The DOI matches its Crossref record; 237 of the 238 references it cites were found in a registry or an index.
Histone post-translational modifications - cause and consequence of genome function
Abstract
Much has been learned since the early 1960s about histone post-translational modifications (PTMs) and how they affect DNA-templated processes at the molecular level. This understanding has been bolstered in the past decade by the identification of new types of histone PTM, the advent of new genome-wide mapping approaches and methods to deposit or remove PTMs in a locally and temporally controlled manner. Now, with the availability of vast amounts of data across various biological systems, the functional role of PTMs in important processes (such as transcription, recombination, replication, DNA repair and the modulation of genomic architecture) is slowly emerging. This Review explores the contribution of histone PTMs to the regulation of genome function by discussing when these modifications play a causative (or instructive) role in DNA-templated processes and when they are deposited as a consequence of such processes, to reinforce and record the event. Important advances in the field showing that histone PTMs can exert both direct and indirect effects on genome function are also presented.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“These PTMs predominantly occur on the N-terminal histone tails and include acetylation, methylation, phosphorylation, and ubiquitination, forming combinatorial patterns often referred to as the “histone code,” which influences transcription in a context-dependent manner (Millán-Zambrano et al., 2022; Miziak et al., 2024; Jenuwein and Allis, 2001; Lam et al., 2019).”
From Histone modifications and depression: epigenetic mechanisms, therapeutic targets, and translational outlook (2026) · cites this paper as Millán-Zambrano et al., 2022
In the citing paper
“The flexible N-terminal tails of histones protrude from the nucleosome and serve as major sites for post-translational modifications (PTMs), including acetylation, methylation, and phosphorylation (Millán-Zambrano et al., 2022; Le et al., 2023).”
From Histone modifications and depression: epigenetic mechanisms, therapeutic targets, and translational outlook (2026) · cites this paper as Millán-Zambrano et al., 2022
Citations
Cites
Hanahan, D., & Weinberg, R. A. (2000) · Cell · doi:10.1016/s0092-8674(00)81683-9 · Cited by 29,219
Comprehensive Mapping of Long-Range Interactions Reveals Folding Principles of the Human Genome
Lieberman-Aiden, E., van Berkum, N. L., Williams, L., Imakaev, M., Ragoczy, T., Telling, A., Amit, I., Lajoie, B. R., Sabo, P. J., Dorschner, M. O., et al. (2009) · Science · doi:10.1126/science.1181369 · Cited by 8,898
High-Resolution Profiling of Histone Methylations in the Human Genome
Barski, A., Cuddapah, S., Cui, K., Roh, T.-Y., Schones, D. E., Wang, Z., Wei, G., Chepelev, I., & Zhao, K. (2007) · Cell · doi:10.1016/j.cell.2007.05.009 · Cited by 6,845
Topological domains in mammalian genomes identified by analysis of chromatin interactions
Dixon, J. R., Selvaraj, S., Yue, F., Kim, A., Li, Y., Shen, Y., Hu, M., Liu, J. S., & Ren, B. (2012) · Nature · doi:10.1038/nature11082 · Cited by 6,829
DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139
Rogakou, E. P., Pilch, D. R., Orr, A. H., Ivanova, V. S., & Bonner, W. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.10.5858 · Cited by 5,438
Metabolic regulation of gene expression by histone lactylation
Zhang, D., Tang, Z., Huang, H., Zhou, G., Cui, C., Weng, Y., Liu, W., Kim, S., Lee, S., Perez-Neut, M., et al. (2019) · Nature · doi:10.1038/s41586-019-1678-1 · Cited by 4,371
Histone H3K27ac separates active from poised enhancers and predicts developmental state
Creyghton, M. P., Cheng, A. W., Welstead, G. G., Kooistra, T., Carey, B. W., Steine, E. J., Hanna, J., Lodato, M. A., Frampton, G. M., Sharp, P. A., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1016071107 · Cited by 4,302
ZFN, TALEN, and CRISPR/Cas-based methods for genome engineering
Gaj, T., Gersbach, C. A., & Barbas, C. F. (2013) · Trends in Biotechnology · doi:10.1016/j.tibtech.2013.04.004 · Cited by 3,820
Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain
Bannister, A. J., Zegerman, P., Partridge, J. F., Miska, E. A., Thomas, J. O., Allshire, R. C., & Kouzarides, T. (2001) · Nature · doi:10.1038/35065138 · Cited by 2,903
Self-citationMethylation of histone H3 lysine 9 creates a binding site for HP1 proteins
Lachner, M., O'Carroll, D., Rea, S., Mechtler, K., & Jenuwein, T. (2001) · Nature · doi:10.1038/35065132 · Cited by 2,868
Research works printed but not linked: 3
- Xhemalce B., Dawson M. A. & Bannister A. J. In Epigenetic Regulation and Epigenomics (ed. Meyers, R. A.) 657–703 (Wiley–Blackwell, 2012).
- Meers, M. P., Janssens, D. H. & Henikoff, S. Multifactorial chromatin regulatory landscapes at single cell resolution. Preprint at bioRxiv https://doi.org/10.1101/2021.07.08.451691v1.full (2021). · DOI
- Altemose, N. et al. DiMeLo-seq: a long-read, single-molecule method for mapping protein-DNA interactions genome-wide. Preprint at bioRxiv https://doi.org/10.1101/2021.07.06.451383v1 (2021). · DOI
Cited by
Sorted by citations
Items 601–700 of 1,001
Li, D., Zhang, L., Li, Y., Wu, J., Mou, Y., He, Y., Zhou, T., Gong, Q., Ma, L., Xu, Y., et al. (2026) · Clinical Epigenetics · doi:10.1186/s13148-026-02111-2 · Cited by 3
Exploring the interplay of epigenetics and individualization
Meuthen, D., Hoffman, J. I., Kurtz, J., Berthelsen, A. L., Chakarov, N., Chen, R. S., Coculla, A., Gadau, J. R., Gossmann, T. I., Mühlenhaupt, M., et al. (2026) · Trends in Ecology & Evolution · doi:10.1016/j.tree.2025.12.010 · Cited by 3
Evolution of a distinct chromatin regulatory landscape in brown algae
Vigneau, J., Lotharukpong, J. S., Liu, P., Luthringer, R., Lombard, B., Loew, D., Haas, F. B., Borg, M., & Coelho, S. M. (2026) · Nature Ecology & Evolution · doi:10.1038/s41559-026-03031-3 · Cited by 7
Engineering epigenome editing tools: Current progress and future perspectives
Fischer, C., Bashtrykov, P., & Jeltsch, A. (2026) · Current Opinion in Biomedical Engineering · doi:10.1016/j.cobme.2026.100662 · Cited by 3
Pîrlog, L.-M., Catana, A. M., Pitforodeschi, A.-D., Pilatec, A.-N., Băilă, R.-M., Rusu, I., Militaru, M.-S., Iordănescu, I. I., & Belbe, A.-A. (2026) · Genes · doi:10.3390/genes17060681 · Cited by 4
Epigenetic regulation in atherosclerosis and its therapeutic potential
Santovito, D., Atzler, D., & Weber, C. (2026) · Nature Reviews Cardiology · doi:10.1038/s41569-026-01313-8 · Cited by 3
Fraser, O. A., Namitz, K. E. W., & Showalter, S. A. (2023) · Methods · doi:10.1016/j.ymeth.2023.07.010 · Cited by 3
The role of circRNAs in regulation of drug resistance in ovarian cancer
Zhan, J., Li, Z., Lin, C., Wang, D., Yu, L., & Xiao, X. (2023) · Frontiers in Genetics · doi:10.3389/fgene.2023.1320185 · Cited by 3
Role of Genetic Variation in Transcriptional Regulatory Elements in Heart Rhythm
Jonker, T., Barnett, P., Boink, G. J. J., & Christoffels, V. M. (2023) · Cells · doi:10.3390/cells13010004 · Cited by 3
Single-Macromolecule Studies of Eukaryotic Genomic Maintenance
Rudnizky, S., Murray, P. J., Wolfe, C. H., & Ha, T. (2024) · Annual Review of Physical Chemistry · doi:10.1146/annurev-physchem-090722-010601 · Cited by 3
Epigenetic modifications of gonadotropin receptors can regulate follicular development
Yang, Y., Feng, W., Zhou, J., Zhang, R., Lin, X., Sooranna, S. R., Yanfei, D., & Shi, D. (2024) · Animal Reproduction Science · doi:10.1016/j.anireprosci.2024.107534 · Cited by 4
Targeting the Tumor Epigenetic Regulator SETDB1 for Tumor Therapy
Peng, C. Y., Zhou, N., Chen, T., Lei, J., Chen, C., & Zhu, S. (2024) · Current Cancer Drug Targets · doi:10.2174/0115680096311909240721160523 · Cited by 2
Zhang, H., & Peng, Y. (2024) · Journal of Computational Biophysics and Chemistry · doi:10.1142/s2737416524300013 · Cited by 3
Epigenetics of Conjunctival Melanoma: Current Knowledge and Future Directions
Flick, K. M., Demirci, H., & Demirci, F. Y. (2024) · Cancers · doi:10.3390/cancers16213687 · Cited by 3
Wang, Y., Ge, J., Xian, W., Tang, Z., Xue, B., Yu, J., Yao, Y.-F., Liu, H., Qiu, J., & Liu, X. (2024) · Microbiological Research · doi:10.1016/j.micres.2024.128041 · Cited by 3
Epigenetics in autosomal dominant polycystic kidney disease
Yan, Z., Cao, F., shao, T., Liao, B., Wang, G., Tang, X., Luo, H., Zhu, F., Liao, Y., Zhang, F., et al. (2025) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2024.167652 · Cited by 3
Dietary modulation of epigenetics: Implications for cancer prevention and progression
Zhu, S., Liang, X., Bai, Q., Ni, X., & Wang, J. (2025) · journal of nutritional oncology · doi:10.1097/jn9.0000000000000048 · Cited by 3
Selenalysine as a Chemical Tool for Probing Histone Post-Translational Modifications
Martín, S. P., & Mecinović, J. (2025) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.4c00567 · Cited by 3
Emerging role of SETD2 in the development and function of immune cells
Chen, L., Zou, Y., Dong, Y., Hong, T., Xu, Q., & Zhang, J. (2025) · Genes & Diseases · doi:10.1016/j.gendis.2025.101622 · Cited by 3
Feng, M., & Nakamura, F. (2025) · ACS Omega · doi:10.1021/acsomega.5c02459 · Cited by 3
Kállai, B. M., Sawasaki, T., Endo, Y., & Mészáros, T. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26083577 · Cited by 3
Histone tetrasome dynamics affects chromatin transcription
Shi, X., Fedulova, A. S., Kotova, E., Maluchenko, N. V., Armeev, G. A., Chen, Q., Prasanna, C., Sivkina, A. L., Feofanov, A. V., Kirpichnikov, M. P., et al. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf356 · Cited by 3
Sashiyama, S., Nakagawa, T., Nakagawa, M., Hosogane, M., Watanabe, Y., Ashitomi, H., Yamane, K., Shibuya, N., Moroishi, T., Nakayama, K., et al. (2025) · iScience · doi:10.1016/j.isci.2025.112699 · Cited by 3
Liu, B., Wang, M., Pu, N., Wang, J., Fan, W., Qu, C., Wu, H., Song, Z., & Tao, Y. (2025) · Ageing Research Reviews · doi:10.1016/j.arr.2025.102788 · Cited by 3
An epigenome atlas of mouse adipocytes
Hinte, L. C., Ghosh, A., Castellano‐Castillo, D., Wolfrum, C., & von Meyenn, F. (2025) · Molecular Metabolism · doi:10.1016/j.molmet.2025.102197 · Cited by 4
Baweja, L., & Wereszczynski, J. (2025) · Epigenetics & Chromatin · doi:10.1186/s13072-025-00635-0 · Cited by 3
Unnatural Amino Acid Crosslinking for Increased Spatiotemporal Resolution of Chromatin Dynamics
Moleri, P., & Wilkins, B. J. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241612879 · Cited by 3
Epigenetic mechanisms of non-retinal components of the aging eye and novel therapeutic strategies
Lamas, M. (2023) · Experimental Eye Research · doi:10.1016/j.exer.2023.109673 · Cited by 3
Shu, Q., Fan, J., Wang, B., & Shi, J. M. (2023) · Tetrahedron Letters · doi:10.1016/j.tetlet.2023.154888 · Cited by 3
Li, W., Cao, P., Xu, P., Sun, F., Wang, C., Zhang, J., Dong, S., Wilson, J. R., Xu, D., Fan, H., et al. (2024) · Cell & Bioscience · doi:10.1186/s13578-024-01265-x · Cited by 3
Histone H3 Variants in the Multiverse of Cancer
Simeonova, I., & Almouzni, G. (2024) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-062722-021823 · Cited by 3
Zhou, X., Zhang, N., Gong, J., Zhang, K., Chen, P., Cheng, X. L., Ye, B., Zhao, G., Jing, X., & Li, X. (2024) · Communications Biology · doi:10.1038/s42003-024-07211-4 · Cited by 3
Mechanisms of Autophagy in Ineffective Reperfusion After Ischemic Stroke
Bai, S., Ding, Y., Simo, L., Li, F., & Geng, X. (2025) · Journal of Neuroscience Research · doi:10.1002/jnr.70017 · Cited by 3
Oncohistone-sculpted epigenetic mechanisms in pediatric brain cancer
Pandey, D. P., & Somyajit, K. (2025) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2025.102505 · Cited by 3
Hou, X., Yu, T., Chol, C. H., An, J., Zhang, L., Sun, M., Mecinović, J., Gao, P., & Li, L. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.140601 · Cited by 3
Histone H3E50K remodels chromatin to confer oncogenic activity and support an EMT phenotype
Sad, K., Fawwal, D. V., Jones, C. Y., Hill, E. J., Skinner, K. T., Adams, M., Lustenberger, S., Lee, R. S., Lohano, S. V., Elayavalli, S., et al. (2025) · NAR Cancer · doi:10.1093/narcan/zcaf002 · Cited by 3
Dens, C., Yeung, D., Krokhin, O. V., Laukens, K., & Bittremieux, W. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.12.18.629045 · Cited by 2
Cis and Trans Regulatory Mechanisms of ecDNA SegregationPreprint
Xie, Y.-P., Lim, J., Liu, W., Gilbreath, C., Sun, X., Qiao, K., Kim, Y., & Wu, S.-H. (2026) · bioRxiv · doi:10.1101/2024.12.31.630921 · Cited by 5
Acetylation of histone H2B on lysine 120 regulates BRD4 binding to intergenic enhancersPreprint
Hamilton, G. A., Ruiz, P. D., Ye, K. Q., & Gamble, M. J. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.02.07.637147 · Cited by 3
Cumulative TF binding and H3K27 Acetylation drive enhancer activation frequencyPreprint
Baderna, V., Barzaghi, G., Kleinendorst, R., Chatsirisupachai, K., Moniot-Perron, L., Schopp, M., Hochepied, T., Libert, C., Odom, D. T., Zaugg, J. B., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.03.26.645413 · Cited by 3
Rewiring of chromatin regulation underlies the evolution of brown algal multicellularityPreprint
Vigneau, J., Lotharukpong, J. S., Liu, P., Luthringer, R., Lombard, B., Loew, D., Haas, F. B., Borg, M., & Coelho, S. M. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.09.16.676480 · Cited by 3
Lead-oriented synthesis of epigenetic relevant scaffolds
Maujean, T., Kannaboina, P., Green, A. I., & Burslem, G. M. (2023) · Chemical Communications · doi:10.1039/d3cc04317g · Cited by 2
Heterochromatin-dependent transcription links the PRC2 complex to small RNA-mediated DNA elimination
Solberg, T., Wang, C., Matsubara, R., Wen, Z., & Nowacki, M. (2024) · EMBO Reports · doi:10.1038/s44319-024-00332-1 · Cited by 2
Timsit, Y. (2025) · Genes · doi:10.3390/genes16010045 · Cited by 2
Wang, J., & Yan, S. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1523779 · Cited by 2
Lin, C.-J., Liu, S., Wu, Z.-S., Huang, S., & Chen, T.-W. (2025) · Scientific Reports · doi:10.1038/s41598-025-85766-w · Cited by 2
Epigenetic Mechanisms and Functions
Ajjanagadde, A., Fathi, A. T., Bairy, M., Shaheeda, A., & Kabekkodu, S. P. (2025) · Springer eBooks · doi:10.1007/978-981-96-3985-4_2 · Cited by 2
Martín-Zamora, F. M., Cole, J., Donnellan, R. D., Guynes, K., Carrillo‐Baltodano, A. M., Dickman, M. J., Hurd, P. J., & Martín-Durán, J. M. (2025) · Genome biology · doi:10.1186/s13059-025-03626-2 · Cited by 2
A practical guide to sequencing in neuropsychiatric research
Minerva, A. R., DeBerardine, M., Lin, R., Kim, H. J. J., Rogers, F. D., Rashford, R. L., & Peña, C. J. (2025) · NPP—Digital Psychiatry and Neuroscience · doi:10.1038/s44277-025-00041-0 · Cited by 2
Liu, R., Wang, L., Usman, M. A., Sun, W., Wang, Q., Wu, J., Nong, H. T., Zhang, Q., Wang, J., & Zhang, C. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.146910 · Cited by 2
CUT&RUN and CUT&Tag for histone modification and transcription factor binding analyses
Hinte, L. C., & von Meyenn, F. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-26759-8.00003-5 · Cited by 2
Zhang, D., Wang, Y., Guo, J. G., Zhang, X., & Gong, Z. (2025) · Frontiers in Bioscience-Landmark · doi:10.31083/fbl27428 · Cited by 4
Epigenetic modulation in cancer drug discovery: promising targets and clinical applications
Sundaram, V. A., Infant, S. S., Manikandan, S., Saravanan, A., Marimuthu, M. M. C., & Chopra, H. (2025) · Pharmacological Reports · doi:10.1007/s43440-025-00770-1 · Cited by 2
Histone supply: a precious commodity for cell identity
Gonske, S. J., Escobar, T. M., & Loyola, A. (2025) · Biochemical Journal · doi:10.1042/bcj20253163 · Cited by 2
Role of novel protein acylation modifications in sepsis
Wang, J., He, A., Song, L., Jiang, W., Xu, L., Zheng, R., & Yu, J. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1657194 · Cited by 2
Hayat, Y., & Kanlıdere, Z. (2025) · Separations · doi:10.3390/separations12100275 · Cited by 2
Learning and memory in molecular networks
Lissek, T. (2025) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2025.152805 · Cited by 3
Beyond genes: a clinician's guide to epigenetics
Popov, P., & Jurkowska, R. Z. (2025) · Breathe · doi:10.1183/20734735.0227-2024 · Cited by 2
Histone probes for reader and eraser investigations
Yang, J., & Wu, M. (2025) · Chemical Science · doi:10.1039/d5sc05529f · Cited by 2
Miyake, T., Ranaudo, A., Sacco, E., & Greco, C. (2025) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.70081 · Cited by 2
Ju, S., Jin, L., Zheng, Z., Meng, Q., Cai, Y., Chen, D., Ouyang, X., Aishan, N., Lu, L., Li, Z., et al. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.116563 · Cited by 3
Tang, Q., Wang, L., Fu, N., & Chen, L. (2026) · Cell Biochemistry and Function · doi:10.1002/cbf.70171 · Cited by 2
Regulation of mitochondrial biogenesis and energy metabolism in the heart
She, P., 莫非, Zhu, P., & Zhong, T. P. (2026) · Chinese Medical Journal · doi:10.1097/cm9.0000000000004011 · Cited by 2
Seem, K., Kaur, S., Kumar, A., Krishnan, G. S., Viswanathan, C., Mohapatra, T., & Kumar, S. (2026) · Plant Stress · doi:10.1016/j.stress.2026.101313 · Cited by 2
Luo, Y. N., Deng, Y., Liang, Y., Wu, W., Wu, W., & Wang, L. (2026) · Nucleic Acids Research · doi:10.1093/nar/gkag146 · Cited by 2
Epigenetic Regulation of Production Traits in Ruminants: Implications for Breeding and Selection
Liu, H., Qumu, M., Lu, Y., Li, K., Qian, Y., Sheng, Z., Shi, J., Xi, D., & Wu, J. (2026) · Biology · doi:10.3390/biology15050416 · Cited by 2
Structural landscape of H3K27me3 recognition by protein domains and their potential for inhibition
Rosas, R., Baracaldo-Lancheros, L. F., Dykhuizen, E. C., & Musselman, C. A. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.111344 · Cited by 2
González‐Martínez, J., Sánchez-Belmonte, A., Ayala, E., Escobar, B., Gómez, J., Garcia-Diaz, A., Nogueira, E., Muñoz, J., Melati, A., Brandauer, A., et al. (2026) · Science Advances · doi:10.1126/sciadv.adr1776 · Cited by 2
Xia, W., Jiang, M., Huang, Y., Ding, K., & Chen, Y. (2026) · MedComm · doi:10.1002/mco2.70655 · Cited by 2
Update of the Methyltransferase Gene Family: Classification, Evolution and Biological Functions
Katsafadou, A. I., Falnes, P. Ø., Bruford, E. A., Braschi, B., Hanson, Q., Hall, M. D., Thompson, D. C., Nebert, D. W., & Vasiliou, V. (2026) · Human Genomics · doi:10.1186/s40246-026-00949-4 · Cited by 3
Epigenetic regulation of circadian clocks by chromatin dynamics from fungi to mammals
Liu, X.-L., Yu, M., Duan, Z., & Liu, X. (2026) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2026.02.002 · Cited by 2
KDM3A catalyses the oxidation of acetyl-lysine to hydroxyacetyl-lysine on histone H3K9
Belle, R., Bukowski, J., Schiller, R., Cutler, R., Salah, E., Dawber, R. S., Tumber, A., Bonnici, J., Kindrick, J. D., Serrano, L., et al. (2026) · Nature Chemistry · doi:10.1038/s41557-026-02112-x · Cited by 2
Guo, Q., Satthawiwat, N., Sano, A., Meroueh, C., Hamdi, A., 戴新, Warasnhe, K., Washington, A. M., Starlinger, P. P., Krivonos, A., et al. (2026) · Hepatology · doi:10.1097/hep.0000000000001742 · Cited by 2
Functional epigenetic dynamics and transcriptional heterogeneity: Recent advances
van Loosen, Q. C., van Saparoea, A. C. H. V. D. B., Cossins, B. C., & Verschure, P. J. (2026) · Current Opinion in Biomedical Engineering · doi:10.1016/j.cobme.2026.100664 · Cited by 2
Clinical translation of epigenome editing technologies
Ma, A. J., Brown, B. H., Kim, S., & Hilton, I. B. (2026) · Current Opinion in Biomedical Engineering · doi:10.1016/j.cobme.2026.100666 · Cited by 3
Transglutaminase 2 drives histone monoaminylation as an epigenetic mechanism in health and disease
Leaman, A. A., Lin, Z., & Zheng, Q. (2026) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2026.04.003 · Cited by 4
Boruah, R. R., Boro, D., & Das, D. (2026) · Sustainability Sciences in Asia and Africa · doi:10.1007/978-981-95-7746-0_19 · Cited by 2
Mechanical Activation of Piezo1 Drives Osteoarthritis Through Kdm5c‐Mediated Epigenetic Silencing
Kan, T., Li, X., Wang, H. Y., Sun, L., Wang, Y., Wu, J., Cui, J., Yang, Y., Yuan, K., Chu, L., et al. (2026) · Advanced Science · doi:10.1002/advs.76089 · Cited by 2
Wang, L., Liang, Y., Wu, S., Deng, Y., Wu, W., Zhang, Z. Z. Z., Wu, W., & Wang, L. (2026) · Molecular Cell · doi:10.1016/j.molcel.2026.05.022 · Cited by 3
Epigenetic mechanisms of inflammatory memory in the central nervous system
Ye, J. J., & Quintana, F. J. (2026) · Nature Immunology · doi:10.1038/s41590-026-02541-3 · Cited by 3
Antitumor Effect of Ruthenium(II) with 2-Mercaptothiazoline Ligand Complex in Murine Melanoma Model
Fernandes, G., Ribeiro, A. B., de Melo, M. R. S., Squarisi, I. S., da Silva, L. H. D., da Silva, M. M., de Assis, S., Batista, A. A., & Tavares, D. C. (2026) · ACS Omega · doi:10.1021/acsomega.6c01894 · Cited by 2
Grand challenge in chromatin epigenomics: everything, everywhere, all at once
Dent, S. (2023) · Frontiers in Epigenetics and Epigenomics · doi:10.3389/freae.2023.1195690 · Cited by 2
Chromatin-based DNA replication initiation regulation in eukaryotes
Hao, L., Fang, R., & Long, H. (2023) · Genome Instability & Disease · doi:10.1007/s42764-023-00108-2 · Cited by 2
Sun, M., Shi, G., Zhang, X., Kan, C., Xie, S., Peng, W., Liu, W., Wang, P., & Zhang, R. (2024) · Aging · doi:10.18632/aging.205406 · Cited by 3
Dissecting the epigenetic regulation of human brain organoid development in single cells
Zenk, F. L., & Treutlein, B. (2024) · Nature Neuroscience · doi:10.1038/s41593-024-01653-z · Cited by 2
Peng, S., Liu, X., Lu, C., Wang, H., Liu, X., Gong, Q., Tao, H., Xu, H., Tian, C., Xu, G., et al. (2024) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.4c00130 · Cited by 2
Emerging toolkits for decoding the co-occurrence of modified histones and chromatin proteins
Pépin, A.-S., & Schneider, R. (2024) · EMBO Reports · doi:10.1038/s44319-024-00199-2 · Cited by 4
Self-citationNavigating glioblastoma complexity: the interplay of neurotransmitters and chromatin
Romero-Reyes, J., Vázquez-Martínez, E. R., Silva, C., Molina‐Hernández, A., Díaz, N. F., & Camacho‐Arroyo, I. (2024) · Molecular Biology Reports · doi:10.1007/s11033-024-09853-3 · Cited by 2
Niechoda, A., Rosłan, M., Milewska, K., Szoka, P., Maciorowska, K., & Hołownia, A. (2024) · Cells · doi:10.3390/cells13161367 · Cited by 2
The emerging H3K9me3 chromatin landscape during zebrafish embryogenesis
Duval, K. L., Artis, A. R., & Goll, M. G. (2024) · Genetics · doi:10.1093/genetics/iyae138 · Cited by 2
A Live‐Cell Epigenome Manipulation by Photo‐Stimuli‐Responsive Histone Methyltransferase Inhibitor
Wu, C.-S., Sun, X. S., Liu, L., & Cheng, L. (2024) · Advanced Science · doi:10.1002/advs.202404608 · Cited by 2
Абатуров, А. Е., & Нікуліна, А. О. (2024) · GASTROENTEROLOGY · doi:10.22141/2308-2097.58.3.2024.626 · Cited by 2
Optimizing Adoptive Cell Therapy for Solid Tumors via Epigenetic Regulation of T‐cell Destiny
Guo, X., Li, X., Wang, S., Shi, Y., Huang, J., Liu, X., Lu, Y., Zhang, J., Luo, L., & You, J. (2024) · Advanced Healthcare Materials · doi:10.1002/adhm.202402209 · Cited by 2
Epigenetic Modulations by Microbiome in Breast Cancer
Zhao, Y., & Bhatnagar, S. (2024) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-66686-5_4 · Cited by 2
Zhao, Y., Wang, C., Du, J., Wang, W., Wu, J., Liu, T., Xue, P., Ju, Y., Hong, X., Zheng, J., et al. (2024) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2024.117216 · Cited by 2
Epigenetic Dysregulation of Retrotransposons in Cancer
Liu, K. Y., & Leung, D. (2025) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-24-0744 · Cited by 5
Mass spectrometry-based technologies for histone PTM analysis and novel PTM discovery
Chen, K., Zhao, W., Zhang, J., Zhao, S., Li, H., & Tan, M. (2025) · Scientia Sinica Chimica · doi:10.1360/ssc-2025-0043 · Cited by 2
Han, Y., Wu, B., Tan, J., Wu, R., Wang, J., Ren, X., Zhang, Y., Gao, Z., & Xia, X. (2025) · Frontiers in Oncology · doi:10.3389/fonc.2025.1549477 · Cited by 2
Investigation and design of the dual specificity of the PRDM9 protein lysine methyltransferase
Graf, D., Schnee, P., Pleiss, J., Weirich, S., & Jeltsch, A. (2025) · Communications Biology · doi:10.1038/s42003-025-08207-4 · Cited by 2
ciRS-7 expression is epigenetically regulated in cancer cells across human adenocarcinomas
Paasch, T. P., Olesen, M. T. J., García‐Rodríguez, J. L., Assmus, A. M., Fenton, R. A., Kjems, J., Hager, H., & Kristensen, L. S. (2025) · PLoS Genetics · doi:10.1371/journal.pgen.1011726 · Cited by 2
Metadata
- Authors
- Millán-Zambrano, G., Burton, A., Bannister, A. J., & Schneider, R.
- Affiliations
- Consejo Superior de Investigaciones Científicas (ES)
- Helmholtz Munich (DE)
- University of Cambridge (GB)
- Corresponding author
- Bannister, Andrew J.
- Schneider, Robert
- Venue
- Nature Reviews Genetics
- Published
- 2022-03-25
- Volume
- 23
- Issue
- 9
- Pages
- 563-580
- ISSN
- 1471-0056 (ISSN-L)
- 1471-0064
- OpenAlex
- W4220743473
- Semantic Scholar
- 4a452bb0c38ba013f3a90217102ab8f7caf3fdaf
- Cited by
- 1,116
- References
- 238
- Citations by year
- 2026: 241 · 2025: 335 · 2024: 333 · 2023: 170 · 2022: 37
- FWCI
- 23.32
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Nature Reviews Genetics (publishedVersion)
- PubMed (publishedVersion)
- DIGITAL.CSIC (Spanish National Research Council (CSIC)) (submittedVersion)
- Site cant be reached (submittedVersion)
- PuSH - Publication Server of Helmholtz Zentrum München (submittedVersion)
- Funders
- Wellcome Trust (WT203144)
- Cancer Research UK (C6946/A24843, 27321, RG96894)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- 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
- histone modifications, genome function, transcription, DNA recombination, DNA replication, DNA repair, chromatin structure, genome-wide mapping
- MeSH terms
- DNA, DNA Repair, DNA Replication, Histones, Protein Processing, Post-Translational
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