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 301–400 of 1,001

Therapeutic regulation of epigenetics in cancer treatment through drug delivery systems
Su, B., Li, S., Geng, S., Brambilla, D., Sun, R., Sun, T., & Jiang, C. (2024) · Nano Today · doi:10.1016/j.nantod.2024.102251 · Cited by 12
Epigenetics and Control of Tumor Angiogenesis in Melanoma: An Update with Therapeutic Implications
Cazzato, G., Sgarro, N., Casatta, N., Lupo, C., Ingravallo, G., & Ribatti, D. (2024) · Cancers · doi:10.3390/cancers16162843 · Cited by 12
Heterochromatin formation and remodeling by IRTKS condensates counteract cellular senescence
Xie, J., Lu, Z., Bai, S., Cui, X., Lian, H.-Y., Xie, C.-Y., Wang, N., Wang, L., & Han, Z. (2024) · The EMBO Journal · doi:10.1038/s44318-024-00212-3 · Cited by 14
Histone-acetyl epigenome regulates TGF-β pathway-associated chemoresistance in colorectal cancer
Tian, X., Liu, G., Ji, L., Shen, Y., Gu, J., Wang, L., Ma, J., Xia, Z., & Li, X. (2024) · Translational Oncology · doi:10.1016/j.tranon.2024.102166 · Cited by 12
Train and Reprogram Your Brain: Effects of Physical Exercise at Different Stages of Life on Brain Functions Saved in Epigenetic Modifications
Kukla‐Bartoszek, M., & Głombik, K. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252212043 · Cited by 16
A tale of two strands: Decoding chromatin replication through strand-specific sequencing
Li, Z., & Zhang, Z. (2025) · Molecular Cell · doi:10.1016/j.molcel.2024.10.035 · Cited by 13
The ABCs of the H2Bs: The histone H2B sequences, variants, and modifications
Voss, A. J., & Korb, E. (2025) · Trends in Genetics · doi:10.1016/j.tig.2025.01.003 · Cited by 12
HDAC1 controls the generation and maintenance of effector-like CD8+ T cells during chronic viral infection
Rîca, R., Waldherr, M., Miyakoda, E., Kutschat, A. P., Schülein, M., Zhang, J., Orbegozo-Medina, R. A., Sandner, L., Stolz, V., Waltenberger, D., et al. (2025) · The Journal of Experimental Medicine · doi:10.1084/jem.20240829 · Cited by 13
RNF20-mediated H2B monoubiquitination protects stalled forks from degradation and promotes fork restart
Bhattacharya, D., Dwivedi, H. K., & Nagaraju, G. (2025) · EMBO Reports · doi:10.1038/s44319-025-00497-3 · Cited by 12
Combinatorial profiling of multiple histone modifications and transcriptome in single cells using scMTR-seq
Wang, Y., Li, J., Malcolm, A. A., Mansfield, W., Clark, S. J., Argelaguet, R., Biggins, L., Acton, R., Andrews, S., Reik, W., et al. (2025) · Science Advances · doi:10.1126/sciadv.adu3308 · Cited by 11
The role of SELENBP1 and its epigenetic regulation in carcinogenic progression
Zhang, Y., & He, Q. H. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2022.1027726 · Cited by 12
Novel insights into the recognition of acetylated histone H4 tail by the TRIM24 PHD-Bromo module
Bardhan, I., Barman, S., Roy, A., & Sudhamalla, B. (2023) · Biochemical Journal · doi:10.1042/bcj20230011 · Cited by 12
Nuclear envelope, chromatin organizers, histones, and DNA: The many achilles heels exploited across cancers
Balaji, A., Saha, S., Deshpande, S., Poola, D., & Sengupta, K. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.1068347 · Cited by 12
Regulatory role and therapeutic prospect of lactate modification in cancer
Sun, M., Wang, K., Lu, F., Yu, D., & Liu, S. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1508552 · Cited by 12
Lactylation-boosted polycomb repression of KLF4 elicits glycolysis in retinoblastoma: A positive feedback circuit between histone modifications
Yang, L., Zuo, S., Jia, R., Gu, X., Liao, Q., Hua, Y., Ge, S., He, M., Fan, J., Tong, X., et al. (2025) · Cancer Letters · doi:10.1016/j.canlet.2025.217804 · Cited by 11
Protein post-translational modifications in serine synthetic pathway: functions and molecular mechanisms
Shu, M., Liu, Y., & Wang, J. (2025) · Cell Communication and Signaling · doi:10.1186/s12964-025-02327-4 · Cited by 12
Emerging roles of histone methylation in phytopathogenic fungi
Zhang, Q., & Zeng, T. (2025) · aBIOTECH · doi:10.1007/s42994-025-00223-6 · Cited by 11
From allergens to epigenetics: how histone acetylation shapes immune gene expression in allergic diseases
Cai, X., Afthab, M., Hambo, S., Salem, M., Bhitale, R. R., & Harb, H. (2025) · Epigenomics · doi:10.1080/17501911.2025.2548758 · Cited by 11
H4K16 acylations destabilize chromatin architecture and facilitate transcriptional response during metabolic perturbations
Nitsch, S., Coraor, A. E., Schauer, T., Wu, Y., Sun, J., Möritz, N., Funke, J. J., Nagpal, H., Chua, G. N. L., Battistini, F., et al. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.11.030 · Cited by 11
Self-citation
Toxicoepigenomics: Epigenetic disruption by environmental exposures and implications for biomarker development
Kim, J.-Y., & Kim, J.-W. (2026) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2026.141070 · Cited by 14
KLF12 transcriptionally regulates PD‐L1 expression in non‐small cell lung cancer
Pan, X., Zhang, W., Wang, L., Guo, H., Zheng, M., Wu, H., Weng, Q., He, Q., Ding, L., & Yang, B. (2023) · Molecular Oncology · doi:10.1002/1878-0261.13512 · Cited by 13
Interplay between epigenome and 3D chromatin structure
Han, M.-H., Issagulova, D., & Park, M. (2023) · BMB Reports · doi:10.5483/bmbrep.2023-0197 · Cited by 13
Development of Complementary Photo‐arginine/lysine to Promote Discovery of Arg/Lys hPTMs Interactomes
Zong, Y., Weiss, N., Wang, K., Pagano, A. E., Heissel, S., Perveen, S., & Huang, J. (2024) · Advanced Science · doi:10.1002/advs.202307526 · Cited by 11
Mass Spectrometry-Based Profiling of Histone Post-Translational Modifications in Uveal Melanoma Tissues, Human Melanocytes, and Uveal Melanoma Cell Lines – A Pilot Study
Herwig‐Carl, M. C., Sharma, A., Tischler, V., Pelusi, N., Loeffler, K. U., Holz, F. G., Zeschnigk, M., Landreville, S., Auw‐Haedrich, C., Noberini, R., et al. (2024) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.65.2.27 · Cited by 12
Structure-function analyses reveal Arabidopsis thaliana HDA7 to be an inactive histone deacetylase
Saharan, K., Baral, S., Shaikh, N. H., & Vasudevan, D. (2024) · Current Research in Structural Biology · doi:10.1016/j.crstbi.2024.100136 · Cited by 10
Exploring affinity chromatography in proteomics: A comprehensive review
Chamrád, I., Simerský, R., Lenobel, R., & Novák, O. (2024) · Analytica Chimica Acta · doi:10.1016/j.aca.2024.342513 · Cited by 14
New facets in the chromatin-based regulation of genome maintenance
Dabin, J., Giacomini, G., Petit, E., & Polo, S. E. (2024) · DNA repair · doi:10.1016/j.dnarep.2024.103702 · Cited by 11
How Histone Acetyltransferases Shape Plant Photomorphogenesis and UV Response
Boycheva, I., Bonchev, G., Manova, V. I., Stoilov, L., & Vassileva, V. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25147851 · Cited by 11
The Contribution of Genetic and Epigenetic Factors: An Emerging Concept in the Assessment and Prognosis of Inflammatory Bowel Diseases
Minea, H. O., Sîngeap, A.-M., Minea, M., Juncu, S. S., Muzica, C. M., Sfarti, C. V., Gîrleanu, I., Chiriac, S. A., Miftode, D., Stanciu, C., et al. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25158420 · Cited by 11
Lactylation and Ischemic Stroke: Research Progress and Potential Relationship
Zhang, J., lin, F., Xu, Y., Sun, J., Zhang, L., & Chen, W. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-04624-4 · Cited by 11
Identification of a robust promoter in mouse and human hepatocytes by in vivo biopanning of a barcoded AAV library
Becker, J., Domenger, C., Choksi, P. K., Krämer, C., Baumgartl, C., Maiakovska, O., Kim, J.-J., Weinmann, J., Huber, G., Schmidt, F., et al. (2025) · Molecular Therapy · doi:10.1016/j.ymthe.2025.04.027 · Cited by 11
Epitranscriptome–epigenome interactions in development and disease mechanisms
Li, C., Chen, K., Li, X., & Xiong, X. (2025) · Trends in Genetics · doi:10.1016/j.tig.2025.04.009 · Cited by 11
Cancer histone mutations impact protein binding and DNA repair with possible links to genomic instability
Espiritu, D., Sheng, Y., Peng, Y., Ostroverkhova, D. S., Li, S., Landsman, D., Aristizabal, M. J., & Panchenko, A. R. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf899 · Cited by 11
A Strategy to Characterize the Global Landscape of Histone Post-Translational Modifications Within Tissues of Nonmodel Organisms
Mojica, E. A., & Kültz, D. (2023) · Journal of Proteome Research · doi:10.1021/acs.jproteome.3c00246 · Cited by 11
Interplay between epigenetic and genetic alterations in inborn errors of immunity
Rodríguez‐Ubreva, J., Calvillo, C. L., Satter, L. F., & Ballestar, E. (2023) · Trends in Immunology · doi:10.1016/j.it.2023.09.005 · Cited by 11
Single cell proteomics by mass spectrometry reveals deep epigenetic insight into the actions of an orphan histone deacetylase inhibitorPreprint
Orsburn, B. C. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.01.05.574437 · Cited by 11
The GOLM1-ACLY pathway regulates macrophage-secreted EFEMP1 via H3K27ac modifications to drive tumor progression
Zhen, L., Min, M., Mo, X., Zhao, G., Li, H., Liu, M., Wan, L., Yang, X., Huang, L., Zhang, Y., et al. (2025) · Journal of Advanced Research · doi:10.1016/j.jare.2025.07.003 · Cited by 10
Roles of histone post-translational modifications in meiosis
Nie, H., Kong, X., Song, X., Guo, X.-Y., Li, Z., Fan, C., Zhai, B., Yang, X., & Wang, Y. (2024) · Biology of Reproduction · doi:10.1093/biolre/ioae011 · Cited by 9
EP300/CREBBP acetyltransferase inhibition limits steroid receptor and FOXA1 signaling in prostate cancer cells
Huttunen, J., Aaltonen, N., Helminen, L., Rilla, K. J., & Paakinaho, V. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-024-05209-z · Cited by 10
Exploring the epigenome to identify biological links between the urban environment and neurodegenerative disease: an evidence review
Glover, S., Hill, C., McGuinness, B., McKnight, A. J., & Hunter, R. F. (2024) · Cities & Health · doi:10.1080/23748834.2024.2335707 · Cited by 14
CK2-dependent degradation of CBX3 dictates replication fork stalling and PARP inhibitor sensitivity
Ma, J., Ren, D., Wang, Z., Li, W., Li, L., Liu, T., Ye, Q., Lei, Y., Jian, Y., Ma, B., et al. (2024) · Science Advances · doi:10.1126/sciadv.adk8908 · Cited by 10
Molecular models of bidirectional promoter regulation
Nemsick, S., & Hansen, A. S. (2024) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2024.102865 · Cited by 11
A hitchhiker's guide to single‐cell epigenomics: Methods and applications for cancer research
Moreno‐Gonzalez, M., Sierra, I., & Kind, J. (2024) · International Journal of Cancer · doi:10.1002/ijc.35307 · Cited by 11
Epigenetic and epitranscriptomic regulation during oncogenic γ-herpesvirus infection
Singh, R. K., Ramakrishna, V., Torne, A. S., Bose, D., & Robertson, E. S. (2025) · Frontiers in Microbiology · doi:10.3389/fmicb.2024.1484455 · Cited by 10
Mutations in histones dysregulate copper homeostasis leading to defect in Sec61-dependent protein translocation mechanism in Saccharomyces cerevisiae
Acharjee, S., Pal, R., Anand, S., Thakur, P., Anjana, V., Singh, R., Paul, M., Biswas, A., & Tomar, R. S. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.108163 · Cited by 10
Basic Epigenetic Mechanisms
Davie, J., Sattarifard, H., Sudhakar, S. R. N., Roberts, C.-T., Beacon, T. H., Muker, I., Shahib, A. K., & Rastegar, M. (2025) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-031-75980-2_1 · Cited by 12
Setd2 overexpression rescues bivalent gene expression during SCNT-mediated ZGA
Zhang, X., Xu, R., Zhao, Y., Yang, Y., Shi, Q., Wang, H., Liu, X., Gao, S., & Li, C. V. (2025) · Protein & Cell · doi:10.1093/procel/pwaf010 · Cited by 12
Diversity and evolution of chromatin regulatory states across eukaryotes
Navarrete, C., Montgomery, S. A., Mendieta-Esteban, J., Księżopolska, E., Renema, J., Chiva, C., Sabidó, E., Lara‐Astiaso, D., & Sebé-Pedrós, A. (2026) · Nature Genetics · doi:10.1038/s41588-026-02672-1 · Cited by 8
Always on the Move: Overview on Chromatin Dynamics within Nuclear Processes
de Fenffe, C. M. D., Govers, J., & Mattiroli, F. (2025) · Biochemistry · doi:10.1021/acs.biochem.5c00114 · Cited by 10
Exploring lactylation and cancer biology: insights from pathogenesis to clinical applications
Gou, Z., Sun, Q., & Li, J. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1598232 · Cited by 10
Epigenome profiling identifies H3K27me3 regulation of extracellular matrix composition in human corticogenesis
Ditzer, N., Senoglu, E., Kolodziejczyk, A., Schütze, T. M., Nikolaidi, A., Küster, K., Sameith, K., Dietz, S., Derihaci, R. P., Birdir, C., et al. (2025) · Neuron · doi:10.1016/j.neuron.2025.06.016 · Cited by 13
Epigenetic impact of endocrine-disrupting chemicals on atherosclerosis
Lin, T.-A., & Zhou, C. (2025) · Essays in Biochemistry · doi:10.1042/ebc20253022 · Cited by 11
A direct interaction between the Chd1 CHCT domain and Rtf1 controls Chd1 distribution and nucleosome positioning on active genes
Tripplehorn, S. A., Lardo, S. M., Shirra, M. K., Marvil, H. G., Hainer, S. J., & Arndt, K. M. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf816 · Cited by 10
Exercise, Epigenetics, and Body Composition: Molecular Connections
Williams, A., Wadsworth, D. D., & Geetha, T. (2025) · Cells · doi:10.3390/cells14191553 · Cited by 13
Unveiling the influence of polyphenols on histone modifications in human diseases
Wu, Q., Xiao, C., Ouyang, B., Farag, M. A., Yuan, Y., Simal‐Gándara, J., Cao, H., & Xiao, J. (2025) · Phytomedicine · doi:10.1016/j.phymed.2025.157495 · Cited by 12
Arginine methylation in cancer: mechanisms and therapeutic implications
Xu, Y., Wu, Q., Zhang, Y., Gu, Y., Zhu, H., Fu, X., Li, A., & Li, Y. (2025) · Biomarker Research · doi:10.1186/s40364-025-00860-5 · Cited by 13
Post-Translation Modifications and Mutations of Human Linker Histone Subtypes: Their Manifestation in Disease
Kumar, A., Maurya, P., & Hayes, J. J. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24021463 · Cited by 10
Decoding Human Biology and Disease Using Single-Cell Omics Technologies
Shi, Q., Chen, X., & Zhang, Z. (2023) · Genomics Proteomics & Bioinformatics · doi:10.1016/j.gpb.2023.06.003 · Cited by 11
Exploring the effects of topoisomerase II inhibitor XK469 on anthracycline cardiotoxicity and DNA damage
Keresteš, V., Kubeš, J., Applová, L., Kollárová-Brázdová, P., Lenčová-Popelová, O., Melnikova, I., Karabanovich, G., Khazeem, M. M., Piskáčková, H. B., Štěrbová‐Kovaříková, P., et al. (2024) · Toxicological Sciences · doi:10.1093/toxsci/kfae008 · Cited by 10
Nucleosome Dynamics Derived at the Single-Molecule Level Bridges Its Structures and Functions
Chen, P., Li, G., & Li, W. (2024) · JACS Au · doi:10.1021/jacsau.3c00658 · Cited by 8
Histone acetyltransferase Sas3 contributes to fungal development, cell wall integrity, and virulence in Aspergillus fumigatus
Wang, Y., Fan, J., Zhou, Z., Goldman, G. H., Lü, L., & Zhang, Y. (2024) · Applied and Environmental Microbiology · doi:10.1128/aem.01885-23 · Cited by 9
Pathophysiological Implications of Protein Lactylation in Pancreatic Epithelial Tumors
Takata, T., Nakamura, A., Yasuda, H., Miyake, H., Sogame, Y., Sawai, Y., Hayakawa, M., Mochizuki, K., Nakao, R., Ogata, T., et al. (2024) · ACTA HISTOCHEMICA ET CYTOCHEMICA · doi:10.1267/ahc.24-00010 · Cited by 9
Repressing iron overload ameliorates central post-stroke pain via the Hdac2-Kv1.2 axis in a rat model of hemorrhagic stroke
Fang, H., Li, M., Yang, J.-C., Ma, S.-P., Zhang, L., Yang, H.-Q., Tang, Q., Cao, J., & Yang, W.-M. (2024) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-23-01498 · Cited by 9
Epigenetic regulation of heart failure
Deogharia, M., & Gurha, P. (2024) · Current Opinion in Cardiology · doi:10.1097/hco.0000000000001150 · Cited by 8
Bacterial Pangenome: A Review on the Current Strategies, Tools and Applications
Golchha, N. C., Nighojkar, A., & Nighojkar, S. (2024) · Medinformatics · doi:10.47852/bonviewmedin42022496 · Cited by 9
Genome-wide analysis of histone modifications can contribute to the identification of candidate cis-regulatory regions in the threespine stickleback fish
Okude, G., Yamasaki, Y. Y., Toyoda, A., Mori, S., & Kitano, J. (2024) · BMC Genomics · doi:10.1186/s12864-024-10602-w · Cited by 9
Functions of Coenzyme A and Acyl-CoA in Post-Translational Modification and Human Disease
Xie, J., Zhang, Y., Zhu, Y., Zheng, M., & Zhu, Y. P. (2024) · Frontiers in Bioscience-Landmark · doi:10.31083/j.fbl2909331 · Cited by 10
High-resolution multimodal profiling of human epileptic brain activity via explanted depth electrodes
Dwivedi, A. K., Mahesh, A., Sanfeliu, A., Larkin, J., Siwicki, R. A., Sweeney, K. J., O’Brien, D. F., Widdess‐Walsh, P., Picelli, S., Henshall, D. C., et al. (2024) · JCI Insight · doi:10.1172/jci.insight.184518 · Cited by 11
Association of epigenetic landscapes with heterogeneity and plasticity in pancreatic cancer
Manoukian, P., Kuhnen, L. C., van Laarhoven, H. W. M., & Bijlsma, M. F. (2024) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2024.104573 · Cited by 10
Repeated fasting events sensitize enhancers, transcription factor activity and gene expression to support augmented ketogenesis
Korenfeld, N., Charni‐Natan, M., Bruse, J., Goldberg, D. T., Marciano-Anaki, D., Rotaro, D., Gorbonos, T., Radushkevitz-Frishman, T., Polizzi, A., Nasereddin, A., et al. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae1161 · Cited by 12
Phosphoinositide signaling in the nucleus: Impacts on chromatin and transcription regulation
Hifdi, N., Vaucourt, M., Hnia, K., Panasyuk, G., & Vandromme, M. (2024) · Biology of the Cell · doi:10.1111/boc.202400096 · Cited by 9
Acetylation at lysine 27 on maternal H3.3 regulates minor zygotic genome activation
Zhang, J., Li, X., Zhao, Q., Ji, J., Cui, H., Hou, W., Wang, X., Song, E., Xiao, S., Ling, S., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.115148 · Cited by 9
Epigenetic mechanisms in non-small cell lung cancer therapy and chemoresistance
Xu, Y., Yang, M., Xu, Y., Han, J., & Zhu, Q. (2025) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2025.189356 · Cited by 10
Schwann cell reprogramming via EMT-like program following peripheral nerve injury and during nerve regeneration
Dai, W., Miao, Y., & Yi, S. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1621380 · Cited by 9
Molecular mechanisms and functions of protein acetylation in sepsis and sepsis-associated organ dysfunction
Xu, Y.-F., Yang, N., Hao, P.-H., Wen, R., & Zhang, T. (2025) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-025-00773-z · Cited by 10
Epigenetic mechanisms in maternal-fetal crosstalk: inter- and trans-generational inheritance
Tisato, V., D’Aversa, E., Salvatori, F., Sbracia, M., Peluso, G., Scarpellini, F., & Gemmati, D. (2025) · Epigenomics · doi:10.1080/17501911.2025.2568369 · Cited by 11
The complement cascade in Alzheimer’s disease: modern implications of an ancient immune protagonist
Papavergi, M.-T., Bathini, P., Singh, B. B., & Lemere, C. A. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00916-y · Cited by 12
Lactate metabolism and protein lactylation in cancer
Liu, Z., Li, A., Ma, Z., Wang, J., Chen, X., Wang, Z., & Fu, R. (2026) · Molecular Biomedicine · doi:10.1186/s43556-026-00417-4 · Cited by 9
Osteoarthritis: Epidemiology, Pathogenesis, and Treatment
Chen, T., Chen, W., Xu, T., Wang, H., Zhang, Y., Wang, L., Zhu, S., Tao, H., & Yang, X. (2026) · MedComm · doi:10.1002/mco2.70727 · Cited by 14
Catching Nucleosome by Its Decorated Tails Determines Its Functional States
Sehrawat, P., Shobhawat, R., & Kumar, A. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2022.903923 · Cited by 10
An epigenetically inherited UV hyper-resistance phenotype in Saccharomyces cerevisiae
Reardon, R. M., Walsh, A. K., Larsen, C. I. S., Schmidberger, L. H., Morrow, L. A., Thompson, A. E., Wellik, I. G., & Thompson, J. S. (2022) · Epigenetics & Chromatin · doi:10.1186/s13072-022-00464-5 · Cited by 9
Epigenetics of methylmercury
Cediel-Ulloa, A., Lindner, S., Rüegg, J., & Bröberg, K. (2023) · NeuroToxicology · doi:10.1016/j.neuro.2023.05.004 · Cited by 9
Histidine Nτ-methylation identified as a new posttranslational modification in histone H2A at His-82 and H3 at His-39
Hayashi, T., Daitoku, H., Uetake, T., Kako, K., & Fukamizu, A. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105131 · Cited by 9
Post-translational modifications of lysine-specific demethylase 1
Kim, D., Nam, H. J., & Baek, S. H. (2023) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2023.194968 · Cited by 10
Decoding the ubiquitin language: Orchestrating transcription initiation and gene expression through chromatin remodelers and histones
Mandal, K., Tomar, S. K., & Santra, M. K. (2024) · Gene · doi:10.1016/j.gene.2024.148218 · Cited by 9
Histone H3K4ac, as a marker of active transcription start sites and enhancers, plays roles in histone eviction and RNA transcription
Kang, J. G., Kang, Y., & Kim, A. (2024) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2024.195021 · Cited by 9
Research advances of polycomb group proteins in regulating mammalian development
Li, Y., Mo, Y., Chen, C., He, J., & Guo, Z. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1383200 · Cited by 9
3D QSAR pharmacophore based lead identification of G9a lysine methyltransferase towards epigenetic therapeutics
Jana, A., Naga, R., Saha, S., & Banerjee, D. R. (2022) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2022.2135600 · Cited by 9
Reduction of histone proteins dosages increases CFW sensitivity and attenuates virulence of Candida albicans
Dong, Y., Du, J., Deng, Y., Cheng, M., Shi, Z., Zhu, H., Sun, H., Yu, Q., & Li, M. (2023) · Microbiological Research · doi:10.1016/j.micres.2023.127552 · Cited by 8
Development of Locus-Directed Editing of the Epigenome from Basic Mechanistic Engineering to First Clinical Applications
Rots, M. G., & Jeltsch, A. (2024) · Methods in molecular biology · doi:10.1007/978-1-0716-4051-7_1 · Cited by 8
SETDB1 activity is globally directed by H3K14 acetylation via its Triple Tudor Domain
Chandrasekaran, T., Choudalakis, M., Bröhm, A., Weirich, S., Kouroukli, A. G., Ammerpohl, O., Rathert, P., Bashtrykov, P., & Jeltsch, A. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae1053 · Cited by 8
Optimized and Robust Workflow for Quantifying the Canonical Histone Ubiquitination Marks H2AK119ub and H2BK120ub by LC–MS/MS
Lopes, M. D. C., Lund, P. J., & Garcia, B. A. (2024) · Journal of Proteome Research · doi:10.1021/acs.jproteome.4c00519 · Cited by 8
Epigenetic modifications involving ncRNAs in digestive system cancers: focus on histone modification
Yin, X., Li, J., Zhao, J., Zheng, W., Zhang, A., & Ma, J. (2024) · Clinical Epigenetics · doi:10.1186/s13148-024-01773-0 · Cited by 9
H3K4 Methylation and Demethylation in Fungal Pathogens: The Epigenetic Toolbox for Survival and Adaptation in the Host
Rai, M. N., & Rai, R. (2024) · Pathogens · doi:10.3390/pathogens13121080 · Cited by 8
Decoding the epigenetic and transcriptional basis of direct cardiac reprogramming
Peng, W. G., Getachew, A., & Zhou, Y. (2025) · Stem Cells · doi:10.1093/stmcls/sxaf002 · Cited by 9
Mettl3/Eed/Ythdc1 regulatory axis controls endometrial receptivity and function
Hu, X., Li, J., Ding, C., Jiang, J. L., Xia, W., Lu, J., Su, H., Zhang, M., Li, H., Liu, J., et al. (2025) · Communications Biology · doi:10.1038/s42003-025-07667-y · Cited by 8
Epigenetic targets and their inhibitors in the treatment of idiopathic pulmonary fibrosis
Miao, X., Liu, P., Liu, Y., Zhang, W., Li, C., & Wang, X. (2025) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2025.117463 · Cited by 8
Epigenetic drivers of metalloproteinases and metastasis
Seehawer, M., & Polyák, K. (2025) · Trends in Cell Biology · doi:10.1016/j.tcb.2025.02.010 · Cited by 9
Dual roles of methylglyoxal in cancer
Wang, Z., Liu, S., Zhang, M., & Liu, M. (2025) · Frontiers in Oncology · doi:10.3389/fonc.2025.1557162 · Cited by 8
Targeting SLC7A11-mediated cysteine metabolism for the treatment of trastuzumab-resistant HER2-positive breast cancer
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.103953.3 · Cited by 15

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