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
Histone Lysine Methylation Dynamics: Establishment, Regulation, and Biological Impact
Black, J. C., Rechem, C. V., & Whetstine, J. R. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.11.006 · Cited by 1,391
Writing, erasing and reading histone lysine methylations
Hyun, K., Jeon, J., Park, K., & Kim, J. (2017) · Experimental & Molecular Medicine · doi:10.1038/emm.2017.11 · Cited by 1,250
Cancer Genetics and Epigenetics: Two Sides of the Same Coin?
You, J. S., & Jones, P. A. (2012) · Cancer Cell · doi:10.1016/j.ccr.2012.06.008 · Cited by 1,206
Grünewald, T. G. P., Cidre-Aranaz, F., Surdez, D., Tomazou, E. M., de Álava, E., Kovar, H., Sorensen, P. H., Delattre, O., & Dirksen, U. (2018) · Nature Reviews Disease Primers · doi:10.1038/s41572-018-0003-x · Cited by 873
Bender, S., Tang, Y., Lindroth, A. M., Hovestadt, V., Jones, D. T. W., Kool, M., Zapatka, M., Northcott, P. A., Sturm, D., Wang, W., et al. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.10.006 · Cited by 818
Epigenetics of colorectal cancer: biomarker and therapeutic potential
Jung, G., Hernández-Illán, E., Moreira, L., Balaguer, F., & Goel, A. (2020) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/s41575-019-0230-y · Cited by 813
Metabolic reprogramming and epigenetic modifications on the path to cancer
Sun, L., Zhang, H., & Gao, P. (2021) · Protein & Cell · doi:10.1007/s13238-021-00846-7 · Cited by 818
Distinct features of H3K4me3 and H3K27me3 chromatin domains in pre-implantation embryos
Liu, X., Wang, C., Liu, W., Li, J., Li, C., Kou, X., Chen, J., Zhao, Y., Gao, H., Wang, H., et al. (2016) · Nature · doi:10.1038/nature19362 · Cited by 746
Interpreting the language of histone and DNA modifications
Rothbart, S. B., & Strahl, B. D. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.03.001 · Cited by 792
DNA Methylation on N6-Adenine in C. elegans
Greer, E. L., Blanco, M. A., Gu, L., Sendinc, E., Liu, J., Aristizábal-Corrales, D., Hsu, C.-H., Aravind, L., He, C., & Shi, Y. (2015) · Cell · doi:10.1016/j.cell.2015.04.005 · Cited by 725
Self-citationHistone Methylation Dynamics and Gene Regulation Occur through the Sensing of One-Carbon Metabolism
Mentch, S. J., Mehrmohamadi, M., Huang, L., Liu, X., Gupta, D., Mattocks, D. A. L., Padilla, P. G., Ables, G. P., Bamman, M. M., Thalacker‐Mercer, A. E., et al. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.08.024 · Cited by 706
Medulloblastomics: the end of the beginning
Northcott, P. A., Jones, D., Kool, M., Robinson, G. W., Gilbertson, R. J., Cho, Y., Pomeroy, S. L., Korshunov, A., Lichter, P., Taylor, M. D., et al. (2012) · Nature reviews. Cancer · doi:10.1038/nrc3410 · Cited by 688
Salinomycin kills cancer stem cells by sequestering iron in lysosomes
Mai, T. T., Hamaï, A., Hienzsch, A., Cañeque, T., Müller, S., Wicinski, J., Cabaud, O., Leroy, C., David, A., Acevedo, V., et al. (2017) · Nature Chemistry · doi:10.1038/nchem.2778 · Cited by 621
Epigenetic regulation of ageing: linking environmental inputs to genomic stability
Benayoun, B. A., Pollina, E. A., & Brunet, A. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm4048 · Cited by 610
Highly evolvable malaria vectors: The genomes of 16 Anopheles mosquitoes
Neafsey, D. E., Waterhouse, R. M., Abai, M. R., Aganezov, S. S., Alekseyev, M. A., Allen, J. E., Amon, J., Arcà, B., Arensburger, P., Николаевич, А. Г., et al. (2014) · Science · doi:10.1126/science.1258522 · Cited by 573
Epigenetic modifications of histones in cancer
Zhao, Z., & Shilatifard, A. (2019) · Genome biology · doi:10.1186/s13059-019-1870-5 · Cited by 591
Constitutive heterochromatin formation and transcription in mammals
Saksouk, N., Simboeck, E., & Déjardin, J. (2015) · Epigenetics & Chromatin · doi:10.1186/1756-8935-8-3 · Cited by 607
Interplay between Metabolism and Epigenetics: A Nuclear Adaptation to Environmental Changes
Etchegaray, J., & Mostoslavsky, R. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.05.029 · Cited by 546
The impact of cellular metabolism on chromatin dynamics and epigenetics
Reid, M. A., Dai, Z., & Locasale, J. W. (2017) · Nature Cell Biology · doi:10.1038/ncb3629 · Cited by 515
Regulation of chromatin and gene expression by metabolic enzymes and metabolites
Li, X., Egervári, G., Wang, Y., Berger, S. L., & Lu, Z. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0029-7 · Cited by 491
Overview of Histone Modification
Zhang, Y., Sun, Z., Jia, J., Du, T., Zhang, N., Tang, Y., Fang, Y., & Fang, D. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-981-15-8104-5_1 · Cited by 530
Global profiling of lysine reactivity and ligandability in the human proteome
Hacker, S. M., Backus, K. M., Lazear, M. R., Forli, S., Correia, B. E., & Cravatt, B. F. (2017) · Nature Chemistry · doi:10.1038/nchem.2826 · Cited by 485
Histone modifications for human epigenome analysis
Kimurâ, H. (2013) · Journal of Human Genetics · doi:10.1038/jhg.2013.66 · Cited by 499
Immunoaffinity Enrichment and Mass Spectrometry Analysis of Protein Methylation
Guo, A., Gu, H., Zhou, J., Mulhern, D., Wang, Y., Lee, K. A., Yang, V., Aguiar, M., Kornhauser, J. M., Jia, X., et al. (2013) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o113.027870 · Cited by 473
Non-histone protein methylation as a regulator of cellular signalling and function
Biggar, K. K., & Li, S. S.-C. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3915 · Cited by 479
KDM2B links the Polycomb Repressive Complex 1 (PRC1) to recognition of CpG islands
Farcas, A. M., Blackledge, N. P., Sudbery, I. M., Long, H. K., McGouran, J. F., Rose, N. R., Lee, S., Sims, D., Cerase, A., Sheahan, T. W., et al. (2012) · eLife · doi:10.7554/elife.00205 · Cited by 502
Histone lysine demethylases as targets for anticancer therapy
Højfeldt, J. W., Agger, K., & Helin, K. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd4154 · Cited by 470
Comprehensive Catalog of Currently Documented Histone ModificationsPreprint
Zhao, Y., & Garcia, B. A. (2015) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a025064 · Cited by 484
Editing the epigenome: technologies for programmable transcription and epigenetic modulation
Thakore, P. I., Black, J. B., Hilton, I. B., & Gersbach, C. A. (2016) · Nature Methods · doi:10.1038/nmeth.3733 · Cited by 451
Zhong, Q., Xiao, X., Qiu, Y., Xu, Z., Chen, C., Chong, B., Zhao, X., Hai, S., Li, S., An, Z., et al. (2023) · MedComm · doi:10.1002/mco2.261 · Cited by 442
Wang, Y., Li, Y., Yue, M., Wang, J., Kumar, S., Wechsler‐Reya, R. J., Zhang, Z., Ogawa, Y., Kellis, M., Duester, G., et al. (2018) · Nature Neuroscience · doi:10.1038/s41593-017-0057-1 · Cited by 439
Struck, A., Thompson, M. L., Wong, L. S., & Micklefield, J. (2012) · ChemBioChem · doi:10.1002/cbic.201200556 · Cited by 428
Gan, L., Yang, Y., Li, Q., Feng, Y., Liu, T., & Guo, W.-J. (2018) · Biomarker Research · doi:10.1186/s40364-018-0122-2 · Cited by 440
Protein post-translational modifications in bacteria
Maček, B., Forchhammer, K., Hardouin, J., Weber-Ban, E. U., Grangeasse, C., & Mijakovic̀, I. (2019) · Nature Reviews Microbiology · doi:10.1038/s41579-019-0243-0 · Cited by 433
Th2 Cells in Health and Disease
Nakayama, T., Hirahara, K., Onodera, A., Endo, Y., Hosokawa, H., Shinoda, K., Tumes, D. J., & Okamoto, Y. (2016) · Annual Review of Immunology · doi:10.1146/annurev-immunol-051116-052350 · Cited by 412
Targeting histone methyltransferases and demethylases in clinical trials for cancer therapy
Morera, L., Lübbert, M., & Jung, M. (2016) · Clinical Epigenetics · doi:10.1186/s13148-016-0223-4 · Cited by 412
Epigenetic mechanisms in neurogenesis
Yao, B., Christian, K. M., He, C., Jin, P., Ming, G., & Song, H. (2016) · Nature reviews. Neuroscience · doi:10.1038/nrn.2016.70 · Cited by 406
The epigenetics of aging and neurodegeneration
Lardenoije, R., Iatrou, A., Kenis, G., Kompotis, K., Steinbusch, H. W. M., Mastroeni, D., Coleman, P., Lemere, C. A., Hof, P. R., van den Hove, D. L. A., et al. (2015) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.05.002 · Cited by 381
Click Chemistry in Proteomic Investigations
Parker, C. G., & Pratt, M. R. (2020) · Cell · doi:10.1016/j.cell.2020.01.025 · Cited by 391
Mitochondria and Epigenetics – Crosstalk in Homeostasis and Stress
Matilainen, O., Quirós, P. M., & Auwerx, J. H. (2017) · Trends in Cell Biology · doi:10.1016/j.tcb.2017.02.004 · Cited by 376
An inhibitor of KDM5 demethylases reduces survival of drug-tolerant cancer cells
Vinogradova, M. V., Gehling, V. S., Gustafson, A. E., Arora, S., Tindell, C., WILSON, C. A., Williamson, K. E., Guler, G. D., Gangurde, P., Manieri, W., et al. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2085 · Cited by 363
Chemical reporters for biological discovery
Grammel, M., & Hang, H. C. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1296 · Cited by 351
Use of Epigenetic Drugs in Disease: An Overview
Heerboth, S. A., LAPINSKA, K., Snyder, N., Leary, M., Rollinson, S., & Sarkar, S. (2014) · Genetics & Epigenetics · doi:10.4137/geg.s12270 · Cited by 333
Epigenetics, plasticity, and evolution: How do we link epigenetic change to phenotype?
Duncan, E. J., Gluckman, P. D., & Dearden, P. K. (2014) · Journal of Experimental Zoology Part B Molecular and Developmental Evolution · doi:10.1002/jez.b.22571 · Cited by 329
Regulation of the epigenome by vitamin C
Young, J. I., Züchner, S., & Wang, G. (2015) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-071714-034228 · Cited by 319
SET for life: biochemical activities and biological functions of SET domain-containing proteins
Herz, H.-M., Garruss, A., & Shilatifard, A. (2013) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2013.09.004 · Cited by 314
Fetahu, I. S., Höbaus, J., & Kállay, E. (2014) · Frontiers in Physiology · doi:10.3389/fphys.2014.00164 · Cited by 313
Eight Kinetically Stable but Thermodynamically Activated Molecules that Power Cell Metabolism
Walsh, C. T., Tu, B. P., & Tang, Y. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00510 · Cited by 315
Evolution of Plasticity: Mechanistic Link between Development and Reversible Acclimation
Beaman, J. E., White, C. R., & Seebacher, F. (2016) · Trends in Ecology & Evolution · doi:10.1016/j.tree.2016.01.004 · Cited by 315
CD44 regulates epigenetic plasticity by mediating iron endocytosis
Müller, S., Sindikubwabo, F., Cañeque, T., Lafon, A., Versini, A., Lombard, B., Loew, D., Wu, T., Ginestier, C., Charafe‐Jauffret, E., et al. (2020) · Nature Chemistry · doi:10.1038/s41557-020-0513-5 · Cited by 309
Emerging roles for chromatin as a signal integration and storage platform
Badeaux, A. I., & Shi, Y. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3545 · Cited by 291
Self-citationEpigenetic reprogramming in plant sexual reproduction
Kawashima, T., & Berger, F. (2014) · Nature Reviews Genetics · doi:10.1038/nrg3685 · Cited by 293
Targeting protein modifications in metabolic diseases: molecular mechanisms and targeted therapies
Wu, X., Xu, M., Geng, M., Chen, S., Little, P. J., Xu, S., & Weng, J. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01439-y · Cited by 295
Mozzetta, C., Pontis, J., Fritsch, L., Robin, P., Portoso, M., Proux, C., Margueron, R., & Ait‐Si‐Ali, S. (2014) · Molecular Cell · doi:10.1016/j.molcel.2013.12.005 · Cited by 288
Histone Lysine Methylases and Demethylases in the Landscape of Human Developmental Disorders
Faùndes, V., Newman, W. G., Bernardini, L., Canham, N. L. E., Clayton‐Smith, J., Dallapiccola, B., Davies, S. J., Demos, M. K., Goldman, A. P., Gill, H., et al. (2017) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2017.11.013 · Cited by 274
Targeting Metalloenzymes for Therapeutic Intervention
Chen, A. Y., Adamek, R. N., Dick, B. L., Credille, C. V., Morrison, C. N., & Cohen, S. M. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00201 · Cited by 284
The functional diversity of protein lysine methylation
Lanouette, S., Mongeon, V., Figeys, D., & Couture, J. (2014) · Molecular Systems Biology · doi:10.1002/msb.134974 · Cited by 285
Molecular mechanisms of environmental exposures and human disease
Wu, H., Eckhardt, C. M., & Baccarelli, A. (2023) · Nature Reviews Genetics · doi:10.1038/s41576-022-00569-3 · Cited by 296
Nagarsheth, N., Peng, D., Kryczek, I., Wu, K., Li, W., Zhao, E., Zhao, L., Wei, S., Frankel, T. L., Vatan, L., et al. (2015) · Cancer Research · doi:10.1158/0008-5472.can-15-1938 · Cited by 277
Liu, R., Wu, J., Guo, H., Yao, W., Li, S., Lu, Y., Jia, Y., Liang, X., Tang, J., & Zhang, H. (2023) · MedComm · doi:10.1002/mco2.292 · Cited by 305
Persister cancer cells: Iron addiction and vulnerability to ferroptosis
Rodriguez, R., Schreiber, S. L., & Conrad, M. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.12.001 · Cited by 280
Interplay between epigenetics and metabolism in oncogenesis: mechanisms and therapeutic approaches
Wong, C. C., Qian, Y., & Yu, J. Q. (2017) · Oncogene · doi:10.1038/onc.2016.485 · Cited by 266
Urate‐induced immune programming: Consequences for gouty arthritis and hyperuricemia
Cabău, G., Crișan, T. O., Klück, V., Popp, R. A., & Joosten, L. A. B. (2019) · Immunological Reviews · doi:10.1111/imr.12833 · Cited by 267
Amino acid metabolism in tumor biology and therapy
Chen, J., Cui, L., Lu, S., & Xu, S. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-06435-w · Cited by 277
Epigenetic regulation of Keap1-Nrf2 signaling
Guo, Y., Yu, S., Zhang, C., & Kong, A. T. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.06.013 · Cited by 264
Histone Modifications and Non-Coding RNAs: Mutual Epigenetic Regulation and Role in Pathogenesis
Bure, I. V., Nemtsova, M. V., & Kuznetsova, E. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23105801 · Cited by 277
Saleh, H. A., Yousef, M. H., & Abdelnaser, A. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.606069 · Cited by 269
Epigenetics and Colorectal Cancer Pathogenesis
Bardhan, K., & Liu, K. (2013) · Cancers · doi:10.3390/cancers5020676 · Cited by 266
Histone methylation and the DNA damage response
Gong, F., & Miller, K. M. (2017) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2017.09.003 · Cited by 265
EZH2-Targeted Therapies in Cancer: Hype or a Reality
Eich, M., Athar, M., Ferguson, J. E., & Varambally, S. (2020) · Cancer Research · doi:10.1158/0008-5472.can-20-2147 · Cited by 254
Trials with ‘epigenetic’ drugs: An update
Nebbioso, A., Carafa, V., Benedetti, R., & Altucci, L. (2012) · Molecular Oncology · doi:10.1016/j.molonc.2012.09.004 · Cited by 242
Arginine demethylation is catalysed by a subset of JmjC histone lysine demethylases
Walport, L. J., Hopkinson, R. J., Chowdhury, R., Schiller, R., Ge, W., Kawamura, A., & Schofield, C. J. (2016) · Nature Communications · doi:10.1038/ncomms11974 · Cited by 247
Epigenetics of Aging and Aging-Associated Diseases
Saul, D., & Kosinsky, R. L. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22010401 · Cited by 247
Epigenetic regulation in AKI and kidney repair: mechanisms and therapeutic implications
Guo, C., Dong, G., Liang, X., & Dong, Z. (2019) · Nature Reviews Nephrology · doi:10.1038/s41581-018-0103-6 · Cited by 235
A chemical biology route to site-specific authentic protein modifications
Yang, A., Ha, S., Ahn, J., Kim, R., Kim, S., Lee, Y., Kim, J., Söll, D., Lee, H.-Y., & Park, H.-S. (2016) · Science · doi:10.1126/science.aah4428 · Cited by 232
Inhibition of demethylases by GSK-J1/J4
Heinemann, B., Nielsen, J. M., Hudlebusch, H. R., Lees, M. J., Larsen, D. V., Boesen, T. P., Labelle, M., Gerlach, L., Birk, P., & Helin, K. (2014) · Nature · doi:10.1038/nature13688 · Cited by 233
Xu, B., On, D. M., Ma, A., Parton, T., Konze, K. D., Pattenden, S. G., Allison, D. F., Cai, L., Rockowitz, S., Liu, S., et al. (2014) · Blood · doi:10.1182/blood-2014-06-581082 · Cited by 231
Embryonic stem cell and induced pluripotent stem cell: an epigenetic perspective
Liang, G., & Zhang, Y. (2012) · Cell Research · doi:10.1038/cr.2012.175 · Cited by 232
Putnam, H. M., & Gates, R. D. (2015) · Journal of Experimental Biology · doi:10.1242/jeb.123018 · Cited by 230
PLMD: An updated data resource of protein lysine modifications
Xu, H., Zhou, J., Lin, S., Deng, W., Zhang, Y. W., & Xue, Y. (2017) · Journal of genetics and genomics/Journal of Genetics and Genomics · doi:10.1016/j.jgg.2017.03.007 · Cited by 220
Ramazi, S., Allahverdi, A., & Zahiri, J. (2020) · Journal of Biosciences · doi:10.1007/s12038-020-00099-2 · Cited by 226
Reactivation of latent HIV by histone deacetylase inhibitors
Shirakawa, K., Chávez, L., Hakre, S., Calvanese, V., & Verdin, E. M. (2013) · Trends in Microbiology · doi:10.1016/j.tim.2013.02.005 · Cited by 214
Epigenetic regulation and chromatin remodeling in learning and memory
Kim, S., & Kaang, B. (2017) · Experimental & Molecular Medicine · doi:10.1038/emm.2016.140 · Cited by 217
Undercover: gene control by metabolites and metabolic enzymesPreprint
van der Knaap, J. A., & Verrijzer, C. P. (2016) · Genes & Development · doi:10.1101/gad.289140.116 · Cited by 222
Epigenome Editing: State of the Art, Concepts, and Perspectives
Kungulovski, G., & Jeltsch, A. (2015) · Trends in Genetics · doi:10.1016/j.tig.2015.12.001 · Cited by 212
Ler, L. D., Ghosh, S., Chai, X., Thike, A. A., Heng, H. L., Siew, E. Y., Dey, S., Koh, L. K., Lim, J. Q., Lim, W. K., et al. (2017) · Science Translational Medicine · doi:10.1126/scitranslmed.aai8312 · Cited by 208
The histone LSD1 demethylase in stemness and cancer transcription programs
Amente, S., Lania, L., & Majello, B. (2013) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2013.05.002 · Cited by 207
Putnam, H. M., Davidson, J. M., & Gates, R. D. (2016) · Evolutionary Applications · doi:10.1111/eva.12408 · Cited by 218
Ge, T., Gu, X., Jia, R., Ge, S., Chai, P., Zhuang, A., & Fan, X. (2022) · 癌症:英文版 · doi:10.1002/cac2.12374 · Cited by 220
Disrupted Intricacy of Histone H3K4 Methylation in Neurodevelopmental Disorders
Vallianatos, C. N., & Iwase, S. (2015) · Epigenomics · doi:10.2217/epi.15.1 · Cited by 204
Histone modifications in epigenetic regulation of cancer: Perspectives and achieved progress
Неганова, М. Е., Klochkov, S. G., Aleksandrova, Y. R., & Aliev, G. (2020) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2020.07.015 · Cited by 211
Sound of silence: the properties and functions of repressive Lys methyltransferases
Mozzetta, C., Boyarchuk, E., Pontis, J., & Ait‐Si‐Ali, S. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm4029 · Cited by 217
Terashima, M., Tange, S., Ishimura, A., & Suzuki, T. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.750950 · Cited by 201
The winding path of protein methylation research: milestones and new frontiers
Murn, J., & Shi, Y. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.35 · Cited by 205
Self-citationMechanisms of human histone and nucleic acid demethylases
Walport, L. J., Hopkinson, R. J., & Schofield, C. J. (2012) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2012.09.015 · Cited by 194
Targeting histone lysine demethylases — Progress, challenges, and the future
Thinnes, C. C., England, K. S., Kawamura, A., Chowdhury, R., Schofield, C. J., & Hopkinson, R. J. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.05.009 · Cited by 198
Fang, L., Zhang, L., Wei, W., Jin, X., Wang, P., Tong, Y., Li, J., Du, J. X., & Wong, J. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.06.018 · Cited by 192
Recent Progress in Histone Demethylase Inhibitors
McAllister, T. E., England, K. S., Hopkinson, R. J., Brennan, P. E., Kawamura, A., & Schofield, C. J. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01758 · Cited by 192
Protein methylation at the surface and buried deep: thinking outside the histone box
Clarke, S. G. (2013) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2013.02.004 · Cited by 190
Multiple regulations of Keap1/Nrf2 system by dietary phytochemicals
Qin, S., & Hou, D. (2016) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201501017 · Cited by 191
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