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 101–200 of 1,001
The Dynamics of Histone Modifications during Mammalian Zygotic Genome Activation
Lugo, F. S., Barrameda, N. I., Castillo‐Aleman, Y. M., Hernández, I. C., Valverde, C. A. V., Bencomo‐Hernandez, A. A., Ventura‐Carmenate, Y., & Jimenez, R. A. R. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25031459 · Cited by 36
Dynamic histone modification patterns coordinating DNA processes
López-Hernández, L., Toolan-Kerr, P., Bannister, A. J., & Millán-Zambrano, G. (2025) · Molecular Cell · doi:10.1016/j.molcel.2024.10.034 · Cited by 38
Self-citationTargeting histone H2B acetylated enhanceosomes via p300/CBP degradation in prostate cancer
Luo, J., Chen, Z., Qiao, Y., Tien, J. C.-Y., Young, E., Mannan, R., Mahapatra, S., Bhattacharyya, R., Xiao, L., He, T., et al. (2025) · Nature Genetics · doi:10.1038/s41588-025-02336-6 · Cited by 39
Recent advancement of HDAC inhibitors against breast cancer
Mehmood, S. A., Sahu, K. K., Sengupta, S., Partap, S., Karpoormath, R. V., Kumar, B., & Kumar, D. (2023) · Medical Oncology · doi:10.1007/s12032-023-02058-x · Cited by 34
Liu, T., Wang, H., Chen, Y., Wan, Z., Du, Z., Shen, H., Yu, Y., Ma, S., Xu, Y., Li, Z., et al. (2023) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-023-02789-9 · Cited by 35
Epigenetics and seasonal timing in animals: a concise review
Fishman, B., & Tauber, E. (2023) · Journal of Comparative Physiology A · doi:10.1007/s00359-023-01673-3 · Cited by 38
Gene silencing by RNA interference: a review
Malakondaiah, S., Julius, A., Divyadharshini, P., Gunthoti, S. S., Ashok, J., Krishana, P. S., & Rebecca, J. (2024) · Genome Instability & Disease · doi:10.1007/s42764-024-00135-7 · Cited by 39
Recent advances in epigenetic anticancer therapeutics and future perspectives
Ren, L., Yang, Y., Wan, L., Yang, H., Zhang, Y., Ge, B., Zhang, S., Du, G., & Wang, J. (2023) · Frontiers in Genetics · doi:10.3389/fgene.2022.1085391 · Cited by 33
Inflammation in Heart Failure—Future Perspectives
Arvunescu, A. M., Ionescu, R. F., Creţoiu, S. M., Dumitrescu, S. I., Zaharia, O., & Nanea, I. T. (2023) · Journal of Clinical Medicine · doi:10.3390/jcm12247738 · Cited by 38
Epigenomic insights into common human disease pathology
Bell, C. G. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-024-05206-2 · Cited by 36
Lopes, M. B., Coletti, R., Duranton, F., Glorieux, G., Campos, M. A. J., Klein, J., Ley, M., Perco, P., Sampri, A., & Tur‐Sinai, A. (2025) · PROTEOMICS · doi:10.1002/pmic.202400108 · Cited by 37
Emerging roles of mitochondrial sirtuin SIRT5 in succinylation modification and cancer development
Ke, Z., Shen, K., Wang, L., Xu, H., Pan, X., Qian, Z., Wen, Y., Lv, T., Zhang, X., & Song, Y. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1531246 · Cited by 35
Promoter editing for the genetic improvement of crops
Shi, L., Su, J., Cho, M., Song, H., Dong, O. X., Liang, Y., & Zhang, Z. (2023) · Journal of Experimental Botany · doi:10.1093/jxb/erad175 · Cited by 36
Role of reactive oxygen species in regulating epigenetic modifications
Chen, Y., & Shen, Y. (2024) · Cellular Signalling · doi:10.1016/j.cellsig.2024.111502 · Cited by 32
Epigenetics and Pregnancy: Conditional Snapshot or Rolling Event
Andrawus, M., Sharvit, L. E., & Atzmon, G. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232012698 · Cited by 38
Wang, J., Feng, J., Ni, Y., Wang, Y., Zhang, T., Cao, Y., Zhou, M., & Zhao, C. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1450440 · Cited by 32
Breaking the barrier: Epigenetic strategies to combat platinum resistance in colorectal cancer
Luo, S., Yue, M., Wang, D., Lu, Y., Wu, Q., & Jiang, J. (2024) · Drug Resistance Updates · doi:10.1016/j.drup.2024.101152 · Cited by 34
Regulation of gene expression through protein-metabolite interactions
Hornisch, M., & Piazza, I. (2025) · npj Metabolic Health and Disease · doi:10.1038/s44324-024-00047-w · Cited by 33
Histone 4 lysine 20 tri-methylation: a key epigenetic regulator in chromatin structure and disease
Agredo, A., & Kasinski, A. L. (2023) · Frontiers in Genetics · doi:10.3389/fgene.2023.1243395 · Cited by 32
Nanopore: Emerging for detecting protein post-translational modifications
Zhao, X., Qin, H., Tang, M., Zhang, X., & Qing, G. (2024) · TrAC Trends in Analytical Chemistry · doi:10.1016/j.trac.2024.117658 · Cited by 29
Chemical proteomics approaches for protein post-translational modification studies
Zhang, N., Wu, J., & Zheng, Q. (2024) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2024.141017 · Cited by 31
Liu, B., Li, N., Liu, Y., Zhang, Y., Qu, L., Cai, H., Yang, L., Wu, X., & Geng, Q. (2024) · Burns & Trauma · doi:10.1093/burnst/tkae033 · Cited by 29
Insight into the roles of lactylation in macrophages: functions and clinical implications
Shu, M., Lu, D., Zhu, Z., Yang, F., & Ma, Z. (2025) · Clinical Science · doi:10.1042/cs20242737 · Cited by 29
The function of histone methylation and acetylation regulators in GBM pathophysiology
McCornack, C. R., Woodiwiss, T. R., Hardi, A., Yano, H., & Kim, A. H. (2023) · Frontiers in Oncology · doi:10.3389/fonc.2023.1144184 · Cited by 33
Emerging Role of Epigenetic Modifiers in Breast Cancer Pathogenesis and Therapeutic Response
Lee, R. S., Sad, K., Fawwal, D. V., & Spangle, J. M. (2023) · Cancers · doi:10.3390/cancers15154005 · Cited by 29
Tumor microenvironment, histone modifications, and myeloid-derived suppressor cells
Tian, X., Wang, T., Shen, H., & Wang, S. (2023) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2023.08.002 · Cited by 28
Hallmarks of aging: A user’s guide for comparative biologists
Biga, P. R., Duan, J. E., Young, T. E., Marks, J. R., Bronikowski, A. M., Decena-Segarra, L. P., Randolph, E. C., Pavuluri, A., Li, G., Fang, Y., et al. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102616 · Cited by 33
Mesangial Cells in Diabetic Kidney Disease: From Mechanisms to Therapeutic Implications
Li, F., Feng, Y., Ren, Q., Fu, P., & Ma, L. (2025) · International Journal of Biological Sciences · doi:10.7150/ijbs.114907 · Cited by 30
Epigenetic editing: from concept to clinic
Heller, E. A., Bintu, L., & Rots, M. G. (2025) · Nature Reviews Drug Discovery · doi:10.1038/s41573-025-01323-0 · Cited by 37
CTCF and Its Multi-Partner Network for Chromatin Regulation
Moral‐Morales, A. D., Salgado-Albarrán, M., Sánchez-Pérez, Y., Wenke, N. K., Baumbach, J., & Soto‐Reyes, E. (2023) · Cells · doi:10.3390/cells12101357 · Cited by 30
Epigenetics in obesity: Mechanisms and advances in therapies based on natural products
Chen, P., Wang, Y., Chen, F., & Zhou, B. (2024) · Pharmacology Research & Perspectives · doi:10.1002/prp2.1171 · Cited by 27
Unlocking the power of precision medicine: exploring the role of biomarkers in cancer management
Gadade, D. D., Jha, H., Kumar, C., & Khan, F. (2024) · Future Journal of Pharmaceutical Sciences · doi:10.1186/s43094-023-00573-2 · Cited by 27
An Overview of Epigenetic Changes in the Parkinson’s Disease Brain
Klokkaris, A., & Migdalska‐Richards, A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25116168 · Cited by 31
Small-molecule-based targeted therapy in liver cancer
Ming, Y., Gong, Y., Fu, X., Ouyang, X., Peng, Y., & Pu, W. (2024) · Molecular Therapy · doi:10.1016/j.ymthe.2024.08.001 · Cited by 27
Jurkowska, R. Z. (2024) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2024.108732 · Cited by 29
Genetic and epigenetic alterations in aging and rejuvenation of human
Park, K., Jeon, M. C., Lee, D., Kim, J., & Im, S.-W. (2024) · Molecules and Cells · doi:10.1016/j.mocell.2024.100137 · Cited by 30
Kovalev, M. A., Mamaeva, N. Y., Kristovskiy, N. V., Feskin, P. G., Vinnikov, R. S., Oleinikov, P. D., Sosnovtseva, A. O., Yakovlev, V. A., Glukhov, G. S., & Shaytan, A. К. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26136371 · Cited by 29
The Role of the Histone Variant H2A.Z in Metazoan Development
Dijkwel, Y., & Tremethick, D. J. (2022) · Journal of Developmental Biology · doi:10.3390/jdb10030028 · Cited by 26
Vai, A., Noberini, R., Ghirardi, C., de Paula, D. R., Carminati, M., Pallavi, R., Araújo, N. V. P., Varga‐Weisz, P., & Bonaldi, T. (2024) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2024.100799 · Cited by 26
Lactylation: From Homeostasis to Pathological Implications and Therapeutic Strategies
Chen, X., Yuan, Y., Zhou, F., Li, L., Pu, J., Zeng, Y., & Jiang, X. (2025) · MedComm · doi:10.1002/mco2.70226 · Cited by 28
Characterizing crosstalk in epigenetic signaling to understand disease physiology
Lempiäinen, J. K., & Garcia, B. A. (2023) · Biochemical Journal · doi:10.1042/bcj20220550 · Cited by 29
Liquid–liquid phase separation of H3K27me3 reader BP1 regulates transcriptional repression
Tang, G., Xia, H., Huang, Y., Guo, Y., Chen, Y., Ma, Z., & Liu, W. (2024) · Genome biology · doi:10.1186/s13059-024-03209-7 · Cited by 26
Rehman, S., Ahmad, Z., Ramakrishnan, M., Kalendar, R. N., & Zhuge, Q. (2023) · Functional & Integrative Genomics · doi:10.1007/s10142-023-01219-5 · Cited by 33
Molecular dynamics simulations of nucleosomes are coming of age
Fedulova, A. S., Armeev, G. A., Romanova, T. A., Singh‐Palchevskaia, L., Kosarim, N. A., Motorin, N. A., Komarova, G. A., & Shaytan, A. К. (2024) · Wiley Interdisciplinary Reviews Computational Molecular Science · doi:10.1002/wcms.1728 · Cited by 28
Chang, Y., Liu, J., Guo, M., Ouyang, W., Yan, J., Xiong, L., & Li, X. (2024) · Genome biology · doi:10.1186/s13059-024-03408-2 · Cited by 25
Wang, P., Zhang, H., Yin, Y., Ge, Y., Chen, B., Hu, J. R., Wang, Y., Ni, D., & Guo, F. (2025) · Genome biology · doi:10.1186/s13059-025-03618-2 · Cited by 25
Where and when to start: Regulating DNA replication origin activity in eukaryotic genomes
Lee, C. S. K., Weiβ, M., & Hamperl, S. (2023) · Nucleus · doi:10.1080/19491034.2023.2229642 · Cited by 25
Applications of single-cell multi-omics in liver cancer
Peeters, F., Cappuyns, S., Piqué‐Gili, M., Phillips, G., Verslype, C., Lambrechts, D., & Dekervel, J. (2024) · JHEP Reports · doi:10.1016/j.jhepr.2024.101094 · Cited by 26
Wang, Y., Tian, X., Wang, Z., Liu, D., Zhao, X., Sun, X., Tu, Z., Li, Z., Zhao, Y., Zheng, S., et al. (2024) · Clinical and Translational Medicine · doi:10.1002/ctm2.1801 · Cited by 23
Huang, X., Zhang, J., Cun, Y., Ye, M., Ren, Z., Guo, W., Ma, X., Liu, J., Weiwei, L., Sun, X., et al. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.02.016 · Cited by 24
Epigenetic Echoes: Bridging Nature, Nurture, and Healing Across Generations
Banushi, B., Collova, J. R., & Milroy, H. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26073075 · Cited by 30
Anticancer Potential of Bioactive Molecule Luteolin and Its Analogs: An Update
Basha, N. J., & Basavarajaiah, S. M. (2022) · Polycyclic aromatic compounds · doi:10.1080/10406638.2022.2080728 · Cited by 24
Li, F., Wang, Y., Hwang, I., Jang, J.-Y., Xu, L., Deng, Z., Yu, E. Y., Cai, Y., Wu, C., Han, Z., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-37480-2 · Cited by 25
Wu, J., Luo, J., He, Q., Xia, Y., Tian, H., Zhu, L., Li, C., & Loor, J. J. (2023) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.3c01606 · Cited by 24
Liu, T., Du, D., Zhao, R., Xie, Q., & Dong, Z. (2023) · Microbiological Research · doi:10.1016/j.micres.2023.127440 · Cited by 24
Tian, Z., Li, K., Sun, Y., Chen, B., Pan, Z., Wang, Z., Pang, B., He, S., Miao, Y., & Du, X. (2023) · Plant Science · doi:10.1016/j.plantsci.2023.111920 · Cited by 24
A di-acetyl-decorated chromatin signature couples liquid condensation to suppress DNA end synapsis
Bao, K., Ma, Y., Li, Y., Shen, X., Zhao, J., Tian, S., Zhang, C., Liang, C., Zhao, Z., Yang, Y., et al. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.02.002 · Cited by 24
Lactate-induced lactylation and cardiometabolic diseases: From epigenetic regulation to therapeutics
Lin, J., & Ren, J. T. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2024.167247 · Cited by 24
Mun, D., Bhat, F. A., Joshi, N. S., Sandoval, L., Ding, H., Jain, A., Peterson, J. A., Kang, T., Pujari, G. P., Tomlinson, J. L., et al. (2024) · Communications Biology · doi:10.1038/s42003-024-06579-7 · Cited by 23
Targeting esophageal carcinoma: molecular mechanisms and clinical studies
Wang, W., Ye, L., Li, H., Mao, W., & Xu, X. (2024) · MedComm · doi:10.1002/mco2.782 · Cited by 24
Histone Deacetylases (HDACs) Roles in Inflammation-mediated Diseases; Current Knowledge
Jasim, S. A., Altalbawy, F. M. A., Abohassan, M., Oghenemaro, E. F., Bishoyi, A. K., Singh, R. P., Kaur, P., Sivaprasad, G. V., Mohammed, J. S., & Hulail, H. M. (2024) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-024-01587-0 · Cited by 27
Hu, H., Tang, J., Wang, H., Guo, X., Tu, C., & Li, Z. (2024) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-024-00662-x · Cited by 23
Bajikar, S. S., Zhou, J., O’Hara, R. A., Tirumala, H. P., Durham, M. A., Trostle, A. J., Dias, M., Shao, Y., Chen, H., Wang, W., et al. (2024) · Neuron · doi:10.1016/j.neuron.2024.11.006 · Cited by 25
The epigenetic landscape of brain metastasis
Powell, A. M., Watson, L., Luzietti, L., Preković, S., Young, L. S., & Varešlija, D. (2025) · Oncogene · doi:10.1038/s41388-025-03315-1 · Cited by 28
Zhou, Y.-Q., Jiang, J., He, S., Li, Y., Cheng, X.-X., Liu, S., Wei, P., Guan, X., Ong, C. K., Wang, V. Y., et al. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02163-5 · Cited by 23
Huang, T., You, Q., Liu, J., Shen, X., Huang, D., Tao, X., He, Z., Wu, C., Xi, X., Yu, S., et al. (2025) · Advanced Science · doi:10.1002/advs.202506529 · Cited by 26
New Insights into the Genetics and Epigenetics of Aging Plasticity
Zhang, J., Wang, S., & Liu, B. (2023) · Genes · doi:10.3390/genes14020329 · Cited by 25
Transcription-coupled nucleosome assembly
Robert, F., & Jerónimo, C. (2023) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2023.08.003 · Cited by 23
Unlocking the potential of targeting histone-modifying enzymes for treating IBD and CRC
Liang, B., Wang, Y., Xu, J., Shao, Y., & Xing, D. (2023) · Clinical Epigenetics · doi:10.1186/s13148-023-01562-1 · Cited by 24
Du, J., Liao, W., Wang, H., Hou, G., Liao, M., Xu, L., Huang, J., Yuan, K., Chen, X., & Zeng, Y. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01575-5 · Cited by 24
Gao, H., Chen, Z., Zhao, L., Ji, C., & Xing, F. (2024) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2024.189099 · Cited by 23
ENL reads histone β-hydroxybutyrylation to modulate gene transcription
Chen, C., Chen, C., Wang, A., Jiang, Z., Zhao, F. L., Li, Y., Han, Y., Niu, Z., Tian, S., Bai, X., et al. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae504 · Cited by 22
Fang, F., Gao, G., Wang, Q., Wang, Q., & Sun, L. (2024) · PROTEOMICS · doi:10.1002/pmic.202300650 · Cited by 22
Wang, P., Wang, G., Li, H., Yuan, Y., Chen, H., Wang, S., Sun, Z., Meng, F., Li, Y., Yang, F., et al. (2024) · 癌症:英文版 · doi:10.1002/cac2.12633 · Cited by 22
Luqman, T., Hussain, M., Ahmed, S. R., Ijaz, I., Maryum, Z., Nadeem, S., Khan, Z., Khan, S. M. U. D., Aslam, M., Liu, Y., et al. (2025) · Frontiers in Genetics · doi:10.3389/fgene.2025.1553406 · Cited by 31
Li, J., Li, Z., Zhang, H., Zhang, H., Tang, Y., Tang, Y., Guo, S., Ye, T., Wang, J., & Li, J. (2025) · Cancer Letters · doi:10.1016/j.canlet.2025.218227 · Cited by 22
Epigenetic and epitranscriptomic mechanisms of chromium carcinogenesis
Wang, Z., & Yang, C. (2022) · Advances in pharmacology · doi:10.1016/bs.apha.2022.07.002 · Cited by 21
Zhang, Y., Cai, Q., Luo, Y., Zhang, Y., & Li, H. (2022) · Journal of Pharmaceutical Analysis · doi:10.1016/j.jpha.2022.11.003 · Cited by 24
Lactate: a pearl dropped in the ocean—an overlooked signal molecule in physiology and pathology
Wu, Y. X., Ma, W., Liu, W., & Zhang, S. (2022) · Cell Biology International · doi:10.1002/cbin.11975 · Cited by 23
Viita, T., & Côté, J. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.1115903 · Cited by 22
Schwartz, L., Bochter, M. S., Simoni, A. A., Bender, K., Ruiz‐Rosado, J. D. D., Cotzomi-Ortega, I., Sánchez-Zamora, Y. I., Becknell, B., Linn, S. C., Li, B., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2213363120 · Cited by 22
Liquid biopsies for cancer: From bench to clinic
Chen, Z., Li, C., Zhou, Y., Yao, Y., Liu, J., Wu, M., & Su, J. (2023) · MedComm · doi:10.1002/mco2.329 · Cited by 22
The Killer’s Web: Interconnection between Inflammation, Epigenetics and Nutrition in Cancer
Mecca, M., Picerno, S., & Cortellino, S. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25052750 · Cited by 24
Tackling triple negative breast cancer with HDAC inhibitors: 6 is the isoform!
Guadagni, A., Barone, S., Alfano, A. I., Pelliccia, S., Bello, I., Panza, E., Summa, V., & Brindisi, M. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116884 · Cited by 22
Xu, M., Hou, Y., Li, N., Yu, W., & Chen, L. (2024) · Journal of Translational Medicine · doi:10.1186/s12967-024-05169-9 · Cited by 22
Chromatin lysine acylation: On the path to chromatin homeostasis and genome integrity
Chen, F., He, X., Xu, W., Zhou, L., Liu, Q., Chen, W., Zhu, W., & Zhang, J. (2024) · Cancer Science · doi:10.1111/cas.16321 · Cited by 21
Sindhu, P., Magotra, A., Sindhu, V., & Chaudhary, P. (2024) · Zygote · doi:10.1017/s0967199424000224 · Cited by 23
Quantitative spatial analysis of chromatin biomolecular condensates using cryoelectron tomography
Zhou, H., Hutchings, J., Shiozaki, M., Zhao, X., Doolittle, L. K., Yang, S., Yan, R., Jean, N., Riggi, M., Yu, Z., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2426449122 · Cited by 23
Structural perspectives on transcription in chromatin
Sekine, S., Ehara, H., Kujirai, T., & Kurumizaka, H. (2023) · Trends in Cell Biology · doi:10.1016/j.tcb.2023.07.011 · Cited by 21
Protein modification by short-chain fatty acid metabolites in sepsis: a comprehensive review
Zhang, L., Shi, X., Qiu, H., Liu, S., Yang, T., Li, X., & Liu, X. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1171834 · Cited by 22
Interrogating epigenetic mechanisms with chemically customized chromatin
Hananya, N., Koren, S., & Muir, T. W. (2023) · Nature Reviews Genetics · doi:10.1038/s41576-023-00664-z · Cited by 20
NSD family proteins: Rising stars as therapeutic targets
He, L., Cao, Y., & Sun, L. (2024) · Cell Insight · doi:10.1016/j.cellin.2024.100151 · Cited by 22
Weinzapfel, E. N., Fedder-Semmes, K. N., Sun, Z., & Keogh, M. (2024) · Biochemical Journal · doi:10.1042/bcj20230342 · Cited by 23
Ri-Wen, Yang, Y., Zhang, T., Liu, C., & Yang, N. (2024) · Pharmacological Research · doi:10.1016/j.phrs.2024.107182 · Cited by 25
Gómez‐Pinilla, F., & Thapak, P. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.04.237 · Cited by 24
Epigenetic mechanisms linking early-life adversities and mental health
Cánepa, E. T., & Berardino, B. G. (2024) · Biochemical Journal · doi:10.1042/bcj20230306 · Cited by 22
Histone Modifications and Their Contributions to Hypertension
Ray, A., Stelloh, C. T., Liu, Y., Meyer, A. E., Geurts, A. M., Cowley, A. W., Greene, A. S., Liang, M., & Rao, S. (2023) · Hypertension · doi:10.1161/hypertensionaha.123.21755 · Cited by 22
Yin, J., & Horzmann, K. A. (2024) · Biomedicines · doi:10.3390/biomedicines12071559 · Cited by 20
Masnikosa, R., Cvetković, Z., & Pirić, D. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252111384 · Cited by 22
Liu, N., Zhu, X., Wu, C., Liu, Y.-Y., Chen, M., & Gu, J.-H. (2024) · Cell Death Discovery · doi:10.1038/s41420-024-02240-8 · Cited by 21
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