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 501–600 of 999
New twists to the ALTernative endings at telomeres
Bhargava, R., Lynskey, M. L., & O’Sullivan, R. J. (2022) · DNA repair · doi:10.1016/j.dnarep.2022.103342 · Cited by 37
Not just a writer: PRC2 as a chromatin reader
Uckelmann, M., & Davidovich, C. (2021) · Biochemical Society Transactions · doi:10.1042/bst20200728 · Cited by 40
Bočkaj, I., Martini, T. E. I., Magalhães, E. S. D. C., Bakker, P. L., Boer, T. M.-D., Armandari, I., Meuleman, S. L., Mondria, M. T., Stok, C., Kok, Y. P., et al. (2021) · PLoS Genetics · doi:10.1371/journal.pgen.1009868 · Cited by 35
Multistate structures of the MLL1-WRAD complex bound to H2B-ubiquitinated nucleosome
Rahman, S., Hoffmann, N. A., Worden, E. J., Smith, M. L., Namitz, K. E. W., Knutson, B. A., Cosgrove, M. S., & Wolberger, C. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2205691119 · Cited by 34
Targeting Menin disrupts the KMT2A/B and polycomb balance to paradoxically activate bivalent genes
Sparbier, C. E., Gillespie, A., Gomez, J., Kumari, N., Motazedian, A., Chan, K. L., Bell, C. C., Gilan, O., Chan, Y.-C., Popp, S., et al. (2023) · Nature Cell Biology · doi:10.1038/s41556-022-01056-x · Cited by 38
HIRA vs. DAXX: the two axes shaping the histone H3.3 landscape
Choi, J., Kim, T., & Cho, E. (2024) · Experimental & Molecular Medicine · doi:10.1038/s12276-023-01145-3 · Cited by 41
Pediatric CNS tumors and 2021 WHO classification: what do oncologists need from pathologists?
d’Amati, A., Bargiacchi, L., Rossi, S., Carai, A., Bertero, L., Barresi, V., Errico, M. E., Buccoliero, A. M., Asioli, S., Marucci, G., et al. (2024) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2024.1268038 · Cited by 39
New insights and challenges in mismatch repair: Getting over the chromatin hurdle
Li, G. (2014) · DNA repair · doi:10.1016/j.dnarep.2014.03.027 · Cited by 38
Examining the impact of gene variants on histone lysine methylation
Rechem, C. V., & Whetstine, J. R. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.05.014 · Cited by 37
Mozzetta, C., Pontis, J., & Ait‐Si‐Ali, S. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6116 · Cited by 37
Fellenberg, J., Sähr, H., Mancarella, D., Plass, C., Lindroth, A. M., Westhauser, F., Lehner, B., & Ewerbeck, V. (2019) · Cancer Letters · doi:10.1016/j.canlet.2019.02.001 · Cited by 38
Wang, X., Zhou, W., Li, X., Ren, J. T., Ji, G., Du, J., Tian, W., Liu, Q., & Hao, A. (2020) · Journal of Translational Medicine · doi:10.1186/s12967-020-02359-z · Cited by 38
Palmisciano, P., Ahmadieh, T. Y. E., Haider, A. S., Bin-Alamer, O., Robertson, F. C., Plitt, A. R., Aoun, S. G., Yu, K. K. H., Cohen‐Gadol, A., Moss, N. S., et al. (2021) · Journal of Neuro-Oncology · doi:10.1007/s11060-021-03898-1 · Cited by 36
Pediatric High Grade Glioma Classification Criteria and Molecular Features of a Case Series
Buccoliero, A. M., Giunti, L., Moscardi, S., Castiglione, F., Provenzano, A., Sardi, I., Scagnet, M., Genitori, L., & Caporalini, C. (2022) · Genes · doi:10.3390/genes13040624 · Cited by 41
Histone H3 Mutations in Pediatric Brain TumorsPreprint
Liu, X., McEachron, T. A., Schwartzentruber, J., & Wu, G. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a018689 · Cited by 37
Andrade, A. F., Annett, A., Karimi, E., Topouza, D. G., Rezanejad, M., Liu, Y., McNicholas, M., Santiago, E. G. G., Llivichuzhca-Loja, D., Gehlhaar, A., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-52096-w · Cited by 40
Functional roles of enhancer of zeste homolog 2 in gliomas
Yin, Y., Qiu, S., & Peng, Y. (2015) · Gene · doi:10.1016/j.gene.2015.09.080 · Cited by 35
Hemispherical Pediatric High-Grade Glioma: Molecular Basis and Therapeutic Opportunities
Haase, S., Núñez, F. M., Gauss, J. C., Thompson, S., Brumley, E. K., Lowenstein, P. R., & Castro, M. G. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21249654 · Cited by 35
Leszczyńska, K. B., Jayaprakash, C., Kaminska, B., & Mieczkowski, J. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2021.742561 · Cited by 35
Maeda, S., Ohka, F., Okuno, Y., Aoki, K., Motomura, K., Takeuchi, K., Hironao, K., Yanagisawa, N., Sato, S., Yamaguchi, J., et al. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-0882-4 · Cited by 34
Clinical and Genomic Characteristics of Adult Diffuse Midline Glioma
Park, C., Kim, T. M., Bae, J. M., Yun, H., Kim, J., Choi, S. H., Lee, S., Lee, J. H., Park, S., & Park, C. (2020) · Cancer Research and Treatment · doi:10.4143/crt.2020.694 · Cited by 34
Polycomb‐mediated gene regulation in human brain development and neurodevelopmental disorders
Bölicke, N., & Albert, M. (2022) · Developmental Neurobiology · doi:10.1002/dneu.22876 · Cited by 39
Antisense oligonucleotide therapy for H3.3K27M diffuse midline glioma
Zhang, Q., Yang, L., Liu, Y. H., Wilkinson, J. E., & Krainer, A. R. (2023) · Science Translational Medicine · doi:10.1126/scitranslmed.add8280 · Cited by 32
Developmental origins shape the paediatric cancer genome
Chen, X., Yang, W., Roberts, C. W. M., & Zhang, J. (2024) · Nature reviews. Cancer · doi:10.1038/s41568-024-00684-9 · Cited by 49
Han, H. J., Jain, P., & Resnick, A. C. (2017) · Bone · doi:10.1016/j.bone.2017.08.001 · Cited by 37
An, S., Camarillo, J. M., Huang, T. Y.-T., Li, D. D., Morris, J. A., Zoltek, M., Qi, J., Behbahani, M., Kambhampati, M., Kelleher, N. L., et al. (2020) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-020-01773-x · Cited by 34
Zaghloul, M. S., Nasr, A. M., Tolba, M., Refaat, A., Youssef, A. A., Mosaab, A., Enayet, A., Arafa, O., Maher, E., & Eldebawy, E. (2022) · International Journal of Radiation Oncology*Biology*Physics · doi:10.1016/j.ijrobp.2022.01.054 · Cited by 34
Patel, A. J., Warda, S., Mååg, J. L. V., Misra, R., Miranda-Román, M. A., Pachai, M. R., Lee, C. J., Li, D., Wang, N., Bayshtok, G., et al. (2022) · Cancer Discovery · doi:10.1158/2159-8290.cd-21-1671 · Cited by 36
McNicholas, M., Cola, A. D., Bashardanesh, Z., Foss, A., Lloyd, C. B., Hébert, S., Faury, D., Andrade, A. F., Jabado, N., Kleinman, C. L., et al. (2023) · Cancer Discovery · doi:10.1158/2159-8290.cd-23-0004 · Cited by 32
Shaping Chromatin in the Nucleus: The Bricks and the ArchitectsPreprint
Sitbon, D., Podsypanina, K., Yadav, T., & Almouzni, G. (2017) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2017.82.033753 · Cited by 37
Diffuse midline glioma invasion and metastasis rely on cell-autonomous signaling
Bruschi, M., Midjek, L., Ajlil, Y., Vairy, S., Lancien, M., Ghermaoui, S., Kergrohen, T., Verreault, M., Idbaïh, A., de Biagi, C. A. O., et al. (2023) · Neuro-Oncology · doi:10.1093/neuonc/noad161 · Cited by 36
Liquid Biopsy for Glioma Using Cell-Free DNA in Cerebrospinal Fluid
Otsuji, R., Fujioka, Y., Hata, N., Kuga, D., Hatae, R., Sangatsuda, Y., Nakamizo, A., Mizoguchi, M., & Yoshimoto, K. (2024) · Cancers · doi:10.3390/cancers16051009 · Cited by 37
Misuraca, K. L., Barton, K. L., Chung, A., Diaz, A. K., Conway, S. J., Corcoran, D. L., Baker, S. J., & Becher, O. J. (2014) · Acta Neuropathologica Communications · doi:10.1186/s40478-014-0134-6 · Cited by 33
Self-citationChromatin Dynamics in Vivo: A Game of Musical Chairs
Melters, D. P., Nye, J., Zhao, H., & Dalal, Y. (2015) · Genes · doi:10.3390/genes6030751 · Cited by 36
Sundriyal, S., Chen, P. B., Lubin, A., Lueg, G. A., Li, F., White, A. J. P., Malmquist, N. A., Vedadi, M., Scherf, A., & Fuchter, M. J. (2017) · MedChemComm · doi:10.1039/c7md00052a · Cited by 34
Kang, T. Z. E., Zhu, L., Du, Y., Ding, D., Zhu, X., Wan, Y. C. E., Liu, J., Ramakrishnan, S., Chan, L. L., Chan, S. Y., et al. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100374 · Cited by 33
DNA methylation and histone variants in aging and cancer
Mangelinck, A., & Mann, C. (2021) · International review of cytology · doi:10.1016/bs.ircmb.2021.06.002 · Cited by 35
Soshnev, A. A., Allis, C. D., Cesarman, E., & Melnick, A. M. (2021) · Cancer Research · doi:10.1158/0008-5472.can-21-2619 · Cited by 30
Self-citationTessadori, F., Duran, K. J., Knapp, K., Fellner, M., Smithson, S., Beleza‐Meireles, A., Elting, M. W., Waisfisz, Q., O’Donnell‐Luria, A., Nowak, C. B., et al. (2022) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2022.02.003 · Cited by 34
Taylor‐Papadimitriou, J., & Burchell, J. (2022) · Cells · doi:10.3390/cells11071113 · Cited by 34
Castro, L. N. G., Liu, I., & Filbin, M. G. (2022) · Neuro-Oncology · doi:10.1093/neuonc/noac211 · Cited by 34
Molecular characteristics of pediatric high-grade gliomas
Chamdine, O., & Gajjar, A. J. (2014) · CNS Oncology · doi:10.2217/cns.14.43 · Cited by 36
Deregulated proliferation and differentiation in brain tumors
Swartling, F. J., Čančer, M., Frantz, A., Weishaupt, H., & Persson, A. I. (2014) · Cell and Tissue Research · doi:10.1007/s00441-014-2046-y · Cited by 32
Pediatric high-grade astrocytomas: a distinct neuro-oncological paradigm
Gerges, N., Fontebasso, A. M., Albrecht, S., Faury, D., & Jabado, N. (2013) · Genome Medicine · doi:10.1186/gm470 · Cited by 33
Impact of H3K27 Demethylase Inhibitor GSKJ4 on NSCLC Cells Alone and in Combination with Metformin
WATARAI, H., Okada, M., Kuramoto, K., TAKEDA, H., SAKAKI, T., Suzuki, S., Seino, S., Oizumi, H., Sadahiro, M., & Kitanaka, C. (2016) · Anticancer Research · doi:10.21873/anticanres.11198 · Cited by 34
Jiao, F., Li, Z., He, C., Xu, W., Yang, G., Liu, T., Shen, H., Cai, J., Anastas, J. N., Mao, Y. Q., et al. (2020) · Science Advances · doi:10.1126/sciadv.aba2113 · Cited by 32
Huang, T., Piunti, A., Qi, J., Morgan, M. A., Bartom, E. T., Shilatifard, A., & Saratsis, A. M. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-01092-4 · Cited by 32
Molecular Mechanisms of Oncogenesis through the Lens of Nucleosomes and Histones
Espiritu, D., Gribkova, A. K., Gupta, S., Shaytan, A. К., & Panchenko, A. R. (2021) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.1c00694 · Cited by 31
A conserved BAH module within mammalian BAHD1 connects H3K27me3 to Polycomb gene silencing
Fan, H., Guo, Y., Tsai, Y., Storey, A. J., Kim, A., Gong, W., Edmondson, R. D., Mackintosh, S. G., Li, H., Byrum, S. D., et al. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab210 · Cited by 35
Pioneer factors in development and cancer
Sunkel, B. D., & Stanton, B. Z. (2021) · iScience · doi:10.1016/j.isci.2021.103132 · Cited by 32
Xin, D. E., Liao, Y., Rao, R., Ogurek, S., Sengupta, S., Xin, M., Bayat, A. E., Seibel, W. L., Graham, R. T., Koschmann, C. J., et al. (2023) · Neuro-Oncology · doi:10.1093/neuonc/noad222 · Cited by 30
Somatic alterations and dysregulation of epigenetic modifiers in cancers
Aumann, S., & Abdel-Wahab, O. I. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.08.004 · Cited by 31
Fellenberg, J., Sähr, H., Kunz, P., Zhao, Z., Liu, L., Tichy, D., & Herr, I. (2015) · Cancer Letters · doi:10.1016/j.canlet.2015.10.039 · Cited by 31
Compartmentalization of HP1 Proteins in Pluripotency Acquisition and Maintenance
Zaidan, N. Z., Walker, K. J., Brown, J. E., Schaffer, L. V., Scalf, M., Shortreed, M. R., Iyer, G., Smith, L. M., & Sridharan, R. (2018) · Stem Cell Reports · doi:10.1016/j.stemcr.2017.12.016 · Cited by 31
Epigenetic Reprogramming for Targeting IDH-Mutant Malignant Gliomas
Park, J., & Turcan, Ş. (2019) · Cancers · doi:10.3390/cancers11101616 · Cited by 33
H2A.Z's ‘social’ network: functional partners of an enigmatic histone variant
Kreienbaum, C., Paasche, L. W., & Hake, S. B. (2022) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2022.04.014 · Cited by 31
Common molecular features of H3K27M DMGs and PFA ependymomas map to hindbrain developmental pathways
Pun, M. J., Pratt, D. W., Nano, P. R., Joshi, P. K., Jiang, L., Englinger, B., Rao, A. U. K., Cieslik, M. P., Chinnaiyan, A. M., Aldape, K., et al. (2023) · Acta Neuropathologica Communications · doi:10.1186/s40478-023-01514-z · Cited by 31
The emerging role of NG2 in pediatric diffuse intrinsic pontine glioma
Yadavilli, S., Scafidi, J., Becher, O. J., Saratsis, A. M., Hiner, R. L., Kambhampati, M., Santi, M., MacDonald, T. J., Codispoti, K.-E., Magge, S. N., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.3716 · Cited by 30
Self-citationHistone H3.3 and cancer: A potential reader connection
Lan, F., & Shi, Y. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1418996111 · Cited by 32
Epigenetic regulation in medulloblastoma
Yi, J., & Wu, J. I. (2017) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2017.09.003 · Cited by 32
Poisoning the “histone code” in pediatric gliomagenesis
Lewis, P. W., & Allis, C. D. (2013) · Cell Cycle · doi:10.4161/cc.26356 · Cited by 30
Self-citationAn epigenetic therapy for diffuse intrinsic pontine gliomas
Ramaswamy, V., Remke, M., & Taylor, M. D. (2014) · Nature Medicine · doi:10.1038/nm.3769 · Cited by 30
Ishibashi, K., Inoue, T., Fukushima, H., Watanabe, Y., Iwai, Y., Sakamoto, H., Yamasaki, K., Hara, J., Shofuda, T., Kanematsu, D., et al. (2016) · Child s Nervous System · doi:10.1007/s00381-016-3161-8 · Cited by 30
Genetic Abnormalities, Clonal Evolution, and Cancer Stem Cells of Brain Tumors
Testa, U., Castelli, G., & Pelosi, E. (2018) · Medical Sciences · doi:10.3390/medsci6040085 · Cited by 33
Detection of H3K27M mutation in cases of brain stem subependymoma
Yao, K., Duan, Z., Wang, Y., Zhang, M., Fan, T., Wu, B., & Qi, X. (2018) · Human Pathology · doi:10.1016/j.humpath.2018.10.011 · Cited by 30
Wan, Y. C. E., Leung, T. C. S., Ding, D., Sun, X., Liu, J., Zhu, L., Kang, T. Z. E., Du, Y., Zhang, Y., Zhang, J., et al. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-0131-0 · Cited by 30
Pratt, D. W., Quezado, M., Abdullaev, Z., Hawes, D., Yang, F., Garton, H. J. L., Judkins, A. R., Mody, R. J., Chinnaiyan, A. M., Aldape, K., et al. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-00905-w · Cited by 31
Radio-Resistance and DNA Repair in Pediatric Diffuse Midline Gliomas
Pedersen, H., Schmiegelow, K., & Hamerlik, P. (2020) · Cancers · doi:10.3390/cancers12102813 · Cited by 29
Therapeutic targeting of prenatal pontine ID1 signaling in diffuse midline glioma
Messinger, D., Harris, M. K., Cummings, J. R., Thomas, C., Yang, T., Sweha, S. R., Woo, R. W. L., Siddaway, R., Burkert, M., Stallard, S., et al. (2022) · Neuro-Oncology · doi:10.1093/neuonc/noac141 · Cited by 33
CK2-mediated phosphorylation of SUZ12 promotes PRC2 function by stabilizing enzyme active site
Gong, L., Liu, X., Jiao, L., Yang, X., Lemoff, A. S., & Liu, X. (2022) · Nature Communications · doi:10.1038/s41467-022-34431-1 · Cited by 33
Ohhata, T., Matsumoto, M., Leeb, M., Shibata, S., Sakai, S., Kitagawa, K., Niida, H., Kitagawa, M., & Wutz, A. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.00561-15 · Cited by 28
Wu, R., Nie, Q., Tapper, E. E., Jerde, C. R., Dunlap, G. S., Shrestha, S., Elraiyah, T. A., Offer, S. M., & Diasio, R. B. (2016) · Cancer Research · doi:10.1158/0008-5472.can-16-1306 · Cited by 29
Targeting Epigenetic Pathways in the Treatment of Pediatric Diffuse (High Grade) Gliomas
Vanan, M., Underhill, D. A., & Eisenstat, D. D. (2017) · Neurotherapeutics · doi:10.1007/s13311-017-0514-2 · Cited by 29
Ogura, K., Hosoda, F., Nakamura, H., Hama, N., Totoki, Y., Yoshida, A., Ohashi, S., Rokutan, H., Takai, E., Yachida, S., et al. (2017) · Genes, Chromosomes and Cancer · doi:10.1002/gcc.22469 · Cited by 30
Bozkurt, S., Dagcinar, A., Tanrıkulu, B., Çomunoğlu, N., Meydan, B. C., Özek, M. M., & Öz, B. (2017) · Child s Nervous System · doi:10.1007/s00381-017-3633-5 · Cited by 30
Paediatric Gliomas: BRAF and Histone H3 as Biomarkers, Therapy and Perspective of Liquid Biopsies
Tan, J. Y., Wijesinghe, I. V. S., Kamarudin, M. N. A., & Parhar, I. S. (2021) · Cancers · doi:10.3390/cancers13040607 · Cited by 30
Polycomb repressive complex 2 in the driver’s seat of childhood and young adult brain tumours
Krug, B., Harutyunyan, A. S., Deshmukh, S., & Jabado, N. (2021) · Trends in Cell Biology · doi:10.1016/j.tcb.2021.05.006 · Cited by 29
Yan, J., Chen, Y., Patel, A. J., Warda, S., Lee, C. J., Nixon, B. G., Wong, E. W. P., Miranda-Román, M. A., Yang, N., Wang, Y., et al. (2022) · Journal of Clinical Investigation · doi:10.1172/jci153437 · Cited by 30
Targeting SWI/SNF ATPases in H3.3K27M diffuse intrinsic pontine gliomas
Mota, M., Sweha, S. R., Pun, M. J., Natarajan, S. K., Ding, Y., Chung, C., Hawes, D., Yang, F., Judkins, A. R., Samajdar, S., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2221175120 · Cited by 27
Epigenetic Pathways and Glioblastoma Treatment: Insights From Signaling Cascades
Allen, B. K., Stathias, V., Maloof, M. E., Vidović, D., Winterbottom, E. F., Capobianco, A. J., Clarke, J., Schürer, S. C., Robbins, D. J., & Ayad, N. G. (2014) · Journal of Cellular Biochemistry · doi:10.1002/jcb.24990 · Cited by 28
An Update on the Epigenetics of Glioblastomas
Ferreira, W. A. S., Pinheiro, D. D. R., da Costa, C. A., Rodrigues-Antunes, S., Araújo, M. D., Barros, M. B. L., Teixeira, A. C. D. S., Faro, T. A. S., Burbano, R. M. R., de Oliveira, E. H. C., et al. (2016) · Epigenomics · doi:10.2217/epi-2016-0040 · Cited by 29
Funato, K., & Tabar, V. S. (2017) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-030617-050143 · Cited by 30
Chromatin targeting drugs in cancer and immunityPreprint
Prinjha, R. K., & Tarakhovsky, A. (2013) · Genes & Development · doi:10.1101/gad.221895.113 · Cited by 29
Malignant brainstem tumors in children, excluding diffuse intrinsic pontine gliomas
Klimo, P. D., Nesvick, C. L., Broniscer, A., Orr, B. A., & Choudhri, A. F. (2015) · Journal of Neurosurgery Pediatrics · doi:10.3171/2015.6.peds15166 · Cited by 28
Polycomb Repressive Complex 2: Emerging Roles in the Central Nervous System
Liu, P., Xu, Y., Teng, Z., & Liu, C. (2017) · The Neuroscientist · doi:10.1177/1073858417747839 · Cited by 29
Extraskeletal osteosarcoma: MDM 2 and H3K27me3 analysis of 19 cases suggest disease heterogeneity
Makise, N., Sekimizu, M., Kubo, T., Wakai, S., WATANABE, S.-I. I., Kato, T., Kinoshita, T., Hiraoka, N., Fukayama, M., Kawai, A., et al. (2018) · Histopathology · doi:10.1111/his.13506 · Cited by 28
Mechanism of cancer: Oncohistones in action
Qiu, L., Hu, X., Jing, Q., Zeng, X., Chan, K. M., & Han, J. (2018) · Journal of genetics and genomics/Journal of Genetics and Genomics · doi:10.1016/j.jgg.2018.04.004 · Cited by 27
Diagnostic tools in the differential diagnosis of giant cell-rich lesions of bone at biopsy
Rehkämper, J., Steinestel, K., Jeiler, B., Elges, S., Hekeler, E., Huss, S., Sperveslage, J., Hardes, J., Streitbürger, A., Gosheger, G., et al. (2018) · Oncotarget · doi:10.18632/oncotarget.25725 · Cited by 28
Regeneration enhancers: A clue to reactivation of developmental genes
Suzuki, N., & Ochi, H. (2020) · Development Growth & Differentiation · doi:10.1111/dgd.12654 · Cited by 26
Turkalo, T. K., Maffia, A., Schabort, J. J., Regalado, S. G., Bhakta, M. S., Blanchette, M., Spierings, D. C. J., Lansdorp, P. M., & Hockemeyer, D. F. (2023) · Nature Communications · doi:10.1038/s41467-023-36294-6 · Cited by 30
Low-Grade Gliomas: Histological Subtypes, Molecular Mechanisms, and Treatment Strategies
Toader, C., Eva, L., Costea, D., Corlatescu, A.-D., Covache-Busuioc, R.-A., Bratu, B.-G., Glavan, L.-A., Costin, H. P., Popa, A. A., & Ciurea, A. V. (2023) · Brain Sciences · doi:10.3390/brainsci13121700 · Cited by 31
Ishi, Y., Takamiya, S., Seki, T., Yamazaki, K., Hida, K., Hatanaka, K. C., Ishida, Y., Oda, Y., Tanaka, S., & Yamaguchi, S. (2020) · Brain Tumor Pathology · doi:10.1007/s10014-020-00369-9 · Cited by 28
Pediatric Diffuse Midline Glioma H3K27-Altered: From Developmental Origins to Therapeutic Challenges
Mandorino, M., Maitra, A., Armenise, D., Baldelli, O. M., Miciaccia, M., Ferorelli, S., Perrone, M. G., & Scilimati, A. (2024) · Cancers · doi:10.3390/cancers16101814 · Cited by 28
Pediatric Cancer Epigenome and the Influence of Folate
Yiu, T. T., & Li, W. (2015) · Epigenomics · doi:10.2217/epi.15.42 · Cited by 27
Elucidating Combinatorial Chromatin States at Single-Nucleosome Resolution
Sadeh, R., Launer-Wachs, R., Wandel, H., Rahat, A., & Friedman, N. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.07.023 · Cited by 27
Lin, G., Zhou, Y., Li, M., & Fang, Y. (2017) · Science China Life Sciences · doi:10.1007/s11427-017-9162-1 · Cited by 27
Therapeutic targeting of transcriptional elongation in diffuse intrinsic pontine glioma
Katagi, H., Takata, N., Aoi, Y., Zhang, Y., Rendleman, E. J., Blyth, G. T., Eckerdt, F., Tomita, Y., Sasaki, T., Saratsis, A. M., et al. (2021) · Neuro-Oncology · doi:10.1093/neuonc/noab009 · Cited by 27
Self-citationClassification and Treatment of Pediatric Gliomas in the Molecular Era
Hauser, P. (2021) · Children · doi:10.3390/children8090739 · Cited by 25
Human germline and pan-cancer variomes and their distinct functional profiles
Pan, Y., Karagiannis, K., Zhang, H., Dingerdissen, H., Shamsaddini, A., Wan, Q., Simonyan, V. V., & Mazumder, R. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku772 · Cited by 27
Ueda, T., Nakata, Y., Nagamachi, A., Yamasaki, N., Kanai, A., Sera, Y., Sasaki, M., Matsui, H., Honda, Z., Oda, H., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1600070113 · Cited by 27
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
