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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.
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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.
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Sorted by citations
Items 801–900 of 1,002
Simithy, J., Sidoli, S., & Garcia, B. A. (2018) · PROTEOMICS · doi:10.1002/pmic.201700309 · Cited by 31
Identification of SUV39H2 as a potential oncogene in lung adenocarcinoma
Zheng, Y., Li, B., Wang, J., Xiong, Y., Wang, K., Qi, Y., Sun, H., Wu, L., & Yang, L. (2018) · Clinical Epigenetics · doi:10.1186/s13148-018-0562-4 · Cited by 29
Zhang, Y., Yan, L., Yao, W., Chen, K., Xu, H., & Ye, Z. (2019) · Medical Science Monitor · doi:10.12659/msm.912294 · Cited by 30
The current status of blood epigenetic biomarkers for dementia
Fransquet, P., & Ryan, J. L. (2019) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408363.2019.1639129 · Cited by 30
Serganova, I. S., Chakraborty, S., Yamshon, S., Isshiki, Y., Bucktrout, R., Melnick, A. M., Béguelin, W., & Zappasodi, R. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.805195 · Cited by 30
Epigenetic biomarkers in aging and longevity: Current and future application
Izadi, M., Sadri, N., Abdi, A., Serajian, S., Jalalei, D., & Tahmasebi, S. (2024) · Life Sciences · doi:10.1016/j.lfs.2024.122842 · Cited by 32
Shimazu, T., Furuse, T., Balan, S., Yamada, I., Okuno, S., Iwanari, H., Suzuki, T., Hamakubo, T., Dohmae, N., Yoshikawa, T., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-19615-4 · Cited by 29
Ngwa, C. J., Kiesow, M. J., Orchard, L., Farrukh, A., Llinás, M., & Pradel, G. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20205087 · Cited by 29
Liu, Q., Borcherding, N. C., Shao, P., Maina, P. K., Zhang, W., & Qi, H. H. (2020) · EBioMedicine · doi:10.1016/j.ebiom.2019.102612 · Cited by 30
The Mitochondrial Protein VDAC1 at the Crossroads of Cancer Cell Metabolism: The Epigenetic Link
Amsalem, Z., Arif, T., Shteinfer‐Kuzmine, A., Caspi, V. C., & Shoshan‐Barmatz, V. (2020) · Cancers · doi:10.3390/cancers12041031 · Cited by 30
Pereira, D., Richert, A., Medjkane, S., Hénon, S., & Weitzman, J. B. (2020) · Scientific Reports · doi:10.1038/s41598-020-75833-9 · Cited by 29
Histone Modifications and Chondrocyte Fate: Regulation and Therapeutic Implications
Wan, C., Zhang, F., Yao, H., Li, H., & Tuan, R. S. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.626708 · Cited by 31
Histone methyltransferase Smyd2 contributes to blood‐brain barrier breakdown in stroke
Wang, J., Zhong, W., Cheng, Q., Xiao, C., Xu, J., Su, Z., Su, H., & Liu, X. (2022) · Clinical and Translational Medicine · doi:10.1002/ctm2.761 · Cited by 29
The Role of Epigenetic Modifications in Late Complications in Type 1 Diabetes
Kern, B. Č., Podkrajšek, K. T., Kovač, J., Šket, R., Bizjan, B. J., Tesovnik, T., Debeljak, M., Battelino, T., & Bratina, N. (2022) · Genes · doi:10.3390/genes13040705 · Cited by 30
The function of histone methylation and acetylation regulators in GBM pathophysiology
McCornack, C. R., Woodiwiss, T. R., Hardi, A., Yano, H., & Kim, A. H. (2023) · Frontiers in Oncology · doi:10.3389/fonc.2023.1144184 · Cited by 33
Histone methyltransferase Dot1L plays a role in postembryonic development in Xenopus tropicalis
Wen, L., Fu, L., Guo, X., Chen, Y., & Shi, Y. (2014) · The FASEB Journal · doi:10.1096/fj.14-252171 · Cited by 29
Self-citationEmerging roles for histone modifications in DNA excision repair
Mao, P., & Wyrick, J. J. (2016) · FEMS Yeast Research · doi:10.1093/femsyr/fow090 · Cited by 31
Małecki, J., Willemen, H. L. D. M., Pinto, R., Ho, A. Y. Y., Moen, A. R., Kjønstad, I. F., Burgering, B. M. T., Zwartkruis, F. J. T., Eijkelkamp, N., & Falnes, P. Ø. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005473 · Cited by 29
Epigenetic Modifications and Neurodegenerative Disorders: A Biochemical Perspective
Zhang, X., Zhang, J., Wang, Y., Wang, M., Tang, M., Lin, Y.-H., & Liu, Q. (2022) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00701 · Cited by 28
A bacteriocyte symbiont determines whitefly sex ratio by regulating mitochondrial function
Yao, Y. T., Ma, X., Wang, T., Yan, J.-Y., Chen, N., Hong, J., Liu, B., Xu, Z.-Q., Zhang, N., Lv, C., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112102 · Cited by 28
Epigenetics of Fear, Anxiety and Stress – Focus on Histone Modifications
Ell, M. A., Schiele, M. A., Iovino, N., & Domschke, K. (2023) · Current Neuropharmacology · doi:10.2174/1570159x21666230322154158 · Cited by 29
EED regulates epithelial–mesenchymal transition of cancer cells induced by TGF-β
Oktyabri, D., Tange, S., Terashima, M., Ishimura, A., & Suzuki, T. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.09.082 · Cited by 28
A positive role for polycomb in transcriptional regulation via H4K20me1
Lv, X., Han, Z., Chen, H., Yang, B., Yang, X., Xia, Y., Pan, C., Fu, L., Zhang, S., Han, H. L., et al. (2016) · Cell Research · doi:10.1038/cr.2016.33 · Cited by 28
Oncogenic roles of the SETDB2 histone methyltransferase in gastric cancer
Nishikawaji, T., Akiyama, Y., Shimada, S., Kojima, K., Kawano, T., Eishi, Y., Yuasa, Y., & Tanaka, S. (2016) · Oncotarget · doi:10.18632/oncotarget.11625 · Cited by 29
Hypoxia and Hormone-Mediated Pathways Converge at the Histone Demethylase KDM4B in Cancer
Yang, J., Harris, A. L., & Davidoff, A. M. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19010240 · Cited by 30
Li, L., Miao, W., Huang, M., Williams, P. B., & Wang, Y. (2018) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra118.000957 · Cited by 28
The Histone Demethylase JMJD1C Regulates CAMKK2-AMPK Signaling to Participate in Cardiac Hypertrophy
Shuang, Y., Li, Y., Zhao, H., Wang, Q., & Chen, P. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00539 · Cited by 28
Lysine demethylase 2A expression in cancer-associated fibroblasts promotes breast tumour growth
Chen, J., Li, C., Lai, Y.-S., & Hung, W. (2020) · British Journal of Cancer · doi:10.1038/s41416-020-01112-z · Cited by 28
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HDAC1 SUMOylation promotes Argonaute-directed transcriptional silencing in C. elegans
Kim, H., Ding, Y., Zhang, G., Yan, Y., Conte, D., Dong, M., & Mello, C. C. (2021) · eLife · doi:10.7554/elife.63299 · Cited by 27
Verdikt, R., & Allard, P. (2021) · Biology of Reproduction · doi:10.1093/biolre/ioab118 · Cited by 25
Epigenetic regulation of inflammatory factors in adipose tissue
Jung, B. C., & Kang, S. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2021.159019 · Cited by 28
Drug discovery of histone lysine demethylases (KDMs) inhibitors (progress from 2018 to present)
He, X., Zhang, H., Zhang, Y., Ye, Y., Wang, S., Bai, R., Xie, T., & Ye, X. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114143 · Cited by 28
Epi‐miRNAs : Modern mediators of methylation status in human cancers
Papadimitriou, M., Panoutsopoulou, K., Pilala, K., Scorilas, A., & Avgeris, M. (2022) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1735 · Cited by 29
Role of histone modification in the occurrence and development of osteoporosis
Sun, P., Huang, T., Huang, C., Wang, Y., & Tang, D. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.964103 · Cited by 27
Epigenetic regulation of autophagy by histone-modifying enzymes under nutrient stress
Yu, Y. S., Kim, H.-K., Kim, K. I., & Baek, S. H. (2023) · Cell Death and Differentiation · doi:10.1038/s41418-023-01154-9 · Cited by 31
Neuroepigenetics of ageing and neurodegeneration-associated dementia: An updated review
Mir, F. A., Amanullah, A., Jain, B. P., Hyderi, Z., & Gautam, A. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.102067 · Cited by 30
Perez, M. F., & Sarkies, P. (2023) · PLoS Biology · doi:10.1371/journal.pbio.3002354 · Cited by 31
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Yan, B., Yao, J., Tao, Z.-F., & Jiang, Q. L. (2013) · Journal of Cellular Physiology · doi:10.1002/jcp.24522 · Cited by 28
Mariani, L. L., Lussi, Y., Vandamme, J., Riveiro, A. R., & Salcini, A. E. (2016) · Development · doi:10.1242/dev.132985 · Cited by 26
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Deng, X., Liang, S., Tang, Y., Li, Y., Xu, R., Lu, L., Wang, Q., Zhang, X., & Liu, Y. (2024) · Environmental Pollution · doi:10.1016/j.envpol.2024.123393 · Cited by 27
Hua, W., Han, X., Li, F., Lu, L., Sun, Y., Hassanian‐Moghaddam, H., Tian, M., Lu, Y.-Y., & Huang, Q. (2024) · Environmental Science & Technology · doi:10.1021/acs.est.3c07989 · Cited by 27
Piao, L., Nakakido, M., Suzuki, T., Dohmae, N., Nakamura, Y., & Hamamoto, R. (2016) · Oncotarget · doi:10.18632/oncotarget.8072 · Cited by 27
Analysis of the role of mutations in the KMT 2D histone lysine methyltransferase in bladder cancer
Ding, B., Yan, L., Zhang, Y., Wang, Z., Zhang, Y., Ding, X., Ye, Z., & Xu, H. (2019) · FEBS Open Bio · doi:10.1002/2211-5463.12600 · Cited by 27
Waves of chromatin modifications in mouse dendritic cells in response to LPS stimulation
Vandenbon, A., Kumagai, Y., Lin, M., Suzuki, Y., & Nakai, K. (2018) · Genome biology · doi:10.1186/s13059-018-1524-z · Cited by 28
Zhou, S., Feng, S., Qin, W., Wang, X., Tang, Y., & Yuan, S. (2020) · Stem Cell Reviews and Reports · doi:10.1007/s12015-020-10044-3 · Cited by 29
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Coppedè, F. (2021) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2021.1916469 · Cited by 30
Yu, Y., Tan, P., Zhuang, Z., Wang, Z., Zhu, L., Qiu, R., & Xu, H. (2021) · BMC Medical Genomics · doi:10.1186/s12920-021-00962-7 · Cited by 27
Dynamic changes of histone methylation in mammalian oocytes and early embryos
Bilmez, Y., Talibova, G., & Öztürk, S. (2021) · Histochemistry and Cell Biology · doi:10.1007/s00418-021-02036-2 · Cited by 27
Ho, L., Hossen, M. N., Nguyen, T. B., Vo, A., & Ahsan, F. (2022) · Biomedicines · doi:10.3390/biomedicines10010170 · Cited by 27
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Wu, W.-F., Lin, J.-T., Qiu, Y.-K., Dong, W., Wan, J., Li, S., Zheng, H., & Wu, Y.-Q. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101983 · Cited by 28
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Andreoli, F., & Río, A. D. (2014) · Drug Discovery Today · doi:10.1016/j.drudis.2014.05.005 · Cited by 29
Histone lysine demethylases in Drosophila melanogaster
Holowatyj, A., Yang, Z.-Q., & Pile, L. A. (2015) · Fly · doi:10.1080/19336934.2015.1074787 · Cited by 27
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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
Li, F., Ortega, J., Gu, L., & Li, G. (2015) · DNA repair · doi:10.1016/j.dnarep.2015.11.021 · Cited by 27
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Milite, C., Feoli, A., Viviano, M., Rescigno, D., Mai, A., Castellano, S., & Sbardella, G. (2016) · ChemMedChem · doi:10.1002/cmdc.201600272 · Cited by 27
Duan, J. E., Zhu, L., Dong, H., Zheng, X., Jiang, Z., Chen, J., & Tian, X. (2019) · Scientific Reports · doi:10.1038/s41598-018-38083-4 · Cited by 30
Samec, M., Líšková, A., Koklesová, L., Mešťanová, V., Franekova, M., Kassayová, M., Bojková, B., Uramova, S., Žúbor, P., Janíková, K., et al. (2019) · Biomolecules · doi:10.3390/biom9120829 · Cited by 27
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Sopić, M., Robinson, E. L., Emanueli, C., Srivastava, P. K., Angione, C., Gaetano, C., Condorelli, G., Martelli, F., Pedrazzini, T., Devaux, Y., et al. (2023) · Basic Research in Cardiology · doi:10.1007/s00395-023-00986-3 · Cited by 28
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Ocaña-Paredes, B., Rivera-Orellana, S., Ramírez-Sánchez, D., Montalvo-Guerrero, J., Freire, M. P., Espinoza-Ferrao, S., Altamirano-Colina, A., Echeverría-Espinoza, P., Ramos-Medina, M. J., Echeverría‐Garcés, G., et al. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1381168 · Cited by 28
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Tan, W. Y., Nagabhyrava, S., Ang-Olson, O., Das, P., Ladel, L., Sailo, B., He, L., Sharma, A. R., & Ahuja, N. (2024) · Current Issues in Molecular Biology · doi:10.3390/cimb46070390 · Cited by 28
Dietz, K. N., Stefano, L. D., Maher, R. C., Zhu, H., MacDonald, M. E., Gusella, J. F., & Walker, J. A. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu446 · Cited by 28
Liu, D., & Zempleni, J. (2014) · Genes & Nutrition · doi:10.1007/s12263-014-0422-6 · Cited by 25
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Yan, H., Tian, S., Slager, S. L., Sun, Z., & Ördög, T. (2015) · American Journal of Epidemiology · doi:10.1093/aje/kwv187 · Cited by 26
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Fratta, E., Montico, B., Rizzo, A., Colizzi, F., Sigalotti, L., & Dolcetti, R. (2016) · Oncotarget · doi:10.18632/oncotarget.10033 · Cited by 26
Glastad, K. M., Chau, L. M., & Goodisman, M. A. D. (2015) · Advances in insect physiology · doi:10.1016/bs.aiip.2014.12.007 · Cited by 26
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Jeon, J., McGinty, R. K., Muir, T. W., Kim, J., & Kim, J. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky920 · Cited by 29
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Kushwaha, A., & Thakur, M. K. (2019) · Biogerontology · doi:10.1007/s10522-019-09850-1 · Cited by 28
Al‐Ghabkari, A., & Narendran, A. (2021) · Cancer Biology & Therapy · doi:10.1080/15384047.2021.1902913 · Cited by 26
Balan, S., Iwayama, Y., Ohnishi, T., Fukuda, M., Shirai, A., Yamada, A., Weirich, S., Schuhmacher, M. K., Dileep, K. V., Endo, T., et al. (2021) · Molecular Psychiatry · doi:10.1038/s41380-021-01199-7 · Cited by 25
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Swift, C. L., Louie, K., Bowen, B. P., Hooker, C. A., Solomon, K., Singan, V. R., Daum, C. G., Pennacchio, C., Barry, K., Shutthanandan, V. S., et al. (2021) · mBio · doi:10.1128/mbio.01442-21 · Cited by 30
Leonen, C. J. A., Shimada, M., Weller, C. E., Nakadai, T., Hsu, P., Tyson, E. L., Mishra, A., Shelton, P. M., Sadilek, M., Hawkins, R. D., et al. (2021) · eLife · doi:10.7554/elife.67952 · Cited by 26
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Yang, J., Hu, Y., Zhang, B., Liang, X., & Li, X. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.881396 · Cited by 26
Lam, M. S. Y., Reales‐Calderón, J. A., Ow, J. R., Aw, J., Tan, D., Vijayakumar, R., Ceccarello, E., Tabaglio, T., Lim, Y. T., Chien, W. L., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36160-5 · Cited by 26
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Suzuki, T., Terashima, M., Tange, S., & Ishimura, A. (2013) · Cancer Science · doi:10.1111/cas.12169 · Cited by 26
Capell, B. C., & Berger, S. L. (2013) · Journal of Investigative Dermatology · doi:10.1038/jid.2013.173 · Cited by 31
Utx loss causes myeloid transformation
Zheng, L., Xu, L., Xu, Q., Yu, L., Zhao, D., Chen, P., Wang, W., Wang, Y., Han, G., & Chen, C. D. (2018) · Leukemia · doi:10.1038/s41375-018-0011-6 · Cited by 26
Jones, D., Wilson, L., Thomas, H., Gaughan, L., & Wade, M. (2019) · Cancers · doi:10.3390/cancers11081122 · Cited by 23
Gsell, C., Richly, H., Coin, F., & Naegeli, H. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz1229 · Cited by 26
Niwa, H., Sato, S., Handa, N., Sengoku, T., Umehara, T., & Yokoyama, S. (2020) · ChemMedChem · doi:10.1002/cmdc.202000014 · Cited by 26
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Coneys, R., & Wood, I. C. (2020) · Neurodegenerative Disease Management · doi:10.2217/nmt-2019-0034 · Cited by 26
Gregory, B. L., & Cheung, V. G. (2013) · Genome Research · doi:10.1101/gr.156141.113 · Cited by 28
Garrett-Bakelman, F. E., & Melnick, A. M. (2016) · Epigenomics · doi:10.2217/epi-2016-0008 · Cited by 25
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Oh, C. K., & Cho, Y. (2024) · Intestinal Research · doi:10.5217/ir.2023.00115 · Cited by 24
Epigenetic biomarkers in Alzheimer's disease: Diagnostic and prognostic relevance
Behl, T., Kyada, A., Roopashree, R., Nathiya, D., Arya, R., Kumar, M., Khalid, M., Gulati, M., Sachdeva, M., Fareed, M., et al. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102556 · Cited by 31
Maher, N., Maiellaro, F., Ghanej, J., Rasi, S., Moia, R., & Gaïdano, G. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26178132 · Cited by 25
Song, M.-J., Kim, M.-K., Choi, Y., Yi, M., Kim, J., Park, S., Yong, T., & Kim, H. (2017) · Scientific Reports · doi:10.1038/srep45365 · Cited by 25
Methylation-Demethylation Dynamics: Implications of Changes in Acute Kidney Injury
Chakraborty, A., & Viswanathan, P. (2018) · Analytical Cellular Pathology · doi:10.1155/2018/8764384 · Cited by 26
Zhang, D., Meng, Y.-R., & Zhang, C. (2019) · Chemical Communications · doi:10.1039/c9cc09019c · Cited by 25
Chen, Y., Liao, L., Wu, Z., Yang, Q., Guo, J., He, J., Wang, S., Xu, X., Wu, J., Pan, F., et al. (2020) · Aging · doi:10.18632/aging.102686 · Cited by 26
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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
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