Cited by 1,116Genomics and Chromatin DynamicsEpigenetics and DNA MethylationChromatin Remodeling and Cancer

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

Millán-Zambrano, Gonzalo, Burton, Adam, Bannister, Andrew J., Schneider, Robert·2022·Nature Reviews Genetics

Open this paper in CoChat — free account

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.

Integrity signals

Registry

Crossref · 10.1038/s41576-022-00468-7

Cites

237 of 237 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

The hallmarks of cancer
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-citation
Methylation 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

Show all 238 references

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

Sorted by citations

Items 701–800 of 1,001

Epigenetic changes in post-traumatic stress disorder: possibilities and limitations of epigenetic therapy
Сучкова, И. О., Patkin, E. L., Tsikunov, S. G., & Софронов, Г. А. (2025) · Medical academic journal · doi:10.17816/maj632018 · Cited by 2
BRPF1 in cancer epigenetics: a key regulator of histone acetylation and a promising therapeutic target
Alexandrova, E., Parisi, R., Smal, M. P., Rosa, D. D., Carleo, A., Orlando, E., Veneri, C., Melone, V., Salvati, A., Tarallo, R., et al. (2025) · Cell Death Discovery · doi:10.1038/s41420-025-02730-3 · Cited by 2
Broad H3K4me3 domains support oocyte genome silencing and maturation but are dispensable for repression in early embryos
Skuland, T., Fosslie, M., Khodeer, S., Alemu, E. A., Johansen, J. V., Indahl, M., Castroviejo, B. C., Li, Y., Lerdrup, M., Dahl, J. A., et al. (2025) · Development · doi:10.1242/dev.204638 · Cited by 2
Multi-omics elucidation of KDM5C, KDM6A, and KMT2B roles in cancer epigenetic dysregulation and transcriptional reprogramming
Li, T., Wang, L., Duan, S., Cui, X., Fu, C., Hu, J., & Li, L. (2025) · Communications Biology · doi:10.1038/s42003-025-09305-z · Cited by 2
Pathophysiological significance of impaired KAT7-dependent histone H3K14 acetylation during zinc deficiency
Fujisawa, T., Takenaka, S., Maekawa, L., Ogawa, M., Kowada, T., Matsui, T., Mizukami, S., Kato, Y., Suzuki, M., Noma, H., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-69476-z · Cited by 2
Recent Advances in Male Reproductive System
Wu, W. (2023) · IntechOpen eBooks · doi:10.5772/intechopen.1000558 · Cited by 2
Post-translational modifications in prion diseases
Bizingre, C., Bianchi, C., Baudry, A., Alleaume‐Butaux, A., Schneider, B., & Pietri, M. (2024) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2024.1405415 · Cited by 2
Editorial: Insights in cardiovascular therapeutics 2022—cardiovascular innate immunity
Xu, K., Zhang, Y., Saaoud, F., Shao, Y., Lu, Y., Jiang, X., Wang, H., & Yang, X. (2023) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2023.1184030 · Cited by 2
Histone H3 E50K mutation confers oncogenic activity and supports an EMT phenotypePreprint
Sad, K., Jones, C. Y., Fawwal, D. V., Hill, E. J., Skinner, K. T., Adams, M., Lustenberger, S., Lee, R. S., Lohano, S. V., Elayavalli, S. R., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.10.11.561775 · Cited by 2
Simulating cell-free chromatin using preclinical models for cancer-specific biomarker discoveryPreprint
Michino, S. D. D., Main, S. C., Penny, L., Kridel, R., Cescon, D. W., Hoffman, M. M., Lupien, M., & Bratman, S. V. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.11.16.567416 · Cited by 2
Bioinformatics for Analyzing the Role of Epigenetics in Plant Disease Resistance
Singh, K., Balyan, H. S., & Gupta, P. K. (2024) · Wiley eBooks · doi:10.1002/9781394209965.ch15 · Cited by 2
Revisiting Evidence for Epigenetic Control of Alternative SplicingPreprint
Manz, Q., & List, M. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.08.30.610315 · Cited by 2
Epigenome Profiling Identifies H3K27me3 Regulation of Extra-Cellular Matrix Composition in Human CorticogenesisPreprint
Ditzer, N., Senoglu, E., Schütze, T. M., Nikolaidi, A., Kolodziejczyk, A., Sameith, K., Dietz, S., Derihaci, R. P., Birdir, C., Eugster, A., et al. (2024) · SSRN Electronic Journal · doi:10.2139/ssrn.5017114 · Cited by 2
Minimal protein list for chromatin replication-coupled symmetric histone recycling revealed through in vitro reconstitutionPreprint
Nagae, F., Endo, S., Murayama, Y., & Terakawa, T. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.11.18.624094 · Cited by 2
Predicting the effect of CRISPR-Cas9-based epigenome editingPreprint
Batra, S. S., Cabrera, A., Spence, J. P., Goell, J., Anand, S. S., Hilton, I. B., & Song, Y. S. (2024) · eLife · doi:10.7554/elife.92991.2 · Cited by 2
Lysine-specific demethylase 1a is obligatory for gene regulation during kidney developmentPreprint
Kota, S. B., & Kota, S. K. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.02.25.640014 · Cited by 2
Genomic and Transcriptomic Signatures of SETD1A Disruption in Human Excitatory Neuron Development and Psychiatric Disease RiskPreprint
Sun, Z., Zhu, H., He, X., Lendemeijer, B., Wang, Z., Fan, J., Sun, Y., Zhang, Z., Markx, S., Kushner, S. A., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.03.26.645419 · Cited by 3
Systems-level feedback loops maintain gene expression homeostasis following RNA polymerase II dosage perturbationPreprint
Olthof, A. M., González, M. N., Poulsen, N. B., Moreno, N. N., Bautu, T., Cugusi, S., & Svejstrup, J. Q. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.09.18.677100 · Cited by 2
Finding a good balance: two distinct chromatin factors fine‐tune stress response in Arabidopsis seedlings
Archacki, R. (2023) · New Phytologist · doi:10.1111/nph.19357 · Cited by 1
Cdc73 is a major regulator of apoptosis‐inducing factor 1 expression in Saccharomyces cerevisiae via H3K36 methylation
Saha, N., Acharjee, S., & Tomar, R. S. (2024) · FEBS Letters · doi:10.1002/1873-3468.14847 · Cited by 1
Targeting Epigenetic Readers Using Small Molecule Binders and PROTAC Degraders
Boccia, E., Gazzillo, E., Chini, M. G., Bifulco, G., & Lauro, G. (2024) · Interdisciplinary cancer research · doi:10.1007/16833_2024_240 · Cited by 1
Fragment‐based discovery of small molecule inhibitors of the HDGFRP 2 PWWP domain
Wei, X., Shu-ju, L., Li, Z., Wang, L., Fan, W., Ruan, K., & Gao, J. (2024) · FEBS Letters · doi:10.1002/1873-3468.14981 · Cited by 1
Histone modification and personalized epigenomics in cancer
Ramazi, S., Dadzadi, M., Sahafnejad, Z., & Allahverdi, A. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-23802-4.00009-0 · Cited by 3
Intrinsic Immune Response of HBV/HDV-Infected Cells and Corresponding Innate (Like) Immune Cell Activation
Groth, C., Wupper, S., Gnouamozi, G. E., Böttcher, K., & Cerwenka, A. (2024) · Livers · doi:10.3390/livers4040040 · Cited by 3
Molecular basis of senescence in osteoarthritis
Lawson, M. G., & Ritchison, H. M. (2024) · doi:10.32948/ajsep.2024.11.22 · Cited by 2
Aberrant acetylation caused by a CDYL splicing mutation contributes to thin mid‐piece related asthenoteratozoospermia and male infertility
Yang, F., Gao, Y., Han, B., Zhu, W., Wang, G., Liu, L., Shen, Q., Song, B., Lv, M., Wu, H., et al. (2025) · Andrology · doi:10.1111/andr.13825 · Cited by 1
Pan-cancer analysis of the transcriptional expression of histone acetylation enzymes in solid tumors defines a new classification scheme for gliomas
Zhang, J., Li, L., Tang, A., Wang, C., Wang, Y., Hu, Y., He, G., Liao, W., & Zhou, R. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1523034 · Cited by 1
Exploring Histone Modifications in Inherited Retinal Disorders
Mazzeo, L., Arsenijévic, Y., & Berger, A. (2025) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-76550-6_31 · Cited by 1
Adolescent cetylpyridinium chloride exposure impairs homologous recombination repair and induces granulosa cell apoptosis and follicular atresia via FOXM1/CREBBP complex suppression
Ma, L., Yin, X. H., Zhang, Y., Ma, Y., Geng, Y., Mu, X., Gao, R., Chen, X., & He, J. (2025) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2025.118193 · Cited by 1
Deciphering Glutaminyl Cyclase Catalytic Pathways Enables Recognition of Anchor Pharmacophores for Inhibitor Discovery
Wu, J.-W., Ning, X.-L., Tang, B.-D., Chen, Y., Yang, Z.-B., Meng, F.-B., Cong, Z., Yu, J., Li, R., Li, Z., et al. (2025) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.5c00498 · Cited by 2
Epigenomic Profiling of Histone Posttranslational Modifications in Frozen Cancer Tissue Using CUT&RUN
Roberti, A., & Fraga, M. F. (2025) · Methods in molecular biology · doi:10.1007/978-1-0716-4558-1_16 · Cited by 1
Nuclear-localized metabolic enzymes: emerging key players in tumor epigenetic regulation
Chen, L., Zhi-hui, W., Yuan, W., Chen, N., Lin, P., Liao, S., & Xie, G. (2025) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-025-05316-w · Cited by 1
Development and application of epigenome editors
Sun, Y., & Ma, H. (2025) · Scientia Sinica Vitae · doi:10.1360/ssv-2025-0142 · Cited by 2
EZH2 in digestive system cancers: Epigenetic regulation, oncogenic interactions, and therapeutic potential
Hjazi, A. M., Hussn, A., Kareem, A. K., Alshahrani, M. Y., Malathi, H., Nayak, P. P., Chauhan, A. S., & Sharma, J. (2025) · Experimental Cell Research · doi:10.1016/j.yexcr.2025.114648 · Cited by 1
Comprehensive multi-omics analysis of histone acetylation modulators identifies ASH1L as a novel aggressive marker for osteosarcoma
Ni, C., Sun, Q., & Yin, H. (2025) · Discover Oncology · doi:10.1007/s12672-025-02920-6 · Cited by 1
Unraveling gene expression: a beginner’s guide from chromatin modifications to mRNA export in Saccharomyces cerevisiae
Serrano‐Quílez, J., & Rodríguez‐Navarro, S. (2025) · Nucleus · doi:10.1080/19491034.2025.2516909 · Cited by 1
Kringle-Dependent Inhibition of Plasmin-Mediated Fibrinolysis by Native and Citrullinated Core Histones
Komorowicz, E., Gurabi, A., Wacha, A., Szabó, L. F., Ozohanics, O., & Kolev, K. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26125799 · Cited by 1
The Drosophila histone variant H2Av facilitates Notch signaling activity in a two-tier regulatory fashion
Chen, Y., Zhang, X., Song, Y., Shen, J., & Zhang, J. (2025) · Cell Communication and Signaling · doi:10.1186/s12964-025-02333-6 · Cited by 1
Reversible Histone Acetylation During Preimplantation Embryo Development in Mammals
Musmeci, G., Franchi, F. F., Mossa, F., Luciano, A. M., Lodde, V., & Franciosi, F. (2025) · Results and problems in cell differentiation · doi:10.1007/978-3-031-91459-1_6 · Cited by 1
Epigenetic factors associated with peri-implantitis: a review
Li, Q.-H., Lu, H., Zhang, M., Ye, Y. J., Chen, Q., & Sun, P. (2025) · Journal of Zhejiang University SCIENCE B · doi:10.1631/jzus.b2400032 · Cited by 2
Genome-wide identification of histone acetyltransferase genes in Solanum melongena reveals two critical regulators of Botrytis cinerea resistance
Yan, Y., Wang, P., Wang, W., Hu, H., Hu, T., Wei, Q., & Bao, C. (2025) · Scientia Horticulturae · doi:10.1016/j.scienta.2025.114255 · Cited by 1
Inflammatory memory in allergic diseases
Wang, Q., Qin, H., & Wu, H. (2025) · Allergy medicine. · doi:10.1016/j.allmed.2025.100064 · Cited by 1
Global Profiling of Lysine Succinylation Reveals the Regulation of Carbon Fixation and Oil Production in Nannochloropsis oceanica
Yu, J., Su, H., & Wei, L. (2025) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.5c05262 · Cited by 1
Omics landscapes in molecular mechanisms with Amomum tsaoko as an example
Fu, D., Wang, Y., & Zhang, J. (2025) · Food Chemistry Molecular Sciences · doi:10.1016/j.fochms.2025.100294 · Cited by 1
A pleiotropic regulator AtrA undergoes liquid-liquid phase separation in regulating quorum sensing
Ma, B., Hu, X., Sun, C., Xie, J., Luo, Y., Wang, B., Feng, Y., Jiang, H., Zhao, Q., & Mao, X. (2025) · 中国科学通报：英文版 · doi:10.1016/j.scib.2025.09.013 · Cited by 1
The Epigenetic Landscape of Hemophilia
Pandey, S. K., Kulshreshtha, A., & Mishra, A. (2025) · Current Molecular Medicine · doi:10.2174/0115665240400998250909063344 · Cited by 1
Effect of histone acetyltransferase inhibitor against middle ear cholesteatoma in mouse model
Akiyama, N., Yamamoto‐Fukuda, T., & Kojima, H. (2025) · Auris Nasus Larynx · doi:10.1016/j.anl.2025.09.006 · Cited by 1
Mechanisms of Substrate Recognition by the Multispecific Protein Lysine Methyltransferase SETD6
Ulu, G. T., Weirich, S., Kehl, J., Chandrasekaran, T., Dorscht, F., Levy, D., & Jeltsch, A. (2025) · Life · doi:10.3390/life15101578 · Cited by 1
Histone Post-Translational Modifications and DNA Double-Strand Break Repair in Neurodegenerative Diseases: An Epigenetic Perspective
Yeasmin, A., & Torrente, M. P. (2025) · Biology · doi:10.3390/biology14111556 · Cited by 1
NSD Family-Mediated H3K36 Methylation in Human Cancer: Mechanisms and Therapeutic Opportunities
Park, J. E., Nguyen, M. T., Kim, J., Lee, C. H., Nam, J., Chung, H., Park, M. K., & Lee, J. (2025) · Biomedicines · doi:10.3390/biomedicines13112749 · Cited by 1
PKA signaling meets ferroptosis: A new perspertive in cancer treatment
Liu, H., Zheng, S., Burenina, O. Y., Ma, X., & Hu, Y. (2025) · Cellular Signalling · doi:10.1016/j.cellsig.2025.112240 · Cited by 1
Dual inhibition of FACT and RRM2 suppresses the progression of pancreatic ductal adenocarcinoma driven by the oncohistone H2BG53D
Qin, T., Wan, Y. C. E., Hu, S., Chen, J., Zhu, X., Zhou, J., Chen, Y., Wang, X., Zheng, Z., Chan, L. L., et al. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.116596 · Cited by 1
Customizing Native Chemical Ligation: A Case Study on Histone Variant H2A.B from Toolbox to Target
Gökler, T., Soydan, M., Barber, L. J., Ferraton, G., & Conibear, A. C. (2025) · Chemistry - Methods · doi:10.1002/cmtd.202500123 · Cited by 1
Parental Histone Recycling During Chromatin Replication
Bi, X. (2025) · Biomolecules · doi:10.3390/biom16010013 · Cited by 1
Interplay Between 3D Chromatin Architecture and Gene Regulation at the APOE Locus Contributes to Alzheimer’s Disease Risk
Lee, E.-G., Leong, L., Chen, S., Tulloch, J., & Yu, C. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms27010302 · Cited by 1
Impact of Arsenite on Transient and Persistent Histone H3 Modifications and Transcriptional Response
Lumpp, T., Hijazi, H., Stößer, S., Tekin, E., Brunner, L., Fischer, F., Brugière, S., Pflieger, D., & Hartwig, A. (2026) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.5c00312 · Cited by 1
Histone H3.3 phosphorylation facilitates H3K9me3-heterochromatin formation during retrotransposon silencing and X-chromosome inactivation via H3.3K27me3–CBX7–KAP1 axis
Chen, J., Chen, J., Yu, Z., Zhang, L., Liu, Y., Ouyang, X., Yu, J., Wang, M., Xie, S., Wang, M., et al. (2026) · 中国科学通报：英文版 · doi:10.1016/j.scib.2026.01.039 · Cited by 2
Integrative Proteomics of Extracellular Vesicles from hiPSC-Derived Cardiac Organoids Reveals Heart Tissue-like Molecular Representativity
Vital, C. M., Inácio, J. M., Carvalho, A. S., Beck, H. C., Matthiesen, R., & Belo, J. A. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27020981 · Cited by 1
Engineering an immuno-nanoprodrug: Photo-controlled pyroptosis synergizing with acid-activatable immunometabolic blockade for potent cancer immunotherapy
Yu, Z., Wang, H., Yu, Q., Miao, F., Chai, R., Tai, Z., Chen, Z., & Zhu, Q. (2026) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2026.01.024 · Cited by 1
Epigenetic mechanisms and steroid-resistant nephrotic syndrome: The future potential for SRNS diagnosis
Zhu, Y., Wang, Y., Haider, C. G., Cao, C., Ouzaouit, A., Fu, Y., Huang, H., Jiang, T., Zhou, Y., Zhang, X., et al. (2026) · iScience · doi:10.1016/j.isci.2026.114973 · Cited by 1
GAL3ST1-Mediated Histone Tyrosine Sulfation Induced by Cancer-Associated Fibroblasts Promotes Gastric Cancer Metastasis
Lu, Y., Wu, X., Li, B., Yao, L., Hou, J., Yu, B., Li, J., Li, C., Yan, M., Yang, Z., et al. (2026) · Cancer Research · doi:10.1158/0008-5472.can-25-2452 · Cited by 1
Mechanisms of DNA methyltransferase 3A1-mediated DNA methylation of nucleosomes
Ward, E., McDonald, D. T., Holl, T., & Reich, N. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.111303 · Cited by 2
An RNAi-based platform for spatiotemporal control of histone gene expression during animal development
Arroyo, O., Leatham-Jensen, M. P., & McKay, D. A. (2026) · Epigenetics & Chromatin · doi:10.1186/s13072-025-00657-8 · Cited by 1
Insights from single-molecule force spectroscopy into chromatin topology
Daris, L. J. C., & Eeftens, J. M. (2026) · Biophysical Reviews · doi:10.1007/s12551-026-01427-w · Cited by 1
Pushing the experimental resolution boundary in chromatin fibre organisation using multiscale simulations
Huertas, J., Maristany, M. J., Pérez-López, J., & Collepardo‐Guevara, R. (2026) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2026.102464 · Cited by 1
CLOCK-catalyzed histone H3K37 glutarylation suppresses H3K36 trimethylation pathways in glioblastoma
Wang, Y., Zhou, R., Zeng, X., Guo, D., Li, N., Li, S., Zhang, X., Shi, M., Jiang, L., Fan, M., et al. (2026) · Science Advances · doi:10.1126/sciadv.aea1127 · Cited by 2
Chromatin organization in Asgard archaea: histones, SMC complexes, and the archaeal roots of eukaryotic chromatin
van Hooff, J. J. E., & Dame, R. T. (2026) · Trends in Genetics · doi:10.1016/j.tig.2026.02.006 · Cited by 1
Cell cycle dynamics regulate H3K27 and H3K9 histone modifications in Drosophila
Nogay, L., Maya, A. V., Heckmann, L., Cardamone, F., Grass, I., Singh, A., Frey, A., Ernst, L., Iovino, N., & Classen, A.-K. (2026) · PLoS Biology · doi:10.1371/journal.pbio.3003371 · Cited by 1
Targeting the Polycomb repressive complexes in hepatocellular carcinoma: A comprehensive and updated analysis of mechanistic insights and clinical application
Liu, Z., Wu, D., Zhao, X., Deng, H., & Guan, X. (2026) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2026.189589 · Cited by 1
The Gut Microbiota-Metabolite-Host Axis in Cardiometabolic Diseases: Bridging Bench to Bedside
Chen, L., & Yang, D. (2026) · Cardiovascular Drugs and Therapy · doi:10.1007/s10557-026-07875-6 · Cited by 1
Traceless protein semisynthesis in cells using the promiscuous ultra-fast split intein NrdJ-1
Ye, X., Sokol, J., Kofoed, C., Dheer, A., Zhang, J., & Muir, T. W. (2026) · Chemical Science · doi:10.1039/d6sc01808d · Cited by 1
Differential histone tail citrullination by protein arginine deiminases observed via NMR spectroscopy
Kowalczyk, A. J., & Morrison, E. A. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.113639 · Cited by 1
Coming to light: the transcriptional regulatory roles of histone lysine crotonylation in health and disease
Dai, S., Ren, N., Liu, C.-M., & Yang, F. (2026) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-026-00935-7 · Cited by 1
Metabolic–Epigenetic Crosstalk and Traditional Chinese Medicine in Polycystic Kidney Disease
Cao, X., Zhang, L., & Chen, Y. (2026) · Integrative Medicine in Nephrology and Andrology · doi:10.1097/imna-d-24-00026 · Cited by 1
Peptidylarginine deiminase 4-mediated citrullination in human disease: molecular mechanisms and therapeutic targeting
邹萍, Su, X.-D., Tian, W., Xie, X.-Y., & Yang, K. (2026) · Frontiers in Pharmacology · doi:10.3389/fphar.2026.1854078 · Cited by 1
Histone Modifications: Decoding the Epigenetic Basis of Economic Traits in Livestock and Poultry
Su, Y., Li, W., Lv, Q., & Su, R. (2026) · Genes · doi:10.3390/genes17050571 · Cited by 1
The cumulative impact of seizures: the science underlying how seizures beget seizures
Gustin, R. M., Gholipour, T., & Peters, J. M. (2026) · Frontiers in Neurology · doi:10.3389/fneur.2026.1793970 · Cited by 1
Epigenetic Regulation of Salt Stress Responses in Tomato: From DNA Methylation to Stress Memory
Chen, C., Li, C., Zhu, H., & Yang, J. (2026) · Horticulturae · doi:10.3390/horticulturae12060649 · Cited by 1
Built Environment-Modulated Epigenetics: The Epigenetic Consequences of Architecturally Mediated Allostatic Overload in the Built Environment
Valentine, C., Mitcheltree, H., Sjövall, I. A. K., & Khalil, M. H. (2026) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph23060688 · Cited by 1
Gut microbiota-epigenetic interactions in systemic aging: mechanistic drivers for endocrine and reproductive network remodeling and therapeutic modulation
Birigwa, C., Tong, Q., Qu, B., Zuo, T., Yuan, W., Xiong, J., & Luo, J. (2026) · Frontiers in Aging · doi:10.3389/fragi.2026.1826382 · Cited by 2
The Complex Role of Methylation in Regulating Vascular Smooth Muscle Cell Phenotypic States in Vascular Remodeling and Atherosclerosis
Basak, S. C., & Gomez, D. A. (2026) · Biomolecules · doi:10.3390/biom16060825 · Cited by 1
Metabolic Fuel, Molecular Code: How Cancer Rewires Metabolite-Driven Post-Translational Modifications to Shape Tumor Fate
Wang, Y., Li, C., Liu, B., & Chen, X. (2026) · Cancer Bioscience · doi:10.1016/j.cbs.2026.100005 · Cited by 1
Epigenetic remodeling during UV exposure: high resolution analysis of histone post-translational modifications in a DNA binding protein 2 mutant model
Casali, C., Cavallo, M., Diaf, A., Tunesi, D., Furfaro, M., Tricarico, A., Milanesi, G., Perucca, P., Cazzalini, O., & Biggiogera, M. (2026) · Histochemistry and Cell Biology · doi:10.1007/s00418-026-02514-5 · Cited by 1
HK2 drives synaptic dysfunction in fragile X syndrome via epigenetic regulation of H3K18 lactylation
Luan, Y., Zhang, H., Ma, N., Zhang, Y., Xu, Z., Zhang, W., Zhang, X., & Liu, Y. (2026) · Frontiers in Pharmacology · doi:10.3389/fphar.2026.1903604 · Cited by 1
Histone Demethylase KDM5A Is Activated and Pathogenic in a Mouse Model of LMNA-Cardiomyopathy
Deogharia, M., Reddy, C. L., Chaudhuri, R., Chirasani, M. S., Jain, A. K., Rouhi, L., Marian, A. J., & Gurha, P. (2026) · JACC Basic to Translational Science · doi:10.1016/j.jacbts.2026.101714 · Cited by 1
Epigenetics
Millán-Zambrano, G., & Casadesús, J. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-822563-9.00047-0 · Cited by 1
Self-citation
Functional tug of war between kinases, phosphatases, and the Gcn5 acetyltransferase in chromatin and cell cycle checkpoint controls
Liu, Q., Pillus, L., & Petty, E. L. (2023) · G3 Genes Genomes Genetics · doi:10.1093/g3journal/jkad021 · Cited by 1
POS0410 A BIOPSYCHOSOCIAL APPROACH TO PHENOTYPE KNEE OSTEOARTHRITIS PATIENTS AWAITING TOTAL KNEE ARTHROPLASTY: A CROSS-SECTIONAL STUDY
Vervullens, S., Meert, L., van der Nest, G., Verbrugghe, J., VERDONK, P. C. M., Rahusen, F. T. G., Smeets, R., & Meeus, M. (2023) · Annals of the Rheumatic Diseases · doi:10.1136/annrheumdis-2023-eular.2014 · Cited by 1
Variations in chromatin architectural proteins in human diseases
Hong, C. A. O., Di, W. U., Yu, W. E. I., HaiYan, L. I. N., & Li, G. (2023) · Scientia Sinica Vitae · doi:10.1360/ssv-2023-0221 · Cited by 1
ROLE OF EPIGENETIC FACTORS IN THE DEVELOPMENT AND DIAGNOSIS OF CORONARY HEART DISEASE
Рифгатовна, С. А., SAFIULLINA, A. R., NURIAKHMETOVA, K. R., MAKAROV, M. A., Sadykova, A. M., & Krivonosova, S. S. (2023) · The Bulletin of Contemporary Clinical Medicine · doi:10.20969/vskm.2023.16(6).123-129 · Cited by 1
Chromatin accessibility and cell cycle progression are controlled by the HDAC-associated Sin3B protein in murine hematopoietic stem cells
Calderon, A., Mestvirishvili, T., Boccalatte, F. E., Ruggles, K. V., & David, G. (2024) · Epigenetics & Chromatin · doi:10.1186/s13072-024-00526-w · Cited by 2
Dissecting the Immune System through Gene Regulation
Yoshida, H. (2024) · Advances in experimental medicine and biology · doi:10.1007/978-981-99-9781-7_15 · Cited by 2
Phase Separation of Chromatin Structure-related Biomolecules: A Driving Force for Epigenetic Regulations
Wang, J., Chen, Y., Xiao, Z., Liu, X., Liu, C., Huang, K., & Chen, H. (2024) · Current Protein and Peptide Science · doi:10.2174/0113892037296216240301074253 · Cited by 1
Identification of a novel histone H2A mono-ubiquitination-inhibiting cell-active small molecule
Ni, S., Takada, Y., Ando, T., Yu, S., Yamashita, Y., Takahashi, Y., Sawada, M., Oba, M., Itoh, Y., & Suzuki, T. (2024) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2024.129759 · Cited by 1
Discovering the nucleus in a world of biomaterials
Vermeulen, S., & Balmayor, E. R. (2024) · Biomaterials and Biosystems · doi:10.1016/j.bbiosy.2024.100096 · Cited by 1
Histone modifications
Morse, R. H. (2024) · Elsevier eBooks · doi:10.1016/b978-0-12-814809-9.00002-0 · Cited by 1
The spread of chemical biology into chromatin
Hegazi, E., & Muir, T. W. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107776 · Cited by 1
The Evolutionary Reasons of Epigenetics
Camilloni, G. (2025) · DNA · doi:10.3390/dna5010006 · Cited by 1
PERCEPTIVE: an R shiny pipeline for the prediction of epigenetic modulators in novel species
Small, E. M., & Steadman, C. R. (2025) · Algal Research · doi:10.1016/j.algal.2025.104142 · Cited by 1
KMT2D upregulates SMG1 via histone methylation to antagonize mTOR and reinforce DLBCL ferroptosis
Sun, Y., Xu, Z., Wang, Z., Zhang, Y., Zhang, P., Sheng, L., Yang, S., & Ouyang, G. (2025) · Journal of Leukocyte Biology · doi:10.1093/jleuko/qiaf092 · Cited by 1

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
ORCID: Millán-Zambrano, Gonzalo
Burton, Adam
Bannister, Andrew J.
Schneider, Robert
Venue: Nature Reviews Genetics
Publisher: Springer Science and Business Media LLC
Published: 2022-03-25
Volume: 23
Issue: 9
Pages: 563-580
ISSN: 1471-0056 (ISSN-L)
1471-0064
DOI: 10.1038/s41576-022-00468-7
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
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
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

Histone post-translational modifications - cause and consequence of genome function

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks