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Oncometabolite 2-Hydroxyglutarate Is a Competitive Inhibitor of α-Ketoglutarate-Dependent Dioxygenases
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IDH1 and IDH2 mutations occur frequently in gliomas and acute myeloid leukemia, leading to simultaneous loss and gain of activities in the production of α-ketoglutarate (α-KG) and 2-hydroxyglutarate (2-HG), respectively. Here we demonstrate that 2-HG is a competitive inhibitor of multiple α-KG-dependent dioxygenases, including histone demethylases and the TET family of 5-methlycytosine (5mC) hydroxylases. 2-HG occupies the same space as α-KG does in the active site of histone demethylases. Ectopic expression of tumor-derived IDH1 and IDH2 mutants inhibits histone demethylation and 5mC hydroxylation. In glioma, IDH1 mutations are associated with increased histone methylation and decreased 5-hydroxylmethylcytosine (5hmC). Hence, tumor-derived IDH1 and IDH2 mutations reduce α-KG and accumulate an α-KG antagonist, 2-HG, leading to genome-wide histone and DNA methylation alterations.
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“Therefore, it is plausible that increased levels of 2-HG may enable a switch to an entirely HIF-independent mechanism.”
From HIF-1-Independent Mechanisms Regulating Metabolic Adaptation in Hypoxic Cancer Cells (2021) · cites this paper as [152]
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In the citing paper
“Mutant IDH protein produces a novel onco-metabolite, 2-hydroxyglutarate (2-HG), that interferes with iron-dependent hydroxylases, including the TET family of 5′-methylcytosine hydroxylases3–7.”
From Insulator dysfunction and oncogene activation in IDH mutant gliomas (2016) · cites this paper as [5]
The cited source says what the claim attributes to it.
In the citing paper
“Mutant IDH protein produces a novel onco-metabolite, 2-hydroxyglutarate (2-HG), that interferes with iron-dependent hydroxylases, including the TET family of 5′-methylcytosine hydroxylases3–7.”
From Insulator dysfunction and oncogene activation in IDH mutant gliomas (2016) · cites this paper as [5]
In the citing paper
“The observation that IDH1 and IDH2 mutations can partially phenocopy the loss of TET function may explain the mutual exclusivity of these mutations in cancer 95,97 .”
From The roles of DNA, RNA and histone methylation in ageing and cancer (2019) · cites this paper as [97]
In the citing paper
“Mutant IDH protein is a competitive inhibitor of hydroxylases, including the TET family of 5mC hydroxylases120–122.”
From Transcription factors as readers and effectors of DNA methylation (2016) · cites this paper as [122]
In the citing paper
“These observations support a model in which PU.1 guides TET2 to a specific subset of genomic regions to facilitate the oxidation of 5mC to 5hmC, a reaction that is inhibited by 2-hydroxyglutarate47 and enhanced by vitamin C13 (Figure 5d).”
From Vitamin C-induced epigenomic remodelling in IDH1 mutant acute myeloid leukaemia (2018) · cites this paper as [47]
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“In the cancer setting, 2-HG has been shown to influence a number of biological processes, including cell differentiation, DNA methylation, and histone methylation (79–82), leading to its classification as an oncometabolite.”
From Fueling Immunity: Insights into Metabolism and Lymphocyte Function (2013) · cites this paper as [81]
In the citing paper
“For example, 2-HG acts as a competitive inhibitor of α-KG, and its production by mutant IDH1 consumes α-KG (81, 99), leading to reduced TET2 and JmjC activity in tumor cells (79, 80).”
From Fueling Immunity: Insights into Metabolism and Lymphocyte Function (2013) · cites this paper as [81]
In the citing paper
“Furthermore, TH17 cell differentiation could be initiated by exogenous addition of D-2-HG to naïve CD4+ T cells or by genetic silencing of TET1 and TET2, established targets of 2-HG143-145.”
From Coupling Krebs cycle metabolites to signalling in immunity and cancer (2018) · cites this paper as [145]
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Verhaak, R. G. W., Hoadley, K. A., Purdom, E., Wang, V., Qi, Y., Wilkerson, M. D., Miller, C. R., Ding, L., Golub, T., Mesirov, J. P., et al. (2010) · Cancer Cell · doi:10.1016/j.ccr.2009.12.020 · Cited by 7,575
An Integrated Genomic Analysis of Human Glioblastoma Multiforme
Parsons, D. W., Jones, S., Zhang, X., Lin, J. C.-H., Leary, R. J., Angenendt, P., Mankoo, P., Carter, H., Siu, I.-M., Gallia, G. L., et al. (2008) · Science · doi:10.1126/science.1164382 · Cited by 5,857
IDH1 and IDH2 Mutations in Gliomas
Yan, H., Parsons, D. W., Jin, G., McLendon, R., Rasheed, B. A., Yuan, W., Kos, I., Batinic-Haberle, I., Jones, S., Riggins, G. J., et al. (2009) · New England Journal of Medicine · doi:10.1056/nejmoa0808710 · Cited by 5,847
Conversion of 5-Methylcytosine to 5-Hydroxymethylcytosine in Mammalian DNA by MLL Partner TET1
Tahiliani, M., Koh, K. P., Shen, Y., Pastor, W. A., Bandukwala, H., Brudno, Y., Agarwal, S., Iyer, L. M., Liu, D. R., Aravind, L., et al. (2009) · Science · doi:10.1126/science.1170116 · Cited by 5,836
Jaakkola, P., Mole, D. R., Tian, Y.-M., Wilson, M. I., Gielbert, J., Gaskell, S. J., Kriegsheim, A. V., Hebestreit, H. F., Mukherji, M., Schofield, C. J., et al. (2001) · Science · doi:10.1126/science.1059796 · Cited by 5,535
HIFα Targeted for VHL-Mediated Destruction by Proline Hydroxylation: Implications for O 2 Sensing
Ivan, M., Kondo, K., Yang, H., Kim, W., Valiando, J., Ohh, M., Salic, A., Asara, J. M., Lane, W. S., & Kaelin Jr., W. G. (2001) · Science · doi:10.1126/science.1059817 · Cited by 4,735 · cited 2×
“HIF-1a is a transcription factor whose function is linked to metabolism, angiogenesis and tumorigenesis, and whose protein level is downregulated under normoxic conditions by PHD-mediated hydroxylation and subsequent hydroxylation-targeted ubiquitination (Bruick and McKnight, 2001; Epstein et al., 2001; Ivan et al., 2…”
Self-citationEndostatin: an endogenous inhibitor of angiogenesis and tumor growth
O'Reilly, M. S., Boehm, T., Shing, Y., Fukai, N., Vasios, G., Lane, W. S., Flynn, E., Birkhead, J. R., Olsen, B. R., & Folkman, J. (1997) · Cell · doi:10.1016/s0092-8674(00)81848-6 · Cited by 4,486
Cancer-associated IDH1 mutations produce 2-hydroxyglutarate
Dang, L., White, D. W., Gross, S., Bennett, B. D., Bittinger, M. A., Driggers, E. M., Fantin, V. R., Jang, H. G., Jin, S., Keenan, M. C., et al. (2009) · Nature · doi:10.1038/nature08617 · Cited by 4,154
Epstein, A. C. R., Gleadle, J. M., McNeill, L. A., Hewitson, K. S., O'Rourke, J., Mole, D. R., Mukherji, M., Metzen, E., Wilson, M. I., Dhanda, A., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00507-4 · Cited by 3,333
Figueroa, M. E., Abdel-Wahab, O., Lu, C., Ward, P. S., Patel, J., Shih, A., Li, Y., Bhagwat, N., Vasanthakumar, A., Fernandez, H. F., et al. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.11.015 · Cited by 2,766
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- Han, 2007, Structural basis for histone demethylation by JHDM1, Frontier Science, 1, 52
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Items 501–600 of 1,006
A Tale of Two Subunits: How the Neomorphic R132H IDH1 Mutation Enhances Production of αHG
Pietrak, B., Zhao, H., Qi, H., Quinn, C. J., Gao, E. N., Boyer, J. G., Concha, N. O., Brown, K., Duraiswami, C., Wooster, R. F., et al. (2011) · Biochemistry · doi:10.1021/bi200499m · Cited by 112
Colvin, H. S., Nishida, N., Konno, M., Haraguchi, N., Takahashi, H., Nishimura, J., Hata, T., Kawamoto, K., Asai, A., Tsunekuni, K., et al. (2016) · Scientific Reports · doi:10.1038/srep36289 · Cited by 111
Kaminska, B., Czapski, B., Guzik, R., Król, S. K., & Gielniewski, B. (2019) · Molecules · doi:10.3390/molecules24050968 · Cited by 113
Liu, Q., Zhu, F., Liu, X., Lu, Y., Yao, K., Tian, N., Tong, L., Figge, D. A., Wang, X., Han, Y., et al. (2022) · Nature Metabolism · doi:10.1038/s42255-022-00575-z · Cited by 122
Self-citationMolenaar, R. J., Radivoyevitch, T., Nagata, Y., Khurshed, M., Przychodzen, B., Makishima, H., Xu, M., Bleeker, F. E., Wilmink, J. W., Carraway, H. E., et al. (2018) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-17-2796 · Cited by 112
Liu, J., Jiang, J., Mo, J., Liu, D., Cao, D., Wang, H., He, Y., & Wang, H. (2018) · Hepatology · doi:10.1002/hep.30146 · Cited by 108
Self-citationIsocitrate dehydrogenase inhibitors in acute myeloid leukemia
Liu, X., & Gong, Y. (2019) · Biomarker Research · doi:10.1186/s40364-019-0173-z · Cited by 111
Cancer cell-intrinsic mechanisms driving acquired immune tolerance
Ghorani, E., Swanton, C., & Quezada, S. A. (2023) · Immunity · doi:10.1016/j.immuni.2023.09.004 · Cited by 116
Sakamoto, A., Hino, S., Nagaoka, K., Anan, K., Takase, R., Matsumori, H., Ojima, H., Kanai, Y., Arita, K., & Nakao, M. (2015) · Cancer Research · doi:10.1158/0008-5472.can-14-1560 · Cited by 113
CRL4VprBP E3 Ligase Promotes Monoubiquitylation and Chromatin Binding of TET Dioxygenases
Nakagawa, T., Lv, L., Nakagawa, M., Yu, Y., Yu, C. Y., D’Alessio, A. C., Nakayama, K., Fan, H., Chen, X., & Xiong, Y. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.12.002 · Cited by 114
Self-citationSalamanca-Cardona, L., Shah, H., Poot, A. J., Correa, F. M., Di Gialleonardo, V., Lui, H., Miloushev, V. Z., Granlund, K. L., Tee, S. S., Cross, J. R., et al. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.10.001 · Cited by 106
Metabolic recoding of epigenetics in cancer
Wang, Y., & Lei, Q. (2018) · 癌症：英文版 · doi:10.1186/s40880-018-0302-3 · Cited by 109
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Sciacovelli, M., Gaude, E., Hilvo, M., & Frezza, C. (2014) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-416618-9.00001-7 · Cited by 108
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Smolková, K., & Ježek, P. (2012) · International Journal of Cell Biology · doi:10.1155/2012/273947 · Cited by 114
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Yan, M., & Xu, G. (2018) · Analytica Chimica Acta · doi:10.1016/j.aca.2018.04.006 · Cited by 105
How metabolites modulate metabolic flux
Wegner, A., Meiser, J., Weindl, D., & Hiller, K. (2014) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2014.11.008 · Cited by 108
Li, L., Paz, A. C., Wilky, B. A., Johnson, B. A., Galoian, K. A., Rosenberg, A. E., Hu, G., Tinoco, G., Bodamer, O. A., & Trent, J. C. (2015) · PLoS ONE · doi:10.1371/journal.pone.0133813 · Cited by 107
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Haws, S. A., Leech, C. M., & Denu, J. M. (2020) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2020.04.002 · Cited by 112
Salminen, A., Haapasalo, A., Kauppinen, A., Kaarniranta, K., Soininen, H. S., & Hiltunen, M. O. (2015) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.05.001 · Cited by 107
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Kerr, D. A., Lopez, H. U., Deshpande, V., Hornicek, F. J., Duan, Z., Zhang, Y., Rosenberg, A. E., Borger, D. R., & Nielsen, G. P. (2013) · The American Journal of Surgical Pathology · doi:10.1097/pas.0b013e31827ab703 · Cited by 105
Self-citationNew Developments in the Pathogenesis and Therapeutic Targeting of the IDH1 Mutation in Glioma
Dimitrov, L., Hong, C. S., Yang, C., Zhuang, Z., & Heiss, J. D. (2015) · International Journal of Medical Sciences · doi:10.7150/ijms.11047 · Cited by 108
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Todisco, S., Convertini, P., Iacobazzi, V., & Infantino, V. (2019) · Cancers · doi:10.3390/cancers12010068 · Cited by 105
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Lawlor, E. R., & Thiele, C. J. (2012) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-11-1921 · Cited by 104
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Lee, N., & Kim, D. (2016) · Molecules and Cells · doi:10.14348/molcells.2016.0310 · Cited by 102
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Carell, T., Kurz, M. Q., Müller, M., Rossa, M., & Spada, F. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201708228 · Cited by 104
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Johannessen, T.-C. A., Mukherjee, J., Viswanath, P., Ohba, S., Ronen, S. M., Bjerkvig, R., & Pieper, R. O. (2016) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-16-0141 · Cited by 105
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Chang, C.-F., Diers, A. R., & Hogg, N. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.11.012 · Cited by 103
He, X., Yan, B., Liu, S., Jia, J., Lai, W., Xing, X., Tang, C., Luo, D., Tan, T., Jiang, Y., et al. (2016) · Cancer Research · doi:10.1158/0008-5472.can-16-0268 · Cited by 105
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Wu, M., Kondo, H., Kammula, A. V., Shi, L., Xiao, Y., Dhiab, S., Xu, Q., Slater, C. J., Avila, O. I., Merritt, J., et al. (2024) · Science · doi:10.1126/science.adl6173 · Cited by 110
Grafodatskaya, D., Chung, B. H., Butcher, D. T., Turinsky, A. L., Goodman, S. J., Choufani, S., Chen, Y. A., Lou, Y., Zhao, C., Rajendram, R., et al. (2013) · BMC Medical Genomics · doi:10.1186/1755-8794-6-1 · Cited by 103
Suijker, J., Oosting, J., Koornneef, A., Struys, E. A., Salomons, G. S., Schaap, F. G., Waaijer, C. J. F., Wijers‐Koster, P. M., Bruijn, I. H. B., Haazen, L. C. J. M., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.3723 · Cited by 106
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Martelli, M. P., Sportoletti, P., Tiacci, E., Martelli, M. F., & Falini, B. (2012) · Blood Reviews · doi:10.1016/j.blre.2012.11.001 · Cited by 104
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Ciccarese, F., & Ciminale, V. (2017) · Frontiers in Oncology · doi:10.3389/fonc.2017.00117 · Cited by 104
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Knorr, S., Sinn, M., Galetskiy, D., Williams, R. M., Wang, C., Müller, N., Mayans, O. M., Schleheck, D., & Hartig, J. S. (2018) · Nature Communications · doi:10.1038/s41467-018-07563-6 · Cited by 97
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Tang, X., Fu, X., Liu, Y., Yu, D., Cai, S. J., & Yang, C. (2019) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-19-0103 · Cited by 100
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Lin, J., Yao, D., Qian, J., Chen, Q., Qian, W., Li, Y., Yang, J. C., Wang, C., Chai, H., Qian, Z. Y., et al. (2011) · Annals of Hematology · doi:10.1007/s00277-011-1352-7 · Cited by 99
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Marshall, L. L., Killinger, B. A., Ensink, E., Li, P., Li, K. X., Cui, W., Lubben, N., Weiland, M. J., Wang, X., Gordevičius, J., et al. (2020) · Nature Neuroscience · doi:10.1038/s41593-020-0690-y · Cited by 99
Hoekstra, A. S., de Graaff, M. A., Briaire-de Bruijn, I. H., Ras, C., Seifar, R. M., van Minderhout, I., Cornelisse, C. J., Hogendoorn, P. C. W., Breuning, M. H., Suijker, J., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.6091 · Cited by 99
Salminen, A., Kauppinen, A., & Kaarniranta, K. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-1978-z · Cited by 99
Madžo, J., Liu, H., Rodriguez, A., Vasanthakumar, A., Sundaravel, S., Caces, D. B., Looney, T. J., Zhang, L., Lepore, J. B., Macrae, T. A., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2013.11.044 · Cited by 99
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Pan, M., Hsu, M., Chen, L., & Hung, W. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2596-8 · Cited by 111
Byun, J. S., & Gardner, K. L. (2013) · American Journal Of Pathology · doi:10.1016/j.ajpath.2013.01.009 · Cited by 104
IDH1 and IDH2 mutations, immunohistochemistry and associations in a series of brain tumors
Mellai, M., Piazzi, A., Caldera, V., Monzeglio, O., Cassoni, P., Valente, G., & Schiffer, D. (2011) · Journal of Neuro-Oncology · doi:10.1007/s11060-011-0596-3 · Cited by 97
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Jia, D., Park, J. H., Kaur, H., Jung, K. H., Yang, S., Tripathi, S., Galbraith, M., Deng, Y., Jolly, M. K., Kaipparettu, B. A., et al. (2021) · British Journal of Cancer · doi:10.1038/s41416-021-01385-y · Cited by 97
Liu, X., Si, W., He, L., Yang, J., Peng, Y., Ren, J., Liu, X., Jin, T., Yu, H., Zhang, Z., et al. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00774-2 · Cited by 97
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Chan, S. Y., & Rubin, L. J. (2017) · European Respiratory Review · doi:10.1183/16000617.0094-2017 · Cited by 97
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Salminen, A., Kaarniranta, K., Hiltunen, M. O., & Kauppinen, A. (2014) · Cellular Signalling · doi:10.1016/j.cellsig.2014.03.030 · Cited by 97
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Kroeze, L. I., van der Reijden, B. A., & Jansen, J. H. (2015) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2015.01.001 · Cited by 97
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Gelman, S. J., Naser, F. J., Mahieu, N. G., McKenzie, L. D., Dunn, G. P., Chheda, M. G., & Patti, G. J. (2018) · Cell Reports · doi:10.1016/j.celrep.2017.12.050 · Cited by 95
The multifaceted contribution of α-ketoglutarate to tumor progression: An opportunity to exploit?
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Rabinowitz, J. D., Purdy, J. G., Vastag, L., Shenk, T. E., & Koyuncu, E. (2011) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2011.76.010694 · Cited by 98
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Mingay, M., Chaturvedi, A., Bilenky, M., Cao, Q., Jackson, L., Hui, T., Moksa, M., Heravi-Moussavi, A., Humphries, R. K., Heuser, M., et al. (2018) · Leukemia · doi:10.1038/leu.2017.171 · Cited by 94
Fan, B., Mellinghoff, I. K., Wen, P. Y., Lowery, M. A., Goyal, L., Tap, W. D., Pandya, S. S., Manyak, E. L., Jiang, L., Liu, G., et al. (2019) · Investigational New Drugs · doi:10.1007/s10637-019-00771-x · Cited by 94
Self-citationZhu, G. G., Nafa, K., Agaram, N. P., Zehir, A., Benayed, R., Sadowska, J., Borsu, L. A., Kelly, C. M., Tap, W. D., Fabbri, N., et al. (2019) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-18-4212 · Cited by 94
Interplay between Cellular Metabolism and the DNA Damage Response in Cancer
Moretton, A., & Loizou, J. I. (2020) · Cancers · doi:10.3390/cancers12082051 · Cited by 97
Signaling pathways in brain tumors and therapeutic interventions
Li, S., Wang, C., Chen, J., Lan, Y., Zhang, W., Kang, Z., Zheng, Y., Zhang, R., Yu, J., & Li, W. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01260-z · Cited by 105
Screen for IDH1, IDH2, IDH3, D2HGDH and L2HGDH Mutations in Glioblastoma
Krell, D., Assoku, M., Galloway, M., Mulholland, P. J., Tomlinson, I. P. M., & Bardella, C. (2011) · PLoS ONE · doi:10.1371/journal.pone.0019868 · Cited by 94
The Changing Mutational Landscape of Acute Myeloid Leukemia and Myelodysplastic Syndrome
Larsson, C. A., Cote, G. J., & Quintás‐Cardama, A. (2013) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-12-0695 · Cited by 97
New drugs in acute myeloid leukemia
Kadia, T. M., Ravandi, F., Cortes, J. E., & Kantarjian, H. M. (2016) · Annals of Oncology · doi:10.1093/annonc/mdw015 · Cited by 94
The TCA cycle as a bridge between oncometabolism and DNA transactions in cancer
Ciccarone, F., Vegliante, R., Leo, L. D., & Ciriolo, M. R. (2017) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2017.06.008 · Cited by 97
Davis, M. I., Größ, S., Shen, M., Straley, K. S., Pragani, R., Lea, W., Popovici-Müller, J. V., DeLaBarre, B., Artin, E., Thorne, N., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.511030 · Cited by 93
Weisenberger, D. J., Liang, G., & Lenz, H. J. (2017) · Oncogene · doi:10.1038/onc.2017.374 · Cited by 96
Ma, B., Meng, H., Tian, Y., Wang, Y., Song, T., Zhang, T., Wu, Q., Cui, Y., Li, H., Zhang, W., et al. (2020) · BMC Cancer · doi:10.1186/s12885-020-06804-6 · Cited by 97
Schmitt, M. J., Dramaretska, Y., Barozzi, I., Göhrig, A., Kertalli, S., Großmann, M., Naumann, H., Sánchez-Bailón, M. P., Hulsman, D., Glaß, R., et al. (2020) · Cancer Discovery · doi:10.1158/2159-8290.cd-20-0219 · Cited by 91
Gupta, V. K., Sharma, N., Durden, B. C., Garrido, V. T., Kesh, K., Edwards, D., Wang, D., Myer, C., Mateo-Victoriano, B., Kollala, S. S., et al. (2021) · Cancer Research · doi:10.1158/0008-5472.can-20-2562 · Cited by 97
Chen, X., Sunkel, B. D., Wang, M., Kang, S., Wang, T., Gnanaprakasam, J. R., Liu, L., Cassel, T., Scott, D. A., Muñoz-Cabello, A. M., et al. (2022) · Science Immunology · doi:10.1126/sciimmunol.abm8161 · Cited by 94
Self-citationUnlocking epigenetic codes in neurogenesisPreprint
Yao, B., & Jin, P. (2014) · Genes & Development · doi:10.1101/gad.241547.114 · Cited by 97
TET2 in Normal and Malignant HematopoiesisPreprint
Bowman, R. L., & Levine, R. L. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a026518 · Cited by 102
Fathi, A. T., & Abdel-Wahab, O. I. (2011) · Advances in Hematology · doi:10.1155/2012/469592 · Cited by 95
Glioblastoma Therapy in the Age of Molecular Medicine
Geraldo, L. H., Garcia, C., da Fonseca, A. C. C., Dubois, L. G., Spohr, T. C. L. D. S. E., Matias, D., Magalhães, E. S. D. C., do Amaral, R. F., da Rosa, B. G., Grimaldi, I., et al. (2018) · Trends in cancer · doi:10.1016/j.trecan.2018.11.002 · Cited by 93
Clinical significance of T cell metabolic reprogramming in cancer
Herbel, C., Patsoukis, N., Bardhan, K., Seth, P., Weaver, J. D., & Boussiotis, V. A. (2016) · Clinical and Translational Medicine · doi:10.1186/s40169-016-0110-9 · Cited by 99
Brain stem cells as the cell of origin in glioma
Modrek, A. S. (2014) · World Journal of Stem Cells · doi:10.4252/wjsc.v6.i1.43 · Cited by 90
The Impact of DNA Methylation in Hematopoietic Malignancies
Guillamot, M., Cimmino, L., & Aifantis, I. (2016) · Trends in cancer · doi:10.1016/j.trecan.2015.12.006 · Cited by 96
SETting the Stage for Cancer Development: SETD2 and the Consequences of Lost MethylationPreprint
Fahey, C. C., & Davis, I. J. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a026468 · Cited by 92
Epigenetic reprogramming of melanoma cells by vitamin C treatment
Gustafson, C. B., Yang, C., Dickson, K. M., Shao, H., Van Booven, D., Harbour, J. W., Liu, Z.-J., & Wang, G. (2015) · Clinical Epigenetics · doi:10.1186/s13148-015-0087-z · Cited by 90
Self-citationMoving toward molecular classification of diffuse gliomas in adults
Theeler, B. J., Yung, W. K. A., Fuller, G. N., & de Groot, J. (2012) · Neurology · doi:10.1212/wnl.0b013e318271f7cb · Cited by 90
Epigenetics in Cancer: A Hematological Perspective
Stahl, M. F., Kohrman, N., Gore, S. D., Kim, T. K., Zeidan, A. M., & Prébet, T. (2016) · PLoS Genetics · doi:10.1371/journal.pgen.1006193 · Cited by 92
Shelar, S. B., Shim, E., Brinkley, G. J., Kundu, A., Carobbio, F., Poston, T. L., Tan, J. C., Parekh, V., Benson, D. G., Crossman, D. K., et al. (2018) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-18-1727 · Cited by 89
Driver mutations in acute myeloid leukemia
Kishtagari, A., Levine, R. L., & Viny, A. D. (2020) · Current Opinion in Hematology · doi:10.1097/moh.0000000000000567 · Cited by 100
Role of Metabolism in Bone Development and Homeostasis
Suzuki, A., Minamide, M., Iwaya, C., Ogata, K., & Iwata, J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21238992 · Cited by 92
Mortazavi, A., Fayed, I., Bachani, M., Dowdy, T., Jahanipour, J., Khan, A. U., Owotade, J., Walbridge, S., Inati, S. K., Steiner, J. P., et al. (2022) · Neuro-Oncology · doi:10.1093/neuonc/noac003 · Cited by 98
Self-citationEpigenetic regulation in cancer therapy: From mechanisms to clinical advances
Tao, L., Zhou, Y., Luo, Y., Qiu, J., Xiao, Y., Zou, J., Zhang, Y., Liu, X., Yang, X., Gou, K., et al. (2024) · MedComm – Oncology · doi:10.1002/mog2.59 · Cited by 95
Self-citationMukasa, A., Takayanagi, S., Saito, K., Shibahara, J., Tabei, Y., Furuya, K., Ide, T., Narita, Y., Nishikawa, R., Ueki, K., et al. (2011) · Cancer Science · doi:10.1111/j.1349-7006.2011.02175.x · Cited by 93
Metadata
- Authors
- Xu, W., Yang, H., Liu, Y., Yang, Y., Wang, P., Kim, S.-H., Ito, S., Yang, C., Wang, P., Xiao, M.-T., Liu, L.-X., Jiang, W.-Q., Liu, J., Zhang, J.-Y., Wang, B., Frye, S., Zhang, Y., Xu, Y.-H., Lei, Q.-Y., Guan, K.-L., Zhao, S.-M., & Xiong, Y.
- Affiliations
- Shanghai Medical College of Fudan University (CN)
- University of North Carolina at Chapel Hill (US)
- Chinese Academy of Sciences (CN)
- Corresponding author
- Guan, Kun-Liang
- Xiong, Yue
- ORCID
- Venue
- Cancer Cell
- Publisher
- Elsevier BV
- Published
- 2011-01
- Volume
- 19
- Issue
- 1
- Pages
- 17-30
- ISSN
- 1535-6108 (ISSN-L)
- PMC
- PMC3229304
- OpenAlex
- W2131860315
- Cited by
- 2,875
- References
- 55
- Citations by year
- 2026: 165 · 2025: 168 · 2024: 192 · 2023: 182 · 2022: 183 · 2021: 270 · 2020: 214 · 2019: 191 · 2018: 195 · 2017: 183 · 2016: 196 · 2015: 180 · 2014: 183 · 2013: 157 · 2012: 137
- FWCI
- 90.25
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 928 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Cancer Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Carolina Digital Repository (University of North Carolina at Chapel Hill) (submittedVersion)
- UNC Libraries
- Funders
- National Natural Science Foundation of China (11079016, 30600112, 30871255, 30971485/C0706)
- Ministry of Education of the People's Republic of China
- National Key Research and Development Program of China (2011CB910600, 2011CB965300)
- Project 985
- Major State Basic Research Development Program of China (2009CB918401, 2009CB918600)
- National Institutes of Health
- Topics
- Health Sciences › Medicine › Oncology › Glioma Diagnosis and Treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
- Keywords
- 2-hydroxyglutarate, oncometabolites, alpha-ketoglutarate-dependent dioxygenase, IDH1 mutation, IDH2 mutation, histone demethylase, 5-hydroxymethylcytosine, competitive inhibition, glioma, acute myeloid leukemia, DNA methylation, histone methylation, active site
- MeSH terms
- Animals, Binding, Competitive, Cytosine, DNA-Binding Proteins, Glioma, Glutarates, Histones, Humans, Mixed Function Oxygenases, Isocitrate Dehydrogenase, Ketoglutaric Acids, Models, Molecular, Oxalates, Oxidoreductases, N-Demethylating, Procollagen-Proline Dioxygenase, Proto-Oncogene Proteins, Gene Expression, Caenorhabditis elegans, Homeodomain Proteins, Amino Acid Substitution, Catalytic Domain, Caenorhabditis elegans Proteins, Endostatins, 5-Methylcytosine, F-Box Proteins, Cell Line, Tumor, Dioxygenases, Hypoxia-Inducible Factor 1, alpha Subunit, Biocatalysis, Histone Demethylases, Jumonji Domain-Containing Histone Demethylases, Hypoxia-Inducible Factor-Proline Dioxygenases
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