The DOI matches its Crossref record; 14 of the 14 references it cites were found in a registry or an index.
Inhibition of PRC2 Activity by a Gain-of-Function H3 Mutation Found in Pediatric Glioblastoma
Open accessAbstract
EZ Inhibition: Missense mutations in the core constituents of the genome packaging material, chromatin, have been implicated in several of human cancers. Nucleosomes are made up of histones, and a mutation of lysine 27 (K27) to methionine in the N-terminal tail of histone variants H3.3 and H3.1 has been identified in various pediatric gliomas. Lewis et al. (p. 857 , published online 28 March; see the Perspective by Morgan and Shilatifard ) show that the polycomb enzyme complex, which can epigenetically modify K27 by addition of a methyl group—and which is often a silencing signal—is itself potently inhibited by replacement of the H3.3/3.1 K27 by methionine. The inhibition of the EZH2 subunit causes an overall reduction of K27 methylation. Methionine mutants of other methylated lysine residues in histone H3 cause similar reductions in methylation levels of the cognate lysine, altering the epigenetic profiles of such cancer cells.
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Consequently, tumor cells with the K27M mutation exhibit low levels of H3K27me3 and aberrant gene silencing (4,(7)(8)(9).”
From S -adenosyl methionine is necessary for inhibition of the methyltransferase G9a by the lysine 9 to methionine mutation on histone H3 (2016) · cites this paper as [7]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“act in a dominant manner to deplete H3K27 methylation by inhibiting PRC2 methyltransferase activity [5, 6]”
From Histone H3 lysine-to-methionine mutants as a paradigm to study chromatin signaling (2014) · cites this paper as [6]
The cited source says what the claim attributes to it.
In the citing paper
“Additional histone H3 lysine-to-methionine mutants possess dominant gain-of-function activities [6]”
From Histone H3 lysine-to-methionine mutants as a paradigm to study chromatin signaling (2014) · cites this paper as [6]
The cited source says what the claim attributes to it.
In the citing paper
“We and others previously showed that K-to-M oncohistones transform the histone H3 proteins into potent inhibitors of specific lysine methyltransferase enzymes (4-7).”
From S -adenosyl methionine is necessary for inhibition of the methyltransferase G9a by the lysine 9 to methionine mutation on histone H3 (2016) · cites this paper as [7]
The cited source says what the claim attributes to it.
In the citing paper
“Previous studies showed that the K27M mutation found in pediatric glioma is sufficient to transform histone H3 into a potent inhibitor of enzymatic activity of PRC2 (4, 5, 7).”
From S -adenosyl methionine is necessary for inhibition of the methyltransferase G9a by the lysine 9 to methionine mutation on histone H3 (2016) · cites this paper as [7]
The cited source says what the claim attributes to it.
In the citing paper
“we previously showed that H3K9M peptides are capable of inhibiting activity of SUV39H1 and G9a, two H3K9-directed methyltransferases, in vitro (7).”
From S -adenosyl methionine is necessary for inhibition of the methyltransferase G9a by the lysine 9 to methionine mutation on histone H3 (2016) · cites this paper as [7]
The cited source says what the claim attributes to it.
In the citing paper
“Previously, we found that only long, unbranched hydrophobic side chains containing methionine (M) and isoleucine (I) at lysine 27 (K27M and K27I) were capable of inhibiting PRC2 in vitro and decreasing H3K27me3 when expressed ectopically in cultured cells (7).”
From S -adenosyl methionine is necessary for inhibition of the methyltransferase G9a by the lysine 9 to methionine mutation on histone H3 (2016) · cites this paper as [7]
In the citing paper
“Despite reports supporting a higher affinity of PRC2 for H3K27M as compared with wild-type H3 108-110 , H3K27M was often inversely correlated with PRC2 occupancy, challenging the idea that H3K27M sequesters PRC2 on chromatin 111,112 .”
From The roles of DNA, RNA and histone methylation in ageing and cancer (2019) · cites this paper as [112]
In the citing paper
“Expression of the histone mutant is accompanied by a reduction in the levels of Polycomb Repressive Complex 2 (PRC2) mediated H3K27 trimethylation (H3K27me3) and this is purported to be a driving event of DIPG oncogenesis4,5.”
From Therapeutic targeting of polycomb and BET bromodomain proteins in diffuse intrinsic pontine gliomas (2017) · cites this paper as [4]
In the citing paper
“Interestingly upon loss of H3K27me3 these nucleosomes acquire H3K27ac resulting in the formation of H3K27M-K27ac heterotypic nucleosomes4 (Figure 1D and Supplementary Fig. 5B–C).”
From Therapeutic targeting of polycomb and BET bromodomain proteins in diffuse intrinsic pontine gliomas (2017) · cites this paper as [4]
In the citing paper
“As shown by our group and others, H3K27M expression is associated with increased levels of H3K27ac4,5 (Fig. 1D).”
From Therapeutic targeting of polycomb and BET bromodomain proteins in diffuse intrinsic pontine gliomas (2017) · cites this paper as [4]
In the citing paper
“Although still functionally active, PRC2 catalytic property toward H3K27M containing nucleosomes is strongly inhibited4.”
From Therapeutic targeting of polycomb and BET bromodomain proteins in diffuse intrinsic pontine gliomas (2017) · cites this paper as [4]
In the citing paper
“Collectively, these results strongly indicate that H3K27M in DIPG cells does not appear to recruit or sequester EZH2 (or in general PRC2), as suggested by other studies4,6,7.”
From Therapeutic targeting of polycomb and BET bromodomain proteins in diffuse intrinsic pontine gliomas (2017) · cites this paper as [4]
In the citing paper
“Attempts to model H3.3K27M-driven HGG formation in vivo via genetic recombination in neural progenitor/stem cells (NPCs) in the postnatal brain failed to demonstrate tumor-driving activity”
From H3.3K27M Cooperates with Trp53 Loss and PDGFRA Gain in Mouse Embryonic Neural Progenitor Cells to Induce Invasive High-Grade Gliomas (2017) · cites this paper as Lewis et al., 2013
In the citing paper
“H3.3K27M has been shown to have gain-of-function activity inhibiting the Polycomb Repressive Complex 2 (PRC2) (Bender et al., 2013; Lewis et al., 2013), which in turn leads to a global reduction in H3K27me3 levels in primary tumors and tumor-derived primary cells.”
From H3.3K27M Cooperates with Trp53 Loss and PDGFRA Gain in Mouse Embryonic Neural Progenitor Cells to Induce Invasive High-Grade Gliomas (2017) · cites this paper as Lewis et al., 2013
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
The Polycomb complex PRC2 and its mark in life
Margueron, R., & Reinberg, D. (2011) · Nature · doi:10.1038/nature09784 · Cited by 3,347
Driver mutations in histone H3.3 and chromatin remodelling genes in paediatric glioblastoma
Schwartzentruber, J., Korshunov, A., Liu, X.-Y., Jones, D. T. W., Pfaff, E., Jacob, K., Sturm, D., Fontebasso, A. M., Quang, D.-A. K., Tönjes, M., et al. (2012) · Nature · doi:10.1038/nature10833 · Cited by 2,631
St. Jude Children's Research Hospital–Washington University Pediatric Cancer Genome Project (2012) · Nature Genetics · doi:10.1038/ng.1102 · Cited by 1,724
Taverna, S. D., Li, H., Ruthenburg, A. J., Allis, C. D., & Patel, D. J. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1338 · Cited by 1,476
Self-citationRole of the polycomb protein EED in the propagation of repressive histone marks
Margueron, R., Justin, N., Ohno, K., Sharpe, M. L., Son, J., Drury, W. J., Voigt, P., Martin, S. R., Taylor, W. R., Marco, V. D., et al. (2009) · Nature · doi:10.1038/nature08398 · Cited by 1,281
Khuong-Quang, D.-A., Buczkowicz, P., Rakopoulos, P., Liu, X.-Y., Fontebasso, A. M., Bouffet, E., Bartels, U., Albrecht, S., Schwartzentruber, J., Letourneau, L., et al. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-0998-0 · Cited by 1,028
Roles of the EZH2 histone methyltransferase in cancer epigenetics
Simon, J. A., & Lange, C. A. (2008) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2008.07.010 · Cited by 880
Sneeringer, C. J., Scott, M. P., Kuntz, K. W., Knutson, S. K., Pollock, R. M., Richon, V. M., & Copeland, R. A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1012525107 · Cited by 719
Yap, D., Chu, J., Berg, T., Schapira, M., Cheng, S., Moradian, A., Morin, R. D., Mungall, A. J. J., Meissner, B., Boyle, M., et al. (2010) · Blood · doi:10.1182/blood-2010-11-321208 · Cited by 633
A Novel Mammalian Flavin-dependent Histone Demethylase
Karytinos, A., Forneris, F., Profumo, A., Ciossani, G., Battaglioli, E., Binda, C., & Mattevi, A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.003087 · Cited by 274
Flagged first, then by citations
Cited by
Sorted by citations
Items 701–800 of 999
Mechanisms of epigenetic remodelling during preimplantation development
Ross, P. J., & Cánovas, S. (2015) · Reproduction Fertility and Development · doi:10.1071/rd15365 · Cited by 21
Newhart, A., Rafalska-Metcalf, I. U., Yang, T., Joo, L. M., Powers, S. L., Kossenkov, A. V., Lopez-Jones, M., Singer, R. H., Showe, L. C., Skordalakes, E., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.473181 · Cited by 21
Brown, Z. Z., Müller, M. M., Kong, H. E., Lewis, P. W., & Muir, T. W. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201500085 · Cited by 17
Self-citationThe Emerging Molecular Foundations of Pediatric Brain Tumors
Huse, J. T., & Rosenblum, M. K. (2015) · Journal of Child Neurology · doi:10.1177/0883073815579709 · Cited by 19
A Rare High-Grade Glioma with a Histone H3 K27M Mutation in the Hypothalamus of an Adult Patient
He, P., Chen, W., Qiu, X. X., Xi, Y. B., Guan, H., & Xia, J. (2019) · World Neurosurgery · doi:10.1016/j.wneu.2019.04.172 · Cited by 18
Zhao, Y., Guan, Y., Zhao, F., Yu, T., Zhang, S., Zhang, Y., Duan, Y., & Zhou, X. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114144 · Cited by 19
Albini, S., Zakharova, V., & Ait‐Si‐Ali, S. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-814879-2.00003-0 · Cited by 22
Cottone, L., Ligammari, L., Lee, H., Knowles, H. J., Henderson, S. R., Bianco, S., Davies, C., Strauss, S. J., Amary, F. M., Leite, A. P., et al. (2022) · Cell Death and Differentiation · doi:10.1038/s41418-022-01031-x · Cited by 19
Wang, D., Yan, K. H., Yu, H., Li, H., Zhou, W., Hong, Y., Guo, S., Wang, Y., Xu, C., Pan, C., et al. (2023) · Cancer Research · doi:10.1158/0008-5472.can-23-0394 · Cited by 18
Casillo, S. M., Gatesman, T. A., Chilukuri, A. S. S., Varadharajan, S., Johnson, B. J., Premkumar, D. R., Jane, E. P., Plute, T. J., Koncar, R. F., Stanton, A.-C. J., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.113557 · Cited by 18
Aberrant DNA repair reveals a vulnerability in histone H3.3-mutant brain tumors
Giacomini, G., Piquet, S., Chevallier, O., Dabin, J., Bai, S., Kim, B., Siddaway, R., Raught, B., Coyaud, É., Shan, C., et al. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkad1257 · Cited by 18
Kim, H., Lebeau, B., Papadopoli, D. J., Jovanović, P., Russo, M. D. S. T., Avizonis, D. Z., Morita, M., Afzali, F., Ursini‐Siegel, J., Postovit, L.-M. M., et al. (2024) · iScience · doi:10.1016/j.isci.2024.109188 · Cited by 17
Sangatsuda, Y., Miura, F., Araki, H., Mizoguchi, M., Hata, N., Kuga, D., Hatae, R., Akagi, Y., Amemiya, T., Fujioka, Y., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-73116-x · Cited by 18
Causes, effects, and clinical implications of perturbed patterns within the cancer epigenome
Oleksiewicz, U., & Machnik, M. (2020) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2020.12.014 · Cited by 18
Proteins in DNA methylation and their role in neural stem cell proliferation and differentiation
Sun, J., Yang, J., Miao, X., Loh, H. H., Pei, D., & Zheng, H. (2021) · Cell Regeneration · doi:10.1186/s13619-020-00070-4 · Cited by 19
Hohm, A., Karremann, M., Gielen, G. H., Pietsch, T., Warmuth‐Metz, M., Vandergrift, L. A., Bison, B., Stock, A., Hoffmann, M., Pham, M., et al. (2021) · Clinical Neuroradiology · doi:10.1007/s00062-021-01120-3 · Cited by 18
Yu, G., Zhang, Y., Gupta, V., Zhang, J., MacCarthy, T., Duan, Z., & Scharff, M. D. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2114743118 · Cited by 18
Characterization of H3.3K36M as a tool to study H3K36 methylation in cancer cells
Sankaran, S. M., & Gozani, O. (2017) · Epigenetics · doi:10.1080/15592294.2017.1377870 · Cited by 17
Molecular Biomarkers of Brain and Spinal Cord Astrocytomas
Коновалов, Н. А., Asyutin, D. S., Shayhaev, E. G., Kaprovoy, S., & Тimonin, S. Y. (2019) · Acta Naturae · doi:10.32607/20758251-2019-11-2-17-27 · Cited by 18
Deligne, C., Tourbez, A., Bénard, F., Meyer, S., Curt, A., Gianesello, M., Hamadou, M., Clavier, L., Coquet, C., Bocquet, C., et al. (2025) · Neuro-Oncology · doi:10.1093/neuonc/noaf007 · Cited by 17
Zune, A. L. D., Olwal, C. O., Tapela, K., Owoicho, O., Nganyewo, N. N., Lyko, F., & Paemka, L. (2021) · Cancers · doi:10.3390/cancers13236051 · Cited by 16
De novo methylation of histone H3K23 by the methyltransferases EHMT1/GLP and EHMT2/G9a
Vinson, D. A., Stephens, K., O’Meally, R. N., Bhat, S., Dancy, B. C. R., Cole, R. N., Yegnasubramanian, S., & Taverna, S. D. (2022) · Epigenetics & Chromatin · doi:10.1186/s13072-022-00468-1 · Cited by 18
Epigenetic and Metabolic Changes in Diffuse Intrinsic Pontine Glioma
Park, J., & Chung, C. (2023) · Brain Tumor Research and Treatment · doi:10.14791/btrt.2023.0011 · Cited by 18
Gliomas: a reflection of temporal gliogenic principles
Sojka, C., & Sloan, S. A. (2024) · Communications Biology · doi:10.1038/s42003-024-05833-2 · Cited by 18
Guo, G., Zhang, Z., Zhang, J., Wang, D., Xu, S., Liu, G., Gao, Y., Mei, J., Yan, Z., Ruijiao, Z., et al. (2024) · Cancer Immunology Immunotherapy · doi:10.1007/s00262-024-03774-7 · Cited by 18
Molecular biomarkers in pediatric glial tumors
Fontebasso, A. M., Béchet, D., & Jabado, N. (2013) · Current Opinion in Oncology · doi:10.1097/cco.0000000000000007 · Cited by 17
Biophysical characterization of histone H3.3 K27M point mutation
Hetey, S., Boros-Oláh, B., Kuik-Rózsa, T., Li, Q., Karányi, Z., Szabó, Z., Roszik, J., Szalóki, N., Vámosi, G., Tóth, K., et al. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.06.133 · Cited by 17
Tsvankin, V., Hashizume, R., Katagi, H., Herndon, J. E., Lascola, C. D., Venkatraman, T. N., Picard, D. J., Burrus, B., Becher, O. J., & Thompson, E. M. (2019) · Neurosurgery · doi:10.1093/neuros/nyz212 · Cited by 17
Self-citationVaughan, R. M., Kupai, A., Foley, C. A., Sagum, C. A., Tibben, B. M., Eden, H. E., Tiedemann, R. L., Berryhill, C. A., Patel, V., Shaw, K. M., et al. (2020) · Epigenetics & Chromatin · doi:10.1186/s13072-020-00366-4 · Cited by 15
Zhao, Y., Jiang, F., Wang, Q., Wang, B., Han, Y., Yang, J., Wang, J., Wang, K., Ao, J., Guo, X., et al. (2020) · Journal of Nanobiotechnology · doi:10.1186/s12951-020-00729-9 · Cited by 17
Yao, K., Liu, H., Yin, J., Yuan, J., & Tao, H. (2021) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-021-02054-x · Cited by 16
Acidic patch histone mutations and their effects on nucleosome remodeling
Dao, H. T., & Pham, L. T. D. (2022) · Biochemical Society Transactions · doi:10.1042/bst20210773 · Cited by 16
Oncohistone Mutations Occur at Functional Sites of Regulatory ADP-Ribosylation
Huang, D., Camacho, C. V., Martire, S., Nagari, A., Setlem, R., Gong, X., Edwards, A. D., Chiu, S.-P., Banaszynski, L. A., & Kraus, W. L. (2022) · Cancer Research · doi:10.1158/0008-5472.can-22-0742 · Cited by 16
Self-citationThangaiah, J. J., Westling, B. E., Roden, A. C., Giannini, C., Tetzlaff, M. T., Cho, W. C., & Folpe, A. L. (2022) · Annals of Diagnostic Pathology · doi:10.1016/j.anndiagpath.2022.151967 · Cited by 15
Advances on Epigenetic Drugs for Pediatric Brain Tumors
Skouras, P., Markouli, M., Strepkos, D., & Piperi, C. (2022) · Current Neuropharmacology · doi:10.2174/1570159x20666220922150456 · Cited by 16
Photo-Cross-Linking To Delineate Epigenetic Interactome
Zhang, Z., Lin, J., Liu, Z., Tian, G., Li, X., Jing, Y., Li, X., & Li, X. (2022) · Journal of the American Chemical Society · doi:10.1021/jacs.2c06135 · Cited by 17
Yang, Y. P., Wang, S., Wang, Z., Gao, R., & Lee, J. (2023) · Epigenetics · doi:10.1080/15592294.2023.2211362 · Cited by 17
Diverse modes of regulating methyltransferase activity by histone ubiquitination
Fields, J. K., Hicks, C. W., & Wolberger, C. (2023) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2023.102649 · Cited by 16
Histone modifications in embryo implantation and placentation: insights from mouse models
Bi, S., Tu, Z., Chen, D., & Zhang, S. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1229862 · Cited by 16
Feierman, E. R., Louzon, S., Prescott, N. A., Biaco, T., Gao, Q., Qiu, Q., Choi, K., Palozola, K. C., Voss, A. J., Mehta, S. D., et al. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.06.025 · Cited by 16
DNAJC12 downregulation induces neuroblastoma progression via increased histone H4K5 lactylation
Yang, Y., Wen, J., Lou, S., Han, Y., Pan, Y., Zhong, Y., He, Q., Zhang, Y., Mo, X., Ma, J., et al. (2024) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjae056 · Cited by 16
Next-generation molecular genetics of brain tumours
Suvà, M. L., & Louis, D. N. (2013) · Current Opinion in Neurology · doi:10.1097/wco.0000000000000027 · Cited by 16
Controversies in Oral and Maxillofacial Pathology
Peacock, Z. S. (2017) · Oral and Maxillofacial Surgery Clinics of North America · doi:10.1016/j.coms.2017.06.005 · Cited by 16
Chromatin remodeling defects in pediatric brain tumors
Κλώνου, Α., Spiliotakopoulou, D., Themistocleous, M. S., Piperi, C., & Papavassiliou, A. G. (2018) · Annals of Translational Medicine · doi:10.21037/atm.2018.04.08 · Cited by 16
Redistribution of EZH2 promotes malignant phenotypes by rewiring developmental programmes
Mortimer, T., Wainwright, E. N., Patel, H., Siow, B. M., Jaunmuktane, Z., Brandner, S., & Scaffidi, P. (2019) · EMBO Reports · doi:10.15252/embr.201948155 · Cited by 15
Chromatin modification and epigenetic control in functional nerve regeneration
Berry, K., & Lu, Q. R. (2019) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2019.07.009 · Cited by 17
Sikder, S., Kaypee, S., & Kundu, T. K. (2020) · Journal of Biosciences · doi:10.1007/s12038-019-9974-3 · Cited by 17
Histone H3K27M Mutation in Brain Tumors
El-Hashash, A. H. K. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-981-15-8104-5_3 · Cited by 18
Advanced Pediatric Diffuse Pontine Glioma Murine Models Pave the Way towards Precision Medicine
Chen, Z., Peng, P., Zhang, X., Mania-Farnell, B. L., Xi, G., & Wan, F. (2021) · Cancers · doi:10.3390/cancers13051114 · Cited by 19
Li, X., Nai, S., Ding, Y., Geng, Q., Zhu, B., Yu, K., Zhu, W., Dong, M., Su, X., Xu, X., et al. (2017) · Cell Cycle · doi:10.1080/15384101.2017.1363942 · Cited by 18
Structural assembly of Polycomb group protein and Insight of EZH2 in cancer progression
Gautam, N., Kaur, M., & Kaur, S. (2020) · Journal of Cancer Research and Therapeutics · doi:10.4103/jcrt.jcrt_1090_19 · Cited by 16
A Role for Monomethylation of Histone H3-K27 in Gene Activity inDrosophila
Wang, L., Joshi, P., Miller, E., Higgins, L., Slattery, M. G., & Simon, J. A. (2017) · Genetics · doi:10.1534/genetics.117.300585 · Cited by 15
Gene of the month: H3F3A and H3F3B
Aldera, A. P., & Govender, D. (2021) · Journal of Clinical Pathology · doi:10.1136/jclinpath-2021-207751 · Cited by 15
The epigenetic dysfunction underlying malignant glioma pathogenesis
Dharmaiah, S., & Huse, J. T. (2022) · Laboratory Investigation · doi:10.1038/s41374-022-00741-7 · Cited by 17
Huchedé, P., Leblond, P., & Castets, M. (2022) · Biomedicines · doi:10.3390/biomedicines10061311 · Cited by 19
Radiotherapy and radio‐sensitization in H3K27M ‐mutated diffuse midline gliomas
Liu, C., Kuang, S., Wu, L., Cheng, Q., Gong, X., Wu, J., & Zhang, L. (2023) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.14225 · Cited by 16
Contribution of histone variants to aneuploidy: a cancer perspective
Ragusa, D., & Vagnarelli, P. (2023) · Frontiers in Genetics · doi:10.3389/fgene.2023.1290903 · Cited by 16
Therapeutically targeting the unique disease landscape of pediatric high-grade gliomas
Fernando, D., Ahmed, A. U., & Williams, B. R. G. (2024) · Frontiers in Oncology · doi:10.3389/fonc.2024.1347694 · Cited by 15
Myeloid cells as potential targets for immunotherapy in pediatric gliomas
Frederico, S. C., Sharma, N., Darling, C., Taori, S., Dubinsky, A. C., Zhang, X., Raphael, I., & Kohanbash, G. (2024) · Frontiers in Pediatrics · doi:10.3389/fped.2024.1346493 · Cited by 14
Targeting DNA Methylation Machinery in Pediatric Solid Tumors
Cristalli, C., & Scotlandi, K. (2024) · Cells · doi:10.3390/cells13141209 · Cited by 14
Detecting the H3F3A mutant allele found in high-grade pediatric glioma by real-time PCR
Zhang, R., Han, J., Daniels, D. J., Huang, H., & Zhang, Z. (2015) · Journal of Neuro-Oncology · doi:10.1007/s11060-015-1936-5 · Cited by 15
Zou, Y., Meng, L., He, Z., Hu, C., Shan, M., Wang, D., & Yu, X. (2019) · Oncology Letters · doi:10.3892/ol.2019.10804 · Cited by 15
Sekimata, K., Sato, T., & Sakai, N. (2020) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.c19-00882 · Cited by 15
Molecular-Targeted Therapy for Childhood Brain Tumors: A Moving Target
Packer, R. J., & Kilburn, L. B. (2020) · Journal of Child Neurology · doi:10.1177/0883073820931635 · Cited by 15
Janus Bioparticles: Asymmetric Nucleosomes and Their Preparation Using Chemical Biology Approaches
Mitchener, M. M., & Muir, T. W. (2021) · Accounts of Chemical Research · doi:10.1021/acs.accounts.1c00313 · Cited by 15
Self-citationTargets of histone H3 lysine 9 methyltransferases
Levinsky, A. J., McEdwards, G., Sethna, N. S., & Currie, M. A. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.1026406 · Cited by 15
Emerging Interplay of Genetics and Epigenetics in Gliomas: A New Hope for Targeted Therapy
Yong, R. L. M., & Tsankova, N. M. (2014) · Seminars in Pediatric Neurology · doi:10.1016/j.spen.2014.12.004 · Cited by 16
Genome-Wide Identification, Evolutionary, and Expression Analyses of Histone H3 Variants in Plants
Cui, J., Zhang, Z., Shao, Y., Zhang, K., Leng, P., & Liang, Z. (2015) · BioMed Research International · doi:10.1155/2015/341598 · Cited by 15
Klocko, A. D., Uesaka, M., Ormsby, T., Rountree, M. R., Wiles, E. T., Adhvaryu, K. K., Honda, S., & Selker, E. U. (2018) · Genetics · doi:10.1534/genetics.118.301711 · Cited by 15
The 100 most-cited articles about diffuse intrinsic pontine glioma: a bibliometric analysis
Lu, V. M., Power, E. A., Kerezoudis, P., & Daniels, D. J. (2019) · Child s Nervous System · doi:10.1007/s00381-019-04254-5 · Cited by 15
Histone Variant H3.3 Mutations in Defining the Chromatin Function in Mammals
Trovato, M., Patil, V., Gehre, M., & Noh, K. (2020) · Cells · doi:10.3390/cells9122716 · Cited by 15
Relier, S., Amalric, A., Attina, A., Koumare, I. B., Rigau, V., Burel‐Vandenbos, F., Fontaine, D., Baroncini, M., Hugnot, J., Duffau, H., et al. (2022) · Analytical Chemistry · doi:10.1021/acs.analchem.2c01526 · Cited by 16
Shan, C., Kim, J.-K., Wang, J., Bao, K., Sun, Y., Chen, H., Yue, J., Stirpe, A., Zhang, Z., Lü, C., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109137 · Cited by 14
Histone H2B Mutations in Cancer
Wan, Y. C. E., & Chan, K. M. (2021) · Biomedicines · doi:10.3390/biomedicines9060694 · Cited by 14
Know when to fold ‘em: Polycomb complexes in oncogenic 3D genome regulation
Doyle, E. J., Morey, L., & Conway, E. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.986319 · Cited by 16
Identification of nonhistone substrates of the lysine methyltransferase PRDM9
Hanquier, J. N., Sanders, K., Berryhill, C. A., Sahoo, F. K., Hudmon, A., Vilseck, J. Z., & Cornett, E. M. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104651 · Cited by 14
Epigenetic reprogramming in pediatric gliomas: from molecular mechanisms to therapeutic implications
Haase, S., Carney, S. V., Varela, M. L., Mukherji, D., Zhu, Z., Li, Y., Núñez, F. J., Lowenstein, P. R., & Castro, M. G. (2024) · Trends in cancer · doi:10.1016/j.trecan.2024.09.007 · Cited by 14
Origins and clinical relevance of proteoforms in pediatric malignancies
Lorentzian, A. C., Uzozie, A. C., & Lange, P. F. (2019) · Expert Review of Proteomics · doi:10.1080/14789450.2019.1575206 · Cited by 14
Sanders, L., Cheney, A. R., Seninge, L., van den Bout, A., Chen, M., Beale, H. C., Kephart, E. T., Pfeil, J., Learned, K., Lyle, A. G., et al. (2020) · GigaScience · doi:10.1093/gigascience/giaa136 · Cited by 14
Analytical strategies used to identify the readers of histone modifications: A review
Wang, Y., Han, Y., Fan, E., & Zhang, K. (2015) · Analytica Chimica Acta · doi:10.1016/j.aca.2015.06.049 · Cited by 14
Increased chromatin plasticity supports enhanced metastatic potential of mouse melanoma cells
Maizels, Y., Elbaz, A., Hernandez‐Vicens, R., Sandrusy, O., Rosenberg, A., & Gerlitz, G. (2017) · Experimental Cell Research · doi:10.1016/j.yexcr.2017.05.025 · Cited by 15
Lien, H., Jeng, Y., Jhuang, Y., & Yuan, R. (2018) · PLoS ONE · doi:10.1371/journal.pone.0206261 · Cited by 14
Quénet, D. (2017) · International review of cytology · doi:10.1016/bs.ircmb.2017.07.006 · Cited by 18
Synthesis of Oriented Hexasomes and Asymmetric Nucleosomes Using a Template Editing Process
Dao, H. T., Liu, H., Mashtalir, N., Kadoch, C., & Muir, T. W. (2022) · Journal of the American Chemical Society · doi:10.1021/jacs.1c12420 · Cited by 13
Self-citationH3K27M Mutation Doesn’t Mean Worse Prognosis in Old Patients
Hu, X. M., Nie, X. Y., Xu, K., Wang, Y., Tang, F. R., Du, Z. G., & Xiong, J. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.912166 · Cited by 14
Investigating pathological epigenetic aberrations by epi-proteomics
Robusti, G., Vai, A., Bonaldi, T., & Noberini, R. (2022) · Clinical Epigenetics · doi:10.1186/s13148-022-01371-y · Cited by 13
Developing H3K27M mutant selective radiosensitization strategies in diffuse intrinsic pontine glioma
Parsels, L. A., Wahl, D. R., Koschmann, C. J., Morgan, M. A., & Zhang, Q. (2023) · Neoplasia · doi:10.1016/j.neo.2023.100881 · Cited by 12
Methylation of lysine 36 on histone H3 is required to control transposon activities in somatic cells
Lindehell, H., Schwartz, Y. B., & Larsson, J. (2023) · Life Science Alliance · doi:10.26508/lsa.202201832 · Cited by 15
The role of histone H3 lysine demethylases in glioblastoma
Young, D. L., Guha, C., & Sidoli, S. (2023) · Cancer and Metastasis Reviews · doi:10.1007/s10555-023-10114-1 · Cited by 13
Leszczyńska, K. B., Freitas-Huhtamäki, A., Jayaprakash, C., Dźwigońska, M., Vitorino, F. N. D. L., Horth, C., Wojnicki, K., Gielniewski, B., Szadkowska, P., Kaza, B., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.113707 · Cited by 13
Self-citationCrosstalk within and beyond the Polycomb repressive system
Shi, T., Sugishita, H., & Gotoh, Y. (2024) · The Journal of Cell Biology · doi:10.1083/jcb.202311021 · Cited by 12
EZHIP’s role in diffuse midline glioma: echoes of oncohistones?
Cassim, A., Dun, M. D., Gallego‐Ortega, D., & Valdés‐Mora, F. (2024) · Trends in cancer · doi:10.1016/j.trecan.2024.09.002 · Cited by 13
The “Ins and Outs and What-Abouts” of H2A.Z: A tribute to C. David Allis
Diegmüller, F., Leers, J., & Hake, S. B. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.108154 · Cited by 19
Lee, M. P. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.00794 · Cited by 13
Epigenetic mechanisms in paediatric brain tumours: regulators lose control
Badodi, S., & Marino, S. (2022) · Biochemical Society Transactions · doi:10.1042/bst20201227 · Cited by 13
Groves, A. P., Clymer, J. R., & Filbin, M. G. (2022) · Pharmaceuticals · doi:10.3390/ph15060665 · Cited by 12
The Molecular Landscape of Pediatric Brain Tumors in the Next-Generation Sequencing Era
Firme, M. R., & Marra, M. A. (2014) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-014-0474-4 · Cited by 13
Wells, E. M., Kambhampati, M., Damsker, J. M., Gordish‐Dressman, H., Yadavilli, S., Becher, O. J., Gittens, J., Stampar, M., Packer, R. J., & Nazarian, J. (2016) · Oncotarget · doi:10.18632/oncotarget.14070 · Cited by 13
Self-citationGarcia-Fabiani, M. B., Comba, A., Kadiyala, P., Haase, S., Núñez, F. J., Altshuler, D. B., Lowenstein, P. R., & Castro, M. G. (2019) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2019.05.023 · Cited by 13
Pediatric high-grade glioma: A heterogeneous group of neoplasms with different molecular drivers
Giangaspero, F., Gianno, F., Antonelli, M., Ferretti, E., Massimino, M., & Arcella, A. (2018) · Glioma · doi:10.4103/glioma.glioma_27_18 · Cited by 13
Metadata
- Authors
- Lewis, P. W., Müller, M. M., Koletsky, M. S., Cordero, F., Lin, S., Banaszynski, L. A., Garcia, B. A., Muir, T. W., Becher, O. J., & Allis, C. D.
- Affiliations
- Rockefeller University (US)
- Princeton University (US)
- Duke University (US)
- University of Pennsylvania (US)
- Corresponding author
- Allis, C. David
- ORCID
- Venue
- Science
- Published
- 2013-05-17
- Volume
- 340
- Issue
- 6134
- Pages
- 857-861
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC3951439
- OpenAlex
- W1995105508
- Cited by
- 1,345
- References
- 14
- Citations by year
- 2026: 73 · 2025: 82 · 2024: 103 · 2023: 106 · 2022: 103 · 2021: 118 · 2020: 146 · 2019: 112 · 2018: 84 · 2017: 102 · 2016: 90 · 2015: 95 · 2014: 87 · 2013: 40
- FWCI
- 51.21
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Research Portal (King's College London) (submittedVersion)
- Funders
- National Institutes of Health (DP2OD007447)
- National Institute of Mental Health (P50MH096890)
- National Institute of General Medical Sciences (GM040922, R01GM107047, R01GM040922)
- 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 › Molecular Biology › Chromatin Remodeling and Cancer
- Keywords
- pediatric glioblastoma, diffuse intrinsic pontine glioma, H3K27M mutation, histone H3.3, H3K27me3, polycomb repressive complex 2, EZH2, histone methylation, gain-of-function mutations, epigenetic regulation
- MeSH terms
- Enhancer of Zeste Homolog 2 Protein, Animals, Brain Neoplasms, Child, Glioblastoma, Histones, Humans, Lysine, Methionine, Methylation, Transgenes, Amino Acid Substitution, Mutation, Missense, Epigenesis, Genetic, Mice, HEK293 Cells, Polycomb Repressive Complex 2
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
