The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.
Glioma-Derived Mutations in IDH1 Dominantly Inhibit IDH1 Catalytic Activity and Induce HIF-1α
Open accessAbstract
Heterozygous mutations in the gene encoding isocitrate dehydrogenase-1 ( IDH1 ) occur in certain human brain tumors, but their mechanistic role in tumor development is unknown. We have shown that tumor-derived IDH1 mutations impair the enzyme's affinity for its substrate and dominantly inhibit wild-type IDH1 activity through the formation of catalytically inactive heterodimers. Forced expression of mutant IDH1 in cultured cells reduces formation of the enzyme product, α-ketoglutarate (α-KG), and increases the levels of hypoxia-inducible factor subunit HIF-1α, a transcription factor that facilitates tumor growth when oxygen is low and whose stability is regulated by α-KG. The rise in HIF-1α levels was reversible by an α-KG derivative. HIF-1α levels were higher in human gliomas harboring an IDH1 mutation than in tumors without a mutation. Thus, IDH1 appears to function as a tumor suppressor that, when mutationally inactivated, contributes to tumorigenesis in part through induction of the HIF-1 pathway.
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
“HIF is stabilized in IDH-associated gliomas; this has been proposed to be a consequence of intracellular depletion of 2OG following IDH loss of function (Zhao et al, 2009).”
From The oncometabolite 2-hydroxyglutarate inhibits histone lysine demethylases (2011) · cites this paper as Zhao et al, 2009
In the citing paper
“The IDH mutations occur at substrate-binding arginine residues (Arg 132 in IDH1; Arg 140 and Arg 172 in IDH2) and inactivate IDH for conversion of isocitrate to 2-oxoglutarate (2OG; Zhao et al, 2009).”
From The oncometabolite 2-hydroxyglutarate inhibits histone lysine demethylases (2011) · cites this paper as Zhao et al, 2009
In the citing paper
“Overexpression of IDH1 Arg 132 mutants results in elevated HIFa levels (Zhao et al, 2009).”
From The oncometabolite 2-hydroxyglutarate inhibits histone lysine demethylases (2011) · cites this paper as Zhao et al, 2009
In the citing paper
“The stability of HIF‐1α is regulated by α‐KG, and increasing α‐KG reduces the expression of HIF‐1α.”
From Hypoxia signaling in cancer: Implications for therapeutic interventions (2023) · cites this paper as [168]
In the citing paper
“Inhibiting the mitochondrial enzyme SDH during ischaemia by preloading tissues with the SDH inhibitor DMM prevented succinate accumulation during ischaemia and protected against tissue damage upon reperfusion150.”
From Coupling Krebs cycle metabolites to signalling in immunity and cancer (2018) · cites this paper as [150]
In the citing paper
“succinate accumulated during ischaemia and is then oxidised upon reperfusion to drive the mitochondrial superoxide formation that contributes to ischaemia-reperfusion (IR) injury150,151.”
From Coupling Krebs cycle metabolites to signalling in immunity and cancer (2018) · cites this paper as [150]
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
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
Malignant astrocytic glioma: genetics, biology, and paths to treatment
Furnari, F. B., Fenton, T., Bachoo, R. M., Mukasa, A., Stommel, J. M., Stegh, A., Hahn, W. C., Ligon, K. L., Louis, D. N., Brennan, C., et al. (2007) · Genes & Development · doi:10.1101/gad.1596707 · Cited by 2,316
Analysis of the IDH1 codon 132 mutation in brain tumors
Balss, J., Meyer, J., Mueller, W., Korshunov, A., Hartmann, C., & von Deimling, A. (2008) · Acta Neuropathologica · doi:10.1007/s00401-008-0455-2 · Cited by 1,036
Xu, X., Zhao, J., Xu, Z., Peng, B., Huang, Q., Arnold, E., & Ding, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404298200 · Cited by 407
Self-citationBleeker, F. E., Lamba, S., Leenstra, S., Troost, D., Hulsebos, T. J. M., Vandertop, W. P., Frattini, M., Molinari, F., Knowles, M. A., Cerrato, A., et al. (2009) · Human Mutation · doi:10.1002/humu.20937 · Cited by 365
Evaluation of HIF-1 inhibitors as anticancer agents
Semenza, G. L. (2007) · Drug Discovery Today · doi:10.1016/j.drudis.2007.08.006 · Cited by 363
MacKenzie, E. D., Selak, M. A., Tennant, D. A., Payne, L. J., Crosby, S., Frederiksen, C. M., Watson, D. G., & Gottlieb, E. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01927-06 · Cited by 359
Cellular concentrations of enzymes and their substrates
Albe, K. R., Butler, M. H., & Wright, B. E. (1990) · Journal of Theoretical Biology · doi:10.1016/s0022-5193(05)80266-8 · Cited by 318
Multiple NADPH-producing pathways control glutathione (GSH) content in retina
Winkler, B. S., Desantis, N. M., & Solomon, F. (1986) · Experimental Eye Research · doi:10.1016/s0014-4835(86)80013-6 · Cited by 107
Flagged first, then by citations
Cited by
Sorted by citations
Items 201–300 of 999
Molecular characterizations of glioblastoma, targeted therapy, and clinical results to date
Bastien, J., McNeill, K. A., & Fine, H. A. (2014) · Cancer · doi:10.1002/cncr.28968 · Cited by 146
Cancer metabolism and tumor microenvironment: fostering each other?
Yuan, Y., Li, H., Wang, P., Chen, L., Guo, D. S., Jiang, H., He, B., Qin, S., Wang, K., Li, N., et al. (2021) · Science China Life Sciences · doi:10.1007/s11427-021-1999-2 · Cited by 140
Self-citationHypoxia-Inducible Factor-1: A Critical Player in the Survival Strategy of Stressed Cells
Chen, S., & Sang, N. (2015) · Journal of Cellular Biochemistry · doi:10.1002/jcb.25283 · Cited by 137
Advances in histone demethylase KDM4 as cancer therapeutic targets
Lee, D. H., Kim, G. W., Jeon, Y. H., Yoo, J. H., Lee, S. W., & Kwon, S. H. (2020) · The FASEB Journal · doi:10.1096/fj.201902584r · Cited by 137
Glioblastoma, hypoxia and autophagy: a survival-prone ‘ménage-à-trois’
Jawhari, S., Ratinaud, M., & Verdier, M. (2016) · Cell Death and Disease · doi:10.1038/cddis.2016.318 · Cited by 138
Turner, D. A., & Adamson, D. C. (2011) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e31820e1152 · Cited by 133
Jansen, M., Perry, A., Heffner, R. R., & Louis, D. N. (2012) · Elsevier eBooks · doi:10.1016/b978-1-4377-0434-1.00069-4 · Cited by 133
Altered energy metabolism in cancer: A unique opportunity for therapeutic intervention
Zhang, Y., & Yang, J.-M. (2013) · Cancer Biology & Therapy · doi:10.4161/cbt.22958 · Cited by 132
Molecular pathogenesis of IDH mutations in gliomas
Ichimura, K. (2012) · Brain Tumor Pathology · doi:10.1007/s10014-012-0090-4 · Cited by 134
IDH mutations in acute myeloid leukemia
Rakheja, D., Konoplev, S. N., Medeiros, L. J., & Chen, W. (2012) · Human Pathology · doi:10.1016/j.humpath.2012.05.003 · Cited by 135
Murugan, A. K., Bojdani, E., & Xing, M. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.02.095 · Cited by 135
Mutant IDH1 Confers an in Vivo Growth in a Melanoma Cell Line with BRAF Mutation
Shibata, T., Kokubu, A., Miyamoto, M., Sasajima, Y., & Yamazaki, N. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2010.12.011 · Cited by 131
Tseng, C.-W., Kuo, W., Chan, S., Chan, H., Chang, K., & Wang, L. (2018) · Cancer Research · doi:10.1158/0008-5472.can-17-2906 · Cited by 131
2-Hydroxyglutarate in Cancer Cells
Ježek, P. (2020) · Antioxidants & Redox Signaling · doi:10.1089/ars.2019.7902 · Cited by 130
IDH1/2 mutations target a key hallmark of cancer by deregulating cellular metabolism in glioma
Zhang, C., Moore, L. M., Li, X., Yung, W. K. A., & Zhang, W. (2013) · Neuro-Oncology · doi:10.1093/neuonc/not087 · Cited by 136
LncRNA IDH1-AS1 links the functions of c-Myc and HIF1α via IDH1 to regulate the Warburg effect
Xiang, S., Gu, H., Jin, L., Thorne, R. F., Zhang, X. D., & Wu, M. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1711257115 · Cited by 129
Wang, F., Morita, K., Dinardo, C. D., Furudate, K., Tanaka, T. N., Yan, Y., Patel, K. P., MacBeth, K. J., Wu, B., Liu, G., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-22874-x · Cited by 137
Isocitrate Dehydrogenase Mutations Are Rare in Pheochromocytomas and Paragangliomas
Gaal, J., Burnichon, N., Korpershoek, E., Roncelin, I., Bertherat, J. Y., Plouin, P., de Krijger, R. R., Gimenez‐Roqueplo, A., & Dinjens, W. N. M. (2009) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2009-2170 · Cited by 131
Isocitrate dehydrogenases in physiology and cancer: biochemical and molecular insight
Al‐Khallaf, H. (2017) · Cell & Bioscience · doi:10.1186/s13578-017-0165-3 · Cited by 133
New Molecular Considerations for Glioma: IDH, ATRX, BRAF, TERT, H3 K27M
Karsy, M. J., Guan, J., Cohen, A. L., Jensen, R. L., & Colman, H. (2017) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-017-0722-5 · Cited by 128
Hypoxia-inducible factors in cancer stem cells and inflammation
Peng, G., & Liu, Y. (2015) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2015.03.003 · Cited by 127
Novel Delivery Strategies for Glioblastoma
Zhou, J., Atsina, K., Himes, B. T., Strohbehn, G. W., & Saltzman, W. M. (2012) · The Cancer Journal · doi:10.1097/ppo.0b013e318244d8ae · Cited by 128
Role of AHR and HIF-1α in Glioblastoma Metabolism
Gabriely, G., Wheeler, M. A., Takenaka, M. C., & Quintana, F. J. (2017) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2017.02.009 · Cited by 124
IDH1 Mutation Induces Reprogramming of Pyruvate Metabolism
Izquierdo-Garcia, J. L., Viswanath, P., Eriksson, P., Cai, L., Radoul, M., Chaumeil, M. M., Blough, M., Luchman, H. A., Weiss, S., Cairncross, J. G., et al. (2015) · Cancer Research · doi:10.1158/0008-5472.can-15-0840 · Cited by 123
Effective immuno-targeting of the IDH1 mutation R132H in a murine model of intracranial glioma
Pellegatta, S., Valletta, L., Corbetta, C., Patanè, M., Zucca, I., Sirtori, F. R., Bruzzone, M. G., Fogliatto, G., Isacchi, A., Pollo, B., et al. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-014-0180-0 · Cited by 123
Proteomic and phosphoproteomic landscapes of acute myeloid leukemia
Kramer, M. H., Zhang, Q., Sprung, R. W., Day, R. B., Erdmann-Gilmore, P., Li, Y., Xu, Z., Helton, N., George, D. R., Mi, Y., et al. (2022) · Blood · doi:10.1182/blood.2022016033 · Cited by 124
Alterations of metabolic genes and metabolites in cancer
Oermann, E. K., Wu, J., Guan, K., & Xiong, Y. (2012) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2012.01.013 · Cited by 125
Self-citationGlioma Stem Cells and Their Microenvironments: Providers of Challenging Therapeutic Targets
Codrici, E., Enciu, A., Popescu, I. D., Mihai, S., & Tănase, C. (2016) · Stem Cells International · doi:10.1155/2016/5728438 · Cited by 125
Grassian, A. R., Lin, F., Barrett, R., Liu, Y., Jiang, W., Korpal, M., Astley, H. M., Gitterman, D. P., Henley, T., Howes, R., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.417832 · Cited by 122
Self-citationQuantitative metabolome analysis profiles activation of glutaminolysis in glioma with IDH1 mutation
Ohka, F., Ito, M., Ranjit, M., Senga, T., Motomura, A., Motomura, K., Saito, K., Kato, K., Kato, Y., Wakabayashi, T., et al. (2014) · Tumor Biology · doi:10.1007/s13277-014-1784-5 · Cited by 124
Mitochondrial dysfunction in cancer: Potential roles of ATF5 and the mitochondrial UPR
Deng, P., & Haynes, C. M. (2017) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2017.05.002 · Cited by 121
Konopleva, M., Thall, P. F., Yi, C. A., Borthakur, G. M., Coveler, A. L., Bueso‐Ramos, C. E., Benito, J., Konoplev, S. N., Gu, Y., Ravandi, F., et al. (2015) · Haematologica · doi:10.3324/haematol.2014.118455 · Cited by 120
Diverse modes of genomic alteration in hepatocellular carcinoma
Jhunjhunwala, S., Jiang, Z., Stawiski, E. W., Gnad, F., Liu, J., Mayba, O., Du, P., Diao, J., Johnson, S., Wong, K., et al. (2014) · Genome biology · doi:10.1186/s13059-014-0436-9 · Cited by 118
Spitz melanoma is a distinct subset of spitzoid melanoma
Raghavan, S. S., Peternel, S., Mully, T. W., North, J. P., Pincus, L. B., LeBoit, P. E., McCalmont, T. H., Bastian, B. C., & Yeh, I. (2020) · Modern Pathology · doi:10.1038/s41379-019-0445-z · Cited by 125
Glioblastoma: Current Status, Emerging Targets, and Recent Advances
Thakur, A., Faujdar, C., Sharma, R., Sharma, S., Malik, B., Nepali, K., & Liou, J. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01946 · Cited by 122
Hypoxia signaling in cancer: Implications for therapeutic interventions
Zhuang, Y., Liu, K., He, Q., Gu, X., Jiang, C., & Wu, J. (2023) · MedComm · doi:10.1002/mco2.203 · Cited by 119
Zou, P., Xu, H., Chen, P., Yan, Q., Zhao, L., Zhao, P., & Gu, A. (2013) · PLoS ONE · doi:10.1371/journal.pone.0068782 · Cited by 127
Glioblastoma, Cancer Stem Cells and Hypoxia
Bar, E. E. (2010) · Brain Pathology · doi:10.1111/j.1750-3639.2010.00460.x · Cited by 125
Yang, B., Zhong, C., Peng, Y., Lai, Z., & Ding, J. (2010) · Cell Research · doi:10.1038/cr.2010.145 · Cited by 121
Self-citationBayley, J., & Devilee, P. (2010) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2010.02.008 · Cited by 119
Cancer Missense Mutations Alter Binding Properties of Proteins and Their Interaction Networks
Nishi, H., Tyagi, M. G., Teng, S., Shoemaker, B. A., Hashimoto, K., Alexov, E. G., Wuchty, S., & Panchenko, A. R. (2013) · PLoS ONE · doi:10.1371/journal.pone.0066273 · Cited by 117
Regulated oxygen sensing by protein hydroxylation in renal erythropoietin-producing cells
Wenger, R. H., & Hoogewijs, D. (2010) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00736.2009 · Cited by 120
JmjC enzyme KDM2A is a regulator of rRNA transcription in response to starvation
Tanaka, Y., Okamoto, K., Teye, K., Umata, T., Yamagiwa, N., Suto, Y., Zhang, Y., & Tsuneoka, M. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.56 · Cited by 118
Liu, G., Bi, Y., Xue, L., Zhang, Y., Yang, H., Chen, X., Lu, Y., Zhang, Z., Liu, H., Wang, X. Q., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1420419112 · Cited by 119
Chotirat, S., Thongnoppakhun, W., Promsuwicha, O., Boonthimat, C., & Auewarakul, C. U. (2012) · Journal of Hematology & Oncology · doi:10.1186/1756-8722-5-5 · Cited by 116
Detection of IDH1 mutation in human gliomas: comparison of immunohistochemistry and sequencing
Takano, S., Tian, W., Matsuda, M., Yamamoto, T., Ishikawa, E., Kaneko, M. K., Yamazaki, K., Kato, Y., & Matsumura, A. (2011) · Brain Tumor Pathology · doi:10.1007/s10014-011-0023-7 · Cited by 113
Metabolic gene alterations impact the clinical aggressiveness and drug responses of 32 human cancers
Sinkala, M., Mulder, N., & Martin, D. P. (2019) · Communications Biology · doi:10.1038/s42003-019-0666-1 · Cited by 111
Jin, G., Reitman, Z. J., Spasojevic, I., Batinic-Haberle, I., Yang, J., Schmidt-Kittler, O., Bigner, D. D., & Yan, H. (2011) · PLoS ONE · doi:10.1371/journal.pone.0016812 · Cited by 112
Targeting Cancer Metabolism - Revisiting the Warburg Effects
Tran, Q., Lee, H., Park, J., Kim, S., & Park, J. (2016) · Toxicological Research · doi:10.5487/tr.2016.32.3.177 · Cited by 116
Dendritic cell Piezo1 directs the differentiation of TH1 and Treg cells in cancer
Wang, Y., Yang, H., Jia, A., Wang, Y., Yang, Q., Dong, Y., Hou, Y., Cao, Y., Dong, L., Bi, Y., et al. (2022) · eLife · doi:10.7554/elife.79957 · Cited by 121
Pheochromocytomas: The (pseudo)-hypoxia hypothesis
Favier, J., & Gimenez‐Roqueplo, A. (2010) · Best Practice & Research Clinical Endocrinology & Metabolism · doi:10.1016/j.beem.2010.10.004 · Cited by 117
Endothelial cell metabolism: parallels and divergences with cancer cell metabolism
Verdegem, D., Moens, S., Stapor, P. C., & Carmeliet, P. (2014) · Cancer & Metabolism · doi:10.1186/2049-3002-2-19 · Cited by 117
Kaminska, B., Czapski, B., Guzik, R., Król, S. K., & Gielniewski, B. (2019) · Molecules · doi:10.3390/molecules24050968 · Cited by 113
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
Tran, A. N., Lai, A., Li, S., Pope, W. B., Teixeira, S., Harris, R. J., Woodworth, D. C., Nghiemphu, P. L., Cloughesy, T. F., & Ellingson, B. M. (2013) · Neuro-Oncology · doi:10.1093/neuonc/not198 · Cited by 108
Molecular pathology in adult high‐grade gliomas: from molecular diagnostics to target therapies
Masui, K., Cloughesy, T. F., & Mischel, P. S. (2011) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2011.01238.x · Cited by 113
Glioma cells showing IDH1 mutation cannot be propagated in standard cell culture conditions
Piaskowski, S., Bieńkowski, M., Stoczyńska-Fidelus, E., Stawski, R. S., Sieruta, M., Szybka, M., Papierz, W., Wolańczyk, M., Jaskólski, D. J., Liberski, P. P., et al. (2011) · British Journal of Cancer · doi:10.1038/bjc.2011.27 · Cited by 107
Kato, Y., Jin, G., Kuan, C.-T., McLendon, R. E., Yan, H., & Bigner, D. D. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.10.001 · Cited by 106
Role of Mitochondria in Cancer Stem Cell Resistance
García-Heredia, J. M., & Carnero, A. (2020) · Cells · doi:10.3390/cells9071693 · Cited by 109
The Role of Mitochondrial NADPH-Dependent Isocitrate Dehydrogenase in Cancer Cells
Smolková, K., & Ježek, P. (2012) · International Journal of Cell Biology · doi:10.1155/2012/273947 · Cited by 114
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
New 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
Liu, J. M., Pan, F., Li, L., Liu, Q. R., Chen, Y., Xiong, X., Cheng, K., Yu, S., Shi, Z., Yu, A. C., et al. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.06.042 · Cited by 102
Cancer cell metabolism and the modulating effects of nitric oxide
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
TET-Mediated Hypermethylation Primes SDH-Deficient Cells for HIF2α-Driven Mesenchymal Transition
Morin, A., Goncalves, J., Moog, S., Castro‐Vega, L. J., Job, S., Buffet, A., Fontenille, M., Woszczyk, J., Gimenez‐Roqueplo, A., Letouzé, É., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.03.022 · Cited by 110
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
Escaping Death: Mitochondrial Redox Homeostasis in Cancer Cells
Ciccarese, F., & Ciminale, V. (2017) · Frontiers in Oncology · doi:10.3389/fonc.2017.00117 · Cited by 104
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
Self-citationStructural analysis of oncogenic mutation of isocitrate dehydrogenase 1
Rajendran, V. (2016) · Molecular BioSystems · doi:10.1039/c6mb00182c · Cited by 98
Hypoxia-mediated drug resistance in breast cancers
McAleese, C. E., Choudhury, C., Butcher, N. J., & Minchin, R. F. (2020) · Cancer Letters · doi:10.1016/j.canlet.2020.11.045 · Cited by 99
Receptor Tyrosine Kinase Signaling and Targeting in Glioblastoma Multiforme
Tilak, M., Holborn, J., New, L. A., Lalonde, J., & Jones, N. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22041831 · Cited by 105
Phenylalanine impairs insulin signaling and inhibits glucose uptake through modification of IRβ
Zhou, Q., Sun, W.-W., Chen, J.-C., Zhang, H.-L., Liu, J., Lin, Y., Lin, P., Wu, B., An, Y., Huang, L., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-32000-0 · Cited by 104
Self-citationUnraveling the Genetics of Cancer: Genome Sequencing and Beyond
Wong, K. M., Hudson, T. J., & McPherson, J. D. (2011) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev-genom-082509-141532 · Cited by 96
Ho, P. A., Alonzo, T. A., Kopecky, K. J., Miller, K. L., Kuhn, J., Zeng, R., Gerbing, R. B., Raimondi, S., Hirsch, B. A., Oehler, V. G., et al. (2010) · Leukemia · doi:10.1038/leu.2010.56 · Cited by 96
APC/CCDH1 synchronizes ribose-5-phosphate levels and DNA synthesis to cell cycle progression
Li, Y., Yao, C.-F., Xu, F., Qu, Y., Li, J.-T., Lin, Y., Cao, Z., Lin, P., Xu, W., Zhao, S., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-10375-x · Cited by 96
Self-citationThe role of 5-hydroxymethylcytosine in development, aging and age-related diseases
López, V., Fernández, A. F., & Fraga, M. F. (2017) · Ageing Research Reviews · doi:10.1016/j.arr.2017.05.002 · Cited by 101
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?
Abla, H., Sollazzo, M., Gasparre, G., Iommarini, L., & Porcelli, A. M. (2019) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2019.05.031 · Cited by 99
Metabolomics, metabolic flux analysis and cancer pharmacology
Liang, L., Sun, F., Wang, H., & Hu, Z. (2021) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2021.107827 · Cited by 99
Metabolomics in Drug Target DiscoveryPreprint
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
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
IDH1 and IDH2 mutations in pediatric acute leukemia
Andersson, A., Miller, D. W., Lynch, J. A., Lemoff, A. S., Cai, Z., Pounds, S. B., Radtke, I., Yan, B., Schuetz, J. D., Rubnitz, J. E., et al. (2011) · Leukemia · doi:10.1038/leu.2011.133 · Cited by 96
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
MicroRNA-183 upregulates HIF-1α by targeting isocitrate dehydrogenase 2 (IDH2) in glioma cells
Tanaka, H., Sasayama, T., Tanaka, K., Nakamizo, S., Nishihara, M., Mizukawa, K., Kohta, M., Koyama, J., Miyake, S., Taniguchi, M., et al. (2012) · Journal of Neuro-Oncology · doi:10.1007/s11060-012-1027-9 · Cited by 96
Reactive Oxygen Species, Metabolic Plasticity, and Drug Resistance in Cancer
Bhardwaj, V., & He, J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21103412 · Cited by 88
Wild-type isocitrate dehydrogenase under the spotlight in glioblastoma
Alzial, G., Renoult, O., Paris, F., Gratas, C., Clavreul, A., & Pecqueur, C. (2021) · Oncogene · doi:10.1038/s41388-021-02056-1 · Cited by 101
Isocitrate dehydrogenase mutations in gliomas
Guo, C., Pirozzi, C. J., Lopez, G. Y., & Yan, H. (2011) · Current Opinion in Neurology · doi:10.1097/wco.0b013e32834cd415 · Cited by 93
D-2-hydroxyglutarate produced by mutant IDH2 causes cardiomyopathy and neurodegeneration in micePreprint
Akbay, E. A., Moslehi, J. J., Christensen, C. L., Saha, S. K., Tchaicha, J. H., Ramkissoon, S. H., Stewart, K. M., Carretero, J., Kikuchi, E., Zhang, H., et al. (2014) · Genes & Development · doi:10.1101/gad.231233.113 · Cited by 93
Thon, N., Eigenbrod, S., Kreth, S., Lutz, J., Tonn, J., Kretzschmar, H. A., Peraud, A., & Kreth, F.-W. (2011) · Cancer · doi:10.1002/cncr.26298 · Cited by 88
Alam, M. M., Lal, S., FitzGerald, K. E., & Li, Z. (2016) · Clinical and Translational Medicine · doi:10.1186/s40169-016-0082-9 · Cited by 92
Self-citationKlopfleisch, R., Klose, P., Weise, C., Bondzio, A., Multhaup, G., Einspanier, R., & Gruber, A. D. (2010) · Journal of Proteome Research · doi:10.1021/pr100671c · Cited by 88
Readers of DNA methylation, the MBD family as potential therapeutic targets
Ginder, G. D., & Williams, D. C. (2017) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2017.11.002 · Cited by 92
Obstacles to Glioblastoma Treatment Two Decades after Temozolomide
Cruz, J. V. R., Batista, C., Afonso, B. D. H., Alexandre‐Moreira, M. S., Dubois, L. G., Pontes, B., Moura‐Neto, V., & Mendes, F. A. (2022) · Cancers · doi:10.3390/cancers14133203 · Cited by 92
Friend or foe—IDH1 mutations in glioma 10 years on
Huang, L. E. (2019) · Carcinogenesis · doi:10.1093/carcin/bgz134 · Cited by 84
Damm, F., Thol, F. R., Hollink, I. H. I. M., Zimmermann, M., Reinhardt, K., van den Heuvel‐Eibrink, M. M., Zwaan, C. M., de Haas, V., Creutzig, U., Klusmann, J., et al. (2011) · Leukemia · doi:10.1038/leu.2011.142 · Cited by 87
Kalinina, J., Carroll, A., Wang, L., Yu, Q., Mancheno, D. E., Wu, S., Liu, F., Ahn, J. Y., He, M., Mao, H. Z., et al. (2012) · Journal of Molecular Medicine · doi:10.1007/s00109-012-0888-x · Cited by 84
Badur, M. G., Muthusamy, T., Parker, S. J., Ma, S., McBrayer, S. K., Cordes, T., Magaña, J. H., Guan, K., & Metallo, C. M. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.09.074 · Cited by 87
Self-citationPhysical Exercise and Epigenetic Modulation: Elucidating Intricate Mechanisms
Pareja-Galeano, H., Sanchis‐Gomar, F., & García‐Giménez, J. L. (2014) · Sports Medicine · doi:10.1007/s40279-013-0138-6 · Cited by 87
Identification of several novel non-p.R132 IDH1 variants in thyroid carcinomas
Hemerly, J. P., Bastos, A. U., & Cerutti, J. M. (2010) · European Journal of Endocrinology · doi:10.1530/eje-10-0473 · Cited by 84
Metadata
- Authors
- Zhao, S., Lin, Y., Xu, W., Jiang, W., Zha, Z., Wang, P., Yu, W., Li, Z., Gong, L., Peng, Y., Ding, J., Lei, Q., Guan, K.-L., & Xiong, Y.
- Affiliations
- Shanghai Medical College of Fudan University (CN)
- Molecular and Cell Biology Laboratory, Institute of Biomedical Sciences, Fudan University, 130 Dong-An Road, Shanghai 200032, China.
- University of North Carolina at Chapel Hill (US)
- Corresponding author
- Lin, Yan
- Xu, Wei
- Jiang, Wenqing
- Guan, Kun-Liang
- Xiong, Yue
- ORCID
- Venue
- Science
- Published
- 2009-04-10
- Volume
- 324
- Issue
- 5924
- Pages
- 261-265
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC3251015
- OpenAlex
- W1964150693
- Cited by
- 1,119
- References
- 12
- Citations by year
- 2026: 24 · 2025: 27 · 2024: 43 · 2023: 36 · 2022: 50 · 2021: 62 · 2020: 58 · 2019: 54 · 2018: 63 · 2017: 71 · 2016: 57 · 2015: 71 · 2014: 74 · 2013: 90 · 2012: 84
- FWCI
- 37.70
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Cancer Institute (R01CA068377)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
- Health Sciences › Medicine › Oncology › Glioma Diagnosis and Treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chromatin Remodeling and Cancer
- Keywords
- IDH1 mutation, isocitrate dehydrogenase, glioma, HIF-1α, alpha-ketoglutarate, heterodimer formation, tumor suppressor, hypoxia, carcinogenesis, brain tumors, enzyme activity
- MeSH terms
- Adolescent, Adult, Aged, Astrocytoma, Brain Neoplasms, Cell Line, Child, Female, Glioblastoma, Glioma, Humans, Isocitrate Dehydrogenase, Ketoglutaric Acids, Male, Middle Aged, Oligodendroglioma, Oxalates, Gene Expression Regulation, Neoplastic, Genes, Tumor Suppressor, Mutant Proteins, Hypoxia-Inducible Factor 1, alpha Subunit, Biocatalysis, Protein Multimerization
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
