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 501–600 of 1,001
Liu, Y., & Wang, X. (2025) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuaf045 · Cited by 5
Histone modifications: Unveiling the epigenetic enigma of degenerative skeletal diseases
Zhang, Y., Wang, J., Hua, D., Fan, C., He, W., Deng, Y., Tang, M., Geng, D., Wu, X., & Mao, H. (2025) · Journal of Orthopaedic Translation · doi:10.1016/j.jot.2025.08.013 · Cited by 9
Characterization of the transposable element landscape shaping the Ectocarpus genome
Dinatale, E., Craig, R. J., Martinho, C., Drost, H., & Coelho, S. M. (2025) · Genome biology · doi:10.1186/s13059-025-03742-z · Cited by 6
Epigenetics in forest trees- key driver to phenotypic plasticity and adaptation under stress
Thakur, S., Kumar, R., Thakur, L., & Thakur, S. (2025) · Functional & Integrative Genomics · doi:10.1007/s10142-025-01711-0 · Cited by 5
Selective Comprehensive Online NanoLCxCZE-MS Platform for Top-Down Proteoform Analysis
Waldmann, T., Kaulich, P. T., Stolz, A., Tholey, A., & Neusüß, C. (2025) · Analytical Chemistry · doi:10.1021/acs.analchem.5c03469 · Cited by 4
Gao, Z., Rossler, K. J., Rogers, H. T., Gregorich, Z. R., Aballo, T. J., Chapman, E. A., Price, S. J., Hermsen, J. L., de Lange, W. J., Zhu, Y., et al. (2025) · Circulation Heart Failure · doi:10.1161/circheartfailure.125.012899 · Cited by 6
Cheng, S., Cheng, C., Zhou, J., Ji, Y. S., Liu, Y., Jiang, W., Liu, C., & Wang, H. (2025) · Nutrition Reviews · doi:10.1093/nutrit/nuaf258 · Cited by 7
Cuproptosis promotes inflammatory osteolysis via GYS1-mediated glycogen metabolism
Zhou, L., Mao, H., Wen, Y., Chen, Z., & Zhang, L. (2026) · International Journal of Oral Science · doi:10.1038/s41368-025-00408-1 · Cited by 6
Maccioni, R., Tambaro, S., Doro, L., Bassareo, V., Peana, A. T., & Acquas, E. (2026) · Antioxidants · doi:10.3390/antiox15020216 · Cited by 6
Blood-based epigenetic biomarkers in rheumatoid arthritis: current knowledge and future perspectives
Mołoń, A., Kubis, H., Żurawska, J., & Cieśla, M. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1753808 · Cited by 7
Unraveling the complexity of the histone code: implications for gene regulation and disease
Malone, K. L., Singh, A. K., Lignos, J. M., Cook, E. D., Phillips, M., Boyle, B. W., Kressy, I. A., Vulikh, M., Lathrop, A. K., McKay, K. T., et al. (2026) · Genome biology · doi:10.1186/s13059-026-04011-3 · Cited by 6
Baderna, V., Barzaghi, G., Kleinendorst, R., Chatsirisupachai, K., Moniot-Perron, L., Doyle, C., Schopp, M., Hochepied, T., Libert, C., Odom, D. T., et al. (2026) · Nature Genetics · doi:10.1038/s41588-026-02703-x · Cited by 12
Predicting the effect of CRISPR-Cas9-based epigenome editing
Batra, S. S., Cabrera, A., Spence, J. P., Goell, J., Anand, S. S., Hilton, I. B., & Song, Y. S. (2026) · eLife · doi:10.7554/elife.92991.4 · Cited by 5
Xu, M., Lu, X., Zhu, F., Sun, X., Yao, H., Zhang, J., Chen, W., Zhu, H., Liu, F., Shi, S., et al. (2024) · Journal of Cellular Biochemistry · doi:10.1002/jcb.30535 · Cited by 5
Al‐Aqtash, R., & Collier, D. M. (2024) · Channels · doi:10.1080/19336950.2024.2355150 · Cited by 5
After the Storm: Persistent Molecular Alterations Following HCV Cure
Seurre, C., Suarez, A. A. R., Testoni, B., Zoulim, F., & Grigorov, B. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25137073 · Cited by 5
The Molecular Basis of Differentiation Wave Activity in Embryogenesis
Alicea, B., Bastani, S., Gordon, N. K., Crawford-Young, S. J., & Gordon, R. (2024) · Biosystems · doi:10.1016/j.biosystems.2024.105272 · Cited by 5
Wu, Y., Li, Y., Xie, H., Zhang, Y., Bao, X., Sha, X., Wen, J., Li, Y., & Zhang, Z. (2024) · Nano Today · doi:10.1016/j.nantod.2024.102519 · Cited by 5
Interplay and Dynamics of Chromatin Architecture and DNA Damage Response: An Overview
Ambrosio, S., Noviello, A., Fusco, G. D., Gorini, F., Piscone, A., Amente, S., & Majello, B. (2025) · Cancers · doi:10.3390/cancers17060949 · Cited by 8
APC/C-mediated ubiquitylation of extranucleosomal histone complexes lacking canonical degrons
Skrajna, A., Bodrug, T., Martinez‐Chacin, R. C., Fisher, C. B., Welsh, K. A., Simmons, H. C., Arteaga, E. C., Simmons, J. M., Nasr, M. A., LaPak, K. M., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-57384-7 · Cited by 5
Genomic and Epigenomic Plasticity in the Hypoxic Environment
Cricchi, E., Bertozzo, A., Minisini, M., & Brancolini, C. (2025) · DNA · doi:10.3390/dna5020022 · Cited by 6
Mutant EZH2 alters the epigenetic network and increases epigenetic heterogeneity in B cell lymphoma
Griess, O., Furth, N., Harpaz, N., Bernardo, N. D., Salame, T., Dassa, B., Karagiannidis, I., Isshiki, Y., Gross, M., Melnick, A. M., et al. (2025) · PLoS Biology · doi:10.1371/journal.pbio.3003191 · Cited by 6
Plant chromatin on the move: an overview of chromatin mobility during transcription and DNA repair
Meschichi, A., & Rosa, S. (2023) · The Plant Journal · doi:10.1111/tpj.16159 · Cited by 5
The interplay between viral molecular mimicry and host chromatin dynamics
Shumin, X., Wang, Y., Shan, S., & Zhou, Z. (2023) · Nucleus · doi:10.1080/19491034.2023.2216560 · Cited by 5
Biased eviction of variant histone H3 nucleosomes triggers biofilm growth in Candida albicans
Brahma, P., Aggarwal, R., & Sanyal, K. (2023) · mBio · doi:10.1128/mbio.02063-23 · Cited by 5
Song, Y., Chang, Z., Feng, Y., Wang, T., & Liu, L. (2024) · BMC Plant Biology · doi:10.1186/s12870-024-05318-8 · Cited by 6
Gao, Z., He, T., Zhang, P., Hu, X., Ge, M., Xu, Y.-Q., Wang, P., & Pan, H. (2024) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2024.2375372 · Cited by 5
Godschalk, R., Faulk, C. D., LaRocca, J. L., van Benthem, J., & Marchetti, F. (2024) · Environmental and Molecular Mutagenesis · doi:10.1002/em.22626 · Cited by 8
Berluti, F., Baselious, F., Hagemann, S., Hilscher, S., Schmidt, M., Hüttelmaier, S., Schutkowski, M., Sippl, W., & Ibrahim, H. S. (2024) · Archiv der Pharmazie · doi:10.1002/ardp.202400437 · Cited by 5
Liu, P., Zhang, J., Zhang, J., Yuan, Y., Liu, Z., Chen, S., Chen, K., Li, D., Cheng, Z., Zhang, Y., et al. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1566567 · Cited by 5
Armeev, G. A., Gribkova, A. K., & Shaytan, A. К. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.04.17.537230 · Cited by 5
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. (2023) · eLife · doi:10.7554/elife.92991 · Cited by 6
Lv, L.-Z., Wang, Z.-D., Ren, J.-J., Li, L.-H., Liu, X.-B., Li, J.-L., Zhu, H., Jiang, B., Han, Y.-P., Zhou, X.-M., et al. (2026) · Frontiers in Genetics · doi:10.3389/fgene.2025.1722453 · Cited by 7
ESRP2–microRNA-122 axis promotes the postnatal onset of liver polyploidization and maturation
Bangru, S., Chen, J., Baker, N., Das, D., Chembazhi, U. V., Derham, J. M., Chorghade, S., Arif, W., Alencastro, F., Duncan, A. W., et al. (2025) · Genes & Development · doi:10.1101/gad.352129.124 · Cited by 4
Viral imitation is the sincerest form of epigenetic flattery
Smith, J. R., Arellano, A. A., & Avgousti, D. C. (2024) · Molecular Biology of the Cell · doi:10.1091/mbc.e23-04-0147 · Cited by 4
Plant BCL-DOMAIN HOMOLOG proteins play a conserved role in SWI/SNF complex stability
Candela-Ferre, J., Pérez-Alemany, J., Diego‐Martin, B., Pandey, V., Wohlschlegel, J. A., Lozano‐Juste, J., & Gallego‐Bartolomé, J. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2413346122 · Cited by 4
Chen, C., McCauley, B. S., Matulionis, N., Vogelauer, M., Camacho, D. J., Christofk, H. R., Dang, W., Irwin, N. A. T., & Kurdistani, S. K. (2025) · Science Advances · doi:10.1126/sciadv.adv4082 · Cited by 4
Tubulin Acetylation: A Critical Regulator of Microtubule Function
Delgado, I. L. S., Carmona, B., Nolasco, S., Marques, R., Gonçalves, J., & Soares, H. (2025) · Results and problems in cell differentiation · doi:10.1007/978-3-031-91459-1_4 · Cited by 6
Garg, J., Saettone, A., Nabeel‐Shah, S., Dang, S., Khalid, A. H., Loehr, J., Petrova, A., Burns, J. D., Karabatsos, P., Shibin, S., et al. (2025) · Epigenetics & Chromatin · doi:10.1186/s13072-025-00614-5 · Cited by 4
Deacetylase SIRT1 modulates antiviral innate immunity and autoimmune diseases
Yu, S., Yu, H., Geng, S., Tang, R.-C., Zhang, A., Zhang, Y., Sun, X., & Zhang, J. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.147873 · Cited by 4
Michailidis, T. M., Corveleyn, L., Almey, R., Bader, Y., Odongo, G. A., Herceg, Z., Khoueiry, R., Saeger, S. D., Boevre, M. D., & Dhaenens, M. (2025) · Environment International · doi:10.1016/j.envint.2025.109813 · Cited by 4
Decoding replication stress responses through post-translational modifications
Han, J., Wu, M., Liu, T., & Huang, J. (2025) · Nature Chemical Biology · doi:10.1038/s41589-025-02023-x · Cited by 5
Polyphenols-mediated immune regulation: Metabolite-driven epigenetic regulatory mechanisms
Ouyang, B., Wu, Q., Liang, J., Cao, H., & Xiao, J. (2025) · Phytomedicine · doi:10.1016/j.phymed.2025.157535 · Cited by 6
Ye, Z., Mayila, M., Bu, N., Hao, W., & Maimaitiyiming, Y. (2025) · Environmental Pollution · doi:10.1016/j.envpol.2025.127559 · Cited by 5
Complex-specific inhibitors for interrogating ATAC histone acetyltransferase complex
Liu, S., Liu, J., Wu, Y., Yao, X., Li, X., Dong, X., Li, Q., Cheung, H. J. H., Wong, K. Y., Li, Y., et al. (2026) · Nature Chemical Biology · doi:10.1038/s41589-025-02132-7 · Cited by 4
Zhang, K., Zhu, S., Xing, N., Zhou, Z. G., Chen, J., Si, T., Li, M., Jia, L., Rastegar‐Kashkooli, Y., Wang, T. J., et al. (2026) · British Journal of Pharmacology · doi:10.1111/bph.70302 · Cited by 4
Pervasive Transcription in the Human Genome Exceeds Background Noise
Adey, B. N., Maddock, D. J., Denmat, S. H., Dinger, M. E., Gardner, P. P., Poole, A. M., & Ganley, A. R. D. (2026) · Genome Biology and Evolution · doi:10.1093/gbe/evag042 · Cited by 4
PA200-Mediated Proteasomal Protein Degradation and Regulation of Cellular Senescence
Wen, P., Sun, Y., Jiang, T.-X., & Qiu, X. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25115637 · Cited by 4
Geshkovski, V., Hijazi, H., Manessier, J., Brugière, S., Courçon, M., Vachon, G., Pflieger, D., & Carles, C. C. (2024) · Methods in molecular biology · doi:10.1007/978-1-0716-4228-3_2 · Cited by 4
Wang, J., Lou, Y., Peng, X., Ye, M., Cao, W., Wu, J., Yan, Z., Zhao, X., Zhou, Y., Zheng, C., et al. (2025) · Translational Oncology · doi:10.1016/j.tranon.2025.102275 · Cited by 4
Akter, M., Lyu, X., Lu, J., Wang, X., Phonesavanh, T., Wang, H., Yu, H., & Kang, J. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.108464 · Cited by 4
Kuecks-Winger, H. N., Thambirajah, A. A., Corrie, L. M., & Helbing, C. C. (2025) · Comparative Biochemistry and Physiology Part D Genomics and Proteomics · doi:10.1016/j.cbd.2025.101513 · Cited by 4
Li, J., Liu, C., Qiu, S.-Y., Zheng, S.-M., & He, Y.-Z. (2025) · Current Medical Science · doi:10.1007/s11596-025-00049-9 · Cited by 4
Li, M., Liu, Y., Jiang, C., Zhang, S., Nan, M., Liu, J., & Han, Y. (2025) · Frontiers in Oncology · doi:10.3389/fonc.2025.1569651 · Cited by 4
The epigenetic roles of pirfenidone - implication in liver disease management
Rosas-Campos, R., Franco-Acevedo, A., & Armendáriz‐Borunda, J. (2025) · Epigenomics · doi:10.1080/17501911.2025.2579498 · Cited by 4
Histone Modification Networks Reshape the Metabolism and Treatment Landscape of Urological Cancers
Liu, F., He, L., Yu, M., Chen, J., Huang, Y., Ma, W., Wan, Y., & Zhou, B. (2025) · Frontiers in Bioscience-Landmark · doi:10.31083/fbl42831 · Cited by 6
CUT&Tag for High‐Resolution Epigenomic Profiling From a Low Amount of Arabidopsis Tissue
Fu, Y., Schmid, M. W., & Simonini, S. (2026) · Plant Direct · doi:10.1002/pld3.70161 · Cited by 4
Ye, Y., Li, L., Dai, Q., Liu, Y., & Shen, L. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.991980 · Cited by 4
Pani, B., & Nudler, E. (2023) · Nature Microbiology · doi:10.1038/s41564-023-01509-5 · Cited by 4
Lin, X., Shi, Y., Liu, S., Liu, X., Zhang, M., Zhang, B., Li, S., & Chen, K. (2023) · Food Quality and Safety · doi:10.1093/fqsafe/fyad052 · Cited by 4
Decreased NSD2 impairs stromal cell proliferation in human endometrium via reprogramming H3K36me2
Qin, C., Wei, X., Wu, J., Liu, X., & Lin, Y. (2024) · Reproduction · doi:10.1530/rep-23-0254 · Cited by 4
Systematic investigation of interindividual variation of DNA methylation in human whole blood
Grant, O. A., Meena Kumari, B., Schalkwyk, L. C., & Zabet, N. R. (2026) · Genome biology · doi:10.1186/s13059-026-04021-1 · Cited by 5
Jang, J., Accornero, F., & Li, D. (2024) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2024.108638 · Cited by 4
Guerrero‐Bosagna, C. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-19051-3.00001-2 · Cited by 4
Epigenetics of cerebrovascular diseases: an update review of clinical studies
Ciaccio, A. M., & Tuttolomondo, A. (2024) · Epigenomics · doi:10.1080/17501911.2024.2377947 · Cited by 4
Zhu, J., Qiu, X., Jin, X., Nie, X., Ou, S., Wu, G., Shen, J., & Zhang, R. (2024) · Cellular Oncology · doi:10.1007/s13402-024-00976-0 · Cited by 6
Multi-step HPLC fractionation enabled in-depth and unbiased characterization of histone PTMs
Zhao, W., Chen, K., Zhang, J., Zhang, M., Guo, J., Xie, D., Xu, J., & Tan, M. (2024) · Journal of Chromatography A · doi:10.1016/j.chroma.2024.465368 · Cited by 4
The opportunities and challenges of epigenetic approaches to manage herpes simplex infections
Saddoris, S. M., & Schang, L. M. (2024) · Expert Review of Anti-infective Therapy · doi:10.1080/14787210.2024.2420329 · Cited by 4
Song, M.-J., Kim, M.-K., Seo, J., Kwon, H. M., Yang, C. H., Joo, J.-S., Cho, Y., & Kim, H. (2025) · BMB Reports · doi:10.5483/bmbrep.2024-0175 · Cited by 4
Shueili, B. A., Dantas, A. E., Mahé, E., Chu, T., Yang, Y., Labit, E., Kutluberk, E., Lasaleta, N., Masson, A. O., Omairi, H., et al. (2025) · PLoS ONE · doi:10.1371/journal.pone.0313255 · Cited by 4
Logeman, B. L., Grieco, S. F., Holmes, T. C., & Xu, X. (2025) · Molecular Psychiatry · doi:10.1038/s41380-025-03056-3 · Cited by 4
Song, J., Zhang, L., Song, B.-Q., & Yang, G. (2022) · Chemical Engineering Journal · doi:10.1016/j.cej.2022.141020 · Cited by 2
Zhang, X., Yang, Y., Wang, L., & Qin, Y. (2024) · World Journal of Microbiology and Biotechnology · doi:10.1007/s11274-024-03978-0 · Cited by 4
A screen for histone mutations that affect quiescence in S. cerevisiae
Small, E. M., & Osley, M. A. (2023) · FEBS Journal · doi:10.1111/febs.16759 · Cited by 4
Turki, T., Roy, S. S., & Taguchi, Y. (2023) · Algorithms · doi:10.3390/a16090401 · Cited by 4
Histone H3 as a redox switch in the nucleosome core particle: insights from molecular modeling †Preprint
Karami, Y., González‐Alemán, R., Duch, M., Qiu, Y., Kedjar, Y., & Bignon, E. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.07.616940 · Cited by 4
Hua, Y., Duan, N., Sun, C., Yang, F., Tian, M., Sun, Y., Zhao, S., Gong, J., Liu, Q., Huang, X., et al. (2025) · eLife · doi:10.7554/elife.103953 · Cited by 5
The SWI/SNF nucleosome remodeler constrains enhancer activity during Drosophila wing development
Niederhuber, M. J., Leatham-Jensen, M. P., & McKay, D. J. (2023) · Genetics · doi:10.1093/genetics/iyad196 · Cited by 3
Lu, R.-H., Lin, B., Lin, Z., Xiong, H., Liu, J., Li, L., Gong, Z., Wang, S., Zhang, M., Ding, J., et al. (2024) · Journal of Advanced Research · doi:10.1016/j.jare.2024.11.037 · Cited by 4
Aydemir, M., Kömür, A. İ., Gündüz, E. S., Karaman, C., & Karaman, O. (2025) · Microchemical Journal · doi:10.1016/j.microc.2025.114118 · Cited by 4
Guan, Y., Chen, X., Zhu, X., Liu, F., Ma, Y., Han, W., Yang, R., Li, Y., Bao, L., Wang, S., et al. (2025) · BMC Genomics · doi:10.1186/s12864-025-11776-7 · Cited by 4
Wu, S.-T., Zhu, Z., Lin, Y.-J., Xu, Q.-Y., Lei, X., Wei, J.-G., & Qin, Q.-W. (2025) · Fish and Shellfish Immunology · doi:10.1016/j.fsi.2025.110887 · Cited by 4
Zhao, Y., Nguyen, A., Arteaga, E. C., Skrajna, A., Krajewski, K., Goldfarb, D., & McGinty, R. K. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf897 · Cited by 3
A time-resolved atlas of histone modifications during mitotic entry
Kochanova, N. Y., Deb, M., Borsò, M., Webb, S., Ustun, I., Samejima, K., Forné, I., Samejima, I., Reid, C., Xie, L., et al. (2026) · Molecular Cell · doi:10.1016/j.molcel.2026.03.038 · Cited by 3
Scarpa, E. S., Amatori, S., Caprioli, G., Maggi, F., Moroncini, G., Balercia, G., & Giacchetti, G. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262010142 · Cited by 3
Engineered nanotechnology for epigenetic therapy in cancer treatment
Li, Y., Li, Y., Tan, Y., Cai, Y., Liu, X., Wei, C., Yu, W., Fu, Y., & Cao, H. (2025) · Chemical Engineering Journal · doi:10.1016/j.cej.2025.170485 · Cited by 4
Succinylation of GyrB Is a Mechanism Conferring Fluoroquinolone Resistance
Jha, A. K., Faheem, I., & Nagaraja, V. (2025) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.5c00781 · Cited by 3
Simulating cell-free chromatin using preclinical cancer models for liquid biopsy applications
Main, S. C., Michino, S. D. D., Penny, L., Aamir, A., Keshavarzian, T., Lok, B. H., Kridel, R., Cescon, D. W., Hoffman, M. M., Lupien, M., et al. (2025) · iScience · doi:10.1016/j.isci.2025.114113 · Cited by 3
Shi, W. S., Zhao, L., Wang, Y., Zhang, Y., Liu, S., Wang, Y., Kornberg, R. D., & Zhang, H. (2025) · Nature Communications · doi:10.1038/s41467-025-67049-0 · Cited by 3
Protein post-translational modifications in sepsis: Molecular mechanisms and biomarkers
Wang, Y., Li, H., Zhao, Q., Li, X., Bu, X., Ma, C., Liu, Z., Yang, J.-H., & Sun, T. (2025) · Ageing Research Reviews · doi:10.1016/j.arr.2025.102958 · Cited by 3
Deacetylated PCBP1 licenses PARP1 activity for DNA damage repair
Shu, Y., Zhang, J., Zhou, L., Feng, T., Chen, F., Tang, H., Li, M., Qian, J., Qin, M., Wang, Z., et al. (2026) · Molecular Cell · doi:10.1016/j.molcel.2026.05.008 · Cited by 4
Anesthetic-induced epigenetic alterations: mechanisms and long-term clinical implications
Delshad, E. S., Shamsi, A., Mohseni, M. M., Abak, N., & Saberian, M. (2025) · Epigenetics · doi:10.1080/15592294.2025.2599650 · Cited by 4
Reimagining biogenic amine signaling in the brain and beyond
Vinson, D. A., & Maze, I. S. (2025) · Trends in Neurosciences · doi:10.1016/j.tins.2025.11.003 · Cited by 4
Zhang, J., & Zou, M. (2025) · Cancer Management and Research · doi:10.2147/cmar.s552195 · Cited by 3
Orsburn, B. C. (2025) · Communications Biology · doi:10.1038/s42003-025-09452-3 · Cited by 4
Cardiac epigenome in heart development and disease
Laurette, P., & Gilsbach, R. (2026) · Nature Reviews Cardiology · doi:10.1038/s41569-025-01223-1 · Cited by 4
Liu, C., Lin, L., Yao, G., Fan, Y., & Guo, Y. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1725917 · Cited by 3
Tang, M., Zhu, H., Li, S., & Qiao, L. (2026) · Diabetology & Metabolic Syndrome · doi:10.1186/s13098-026-02129-9 · Cited by 4
Liu, W., Zhang, Z., Du, Q., Li, J., Yang, L., Ren, Z., Guo, J., Zhu, W., Ma, Z., Zhou, Y., et al. (2026) · Journal of Advanced Research · doi:10.1016/j.jare.2026.03.027 · Cited by 3
TNF-α/PAD4 axis drives hyperhomocysteine-induced white matter injury after acute ischemic stroke
Du, W., Guo, H., Wang, Y.-H., Hu, X., Zhang, J.-N., Guo, C., Geng, P., Wang, Y.-J., & Jin, X.-C. (2026) · Acta Pharmacologica Sinica · doi:10.1038/s41401-026-01795-9 · Cited by 3
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