The DOI matches its Crossref record; 52 of the 52 references it cites were found in a registry or an index.
AG-221, a First-in-Class Therapy Targeting Acute Myeloid Leukemia Harboring Oncogenic IDH2 Mutations
Published version of a preprint
Abstract
Somatic gain-of-function mutations in isocitrate dehydrogenases (IDH) 1 and 2 are found in multiple hematologic and solid tumors, leading to accumulation of the oncometabolite (R)-2-hydroxyglutarate (2HG). 2HG competitively inhibits α-ketoglutarate–dependent dioxygenases, including histone demethylases and methylcytosine dioxygenases of the TET family, causing epigenetic dysregulation and a block in cellular differentiation. In vitro studies have provided proof of concept for mutant IDH inhibition as a therapeutic approach. We report the discovery and characterization of AG-221, an orally available, selective, potent inhibitor of the mutant IDH2 enzyme. AG-221 suppressed 2HG production and induced cellular differentiation in primary human IDH2 mutation–positive acute myeloid leukemia (AML) cells ex vivo and in xenograft mouse models. AG-221 also provided a statistically significant survival benefit in an aggressive IDH2R140Q-mutant AML xenograft mouse model. These findings supported initiation of the ongoing clinical trials of AG-221 in patients with IDH2 mutation–positive advanced hematologic malignancies. Significance: Mutations in IDH1/2 are identified in approximately 20% of patients with AML and contribute to leukemia via a block in hematopoietic cell differentiation. We have shown that the targeted inhibitor AG-221 suppresses the mutant IDH2 enzyme in multiple preclinical models and induces differentiation of malignant blasts, supporting its clinical development. Cancer Discov; 7(5); 478–93. ©2017 AACR. See related commentary by Thomas and Majeti, p. 459. See related article by Shih et al., p. 494. This article is highlighted in the In This Issue feature, p. 443
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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
“A specific inhibitor of mutant IDH2, AG-221 (enasidenib) confers survival benefit in a mouse model of IDH2-mutant AML (Quivoron et al., 2014; Yen et al., 2017) and became the first compound targeting mutant IDH to enter clinical trials in 2014. Early results in IDH2-mutant AML patients have suggested enasidenib can provide clinical benefit (DiNardo et al., 2015; Stein et al., 2014), and this drug”
From Targeting Metabolism for Cancer Therapy (2017) · cites this paper as Yen et al., 2017
Citations
Cites
Hallmarks of Cancer: The Next Generation
Hanahan, D., & Weinberg, R. A. (2011) · Cell · doi:10.1016/j.cell.2011.02.013 · Cited by 66,590
[20] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475
Features and development of Coot
Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 29,915
Phaser crystallographic software
McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., & Read, R. J. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807021206 · Cited by 20,612
NMRPipe: A multidimensional spectral processing system based on UNIX pipes
Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., & Bax, A. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00197809 · Cited by 15,961
REFMAC 5 for the refinement of macromolecular crystal structures
Murshudov, G. N., Skubák, P., Lebedev, A. A., Pannu, N. S., Steiner, R. A., Nicholls, R. A., Winn, M., Long, F., & Vagin, A. A. (2011) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444911001314 · Cited by 8,415
The emerging hallmarks of cancer metabolism
Pavlova, N. N., & Thompson, C. B. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2015.12.006 · Cited by 5,926 · cited 1×
“Metabolic reprogramming is a hallmark of cancer, contributing to the initiation and maintenance of tumors (1, 2).”
BackgroundAn 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
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
Self-citation
Cited by
Sorted by citations
Items 401–478 of 478
Nardozza, A. M., Guarnera, L., Travaglini, S., Ottone, T., Divona, M., Bellis, E. D., Savi, A., Banella, C., Noguera, N. I., Fusco, D. D., et al. (2023) · British Journal of Haematology · doi:10.1111/bjh.19216 · Cited by 1
IDH2 Inhibitors Gain a Wildcard Status in the Cancer Therapeutics Competition
Piva, R., Gharari, N., Labrador, M., & Mader, S. (2024) · Cancers · doi:10.3390/cancers16193280 · Cited by 1
Transforming agents: The power of structural modifications in glioblastoma multiforme therapy
Norollahi, S. E., Morovat, S., Keymoradzadeh, A., Hamzei, A., Modaeinama, M., SOLEIMANMANESH, N., Soleimanmanesh, Y., Najafizadeh, A., Bakhshalipour, E., Alijani, B., et al. (2024) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2024.12.001 · Cited by 1
Tong, Z., Yerramilli, U., Yao, S. Y. M., Young, J. D., Hoffmann, M., & Surapaneni, S. (2018) · Xenobiotica · doi:10.1080/00498254.2018.1539783 · Cited by 1
“Nonclinical studies have demonstrated that enasidenib effectively inhibits the activity of IDH mutant protein leading to the reduction of 2-HG in tumors and the reversal of IDH mutation-induced histone and DNA hypermethylation (Kernytsky et al., 2015; Yen et al., 2017).”
BackgroundPrognostic markers in acute myeloid leukemia : A candidate gene approach
Falk, I. J. (2018) · Linköping University medical dissertations · doi:10.3384/diss.diva-153476 · Cited by 1
Future Developments: Novel Agents
Chua, C. C., & Wei, A. H. (2021) · Hematologic malignancies · doi:10.1007/978-3-030-72676-8_17 · Cited by 1
Machine Learning–Guided Differentiation Therapy Targets Cancer Stem Cells in Colorectal CancersPreprint
Sinha, S., Alcantara, J. A., Perry, K., Castillo, V., Ondersma, A., Banerjee, S., McLaren, E., Espinoza, C. R., Taheri, S., Vidales, E., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.09.13.557628 · Cited by 1
Toumpe, I., Masid, M., Vassily Hatzimanikatis, A., & Mišković, L. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.22.682756 · Cited by 2
“66,67 These inhibitors have been produced to selectively target mutant activity rather than wild-type IDH2.”
Signaling Landscape of AML: The Story So Far
Martinelli, C. (2018) · Springer eBooks · doi:10.1007/978-3-319-71553-7_13
Apport du séquençage haut débit dans la prise en charge des hémopathies lymphoïdes
Pastoret, C., & Lamy, T. (2018) · Revue Francophone des Laboratoires · doi:10.1016/s1773-035x(18)30362-9
Recently approved molecularly targeted therapies in AML
Papadantonakis, N., & Erba, H. P. (2019) · Advances in Cell and Gene Therapy · doi:10.1002/acg2.76
Dittakavi, S., Hallur, G., Purra, B. R., Kiran, V., Zakkula, A., & Mullangi, R. (2019) · Drug Research · doi:10.1055/a-1024-3623
“Enasidenib has shown dose-dependent survival advantage in aggressive human AML xenograft model [5].”
BackgroundPharmaceutical applications of organofluorine compounds
Reddy, V. P. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-813286-9.00005-5
Leukemia: Trends in treatment and how close we have achieved eradication
Jain, S., Raza, K., Agrawal, A. K., & Vaidya, A. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-817846-1.00025-4
Taking aim at IDH in fitter patients with AML
Wei, A. H., & Daver, N. G. (2021) · Blood · doi:10.1182/blood.2020009361
Faculty Opinions recommendation of Cutting edge molecular therapy for acute myeloid leukemia.
Liu, M. (2021) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.738375855.793584684
Treatment of Acute Myeloid Leukemia: A Concise Overview
(2020) · Abasyn Journal Life Sciences · doi:10.34091/ajls.3.2.11
A murine model for human early/immature T-cell precursor acute lymphoblastic leukemia (EITP ALL)
Negi, V., & Aplan, P. D. (2022) · Oncoscience · doi:10.18632/oncoscience.567
“Enasidenib (AG-221) is a potent selective inhibitor of the mutant IDH2 enzyme which has recently been approved for treatment of relapsed or refractory AML patients with IDH2 mutations [14].”
BackgroundEpigenetic targeted therapies in hematological malignancies
Venney, D., Greenfield, G., Preston, P., Mohd-Sarip, A., & Mills, K. (2023) · Elsevier eBooks · doi:10.1016/b978-0-323-91367-6.00017-9
Research Progress in the Relationship and Role of IDH1/2 Gene Mutation and Acute My-eloid Leukemia
戚, 栋. (2023) · Advances in Clinical Medicine · doi:10.12677/acm.2023.1361289
Herold, R. A., Schofield, C. J., & Armstrong, F. A. (2023) · Angewandte Chemie · doi:10.1002/ange.202309149
In the Pipeline: Emerging Therapy for MDS and MDS/MPN
Gill, H., Lee, E., & Mo, P. (2023) · Springer eBooks · doi:10.1007/978-981-99-3810-0_35
A commentary: Role of MTA1: a novel modulator reprogramming mitochondrial glucose metabolism
Ma, D., & Liu, F. (2023) · ONCOLOGIE · doi:10.1515/oncologie-2023-0339
Nonclinical Development of Oncology Drugs
Oh, H. H., Surapaneni, S., & Hui, J. Y. (2024) · Elsevier eBooks · doi:10.1016/b978-0-323-85704-8.00027-x
Kapoor, P., Gupta, R., Kaushal, S. A., Yerramilli, N. P., Rahman, K., Sharma, A., Mishra, A., Hassan, F., Chandra, D., Singh, M. K., et al. (2024) · Indian Journal of Hematology and Blood Transfusion · doi:10.1007/s12288-024-01855-2
Reinhardt, T., Harraoui, Y. E., Rothemann, R. A., Jauch, A. T., Müller-Deubert, S. M., Köllen, M. F., Risch, T., Jacobs, L. H. C., Müller, R., Traube, F. R., et al. (2025) · Angewandte Chemie · doi:10.1002/ange.202421424
Precision medicine in myeloid neoplasms/acute leukemias
Ramalingam, S. H. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-800684-9.00002-2
Combinatorial inhibition of LSD1 and Menin induces therapeutic differentiation in AMLPreprint
Rodríguez, M. F. C., Rico, J., Vijayaraghavan, M., Yan, F., King, A., Petroni, R., Leu, N. A., Goodrow, H., Bernt, K. M., McGeehan, G. M., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.11.09.687496 · Cited by 1
“For example, IDH inhibitors act largely through inducing differentiation in IDH1/2-mutant AML and have been clinically successful 7 .”
Däther, M., Peev, E., Fröhlich, A. S., Vick, B., Fatourechi, S., Gasparoni, G., Heiß, M., Pleintinger, C. C., Bisong, E. A., Hurmiz, H., et al. (2026) · Angewandte Chemie · doi:10.1002/ange.6265286
Aumer, T., Gremmelmaier, C. B., Runtsch, L. S., Pforr, J. C., Yeşiltaç, G. N., Kaiser, S., & Traube, F. R. (2022) · Figshare · doi:10.6084/m9.figshare.21078749
Tateishi, K., Miyake, Y., Nakamura, T., Iwashita, H., Hayashi, T., Oshima, A., Honma, H., Hayashi, H., Sugino, K., Kato, M., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26645494
Tateishi, K., Miyake, Y., Nakamura, T., Iwashita, H., Hayashi, T., Oshima, A., Honma, H., Hayashi, H., Sugino, K., Kato, M., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26645491
Lee, G., Lee, S. M., Lee, S., Jeong, C. W., Song, H., Lee, S. Y., Yun, H., Koh, Y., & Kim, H. U. (2024) · Figshare · doi:10.6084/m9.figshare.25389925
Chen, J., Yang, J., Wei, Q., Weng, L., Wu, F., Shi, Y., Cheng, X., Cai, X., Hu, C., & Cao, P. (2020) · Figshare · doi:10.6084/m9.figshare.12082356
Lee, G., Lee, S. M., Lee, S., Jeong, C. W., Song, H., Lee, S. Y., Yun, H., Koh, Y., & Kim, H. U. (2024) · Figshare · doi:10.6084/m9.figshare.25389463
Yang, J., Chen, J., Chang, J., Sun, X., Wei, Q., Cai, X., & Cao, P. (2024) · Figshare · doi:10.6084/m9.figshare.25210637
Yuan, S., & Gabr, M. T. (2025) · ACS Omega · doi:10.1021/acsomega.5c11235
Rankin, A. W., Keating, A. K., Abu‐Arja, R., Thakar, M. S., & Rangarajan, H. G. (2026) · Molecular Therapy Oncology · doi:10.1016/j.omton.2026.201141
NFS1 Regulates IDH2 to Attenuate Abdominal Aortic Aneurysms via Interacting With SP2
Zhang, L., Zhang, Y., Wen, D., Guo, S., Qi, X., Wang, H., Sun, Y., Yang, G., Wang, Y., & Xue, S. (2026) · Advanced Science · doi:10.1002/advs.202505240
Cancer biology and the principles of targeted cancer drug discovery
Davies, A., Jones, G., Krishnan, S., Krishnamoorthy, M., Maruggi, M., Kaneda, M., & Marjon, K. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-29808-0.00035-2
Origin and pronostic impact of intra-leukemic heterogeneity in acute myeloid leukemias
Duchmann, M. (2022) · theses.fr (ABES) · doi:10.70675/74f56644z3676z489bz8e12z27fa072401b7
Dilitatlı, S., Demirbanka, F. G. Ö., Türkmenoğlu, B., & Köse, M. (2026) · Journal of the Iranian Chemical Society · doi:10.1007/s13738-026-03439-5
“The crystal structures of 5I96 [ 36] and 6U4J [37 ] were used in the performed to protocol [ 38 , 39].”
Asiri, A. (2026) · Frontiers in Medicine · doi:10.3389/fmed.2026.1818483
“It gained FDA approval in August 2017 for treating adults with relapsed or refractory AML harbouring IDH2 mutations (112).”
Identification and Management of Differentiation Syndrome in Emergency Settings: A Narrative Review
Chang, G. A., Bey, T. A., Stroh, J., Qdaisat, A. Z., & Yeung, S. J. (2026) · Cancers · doi:10.3390/cancers18111798
“IDH inhibitors suppress 2HG production and thus enable cell differentiation to proceed [60].”
Shankar, T., Gao, Y., Erebholo, Z., Nakama, N., Kim, K., Williamson, I. K., Snyder, N., Kransdorf, E., DeBerardinis, R. J., Taegtmeyer, H., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.06.06.727699
Guo, R., & Maojun, Y. (2026) · Advances in experimental medicine and biology · doi:10.1007/978-3-032-26629-3_11
Epigenetic Targeting in Myeloid Malignancies
Cardoso, B. A. (2026) · Advances in experimental medicine and biology · doi:10.1007/978-3-032-12166-0_13
Brooks, N. A., Skwarska, A., Salama, V., Bender, M. H., Kays, L. M., DeWalt, R. I., Perria, B., Thete, D., Manro, J. R., Cavitt, R. N., et al. (2026) · Blood Cancer Discovery · doi:10.1158/2643-3230.bcd-25-0379
Khatun, M. M., Sarker, M. A., Podder, M. K., Biswas, M. S., Hasan, M. M., Tamannaa, Z., Hossain, M. N., Badhon, R. S., & Akter, M. A. (2026) · Health Science Reports · doi:10.1002/hsr2.73070
“Other oncometabolites associated with SDH and FH gene mutation, including fumarate and succinate, are also explored as candidate biomarkers and treatments in a variety of cancers [108].”
Biochemical aspects of chromatin-modifying drugs
Ediriweera, M. K., & Jayasena, S. (2026) · Drug Discovery Today · doi:10.1016/j.drudis.2026.104784
Preclinical Evaluation of D-2-Hydroxyglutarate Inhibitor to Target GlioblastomaPreprint
Vignesh Balaji, E., Saha, M., Madalageri, M., Sadashivanavar, V., Kinnal, R., Moorkoth, S., & Pai, K. S. R. (2026) · Research Square · doi:10.21203/rs.3.rs-10617863/v1
Shaldam, M. A., El-Hamaky, A. A., Khattab, N. A., Hefny, S. M., Nafie, M. S., Eldehna, W. M., & Tawfik, H. O. (2026) · Drug Discovery Today · doi:10.1016/j.drudis.2026.104797
Hosono, N., Ida, N., & Yamauchi, T. (2026) · Biochemical Pharmacology · doi:10.1016/j.bcp.2026.118440
Twisting the End Game: How Telomere Chromatin Modifications Shape Telomere Maintenance
Wang, J., Su, Y., Chen, C., Li, Y., Han, J., Du, L., Zheng, L., Dang, Y., & Peng, Y. (2026) · Aging Cell · doi:10.1111/acel.70694
“Relieving such inhibitions can be achieved through therapeutic targeting of mutant IDH to reduce 2-hydroxyglutarate level (Ye et al. 2018; Yen et al. 2017), or through using KDM4B small molecule agonists.”
Iasenza, I. A., Sun, Y. L., Best, L., Dakik, H., Boileau, M., Neumann, A. L., Arreba-Tutusaus, P., Saby, M., Hébert, J., Minden, M. D., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.09.09.750191
Zhang, X., Tian, C., Ding, Y., Dong, L., Yu, J. H., Su, R., & Gao, M. (2026) · Cancers · doi:10.3390/cancers18193091
“Indeed, preclinical and clinical studies have demonstrated promising therapeutic benefits from targeting mitochondrion-associated vulnerabilities in AML, such as BCL2-and IDH2-directed therapies [22–25].”
Fouad, M. A. (2026) · Biochemical Pharmacology · doi:10.1016/j.bcp.2026.118508
Martinello, C., Krug, A., Marin-Escudero, P., Pollet, A., Lemonnier, F., Boyer, L., & Verhoeyen, E. (2026) · Pharmaceutics · doi:10.3390/pharmaceutics18101292
“Enasidenib exerts its therapeutic effect by inhibiting mutant IDH2 , lowering the high 2-HG levels, and restoring DNA/histone methylation-related processes, while maintaining normal metabolic functions [102,103].”
gem -Dimethylcarbinol: A tert -Butyl Bioisostere with Greatly Reduced Lipophilicity
Chiodi, D., & Ishihara, Y. (2026) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6c02769
Fuzzy Interactions Open Perspectives toward Drugging Conformational Heterogeneity
Fidan, V. G., Gürsoy, A., Keskin, Ö., & Fuxreiter, M. (2026) · Biochemistry · doi:10.1021/acs.biochem.6c00665
BindingDB (2024) · UC San Diego · doi:10.7270/q2pg1x06
BindingDB (2025) · UC San Diego · doi:10.7270/q2k078tm
Development of Radioiodinated Tetrahydropyrazolopyridine Inhibitors Targeting mIDH
Kaur, S., Dukić-Stefanović, S., Arnaud, L., Chezal, J., Wenzel, B., Moldovan, R., Kopka, K., & Maisonial‐Besset, A. (2026) · Journal of Labelled Compounds and Radiopharmaceuticals · doi:10.1002/jlcr.70039
Metadata
- Authors
- Yen, K., Travins, J., Wang, F., David, M. D., Artin, E., Straley, K., Padyana, A., Gross, S., DeLaBarre, B., Tobin, E., Chen, Y., Nagaraja, R., Choe, S., Jin, L., Konteatis, Z., Cianchetta, G., Saunders, J. O., Salituro, F. G., Quivoron, C., Opolon, P., Bawa, O., Saada, V., Paci, A., Broutin, S., Bernard, O. A., de Botton, S., Marteyn, B. S., Pilichowska, M., Xu, Y., Fang, C., Jiang, F., Wei, W., Jin, S., Silverman, L., Liu, W., Yang, H., Dang, L., Dorsch, M., Penard-Lacronique, V., Biller, S. A., & Su, S.-S. M.
- Affiliations
- Agios Pharmaceuticals (United States) (US)
- Inserm (FR)
- 1Agios Pharmaceuticals, Inc., Cambridge, Massachusetts.
- Université Paris-Saclay (FR)
- 6Service de Pharmacologie, Département de Biologie et Pathologie Médicales, Gustave Roussy, Université Paris-Saclay, Villejuif, France.
- 2INSERM U1170, Villejuif, France.
- Tufts Medical Center (US)
- 11ShangPharma, Shanghai, China.
- Viva Biotech (China) (CN)
- Corresponding author
- Su, Shin-San Michael
- ORCID
- Yen, Katharine
- Wang, Fang
- David, Muriel D.
- Padyana, Anil
- Tobin, Erica
- Chen, Yue
- Choe, Sung
- Jin, Lei
- Konteatis, Zenon
- Salituro, Francesco G.
- Quivoron, Cyril
- Opolon, Paule
- Bawa, Olivia
- Saada, Véronique
- Broutin, Sophie
- Bernard, Olivier A.
- Marteyn, Benoît S.
- Pilichowska, Monika
- Jiang, Fan
- Wei, Wentao
- Liu, Wei
- Yang, Hua
- Dang, Lenny
- Venue
- Cancer Discovery
- Published
- 2017-04-30
- Volume
- 7
- Issue
- 5
- Pages
- 478-493
- ISSN
- 2159-8274 (ISSN-L)
- 2159-8290
- OpenAlex
- W2588385654
- Cited by
- 471
- References
- 52
- Citations by year
- 2026: 35 · 2025: 47 · 2024: 51 · 2023: 46 · 2022: 48 · 2021: 78 · 2020: 55 · 2019: 37 · 2018: 51 · 2017: 23
- FWCI
- 34.99
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Cancer Discovery (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Cancer Institute (INCa-DGOS-Inserm_6043 and INCa 2012-1-RT-09)
- Association pour la Recherche sur le Cancer (SL220130607089)
- Institut National Du Cancer (INCa-DGOS_5733)
- Topics
- Health Sciences › Medicine › Hematology › Acute Myeloid Leukemia Research
- Health Sciences › Medicine › Oncology › Glioma Diagnosis and Treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chromatin Remodeling and Cancer
- Keywords
- IDH2 inhibitors, acute myeloid leukemia, IDH2 mutation, 2-hydroxyglutarate, oncometabolites, hematopoietic differentiation, TET methylcytosine dioxygenases, histone demethylase, xenograft mouse model
- MeSH terms
- Aminopyridines, Animals, Antineoplastic Agents, Humans, Isocitrate Dehydrogenase, Mutation, Triazines, Leukemia, Myeloid, Acute, Xenograft Model Antitumor Assays, Cell Line, Tumor, Mice
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
