The DOI matches its Crossref record; 276 of the 277 references it cites were found in a registry or an index.
Histone methylation: a dynamic mark in health, disease and inheritance
Open accessAbstract
Organisms require an appropriate balance of stability and reversibility in gene expression programmes to maintain cell identity or to enable responses to stimuli; epigenetic regulation is integral to this dynamic control. Post-translational modification of histones by methylation is an important and widespread type of chromatin modification that is known to influence biological processes in the context of development and cellular responses. To evaluate how histone methylation contributes to stable or reversible control, we provide a broad overview of how histone methylation is regulated and leads to biological outcomes. The importance of appropriately maintaining or reprogramming histone methylation is illustrated by its links to disease and ageing and possibly to transmission of traits across generations.
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.
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
1 retracted
Histone methylation by the Drosophila epigenetic transcriptional regulator Ash1
Beisel, C., Imhof, A., Greene, J., Kremmer, E., & Sauer, F. (2002) · Nature · doi:10.1038/nature01126 · Cited by 310
RetractedChromatin modifications and their function
Kouzarides, T. (2007) · Cell · doi:10.1016/j.cell.2007.02.005 · Cited by 10,883
The language of covalent histone modifications
Strahl, B. D., & Allis, C. D. (2000) · Nature · doi:10.1038/47412 · Cited by 8,679
Regulation of chromatin by histone modifications
Bannister, A. J., & Kouzarides, T. (2011) · Cell Research · doi:10.1038/cr.2011.22 · Cited by 6,012
Chen, X., Xiu, M., Xing, J., Yu, S., Min, D., & Guo, F. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000479439 · Cited by 5,760
A bivalent chromatin structure marks key developmental genes in embryonic stem cells
Bernstein, B. E., Mikkelsen, T. S., Xie, X., Kamal, M., Huebert, D. J., Cuff, J., Fry, B., Meissner, A., Wernig, M., Plath, K., et al. (2006) · Cell · doi:10.1016/j.cell.2006.02.041 · Cited by 5,361
Long non-coding RNA HOTAIR reprograms chromatin state to promote cancer metastasis
Gupta, R. A., Shah, N., Wang, K., Kim, J., Horlings, H. M., Wong, D. J., Tsai, M.-C., Hung, T., Argani, P., Rinn, J. L., et al. (2010) · Nature · doi:10.1038/nature08975 · Cited by 5,205
Rett syndrome is caused by mutations in X-linked MECP2, encoding methyl-CpG-binding protein 2
Amir, R. E., Van den Veyver, I. B., Wan, M., Tran, C. Q., Francke, U., & Zoghbi, H. Y. (1999) · Nature Genetics · doi:10.1038/13810 · Cited by 4,990
Functional Demarcation of Active and Silent Chromatin Domains in Human HOX Loci by Noncoding RNAs
Rinn, J. L., Kertesz, M., Wang, J. K., Squazzo, S. L., Xu, X. H., Brugmann, S. A., Goodnough, L. H., Helms, J. A., Farnham, P., Segal, E., et al. (2007) · Cell · doi:10.1016/j.cell.2007.05.022 · Cited by 4,246
Chromatin signature reveals over a thousand highly conserved large non-coding RNAs in mammals
Guttman, M., Amit, I., Garber, M., French, C., Lin, M. F., Feldser, D., Huarte, M., Zuk, O., Carey, B. W., Cassady, J. P., et al. (2009) · Nature · doi:10.1038/nature07672 · Cited by 4,098
Flagged first, then by citations
1 of the 277 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Items 401–500 of 1,002
Epigenetic Regulation in Chromium-, Nickel- and Cadmium-Induced Carcinogenesis
Zhao, L., Islam, R., Wang, Y.-F., Zhang, X., & Liu, L.-Z. (2022) · Cancers · doi:10.3390/cancers14235768 · Cited by 73
Weaver, I. C. G., Korgan, A. C., Lee, K., Wheeler, R. V., Hundert, A. S., & Goguen, D. (2017) · Frontiers in Behavioral Neuroscience · doi:10.3389/fnbeh.2017.00041 · Cited by 69
PRMT6-mediated H3R2me2a guides Aurora B to chromosome arms for proper chromosome segregation
Kim, S., Kim, N. H., Park, J. E., Hwang, J. W., Myung, N., Hwang, K.-T., Kim, Y. A., Jang, C., & Kim, Y. K. (2020) · Nature Communications · doi:10.1038/s41467-020-14511-w · Cited by 64
Milite, C., Feoli, A., Horton, J. R., Rescigno, D., Cipriano, A., Pisapia, V., Viviano, M., Pepe, G., Amendola, G., Novellino, E., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b02008 · Cited by 65
Gómez, J. L. (2019) · Current Allergy and Asthma Reports · doi:10.1007/s11882-019-0886-y · Cited by 66
The Link Between Hyperhomocysteinemia and Hypomethylation
Barroso, M., Handy, D. E., & Castro, R. (2017) · Journal of Inborn Errors of Metabolism and Screening · doi:10.1177/2326409817698994 · Cited by 63
Rinaldi, G., Rossi, M., & Fendt, S. (2017) · WIREs Systems Biology and Medicine · doi:10.1002/wsbm.1397 · Cited by 65
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
Mechanisms and rationales of SAM homeostasis
Zheng, X., & Tu, B. P. (2025) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2024.12.009 · Cited by 62
Epigenetic modulation as a therapeutic approach for pulmonary arterial hypertension
Kim, J., Lee, A., Choi, J., Park, Y., Kang, H., Chang, W., Lee, M.-S., & Kim, J. (2015) · Experimental & Molecular Medicine · doi:10.1038/emm.2015.45 · Cited by 60
Chemical methods for the proteome-wide identification of posttranslationally modified proteins
Chuh, K. N., & Pratt, M. R. (2014) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2014.10.020 · Cited by 62
Small-Molecule Ligands of Methyl-Lysine Binding Proteins: Optimization of Selectivity for L3MBTL3
James, L. I., Korboukh, V. K., Krichevsky, L., Baughman, B. M., Herold, J. M., Norris, J. L., Jin, J. J., Kireev, D., Janzen, W. P., Arrowsmith, C. H., et al. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm400919p · Cited by 62
Metabolic–Epigenetic Crosstalk in Macrophage Activation
Baardman, J., Licht, I., de Winther, M. P. J., & den Bossche, J. V. (2015) · Epigenomics · doi:10.2217/epi.15.71 · Cited by 64
Epigenetic mechanisms of cell adhesion-mediated drug resistance in multiple myeloma
Furukawa, Y., & Kikuchi, J. (2016) · International Journal of Hematology · doi:10.1007/s12185-016-2048-5 · Cited by 65
Interplay between the miRNome and the epigenetic machinery: Implications in health and disease
Poddar, S., Kesharwani, D., & Datta, M. (2017) · Journal of Cellular Physiology · doi:10.1002/jcp.25819 · Cited by 57
Anticancer Natural Compounds as Epigenetic Modulators of Gene Expression
Ratovitski, E. A. (2017) · Current Genomics · doi:10.2174/1389202917666160803165229 · Cited by 66
Methylated DNMT1 and E2F1 are targeted for proteolysis by L3MBTL3 and CRL4DCAF5 ubiquitin ligase
Leng, F., Yu, J., Zhang, C., Alejo, S., Hoang, N., Sun, H., Lu, F., & Zhang, H. (2018) · Nature Communications · doi:10.1038/s41467-018-04019-9 · Cited by 63
The nematode Caenorhabditis elegans as a model for aging research
Mack, H. I. D., Heimbucher, T., & Murphy, C. T. (2018) · Drug Discovery Today Disease Models · doi:10.1016/j.ddmod.2018.11.001 · Cited by 68
Epigenetic Reprogramming of TGF-β Signaling in Breast Cancer
Suriyamurthy, S., Baker, D. A., ten Dijke, P., & Iyengar, P. V. (2019) · Cancers · doi:10.3390/cancers11050726 · Cited by 63
Histone Methyltransferases as Therapeutic Targets for Kidney Diseases
Yu, C., & Zhuang, S. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.01393 · Cited by 62
Oncogenic Features of PHF8 Histone Demethylase in Esophageal Squamous Cell Carcinoma
Sun, X., Qiu, J. J., Zhu, S., Cao, B., Sun, L., Li, S., Li, P., Zhang, S., & Dong, S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0077353 · Cited by 60
Mews, P., Zee, B. M., Liu, S., Donahue, G., Garcia, B. A., & Berger, S. L. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.00763-14 · Cited by 60
New Insights into Protein Hydroxylation and Its Important Role in Human Diseases
Zurlo, G., Guo, J., Takada, M., Wei, W., & Zhang, Q. H. (2016) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2016.09.004 · Cited by 62
Histone Lysine Methylation and Neurodevelopmental Disorders
Kim, J., Lee, J., Lee, I., Lee, S. B., & Cho, K. S. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18071404 · Cited by 65
Klymenko, Y., & Nephew, K. P. (2018) · Cancers · doi:10.3390/cancers10090295 · Cited by 63
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
Natural variation of histone modification and its impact on gene expression in the rat genomePreprint
Rintisch, C., Heinig, M., Bauerfeind, A., Schäfer, S., Mieth, C., Patone, G., Hummel, O., Chen, W., Cook, S. A., Cuppen, E. P. J. G., et al. (2014) · Genome Research · doi:10.1101/gr.169029.113 · Cited by 59
Fang, S., Shen, Y., Chen, B., Wu, Y., Jia, L., Li, Y., Zhu, Y., Yan, Y., Li, M., Chen, R., et al. (2018) · Annals of Translational Medicine · doi:10.21037/atm.2018.10.21 · Cited by 60
Uramova, S., Kubatka, P., Daňková, Z., Kapinová, A., Zolakova, B., Samec, M., Žúbor, P., Zulli, A., Valentová, V., Kwon, T. K., et al. (2018) · The EPMA Journal · doi:10.1007/s13167-018-0154-6 · Cited by 61
Zhang, Y., Liu, J., Lin, J., Zhou, L., Song, Y., Wei, B., Luo, X., Chen, Z., Chen, Y., Xiong, J., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.7126 · Cited by 60
Ye, Q., Holowatyj, A., Wu, J., Liu, H., Zhang, L., Suzuki, T., & Yang, Z. Q. (2015) · Europe PMC (PubMed Central) · Cited by 60
Role of histone modifications in neurogenesis and neurodegenerative disease development
Zhao, A., Xu, W., Han, R., Wei, J., Qi, Y., Wang, M., Li, H., Li, M., & Chi, G. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102324 · Cited by 65
Didehydroaspartate Modification in Methyl‐Coenzyme M Reductase Catalyzing Methane Formation
Wagner, T., Kahnt, J., Ermler, U., & Shima, S. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201603882 · Cited by 60
Gürsoy-Yüzügüllü, Ö., Carman, C. L., Serafim, R. B., Myronakis, M. E., Valente, V., & Price, B. D. (2017) · Oncotarget · doi:10.18632/oncotarget.15543 · Cited by 61
Interrogating the Roles of Post-Translational Modifications of Non-Histone Proteins
Buuh, Z. Y., Lyu, Z., & Wang, R. E. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01817 · Cited by 61
Krautkramer, K. A., Dhillon, R. S., Denu, J. M., & Carey, H. V. (2017) · Translational research · doi:10.1016/j.trsl.2017.08.005 · Cited by 61
DNA methylation and chromatin modifiers in colorectal cancer
Vymetalkova, V. P., Vodička, P., Vodenková, S., Alonso, S., & Schneider‐Stock, R. (2019) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2019.04.002 · Cited by 58
Advances of Epigenetic Biomarkers and Epigenome Editing for Early Diagnosis in Breast Cancer
Sarvari, P., Sarvari, P., Ramírez‐Díaz, I., Mahjoubi, F., & Rubio, K. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23179521 · Cited by 68
Małecki, J., Ho, A. Y. Y., Moen, A. R., Dahl, H.-A., & Falnes, P. Ø. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.614115 · Cited by 58
A drive in SUVs: From development to disease
Rao, V. K., Pal, A., & Taneja, R. (2017) · Epigenetics · doi:10.1080/15592294.2017.1281502 · Cited by 62
Histone lysine demethylases in mammalian embryonic development
Shen, H., Xu, W., & Lan, F. (2017) · Experimental & Molecular Medicine · doi:10.1038/emm.2017.57 · Cited by 58
Jakobsson, M. E., Małecki, J., Nilges, B. S., Moen, A. R., Leidel, S. A., & Falnes, P. Ø. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx432 · Cited by 58
A novel HER2 gene body enhancer contributes to HER2 expression
Liu, Q., Kulak, M. V., Borcherding, N. C., Maina, P. K., Zhang, W., Weigel, R. J., & Qi, H. H. (2017) · Oncogene · doi:10.1038/onc.2017.382 · Cited by 61
Li, A., You, D., Li, W., Cui, Y., He, Y., Li, W., Chen, Y., Feng, X., Sun, S., Chai, R., et al. (2018) · Drug Delivery · doi:10.1080/10717544.2018.1461277 · Cited by 57
Trimethyllysine: From Carnitine Biosynthesis to Epigenetics
Maas, M. N., Hintzen, J. C. J., Porzberg, M. R. B., & Mecinović, J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21249451 · Cited by 58
Protein methylation in mitochondria
Małecki, J., Davydova, E., & Falnes, P. Ø. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101791 · Cited by 57
Mechanisms of DNA methylation and histone modifications
Acharjee, S., Chauhan, S. K., Pal, R., & Tomar, R. S. (2023) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2023.01.001 · Cited by 61
Li, Z., Xu, L., Tang, N., Xu, Y., Ye, X., Shen, S., Niu, X., Lü, S., & Chen, Z. (2014) · FEBS Letters · doi:10.1016/j.febslet.2014.05.057 · Cited by 58
Histone Methyltransferase Inhibitors: Novel Epigenetic Agents for Cancer Treatment
Zagni, C., Chiacchio, U., & Rescifina, A. (2012) · Current Medicinal Chemistry · doi:10.2174/092986713804806667 · Cited by 59
The histone methyltransferase DOT1L: regulatory functions and a cancer therapy target.
Wong, M., Polly, P., & Liu, T. (2015) · Europe PMC (PubMed Central) · Cited by 57
Chemical Modulation of Cell Fate in Stem Cell Therapeutics and Regenerative Medicine
Liu, K., Chen, Y., Xie, M., Li, K., & Ding, S. (2016) · Cell chemical biology · doi:10.1016/j.chembiol.2016.07.007 · Cited by 60
From a novel HTS hit to potent, selective, and orally bioavailable KDM5 inhibitors
Liang, J., Labadie, S. S., Zhang, B., Ortwine, D. F., Patel, S. D., Vinogradova, M. V., Kiefer, J. R., Mauer, T., Gehling, V. S., Harmange, J.-C., et al. (2017) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2017.05.016 · Cited by 58
Metabolic intermediates – Cellular messengers talking to chromatin modifiers
Nieborak, A., & Schneider, R. (2018) · Molecular Metabolism · doi:10.1016/j.molmet.2018.01.007 · Cited by 57
Ye, C., Sutter, B. M., Wang, Y., Kuang, Z., Zhao, X., Yu, Y., & Tu, B. P. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.01.012 · Cited by 56
Clough, E., Tedeschi, T. R., & Hazelrigg, T. I. (2014) · Developmental Biology · doi:10.1016/j.ydbio.2014.01.014 · Cited by 53
Polycomb group proteins and MYC: the cancer connection
Benetatos, L., Vartholomatos, G., & Hatzimichael, E. C. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1426-x · Cited by 57
Gannon, O. M., de Long, L. M., Endo‐Munoz, L., Hazar-Rethinam, M. H., & Saunders, N. A. (2012) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-12-2505 · Cited by 58
Sen, N. (2014) · NeuroMolecular Medicine · doi:10.1007/s12017-014-8306-x · Cited by 58
Maina, P. K., Shao, P., Liu, Q., Fazli, L., Tyler, S. R., Nasir, M., Dong, X., & Qi, H. H. (2016) · Oncotarget · doi:10.18632/oncotarget.12310 · Cited by 56
Duchenne muscular dystrophy: an updated review of common available therapies
Salmaninejad, A., Valilou, S. F., Bayat, H., Ebadi, N., Daraei, A., Yousefi, M., Nesaei, A., & Mojarrad, M. (2018) · International Journal of Neuroscience · doi:10.1080/00207454.2018.1430694 · Cited by 59
Drug design targeting active posttranslational modification protein isoforms
Meng, F., Liang, Z. T., Zhao, K., & Luo, C. (2020) · Medicinal Research Reviews · doi:10.1002/med.21774 · Cited by 56
Wang, Y., Feng, L., Ji, P., Liu, J.-H., Guo, S., Zhai, Y., Sankey, E. W., Wang, Y., Xue, Y., Wang, N., et al. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2020.602553 · Cited by 55
Tang, Y., Cui, G., Liu, H., Han, Y., Cai, C., Feng, Z., Shen, H., & Zeng, S. (2024) · 癌症:英文版 · doi:10.1002/cac2.12546 · Cited by 56
Nickel and Epigenetic Gene Silencing
Sun, H., SHAMY, M. Y., & Costa, M. (2013) · Genes · doi:10.3390/genes4040583 · Cited by 57
Role of diet in prostate cancer: the epigenetic link
Labbé, D. P., Zadra, G., Ebot, E. M., Mucci, L. A., Kantoff, P. W., Loda, M. F., & Brown, M. A. (2014) · Oncogene · doi:10.1038/onc.2014.422 · Cited by 56
H3K27me3 is an Epigenetic Mark of Relevance in Endometriosis
Colón-Caraballo, M., Monteiro, J. B., & Flores, I. (2015) · Reproductive Sciences · doi:10.1177/1933719115578924 · Cited by 55
Seebacher, F., Holmes, S. P., Roosen, N. J., Nouvian, M., Wilson, R. S., & Ward, A. J. W. (2012) · Functional Ecology · doi:10.1111/j.1365-2435.2012.02052.x · Cited by 55
Upregulated SMYD3 promotes bladder cancer progression by targeting BCLAF1 and activating autophagy
Shen, B., Tan, M., Mu, X., Yan, Q., Zhang, F., Liu, Y., & Fan, Y. (2015) · Tumor Biology · doi:10.1007/s13277-015-4410-2 · Cited by 57
Epigenetic dysregulation in hepatocellular carcinoma: an up‐to‐date review
Nakamura, M., Chiba, T., Kanayama, K., Kanzaki, H., Saito, T., Kusakabe, Y., & Kato, N. (2018) · Hepatology Research · doi:10.1111/hepr.13250 · Cited by 55
The impact of histone post-translational modifications in neurodegenerative diseases
Cobos, S. N., Bennett, S. A., & Torrente, M. P. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.10.019 · Cited by 53
Small molecule modulators of chromatin remodeling: from neurodevelopment to neurodegeneration
Jiang, D., Li, T., Guo, C., Tang, T.-S., & Liu, H. (2023) · Cell & Bioscience · doi:10.1186/s13578-023-00953-4 · Cited by 54
Epigenetic Modulating Agents as a New Therapeutic Approach in Multiple Myeloma
Maes, K., Menu, E., Valckenborgh, E. V., Riet, I. V., Vanderkerken, K., & Bruyne, E. D. (2013) · Cancers · doi:10.3390/cancers5020430 · Cited by 52
Zhang, F., Xu, D., Yuan, L., Sun, Y., & Xu, Z. (2014) · Nature Communications · doi:10.1038/ncomms6815 · Cited by 55
Folate deficiency affects histone methylation
Garcia, B. A., Luka, Z., Loukachevitch, L. V., Bhanu, N. V., & Wagner, C. (2016) · Medical Hypotheses · doi:10.1016/j.mehy.2015.12.027 · Cited by 54
Zhou, D., Kannappan, V., Chen, X. '., Li, J., Leng, X., Zhang, J., & Xuan, S.-Y. (2016) · Experimental & Molecular Medicine · doi:10.1038/emm.2016.37 · Cited by 54
Cheng, X., Yuan, H., Shu, W., Zhao, M., Zhao, C. N., Wu, Y., Peng, X.-D., Yao, P.-F., Xiao, D., Qing, G., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.778001 · Cited by 54
A Drosophila Model of Intellectual Disability Caused by Mutations in the Histone Demethylase KDM5
Zamurrad, S., Hatch, H. A. M., Drelon, C., Belálcazar, H. M., & Secombe, J. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.02.018 · Cited by 55
Targeting of epigenetic regulators in neuroblastoma
Jubierre, L., Jiménez, C., Rovira, E., Soriano, A., Sábado, C., Gros, L., Llort, A., Hladun, R., Roma, J. M., de Toledo, J. S., et al. (2018) · Experimental & Molecular Medicine · doi:10.1038/s12276-018-0077-2 · Cited by 60
Chen, X. '., Liu, X., Zhang, Y., Huai, W., Zhou, Q., Xu, S., Chen, X., Li, N., & Cao, X. (2018) · Cellular and Molecular Immunology · doi:10.1038/s41423-018-0170-4 · Cited by 55
Lysine methylation signaling of non-histone proteins in the nucleus
Levy, D. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03142-0 · Cited by 56
Kinetic characterization of human histone H3 lysine 36 methyltransferases, ASH1L and SETD2
Eram, M. S., Kuznetsova, E., Li, F., Lima‐Fernandes, E., Kennedy, S., Chau, I., Arrowsmith, C. H., Schapira, M., & Vedadi, M. (2015) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2015.05.013 · Cited by 56
Crosstalk Between Inflammatory Signaling and Methylation in Cancer
Das, D., Karthik, N., & Taneja, R. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.756458 · Cited by 54
Oktyabri, D., Ishimura, A., Tange, S., Terashima, M., & Suzuki, T. (2016) · Biochimie · doi:10.1016/j.biochi.2016.01.005 · Cited by 52
Targeting HDAC Complexes in Asthma and COPD
Zwinderman, M. R. H., de Weerd, S., & Dekker, F. J. (2019) · Epigenomes · doi:10.3390/epigenomes3030019 · Cited by 52
Regulation of epigenetic homeostasis in uveal melanoma and retinoblastoma
Chai, P., Jia, R., Li, Y., Zhou, C., Gu, X., Yang, L., Shi, H., Tian, H., Lin, H., Yu, J., et al. (2021) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2021.101030 · Cited by 56
RNA methylation in plants: An overview
Shinde, H., Dudhate, A., Kadam, U. S., & Hong, J. C. (2023) · Frontiers in Plant Science · doi:10.3389/fpls.2023.1132959 · Cited by 50
Role of somatic cancer mutations in human protein lysine methyltransferases
Kudithipudi, S., & Jeltsch, A. (2014) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2014.08.002 · Cited by 55
Seebacher, F., & Grigaltchik, V. S. (2014) · PLoS ONE · doi:10.1371/journal.pone.0106492 · Cited by 52
Huang, B., Ray, P. D., Iwasaki, K., & Tsuji, Y. (2013) · The FASEB Journal · doi:10.1096/fj.12-226043 · Cited by 52
Quinazoline Based HDAC Dual Inhibitors as Potential Anti-Cancer Agents
Dhuguru, J., & Ghoneim, O. (2022) · Molecules · doi:10.3390/molecules27072294 · Cited by 53
Effects of Histone Modification in Major Depressive Disorder
Wu, M.-S., Li, X., Liu, C., Xu, Q., Huang, J., Gu, S., & Chen, J. (2021) · Current Neuropharmacology · doi:10.2174/1570159x19666210922150043 · Cited by 56
Epigenetics and Beyond: Targeting Histone Methylation to Treat Type 2 Diabetes Mellitus
Yang, Y., Luan, Y., Feng, Q., Chen, X., Qin, B., Ren, K., & Luan, Y. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.807413 · Cited by 51
Cruz, E. Y. H., Arancibia‐Hernández, Y. L., Loyola-Mondragón, D. Y., & Pedraza‐Chaverrí, J. (2022) · Oxygen · doi:10.3390/oxygen2020015 · Cited by 59
Mitochondrial Genetic and Epigenetic Regulations in Cancer: Therapeutic Potential
Wagner, A., Kosnacova, H., Chovanec, M., & Jurkovičová, D. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23147897 · Cited by 54
Three distinct Atoh1 enhancers cooperate for sound receptor hair cell development
Luo, Z., Du, Y., Li, S., Zhang, H., Shu, M., Zhang, D., He, S., Wang, G., Lu, F., & Liu, Z. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2119850119 · Cited by 46
Li, J., Braganza, A., & Sobol, R. W. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.5107 · Cited by 50
Epigenetic regulation in heart failure
Kim, S. Y., Morales, C. R., Gillette, T. G., & Hill, J. A. (2016) · Current Opinion in Cardiology · doi:10.1097/hco.0000000000000276 · Cited by 49
A Genetically Encoded Allysine for the Synthesis of Proteins with Site‐Specific Lysine Dimethylation
Wang, Z. A., Zeng, Y., Kurra, Y., Wang, X., Tharp, J. M., Vatansever, E. C., Hsu, W. W., Dai, S. Y., Fang, X., & Liu, W. R. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201609452 · Cited by 51
Histone methylation in the freeze-tolerant wood frog (Rana sylvatica)
Hawkins, L. J., & Storey, K. B. (2017) · Journal of Comparative Physiology B · doi:10.1007/s00360-017-1112-7 · Cited by 54
Targeting histone methyltransferase and demethylase in acute myeloid leukemia therapy
Castelli, G., Pelosi, E., & Testa, U. (2017) · OncoTargets and Therapy · doi:10.2147/ott.s145971 · Cited by 51
Metadata
- Authors
- Greer, E. L., & Shi, Y.
- Affiliations
- Boston Children's Hospital (US)
- Corresponding author
- Shi, Yang
- Venue
- Nature Reviews Genetics
- Published
- 2012-04-03
- Volume
- 13
- Issue
- 5
- Pages
- 343-357
- ISSN
- 1471-0056 (ISSN-L)
- 1471-0064
- PMC
- PMC4073795
- OpenAlex
- W2009858080
- Cited by
- 2,241
- References
- 277
- Citations by year
- 2026: 95 · 2025: 195 · 2024: 173 · 2023: 175 · 2022: 175 · 2021: 167 · 2020: 178 · 2019: 165 · 2018: 164 · 2017: 157 · 2016: 158 · 2015: 149 · 2014: 147 · 2013: 104 · 2012: 38
- FWCI
- 12.84
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Reviews Genetics (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- U.S. Public Health Service (NCI118487)
- National Cancer Institute (R01CA118487)
- National Institute of General Medical Sciences (GM058012, R01GM071004, R01GM058012, GM071004)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer-related gene regulation
- Keywords
- histone methylation, epigenetic regulation, chromatin modification, gene expression regulation, cell identity, development (biology), disease, aging, heredity (biology), transgenerational epigenetic inheritance, histone demethylation
- MeSH terms
- Histone Methyltransferases, Animals, Caenorhabditis, Drosophila, Female, Histones, Humans, Male, Methylation, Neoplasms, Histone-Lysine N-Methyltransferase, Protein Processing, Post-Translational, Epigenesis, Genetic, Mice, Rats, Histone Demethylases
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