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 301–400 of 999
Malzkorn, B., & Reifenberger, G. (2016) · Current Opinion in Oncology · doi:10.1097/cco.0000000000000327 · Cited by 75
Wood, M. D., Halfpenny, A. M., & Moore, S. R. (2019) · Diagnostic Pathology · doi:10.1186/s13000-019-0802-8 · Cited by 74
Brien, G. L., Bressan, R. B., Monger, C., Gannon, D., Lagan, E., Doherty, A. M., Healy, E., Neikes, H. K., Fitzpatrick, D. J., Deevy, O., et al. (2021) · Nature Genetics · doi:10.1038/s41588-021-00897-w · Cited by 80
Synthetic lethal strategies for the development of cancer therapeutics
Ngoi, N. Y. L., Gallo, D., Torrado, C., Nardo, M., Durocher, D., & Yap, T. A. (2024) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-024-00966-z · Cited by 81
Human pontine glioma cells can induce murine tumors
Caretti, V., Sewing, A. C. P., Lagerweij, T., Schellen, P., Bugiani, M., Jansen, M. H. A., van Vuurden, D. G., Navis, A. C., Horsman, I., Vandertop, W. P., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1272-4 · Cited by 73
El-Habr, E. A., Dubois, L. G., Burel‐Vandenbos, F., Bogeas, A., Lipecka, J., Turchi, L., Lejeune, F., Coehlo, P. L. C., Yamaki, T., Wittmann, B. M., et al. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1659-5 · Cited by 79
Lehnertz, B., Zhang, Y. W., Boivin, I., Mayotte, N., Tomellini, E., Chagraoui, J., Lavallée, V., Hébert, J., & Sauvageau, G. (2017) · Blood · doi:10.1182/blood-2017-03-774653 · Cited by 76
Histone deposition pathways determine the chromatin landscapes of H3.1 and H3.3 K27M oncohistones
Sarthy, J. F., Meers, M. P., Janssens, D. H., Henikoff, J. G., Feldman, H. M., Paddison, P. J., Lockwood, C. M., Vitanza, N. A., Olson, J. M., Ahmad, K., et al. (2020) · eLife · doi:10.7554/elife.61090 · Cited by 73
Structural and functional specificity of H3K36 methylation
Lam, U. T. F., Tan, B. K. Y., Poh, J. J. X., & Chen, E. S. (2022) · Epigenetics & Chromatin · doi:10.1186/s13072-022-00446-7 · Cited by 84
Single substitution in H3.3G34 alters DNMT3A recruitment to cause progressive neurodegeneration
Khazaei, S., Chen, C. C. L., Andrade, A. F., Kabir, N., Azarafshar, P., Morcos, S. M., França, J. A., Lopes, M. D. C., Lund, P. J., Danieau, G., et al. (2023) · Cell · doi:10.1016/j.cell.2023.02.023 · Cited by 71
Self-citationPediatric gliomas as neurodevelopmental disorders
Baker, S. J., Ellison, D. W., & Gutmann, D. H. (2015) · Glia · doi:10.1002/glia.22945 · Cited by 76
Characterizing temporal genomic heterogeneity in pediatric high-grade gliomas
Salloum, R., McConechy, M. K., Mikael, L. G., Fuller, C. E., Drissi, R., DeWire, M. D., Nikbakht, H., Jay, N. D., Yang, X., Boué, D. R., et al. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0479-8 · Cited by 71
Spinal cord high-grade infiltrating gliomas in adults: clinico-pathological and molecular evaluation
Alvi, M. A., Ida, C. M., Paolini, M. A., Kerezoudis, P., Meyer, J., Fritcher, E. G. B., Goncalves, S., Meyer, F. B., Bydon, M., & Raghunathan, A. (2019) · Modern Pathology · doi:10.1038/s41379-019-0271-3 · Cited by 71
Histone H3.3 Is Required to Maintain Replication Fork Progression after UV Damage
Frey, A., Listovsky, T., Guilbaud, G., Sarkies, P., & Sale, J. E. (2014) · Current Biology · doi:10.1016/j.cub.2014.07.077 · Cited by 75
Distinct and separable roles for EZH2 in neurogenic astroglia
Hwang, W. W., Salinas, R. D., Siu, J. J., Kelley, K. W., Delgado, R. N., Paredes, M. F., Álvarez-Buylla, A., Oldham, M. C., & Lim, D. A. (2014) · eLife · doi:10.7554/elife.02439 · Cited by 76
Myant, K., Cammareri, P., Hodder, M. C., Wills, J. C., von Kriegsheim, A., Győrffy, B., Rashid, M., Polo, S., Maspero, E., Vaughan, L. S., et al. (2016) · EMBO Molecular Medicine · doi:10.15252/emmm.201606684 · Cited by 75
Accelerating the Field of Epigenetic Histone Modification Through Mass Spectrometry–Based Approaches
Lu, C., Coradin, M., Porter, E. G. P., & Garcia, B. A. (2020) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r120.002257 · Cited by 71
Self-citationSenescence Induced by BMI1 Inhibition Is a Therapeutic Vulnerability in H3K27M-Mutant DIPG
Balakrishnan, I., Danis, E. P., Pierce, A. M., Madhavan, K. P. C., Wang, D., Dahl, N. A., Sanford, B. L., Birks, D. K., Davidson, N., Metselaar, D. S., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108286 · Cited by 75
Epigenetic activation of a RAS/MYC axis in H3.3K27M-driven cancer
Pajovic, S., Siddaway, R., Bridge, T., Sheth, J., Rakopoulos, P., Kim, B., Ryall, S. T., Agnihotri, S., Phillips, L., Yu, M., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-19972-7 · Cited by 70
Pediatric high‐grade glioma: moving toward subtype‐specific multimodal therapy
Chatwin, H. V., Cruz, J. C., & Green, A. L. (2021) · FEBS Journal · doi:10.1111/febs.15739 · Cited by 71
OpenPBTA: The Open Pediatric Brain Tumor Atlas
Shapiro, J. A., Gaonkar, K. S., Spielman, S. J., Savonen, C., Bethell, C. J., Jin, R., Rathi, K. S., Zhu, Y., Egolf, L. E., Farrow, B., et al. (2023) · Cell Genomics · doi:10.1016/j.xgen.2023.100340 · Cited by 70
Oncogenic Mechanisms of Histone H3 MutationsPreprint
Weinberg, D. N., Allis, C. D., & Lü, C. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a026443 · Cited by 74
Self-citationReprogramming: identifying the mechanisms that safeguard cell identity
Brumbaugh, J., Stefano, B. D., & Hochedlinger, K. (2019) · Development · doi:10.1242/dev.182170 · Cited by 66
CRISPR/Cas9-Mediated Genome Editing of Epigenetic Factors for Cancer Therapy
Yao, S., He, Z., & Chen, C. (2015) · Human Gene Therapy · doi:10.1089/hum.2015.067 · Cited by 70
Control of cancer formation by intrinsic genetic noise and microenvironmental cues
Brock, A., Krause, S., & Ingber, D. E. (2015) · Nature reviews. Cancer · doi:10.1038/nrc3959 · Cited by 72
A global assessment of cancer genomic alterations in epigenetic mechanisms
Shah, M. A., Denton, E., Arrowsmith, C. H., Lupien, M., & Schapira, M. (2014) · Epigenetics & Chromatin · doi:10.1186/1756-8935-7-29 · Cited by 71
Nichol, J. N., Dupéré-Richer, D., Ezponda, T., Licht, J. D., & Miller, W. H. (2016) · Advances in cancer research · doi:10.1016/bs.acr.2016.05.001 · Cited by 75
Molecular mechanisms and therapeutic targets in pediatric brain tumors
Liu, K.-W., Pajtler, K. W., Worst, B. C., Pfister, S. M., & Wechsler‐Reya, R. J. (2017) · Science Signaling · doi:10.1126/scisignal.aaf7593 · Cited by 67
Auffret, L., Ajlil, Y., Tauziède‐Espariat, A., Kergrohen, T., Puiseux, C., Riffaud, L., Blouin, P., Bertozzi, A., Leblond, P., Blomgren, K., et al. (2023) · Acta Neuropathologica · doi:10.1007/s00401-023-02651-4 · Cited by 66
Future Clinical Trials in DIPG: Bringing Epigenetics to the Clinic
Madrid, A. M. L., Hashizume, R., & Kieran, M. W. (2015) · Frontiers in Oncology · doi:10.3389/fonc.2015.00148 · Cited by 67
Epigenetic changes in the developing brain: Effects on behavior
Keverne, E. B., Pfaff, D. W., & Tabansky, I. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1501482112 · Cited by 68
Potential New Therapies for Pediatric Diffuse Intrinsic Pontine Glioma
Long, W., Yang, Y., Chen, S., Cao, Q., Zhao, W., & Liu, Q. (2017) · Frontiers in Pharmacology · doi:10.3389/fphar.2017.00495 · Cited by 71
Targeting Chromatin Remodeling for Cancer Therapy
Kaur, J., Daoud, A., & Eblen, S. T. (2019) · Current Molecular Pharmacology · doi:10.2174/1874467212666190215112915 · Cited by 69
Bailey, C. P., Figueroa, M., Gangadharan, A., Yang, Y., Romero, M. M., Kennis, B. A., Yadavilli, S., Henry, V. K., Collier, T. L., Monje, M., et al. (2020) · Neuro-Oncology · doi:10.1093/neuonc/noaa058 · Cited by 68
Self-citationDiffuse intrinsic pontine glioma: current insights and future directions
Srikanthan, D., Taccone, M. S., Ommeren, R. V., Ishida, J., Krumholtz, S. L., & Rutka, J. T. (2021) · Chinese Neurosurgical Journal · doi:10.1186/s41016-020-00218-w · Cited by 63
Önder, Ö., Sidoli, S., Carroll, M. P., & Garcia, B. A. (2015) · Expert Review of Proteomics · doi:10.1586/14789450.2015.1084231 · Cited by 70
Self-citationSitbon, D., Boyarchuk, E., Dingli, F., Loew, D., & Almouzni, G. (2020) · Nature Communications · doi:10.1038/s41467-020-15084-4 · Cited by 71
Histone H1 alterations in cancer
Scaffidi, P. (2015) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2015.09.008 · Cited by 62
Assembly of telomeric chromatin to create ALTernative endings
O’Sullivan, R. J., & Almouzni, G. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.07.007 · Cited by 66
The Multiple Facets of PRC2 Alterations in Cancers
Wassef, M. A., & Margueron, R. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.10.012 · Cited by 72
Solid tumours hijack the histone variant network
Ghiraldini, F. G., Filipescu, D., & Bernstein, E. (2021) · Nature reviews. Cancer · doi:10.1038/s41568-020-00330-0 · Cited by 68
Bae, W. K., Yoo, K. H., Lee, J. S., Kim, Y., Chung, I., Park, M. H., Yoon, J. H., Furth, P. A., & Hennighausen, L. G. (2014) · Molecular Carcinogenesis · doi:10.1002/mc.22188 · Cited by 66
A lesson learned from the H3.3K27M mutation found in pediatric glioma
Chan, K. M., Han, J., Fang, D., Gan, H., & Zhang, Z. (2013) · Cell Cycle · doi:10.4161/cc.25625 · Cited by 64
Combination of EZH2 inhibitor and BET inhibitor for treatment of diffuse intrinsic pontine glioma
Zhang, Y., Dong, W., Zhu, J., Wang, L., Wu, X., & Shan, H. (2017) · Cell & Bioscience · doi:10.1186/s13578-017-0184-0 · Cited by 65
Constructing and Deconstructing Cancers using Human Pluripotent Stem Cells and Organoids
Smith, R. C., & Tabar, V. S. (2018) · Cell stem cell · doi:10.1016/j.stem.2018.11.012 · Cited by 62
Lin, S., Wein, S. P., Gonzales-Cope, M., Otte, G. L., Yuan, Z., Afjehi‐Sadat, L., Maile, T. M., Berger, S. L., Rush, A. J., Lill, J. R., et al. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o113.036459 · Cited by 68
Self-citationH3K4 Methyltransferase Activity Is Required for MLL4 Protein Stability
Jang, Y., Wang, C., Zhuang, L., Liu, C., & Ge, K. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.12.016 · Cited by 62
Live-cell single-molecule dynamics of PcG proteins imposed by the DIPG H3.3K27M mutation
Tatavosian, R., Duc, H. N., Huynh, T. N., Fang, D., Schmitt, B., Shi, X., Deng, Y., Phiel, C. J., Yao, T., Zhang, Z., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-04455-7 · Cited by 64
Nikolaev, A. Y., Fiveash, J. B., & Yang, E. S.-H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21020490 · Cited by 62
Green, A. L., & Kieran, M. W. (2015) · Current Oncology Reports · doi:10.1007/s11912-014-0436-7 · Cited by 64
H3 K27M mutations are extremely rare in posterior fossa group A ependymoma
Ryall, S. T., Guzmán, M. A., Elbabaa, S. K., Luu, B., Mack, S. C., Zápotocký, M., Taylor, M. D., Hawkins, C. E., & Ramaswamy, V. (2017) · Child s Nervous System · doi:10.1007/s00381-017-3481-3 · Cited by 62
Signal Transduction in Diffuse Intrinsic Pontine Glioma
Duchatel, R. J., Jackson, E. R., Alvaro, F., Nixon, B., Hondermarck, H., & Dun, M. D. (2019) · PROTEOMICS · doi:10.1002/pmic.201800479 · Cited by 66
Scelfo, A., Piunti, A., & Pasini, D. (2014) · FEBS Journal · doi:10.1111/febs.13112 · Cited by 61
Molecular pathology of paediatric central nervous system tumours
Chiang, J., & Ellison, D. W. (2016) · The Journal of Pathology · doi:10.1002/path.4813 · Cited by 63
Therapeutic Targeting of Histone Modifications in Adult and Pediatric High-Grade Glioma
Williams, M. J., Singleton, W., Lowis, S. P., Malik, K. T. A., & Kurian, K. M. (2017) · Frontiers in Oncology · doi:10.3389/fonc.2017.00045 · Cited by 62
Brumbaugh, J., Kim, I. S., Ji, F., Huebner, A. J., Stefano, B. D., Schwarz, B. A., Charlton, J., Coffey, A., Choi, J., Walsh, R. M., et al. (2019) · Nature Cell Biology · doi:10.1038/s41556-019-0403-5 · Cited by 63
Workman, P., Al‐Lazikani, B., & Clarke, P. A. (2013) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2013.06.004 · Cited by 60
Histone H3 Mutations in Cancer
Wan, Y. C. E., Liu, J., & Chan, K. M. (2018) · Current Pharmacology Reports · doi:10.1007/s40495-018-0141-6 · Cited by 61
Subashi, E., Cordero, F. J., Halvorson, K. G., Qi, Y. P., Nouls, J. C., Becher, O. J., & Johnson, G. A. (2015) · Journal of Neuro-Oncology · doi:10.1007/s11060-015-1969-9 · Cited by 61
Self-citationGiant cell tumor of soft tissue is genetically distinct from its bone counterpart
Lee, J., Liang, C., & Fletcher, C. D. �. (2017) · Modern Pathology · doi:10.1038/modpathol.2016.236 · Cited by 62
A Novel Mouse Model of Diffuse Intrinsic Pontine Glioma Initiated in Pax3-Expressing Cells
Misuraca, K. L., Hu, G., Barton, K. L., Chung, A., & Becher, O. J. (2016) · Neoplasia · doi:10.1016/j.neo.2015.12.002 · Cited by 63
Self-citationWu, R., Wang, Z., Zhang, H., Gan, H., & Zhang, Z. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw848 · Cited by 61
Panditharatna, E., Yaeger, K., Kilburn, L. B., Packer, R. J., & Nazarian, J. (2015) · Cancer Genetics · doi:10.1016/j.cancergen.2015.04.008 · Cited by 57
Jung, J. S., Choi, Y. S., Ahn, S. S., Yi, S., Kim, S. H., & Lee, S. (2019) · Neuroradiology · doi:10.1007/s00234-019-02154-8 · Cited by 58
Targeting EZH2 as cancer therapy
Hanaki, S., & Shimada, M. (2021) · The Journal of Biochemistry · doi:10.1093/jb/mvab007 · Cited by 56
Functional Roles of Bromodomain Proteins in Cancer
Boyson, S. P., Gao, C., Quinn, K. M., Boyd, J. R., Paculová, H., Frietze, S. E., & Glass, K. C. (2021) · Cancers · doi:10.3390/cancers13143606 · Cited by 59
Single-cell epigenetic analysis reveals principles of chromatin states in H3.3-K27M gliomas
Harpaz, N., Mittelman, T., Beresh, O., Griess, O., Furth, N., Salame, T., Oren, R., Fellus‐Alyagor, L., Harmelin, A., Alexandrescu, S., et al. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.05.023 · Cited by 61
Pre-Clinical Models of Diffuse Intrinsic Pontine Glioma
Misuraca, K. L., Cordero, F. J., & Becher, O. J. (2015) · Frontiers in Oncology · doi:10.3389/fonc.2015.00172 · Cited by 60
Self-citationHistone modifications and a choice of variant: a language that helps the genome express itself
Gurard‐Levin, Z. A., & Almouzni, G. (2014) · F1000Prime Reports · doi:10.12703/p6-76 · Cited by 65
Yoon, S., Wu, X., Armstrong, B., Habib, N. A., & Rossi, J. J. (2018) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2018.11.012 · Cited by 58
Activation and regulation of H2B-Ubiquitin-dependent histone methyltransferases
Worden, E. J., & Wolberger, C. (2019) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2019.05.009 · Cited by 58
Histone Variants: Guardians of Genome Integrity
Ferrand, J., Rondinelli, B., & Polo, S. E. (2020) · Cells · doi:10.3390/cells9112424 · Cited by 63
Broux, M., Prieto, C., Demeyer, S., Bempt, M. V., Servera, L. A., Lodewijckx, I., Vandepoel, R., Mentens, N., Gielen, O., Jacobs, K., et al. (2019) · Blood · doi:10.1182/blood.2019000015 · Cited by 57
Jin, H., Kasper, L. H., Larson, J. D., Wu, G., Baker, S. J., Zhang, J., & Fan, Y. (2020) · Bioinformatics · doi:10.1093/bioinformatics/btz720 · Cited by 57
Is Glioblastoma an Epigenetic Malignancy?
Maleszewska, M., & Kaminska, B. (2013) · Cancers · doi:10.3390/cancers5031120 · Cited by 63
The epigenetics of tumour initiation: cancer stem cells and their chromatin
Avgustinova, A., & Benitah, S. A. (2016) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2016.01.003 · Cited by 58
Histone variant H3F3A promotes lung cancer cell migration through intronic regulation
Park, S., Choi, E.-Y., Bae, M., Kim, S., Park, J. B., Yoo, H., Choi, J. K., Kim, Y., Lee, S., & Kim, I.-H. (2016) · Nature Communications · doi:10.1038/ncomms12914 · Cited by 62
Signaling pathways and mesenchymal transition in pediatric high-grade glioma
Meel, M. H., Schaper, S. A., Kaspers, G. J. L., & Hulleman, E. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2714-7 · Cited by 58
Childhood Malignant Brain Tumors: Balancing the Bench and Bedside
Thorbinson, C., & Kilday, J. (2021) · Cancers · doi:10.3390/cancers13236099 · Cited by 63
Pharmacological targeting of the cancer epigenome
Mabe, N. W., Perry, J. A., Malone, C. F., & Stegmaier, K. (2024) · Nature Cancer · doi:10.1038/s43018-024-00777-2 · Cited by 61
Management of high-grade gliomas in the pediatric patient: Past, present, and future
Vanan, M., & Eisenstat, D. D. (2014) · Neuro-Oncology Practice · doi:10.1093/nop/npu022 · Cited by 55
Plessier, A., Dret, L. L., Varlet, P., Beccaria, K., Lacombe, J., Mériaux, S., Geffroy, F., Fiette, L., Flamant, P., Chrétien, F., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.15002 · Cited by 64
Nuclear condensates of YAP fusion proteins alter transcription to drive ependymoma tumourigenesis
Hu, X., Wu, X., Berry, K., Zhao, C., Xin, D. E., Ogurek, S., Liu, X., Zhang, L., Luo, Z., Sakabe, M., et al. (2023) · Nature Cell Biology · doi:10.1038/s41556-022-01069-6 · Cited by 57
Weichenhan, D., & Plass, C. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt348 · Cited by 58
Pleiotropic Functions of H3K27Me3 Demethylases in Immune Cell Differentiation
Bosselut, R. (2016) · Trends in Immunology · doi:10.1016/j.it.2015.12.004 · Cited by 57
Okada, Y., & Yamaguchi, K. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2447-z · Cited by 57
Epigenetic Targeted Therapy for Diffuse Intrinsic Pontine Glioma
Hashizume, R. (2017) · Neurologia medico-chirurgica · doi:10.2176/nmc.ra.2017-0018 · Cited by 59
Epigenetics as a New Frontier in Orthopedic Regenerative Medicine and Oncology
van Wijnen, A. J., & Westendorf, J. J. (2019) · Journal of Orthopaedic Research® · doi:10.1002/jor.24305 · Cited by 54
Midline Glioma in Adults: Clinicopathological, Genetic, and Epigenetic Analysis
Enomoto, T., Aoki, M., Hamasaki, M., Abe, H., Nonaka, M., Inoue, T., & Nabeshima, K. (2020) · Neurologia medico-chirurgica · doi:10.2176/nmc.oa.2019-0168 · Cited by 56
Williams, E. A., Brastianos, P. K., Wakimoto, H., Zolal, A., Filbin, M. G., Cahill, D. P., Santagata, S., & Juratli, T. A. (2023) · Acta Neuropathologica · doi:10.1007/s00401-023-02609-6 · Cited by 59
Mechanisms of DNA Methylation Regulatory Function and Crosstalk with Histone Lysine Methylation
Tibben, B. M., & Rothbart, S. B. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168394 · Cited by 61
Diffusely infiltrating astrocytomas: pathology, molecular mechanisms and markers
Ichimura, K., Narita, Y., & Hawkins, C. E. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1439-7 · Cited by 56
Yadav, R. K., Jablonowski, C. M., Fernandez, A. G., Lowe, B. R., Henry, R. A., Finkelstein, D., Barnum, K. J., Pidoux, A. L., Kuo, Y., Huang, J., et al. (2017) · eLife · doi:10.7554/elife.27406 · Cited by 53
Lim, J., Park, J. H., Baude, A., Yoo, Y., Lee, Y. K., Schmidt, C. R., Park, J. B., Fellenberg, J., Zustin, J., Haller, F., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-13887-y · Cited by 53
Xiong, C., Wen, Z., Yu, J., Chen, J., Liu, C.-P., Zhang, X., Chen, P., Xu, R.-M., & Li, G. (2018) · BMC Biology · doi:10.1186/s12915-018-0573-9 · Cited by 55
Gehre, M., Bunina, D., Sidoli, S., Lübke, M. J., Diaz, N. S., Trovato, M., Garcia, B. A., Zaugg, J. B., & Noh, K. (2020) · Nature Genetics · doi:10.1038/s41588-020-0586-5 · Cited by 50
Self-citationSETD2: from chromatin modifier to multipronged regulator of the genome and beyond
Molenaar, T. M., & van Leeuwen, F. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04352-9 · Cited by 56
Transitioning from genotypes to epigenotypes: Why the time has come for medulloblastoma epigenomics
Batora, N. V., Sturm, D., Jones, D., Kool, M., Pfister, S. M., & Northcott, P. A. (2013) · Neuroscience · doi:10.1016/j.neuroscience.2013.07.030 · Cited by 52
Song, H., Yu, Z., Sun, X., Feng, J. L., Qi, Y., Khan, H., Zhu, X., Huang, L., Li, M., Mok, M. T. S., et al. (2018) · EBioMedicine · doi:10.1016/j.ebiom.2018.08.043 · Cited by 52
Berry, K., Wang, J., & Lu, Q. R. (2020) · F1000Research · doi:10.12688/f1000research.20904.1 · Cited by 53
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
