal Health and Disease
Morigi, M., Perico, L., & Benigni, A. (2018) · Journal of the American Society of Nephrology · doi:10.1681/asn.2017111218 · Cited by 359
Yang, W., Nagasawa, K., Münch, C., Xu, Y., Satterstrom, F. K., Jeong, S., Hayes, S., Jedrychowski, M. P., Vyas, F. S., Zaganjor, E., et al. (2016) · Cell · doi:10.1016/j.cell.2016.10.016 · Cited by 341
Self-citationSIRT4 is a lysine deacylase that controls leucine metabolism and insulin secretion
Anderson, K. A., Huynh, F. K., Fisher-Wellman, K., Stuart, J. D., Peterson, B. S., Douros, J. D., Wagner, G. R., Thompson, J. W., Madsen, A. S., Green, M. F., et al. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.03.003 · Cited by 326
“Sirt4 ablation in mice activates glutamate dehydrogenase, leading to increased glutamine metabolism (Csibi et al., 2013; Jeong et al., 2013, 2014).”
BackgroundCarrico, C., Meyer, J. G., He, W., Gibson, B. W., & Verdin, E. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.01.016 · Cited by 331
Cloonan, S. M., & Choi, A. M. K. (2016) · Journal of Clinical Investigation · doi:10.1172/jci81113 · Cited by 322
Mitochondrial Sirtuins and Molecular Mechanisms of Aging
van de Ven, R. A. H., Santos, D., & Haigis, M. C. (2017) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2017.02.005 · Cited by 312
Self-citationDysregulated metabolism contributes to oncogenesis
Hirschey, M. D., DeBerardinis, R. J., Diehl, A. M., Drew, J. E., Frezza, C., Green, M. F., Jones, L. W., Ko, Y. H., Le, A., Lea, M. A., et al. (2015) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2015.10.002 · Cited by 316
Tatone, C., Emidio, G. D., Barbonetti, A., Carta, G., Luciano, A. M., Falone, S., & Amicarelli, F. (2018) · Human Reproduction Update · doi:10.1093/humupd/dmy003 · Cited by 296
Nuclear Acetyl-CoA Production by ACLY Promotes Homologous Recombination
Sivanand, S., Rhoades, S., Jiang, Q., Lee, J. V., Benci, J., Zhang, J., Yuan, S., Viney, I., Zhao, S., Carrer, A., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.06.008 · Cited by 295
Self-citationDNA damage response and metabolic disease
Shimizu, I., Yoshida, Y., Suda, M., & Minamino, T. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.10.008 · Cited by 286
Sirtuins: guardians of mammalian healthspan
Giblin, W., Skinner, M. E., & Lombard, D. B. (2014) · Trends in Genetics · doi:10.1016/j.tig.2014.04.007 · Cited by 286
Lüscher, B., Bütepage, M., Eckei, L., Krieg, S., Verheugd, P., & Shilton, B. H. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00122 · Cited by 264
Mitochondrial sirtuins, metabolism, and aging
Ji, Z., Liu, G., & Qu, J. T. (2021) · Journal of genetics and genomics/Journal of Genetics and Genomics · doi:10.1016/j.jgg.2021.11.005 · Cited by 250
DNA Damage, Repair, and Cancer Metabolism
Turgeon, M., Perry, N. J. S., & Poulogiannis, G. (2018) · Frontiers in Oncology · doi:10.3389/fonc.2018.00015 · Cited by 249
Sirtuin regulation in aging and injury
Poulose, N., & Raju, R. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.08.017 · Cited by 236
Arginine Methylation of MDH1 by CARM1 Inhibits Glutamine Metabolism and Suppresses Pancreatic Cancer
Wang, Y.-P., Zhou, W., Wang, J., Huang, X., Zuo, Y., Wang, T.-S., Gao, X. J., Xu, Y., Zou, S., Liu, Y., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.09.028 · Cited by 230
Sirtuins, epigenetics and longevity
Wątroba, M., Dudek, I., Skoda, M., Stangret, A., Rzodkiewicz, P., & Szukiewicz, D. (2017) · Ageing Research Reviews · doi:10.1016/j.arr.2017.08.001 · Cited by 224
Role of NAD+ and mitochondrial sirtuins in cardiac and renal diseases
Hershberger, K. A., Martin, A. S., & Hirschey, M. D. (2017) · Nature Reviews Nephrology · doi:10.1038/nrneph.2017.5 · Cited by 220
Brown, K. K., Spinelli, J. B., Asara, J. M., & Toker, A. (2017) · Cancer Discovery · doi:10.1158/2159-8290.cd-16-0611 · Cited by 198
Farnie, G., Sotgia, F., & Lisanti, M. P. (2015) · Oncotarget · doi:10.18632/oncotarget.5401 · Cited by 206
An overview of Sirtuins as potential therapeutic target: Structure, function and modulators
Wang, Y., He, J., Liao, M., Hu, M., Li, W., Ouyang, H., Wang, X., Ye, T., Zhang, Y., & Ouyang, L. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.10.028 · Cited by 210
Self-citationSIRT3 deficiency impairs mitochondrial and contractile function in the heart
Koentges, C., Pfeil, K., Schnick, T., Wiese, S., Dahlbock, R., Cimolai, M. C., Meyer-Steenbuck, M., Cenkerova, K., Hoffmann, M. M., Jaeger, C., et al. (2015) · Basic Research in Cardiology · doi:10.1007/s00395-015-0493-6 · Cited by 202
Emerging therapeutic roles for NAD+ metabolism in mitochondrial and age‐related disorders
Srivastava, S. (2016) · Clinical and Translational Medicine · doi:10.1186/s40169-016-0104-7 · Cited by 200
Dual Tumor Suppressor and Tumor Promoter Action of Sirtuins in Determining Malignant Phenotype
Carafa, V., Altucci, L., & Nebbioso, A. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.00038 · Cited by 186
Targeting Glutamine Induces Apoptosis: A Cancer Therapy Approach
Chen, L., & Cui, H. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms160922830 · Cited by 184
Allele-Specific Reprogramming of Cancer Metabolism by the Long Non-coding RNA CCAT2
Redis, R. S., Vela, L. E., Lu, W., de Oliveira, J. F., Ivan, C., Rodriguez‐Aguayo, C., Adamóski, D., Pasculli, B., Taguchi, A., Chen, Y., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.01.015 · Cited by 182
The role of mitochondrial sirtuins in health and disease
Osborne, B., Bentley, N. L., Montgomery, M. K., & Turner, N. A. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.197 · Cited by 183
The role of sirtuins in aging and age-related diseases
Wątroba, M., & Szukiewicz, D. (2015) · Advances in Medical Sciences · doi:10.1016/j.advms.2015.09.003 · Cited by 190
Melatonin and sirtuins: A “not-so unexpected” relationship
Mayo, J. C., Sainz, R. M., González Menéndez, P., Cepas, V., Tan, D., & Reiter, R. J. (2017) · Journal of Pineal Research · doi:10.1111/jpi.12391 · Cited by 175
SIRT5 facilitates cancer cell growth and drug resistance in non-small cell lung cancer
Lü, W., Zuo, Y., Feng, Y., & Zhang, M. (2014) · Tumor Biology · doi:10.1007/s13277-014-2372-4 · Cited by 174
Sirtuin Inhibitors as Anticancer Agents
Hu, J., Jing, H., & Lin, H. (2014) · Future Medicinal Chemistry · doi:10.4155/fmc.14.44 · Cited by 174
Fu, S., Li, Z., Xiao, L., Hu, W., Zhang, L., Xie, B., Zhou, Q., He, J., Qiu, Y., Wen, M., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.07.002 · Cited by 169
Sirtuins and their Biological Relevance in Aging and Age-Related Diseases
Zhao, L., Cao, J., Hu, K., He, X., Dou, Y., Tong, T., & Han, L. (2020) · Aging and Disease · doi:10.14336/ad.2019.0820 · Cited by 178
The emerging and diverse roles of sirtuins in cancer: a clinical perspective
Chen, W., Yuan, H., & Su, L. (2013) · OncoTargets and Therapy · doi:10.2147/ott.s37750 · Cited by 169
Oncogenic regulation of tumor metabolic reprogramming
Tarrado‐Castellarnau, M., de Atauri, P., & Cascante, M. (2016) · Oncotarget · doi:10.18632/oncotarget.10911 · Cited by 165
SIRT4 regulates ATP homeostasis and mediates a retrograde signaling via AMPK
Ho, L., Titus, A. S., Banerjee, K. K., George, S., Lin, W., Deota, S., Saha, A. K., Nakamura, K., Gut, P., Verdin, E. M., et al. (2013) · Aging · doi:10.18632/aging.100616 · Cited by 162
Mitochondrial Sirtuins and Their Relationships with Metabolic Disease and Cancer
Kumar, S., & Lombard, D. B. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6213 · Cited by 160
UHRF1 promotes aerobic glycolysis and proliferation via suppression of SIRT4 in pancreatic cancer
Hu, Q., Qin, Y., Ji, S., Xu, W., Liu, W., Sun, Q., Zhang, Z., Liu, M., Ni, Q., Yu, X., et al. (2019) · Cancer Letters · doi:10.1016/j.canlet.2019.03.024 · Cited by 159
Self-citationTumour-suppressive function of SIRT4 in human colorectal cancer
Miyo, M., Yamamoto, H., Konno, M., Colvin, H. S., Nishida, N., Koseki, J., Kawamoto, K., Ogawa, H., Hamabe, A., Uemura, M., et al. (2015) · British Journal of Cancer · doi:10.1038/bjc.2015.226 · Cited by 151
SIRT4 interacts with OPA1 and regulates mitochondrial quality control and mitophagy
Lang, A., Anand, R., Altinoluk-Hambüchen, S., Ezzahoini, H., Stefanski, A., Iram, A., Bergmann, L., Urbach, J., Böhler, P., Hänsel, J., et al. (2017) · Aging · doi:10.18632/aging.101307 · Cited by 145
SIRT5 stabilizes mitochondrial glutaminase and supports breast cancer tumorigenesis
Greene, K. S., Lukey, M. J., Wang, X., Blank, B. S., Druso, J. E., Lin, M.-C. J., Stalnecker, C. A., Zhang, C., Abril, Y. L. N., Erickson, J. W., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1911954116 · Cited by 138
Self-citationLang, A., Grether‐Beck, S., Singh, M., Kuck, F., Jakob, S., Kefalas, A., Altinoluk-Hambüchen, S., Graffmann, N., Schneider, M., Lindecke, A., et al. (2016) · Aging · doi:10.18632/aging.100905 · Cited by 142
Xia, C., Tao, Y., Li, M., Che, T., & Qu, J. (2020) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2020.9073 · Cited by 136
Mitochondria and the hallmarks of cancer
Giampazolias, E., & Tait, S. W. G. (2015) · FEBS Journal · doi:10.1111/febs.13603 · Cited by 144
Fu, L., Dong, Q., He, J., Wang, X., Xing, J., Wang, E.-H., Qiu, X., & Li, Q. (2016) · Oncogene · doi:10.1038/onc.2016.425 · Cited by 136
Self-citationThe Roles of Mitochondrial SIRT4 in Cellular Metabolism
Min, Z., Gao, J., & Yu, Y. (2019) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00783 · Cited by 134
Metabolic Characterization of a Sirt5 deficient mouse model
Yu, J., Sadhukhan, S., Noriega, L. G., Moullan, N., He, B., Weiss, R. S., Lin, H., Schoonjans, K., & Auwerx, J. H. (2013) · Scientific Reports · doi:10.1038/srep02806 · Cited by 130
Sirtuins, metabolism, and DNA repair
Choi, J.-E., & Mostoslavsky, R. (2014) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2014.05.005 · Cited by 136
Caloric restriction and cancer: molecular mechanisms and clinical implications
Meynet, O., & Ricci, J. (2014) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2014.05.001 · Cited by 143
STAT3 Undergoes Acetylation-dependent Mitochondrial Translocation to Regulate Pyruvate Metabolism
Xu, Y. S., Liang, J. J., Wang, Y., Zhao, X., Xu, L., Xu, Y., Zou, Q. C., Zhang, J. M., Tu, C., Cui, Y., et al. (2016) · Scientific Reports · doi:10.1038/srep39517 · Cited by 131
Sirtuins in stress response: guardians of the genome
Bosch‐Presegué, L., & Vaquero, A. (2013) · Oncogene · doi:10.1038/onc.2013.344 · Cited by 126
The Roles of Sirtuin Family Proteins in Cancer Progression
Zhao, E., Hou, J., Ke, X., Abbas, M. N., Kausar, S., Zhang, L., & Cui, H. (2019) · Cancers · doi:10.3390/cancers11121949 · Cited by 125
SIRT4 protein suppresses tumor formation in genetic models of Myc-induced B cell lymphoma
Jeong, S. M., Lee, A., Lee, J., & Haigis, M. C. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.525949 · Cited by 121
Self-citationMetabolism and Epigenetic Interplay in Cancer: Regulation and Putative Therapeutic Targets
Miranda‐Gonçalves, V., Lameirinhas, A., Henrique, R., & Jerónimo, C. (2018) · Frontiers in Genetics · doi:10.3389/fgene.2018.00427 · Cited by 125
Cea, M., Cagnetta, A., Adamia, S., Acharya, C., Tai, Y., Fulciniti, M., Ohguchi, H., Munshi, A., Acharya, P. C., Bhasin, M., et al. (2015) · Blood · doi:10.1182/blood-2015-06-649970 · Cited by 121
The roles of sirtuins family in cell metabolism during tumor development
Zhu, S., Dong, Z., Ke, X., Hou, J., Zhao, E., Zhang, K., Wang, F., Yang, L., Xiang, Z., & Cui, H. (2018) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2018.11.003 · Cited by 113
Coactivator SRC-2–dependent metabolic reprogramming mediates prostate cancer survival and metastasis
Dasgupta, S., Putluri, N., Long, W., Zhang, B., Wang, J., Kaushik, A., Arnold, J. M., Bhowmik, S. K., Stashi, E., Brennan, C. A., et al. (2015) · Journal of Clinical Investigation · doi:10.1172/jci76029 · Cited by 112
Kim, S.-J., Cheresh, P., Williams, D. M., Cheng, Y., Ridge, K. M., Schumacker, P. T., Weitzman, S. A., Bohr, V. A., & Kamp, D. W. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.515130 · Cited by 108
Increased oxidative phosphorylation in response to acute and chronic DNA damage
Brace, L. E., Vose, S. C., Stanya, K. J., Gathungu, R. M., Marur, V. R., Longchamp, A., Treviño-Villarreal, H., Mejia, P., Vargas, D., Inouye, K., et al. (2016) · npj Aging and Mechanisms of Disease · doi:10.1038/npjamd.2016.22 · Cited by 105
Liu, G., Zhu, J., Yu, M., Cai, C., Zhou, Y., Yu, M., Fu, Z., Gong, Y., Yang, B., Li, Y., et al. (2015) · Journal of Translational Medicine · doi:10.1186/s12967-015-0500-6 · Cited by 104
Self-citationPannek, M., Simic, Z., Fuszard, M. A., Meleshin, M., Rotili, D., Mai, A., Schutkowski, M., & Steegborn, C. (2017) · Nature Communications · doi:10.1038/s41467-017-01701-2 · Cited by 103
Sirtuins' control of autophagy and mitophagy in cancer
Aventaggiato, M., Vernucci, E., Barreca, F., Russo, M. A., & Tafani, M. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107748 · Cited by 103
Flux balance analysis predicts essential genes in clear cell renal cell carcinoma metabolism
Gatto, F., Miess, H., Schulze, A., & Nielsen, J. (2015) · Scientific Reports · doi:10.1038/srep10738 · Cited by 99
The role of FAK in tumor metabolism and therapy
Zhang, J., & Hochwald, S. N. (2013) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2013.12.003 · Cited by 104
Negative reciprocal regulation between Sirt1 and Per2 modulates the circadian clock and aging
Wang, R.-H., Zhao, T., Cui, K., Hu, G., Chen, Q., Chen, W., Wang, X. W., Soto–Gutiérrez, A., Zhao, K., & Deng, C. (2016) · Scientific Reports · doi:10.1038/srep28633 · Cited by 103
Self-citationIntracellular Mono-ADP-Ribosylation in Signaling and Disease
Bütepage, M., Eckei, L., Verheugd, P., & Lüscher, B. (2015) · Cells · doi:10.3390/cells4040569 · Cited by 94
Schistosoma mansoni Sirtuins: Characterization and Potential as Chemotherapeutic Targets
Lancelot, J., Caby, S., Dubois, F., Vanderstraete, M., Trolet, J., Oliveira, G., Bracher, F., Jung, M., & Pierce, R. J. (2013) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0002428 · Cited by 96
Glutamine addiction in tumor cell: oncogene regulation and clinical treatment
Li, X., Peng, X., Li, Y., Wei, S., He, G., Liu, J., Li, X., Yang, S., Dai, L., Lin, W., et al. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-023-01449-x · Cited by 103
Self-citationYi, Y. W., Kang, H. J., Kim, H. J., Kong, Y., Brown, M. L., & Bae, I. (2013) · Oncotarget · doi:10.18632/oncotarget.1070 · Cited by 95
Current role of mammalian sirtuins in DNA repair
Lagunas‐Rangel, F. A. (2019) · DNA repair · doi:10.1016/j.dnarep.2019.06.009 · Cited by 93
Molecular link between glucose and glutamine consumption in cancer cells mediated by CtBP and SIRT4
Wang, L., Li, J., Guo, L., Li, P., Zhao, Z., Zhou, H., & Di, L. (2018) · Oncogenesis · doi:10.1038/s41389-018-0036-8 · Cited by 91
Advancing Cancer Treatment by Targeting Glutamine Metabolism—A Roadmap
Halama, A., & Suhre, K. (2022) · Cancers · doi:10.3390/cancers14030553 · Cited by 93
Sirtuins in atherosclerosis: guardians of healthspan and therapeutic targets
Grootaert, M. O. J., & Bennett, M. R. (2022) · Nature Reviews Cardiology · doi:10.1038/s41569-022-00685-x · Cited by 88
Mitochondrial Sirtuins in cardiometabolic diseases
Tang, X., Chen, X., Chen, H., & Liu, D. (2017) · Clinical Science · doi:10.1042/cs20160685 · Cited by 87
Resveratrol’s Anti-Cancer Effects through the Modulation of Tumor Glucose Metabolism
Brockmueller, A., Sameri, S., Líšková, A., Zhai, K., Varghese, E., Samuel, S. M., Büsselberg, D., Kubatka, P., & Shakibaei, M. (2021) · Cancers · doi:10.3390/cancers13020188 · Cited by 89
Papanicolaou, K. N., O'Rourke, B. P., & Foster, D. B. (2014) · Frontiers in Physiology · doi:10.3389/fphys.2014.00301 · Cited by 85
Who watches the watchmen? Regulation of the expression and activity of sirtuins
Buler, M., Andersson, U., & Hakkola, J. (2016) · The FASEB Journal · doi:10.1096/fj.201600410rr · Cited by 92
Sirtuins and the Metabolic Hurdles in Cancer
German, N. J., & Haigis, M. C. (2015) · Current Biology · doi:10.1016/j.cub.2015.05.012 · Cited by 84
Self-citationSirt4: A Multifaceted Enzyme at the Crossroads of Mitochondrial Metabolism and Cancer
Tomaselli, D., Steegborn, C., Mai, A., & Rotili, D. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.00474 · Cited by 80
Zwaans, B. M. M., & Lombard, D. B. (2014) · Disease Models & Mechanisms · doi:10.1242/dmm.016287 · Cited by 81
Mitochondrial Sirtuins in Cancer: Emerging Roles and Therapeutic Potential
George, J., & Ahmad, N. (2016) · Cancer Research · doi:10.1158/0008-5472.can-15-2733 · Cited by 81
Metadata
- Authors
- Jeong, S. M., Xiao, C., Finley, L. W. S., Lahusen, T., Souza, A. L., Pierce, K., Li, Y.-H., Wang, X., Laurent, G., German, N. J., Xu, X., Li, C., Wang, R.-H., Lee, J., Csibi, A., Cerione, R., Blenis, J., Clish, C. B., Kimmelman, A., Deng, C.-X., & Haigis, M. C.
- Affiliations
- Harvard University (US)
- National Institutes of Health (US)
- Broad Institute (US)
- Cornell University (US)
- Corresponding author
- Deng, Chu-Xia
- Haigis, Marcia C.
- ORCID
- Venue
- Cancer Cell
- Publisher
- Elsevier BV
- Published
- 2013-04
- Volume
- 23
- Issue
- 4
- Pages
- 450-463
- ISSN
- 1535-6108 (ISSN-L)
- PMC
- PMC3650305
- OpenAlex
- W2046120998
- Cited by
- 445
- References
- 56
- Citations by year
- 2026: 9 · 2025: 31 · 2024: 27 · 2023: 28 · 2022: 33 · 2021: 43 · 2020: 42 · 2019: 31 · 2018: 41 · 2017: 32 · 2016: 41 · 2015: 38 · 2014: 24 · 2013: 23
- FWCI
- 19.64
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cancer Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Institute on Aging (R01AG032375, AG032375)
- National Cancer Institute (R01CA157490)
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Keywords
- SIRT4, DNA damage response, glutamine metabolism, mitochondrial metabolism, TCA cycle, tumor suppression, genomic instability, cell cycle arrest, lung cancer, genotoxic stress, tumor suppressor
- MeSH terms
- Animals, DNA Damage, DNA Repair, Female, Glutamine, Humans, Male, Mitochondria, Neoplasms, Experimental, Signal Transduction, Mice, Knockout, Mitochondrial Proteins, Tumor Suppressor Proteins, Sirtuins, Cell Line, Tumor, Cell Growth Processes, Mice, Hep G2 Cells, HEK293 Cells
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review