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.
Integrity signals
Registry
Cites
Statistics
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?
Post-translational modifications predominantly occur on N-terminal histone tails and include acetylation, methylation, phosphorylation, and ubiquitination, forming combinatorial patterns known as the histone code.
“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
The flexible N-terminal tails of histones protrude from the nucleosome and serve as major sites for post-translational modifications including acetylation, methylation, and phosphorylation.
“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
Cites
Hanahan, D., & Weinberg, R. A. (2000) · Cell · doi:10.1016/s0092-8674(00)81683-9 · Cited by 29,219 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
ACETYLATION AND METHYLATION OF HISTONES AND THEIR POSSIBLE ROLE IN THE REGULATION OF RNA SYNTHESIS
Allfrey, V. G., Faulkner, R. D., & Mirsky, A. E. (1964) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.51.5.786 · Cited by 2,649 · see citing works
Coactivator condensation at super-enhancers links phase separation and gene control
Sabari, B. R., Dall’Agnese, A., Boija, A., Klein, I. A., Coffey, E. L., Shrinivas, K., Abraham, B. J., Hannett, N. M., Zamudio, A. V., Manteiga, J. C., et al. (2018) · Science · doi:10.1126/science.aar3958 · Cited by 2,595 · see citing works
Histone modifications at human enhancers reflect global cell-type-specific gene expression
Heintzman, N. D., Hon, G. C., Hawkins, R. D., Kheradpour, P., Stark, A., Harp, L. F., Ye, Z., Lee, L. K., Stuart, R. K., Ching, C. W., et al. (2009) · Nature · doi:10.1038/nature07829 · Cited by 2,533 · see citing works
CUT&Tag for efficient epigenomic profiling of small samples and single cells
Kaya-Okur, H. S., Wu, S. J., Codomo, C. A., Pledger, E. S., Bryson, T. D., Henikoff, J. G., Ahmad, K., & Henikoff, S. (2019) · Nature Communications · doi:10.1038/s41467-019-09982-5 · Cited by 2,187 · see citing works
Tan, M., Luo, H., Lee, S., Jin, F., Yang, J. S., Montellier, E., Buchou, T., Cheng, Z., Rousseaux, S., Rajagopal, N., et al. (2011) · Cell · doi:10.1016/j.cell.2011.08.008 · Cited by 1,902 · see citing works
Hilton, I. B., D’Ippolito, A. M., Vockley, C. M., Thakore, P. I., Crawford, G. E., Reddy, T. E., & Gersbach, C. A. (2015) · Nature Biotechnology · doi:10.1038/nbt.3199 · Cited by 1,878 · see citing works
Histone H4-K16 Acetylation Controls Chromatin Structure and Protein Interactions
Shogren‐Knaak, M. A., Ishii, H., Sun, J.-M., Pazin, M. J., Davie, J., & Peterson, C. L. (2006) · Science · doi:10.1126/science.1124000 · Cited by 1,876 · see citing works
Phase separation drives heterochromatin domain formation
Strom, A. R., Emelyanov, A. V., Mir, M., Fyodorov, D. V., Darzacq, X., & Karpen, G. H. (2017) · Nature · doi:10.1038/nature22989 · Cited by 1,813 · see citing works
An efficient targeted nuclease strategy for high-resolution mapping of DNA binding sites
Skene, P. J., & Henikoff, S. (2017) · eLife · doi:10.7554/elife.21856 · Cited by 1,737 · see citing works
DNMT3L connects unmethylated lysine 4 of histone H3 to de novo methylation of DNA
Ooi, S. K. T., Qiu, C., Bernstein, E., Li, K., Jia, D., Yang, Z., Erdjument‐Bromage, H., Tempst, P., Lin, S., Allis, C. D., et al. (2007) · Nature · doi:10.1038/nature05987 · Cited by 1,558 · see citing works
Liquid droplet formation by HP1α suggests a role for phase separation in heterochromatin
Larson, A. G., Elnatan, D., Keenen, M. M., Trnka, M., Johnston, J. B., Burlingame, A., Agard, D., Redding, S., & Narlikar, G. J. (2017) · Nature · doi:10.1038/nature22822 · Cited by 1,554 · see citing works
Single-cell proteomic analysis of S. cerevisiae reveals the architecture of biological noise
Newman, J. R. S., Ghaemmaghami, S., Ihmels, J., Breslow, D. K., Noble, M., DeRisi, J. L., & Weissman, J. S. (2006) · Nature · doi:10.1038/nature04785 · Cited by 1,483 · see citing works
Mediator and RNA polymerase II clusters associate in transcription-dependent condensates
Cho, W.-K., Spille, J.-H., Hecht, M., Lee, C., Li, C., Grube, V., & Cisse, I. I. (2018) · Science · doi:10.1126/science.aar4199 · Cited by 1,403 · see citing works
Mechanisms of Polycomb gene silencing: knowns and unknowns
Simon, J. A., & Kingston, R. E. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2763 · Cited by 1,320 · see citing works
Carrozza, M. J., Li, B., Florens, L. A., Suganuma, T., Swanson, S. K., Lee, K. K., Shia, W.-J., Anderson, S., Yates, J. R., Washburn, M. P., et al. (2005) · Cell · doi:10.1016/j.cell.2005.10.023 · Cited by 1,297 · see citing works
Organizational principles of 3D genome architecture
Rowley, M. J., & Corces, V. G. (2018) · Nature Reviews Genetics · doi:10.1038/s41576-018-0060-8 · Cited by 1,171 · see citing works
Lamina-Associated Domains: Links with Chromosome Architecture, Heterochromatin, and Gene Repression
van Steensel, B., & Belmont, A. S. (2017) · Cell · doi:10.1016/j.cell.2017.04.022 · Cited by 1,140 · see citing works
A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatinPreprint
Schotta, G., Lachner, M., Sarma, K., Ebert, A., Sengupta, R., Reuter, G., Reinberg, D., & Jenuwein, T. (2004) · Genes & Development · doi:10.1101/gad.300704 · Cited by 1,110 · see citing works
Regulation of Alternative Splicing by Histone Modifications
Luco, R. F., Pan, Q., Tominaga, K., Blencowe, B. J., Pereira‐Smith, O. M., & Misteli, T. (2010) · Science · doi:10.1126/science.1184208 · Cited by 1,099 · see citing works
Ng, H., Robert, F., Young, R. A., & Struhl, K. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00092-3 · Cited by 1,097 · see citing works
Organization of Chromatin by Intrinsic and Regulated Phase Separation
Gibson, B. A., Doolittle, L. K., Schneider, M. W. G., Jensen, L. E., Gamarra, N. I., Henry, L., Gerlich, D. W., Redding, S., & Rosen, M. K. (2019) · Cell · doi:10.1016/j.cell.2019.08.037 · Cited by 1,045 · see citing works
Regulation of HP1–chromatin binding by histone H3 methylation and phosphorylation
Fischle, W., Tseng, B. S., Dormann, H. L., Ueberheide, B. M., Garcia, B. A., Shabanowitz, J., Hunt, D. F., Funabiki, H., & Allis, C. D. (2005) · Nature · doi:10.1038/nature04219 · Cited by 996 · see citing works
Botuyan, M. V., Lee, J., Ward, I. M., Kim, J., Thompson, J. R., Chen, J., & Mer, G. (2006) · Cell · doi:10.1016/j.cell.2006.10.043 · Cited by 973 · see citing works
Condensin-driven remodelling of X chromosome topology during dosage compensation
Crane, E. E., Bian, Q., McCord, R. P., Lajoie, B. R., Wheeler, B. S., Ralston, E. J., Uzawa, S., Dekker, J., & Meyer, B. J. (2015) · Nature · doi:10.1038/nature14450 · Cited by 972 · see citing works
Imaging dynamic and selective low-complexity domain interactions that control gene transcription
Chong, S., Dugast-Darzacq, C., Liu, Z., Dong, P., Dailey, G. M., Cattoglio, C., Heckert, A., Banala, S., Lavis, L., Darzacq, X., et al. (2018) · Science · doi:10.1126/science.aar2555 · Cited by 966 · see citing works
A direct link between core histone acetylation and transcriptionally active chromatin.
Hebbes, T. R., Thorne, A. W., & Crane‐Robinson, C. (1988) · The EMBO Journal · doi:10.1002/j.1460-2075.1988.tb02956.x · Cited by 921 · see citing works
Topologically associating domains are stable units of replication-timing regulation
Pope, B. D., Ryba, T., Dileep, V., Yue, F., Wu, W.-S., Denas, O., Vera, D. L., Wang, Y., Hansen, R. S., Canfield, T. K., et al. (2014) · Nature · doi:10.1038/nature13986 · Cited by 902 · see citing works
Soufi, A., Donahue, G., & Zaret, K. S. (2012) · Cell · doi:10.1016/j.cell.2012.09.045 · Cited by 887 · see citing works
Selective Anchoring of TFIID to Nucleosomes by Trimethylation of Histone H3 Lysine 4
Vermeulen, M., Mulder, K. W., Denissov, S., Pijnappel, W. W. M. P., van Schaik, F. M. A., Varier, R. A., Baltissen, M. P. A., Stunnenberg, H. G., Mann, M., & Timmers, H. T. M. (2007) · Cell · doi:10.1016/j.cell.2007.08.016 · Cited by 883 · see citing works
Super-resolution imaging reveals distinct chromatin folding for different epigenetic states
Boettiger, A. N., Bintu, B., Moffitt, J. R., Wang, S. S., Beliveau, B. J., Fudenberg, G., Imakaev, M., Mirny, L. A., Wu, C.-T., & Zhuang, X. (2016) · Nature · doi:10.1038/nature16496 · Cited by 877 · see citing works
50 years of protein acetylation: from gene regulation to epigenetics, metabolism and beyond
Verdin, E. M., & Ott, M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3931 · Cited by 876 · see citing works
Dot1p Modulates Silencing in Yeast by Methylation of the Nucleosome Core
van Leeuwen, F., Gafken, P. R., & Gottschling, D. E. (2002) · Cell · doi:10.1016/s0092-8674(02)00759-6 · Cited by 853 · see citing works
Chromatin Compaction by a Polycomb Group Protein Complex
Francis, N. J., Kingston, R. E., & Woodcock, C. L. F. (2004) · Science · doi:10.1126/science.1100576 · Cited by 841 · see citing works
Schübeler, D., MacAlpine, D. M., Scalzo, D., Wirbelauer, C., Kooperberg, C. L., van Leeuwen, F., Gottschling, D. E., O’Neill, L. P., Turner, B. M., Delrow, J. J., et al. (2004) · Genes & Development · doi:10.1101/gad.1198204 · Cited by 795 · see citing works
Ten principles of heterochromatin formation and function
Allshire, R. C., & Madhani, H. D. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.119 · Cited by 783 · see citing works
Lateral Thinking: How Histone Modifications Regulate Gene Expression.
Lawrence, M., Daujat, S., & Schneider, R. (2016) · Trends in Genetics · doi:10.1016/j.tig.2015.10.007 · Cited by 759 · see citing works
Self-citationNew insights into nucleosome and chromatin structure: an ordered state or a disordered affair?
Luger, K., Dechassa, M. L., & Tremethick, D. J. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3382 · Cited by 753 · see citing works
Distinct features of H3K4me3 and H3K27me3 chromatin domains in pre-implantation embryos
Liu, X., Wang, C., Liu, W., Li, J., Li, C., Kou, X., Chen, J., Zhao, Y., Gao, H., Wang, H., et al. (2016) · Nature · doi:10.1038/nature19362 · Cited by 746 · see citing works
Single-Cell Dynamics of Genome-Nuclear Lamina Interactions
Kind, J., Pagie, L., Ortabozkoyun, H., Boyle, S., de Vries, S., Janssen, H., Amendola, M., Nolen, L. D., Bickmore, W. A., & van Steensel, B. (2013) · Cell · doi:10.1016/j.cell.2013.02.028 · Cited by 716 · see citing works
Rapid spontaneous accessibility of nucleosomal DNA
Gu, L.-Q., Levitus, M., Bustamante, C., & Widom, J. (2005) · Nature Structural &Molecular Biology · doi:10.1038/nsmb869 · Cited by 692 · see citing works
53BP1 is a reader of the DNA-damage-induced H2A Lys 15 ubiquitin mark
Fradet-Turcotte, A., Canny, M. D., Escribano-Díaz, C., Orthwein, A., Leung, C. C. Y., Huang, H., Landry, M.-C., Kitevski-LeBlanc, J., Noordermeer, S. M., Sicheri, F., et al. (2013) · Nature · doi:10.1038/nature12318 · Cited by 686 · see citing works
Histone H3 trimethylation at lysine 36 guides m6A RNA modification co-transcriptionally
Huang, H., Weng, H., Zhou, K., Wu, T., Zhao, B. S., Sun, M., Chen, Z., Deng, X., Xiao, G., Auer, F., et al. (2019) · Nature · doi:10.1038/s41586-019-1016-7 · Cited by 677 · see citing works
Intracellular Crotonyl-CoA Stimulates Transcription through p300-Catalyzed Histone Crotonylation
Sabari, B. R., Tang, Z., Huang, H., Yong-Gonzalez, V., Molina, H., Kong, H. E., Dai, L., Shimada, M., Cross, J. R., Zhao, Y., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.02.029 · Cited by 659 · see citing works
Functional annotation of native enhancers with a Cas9–histone demethylase fusion
Kearns, N. A., Pham, H., Tabak, B., Genga, R. M., Silverstein, N. J., Garber, M., & Maehr, R. (2015) · Nature Methods · doi:10.1038/nmeth.3325 · Cited by 656 · see citing works
RNF168 Ubiquitinates K13-15 on H2A/H2AX to Drive DNA Damage Signaling
Mattiroli, F., Vissers, J. H. A., van Dijk, W. J., Ikpa, P. T., Citterio, E., Vermeulen, W., Marteijn, J. A. F., & Sixma, T. K. (2012) · Cell · doi:10.1016/j.cell.2012.08.005 · Cited by 653 · see citing works
Heterochromatin drives compartmentalization of inverted and conventional nuclei
Falk, M., Feodorova, Y., Naumova, N., Imakaev, M., Lajoie, B. R., Leonhardt, H., Joffe, B., Dekker, J., Fudenberg, G., Solovei, I., et al. (2019) · Nature · doi:10.1038/s41586-019-1275-3 · Cited by 646 · see citing works
Broad histone H3K4me3 domains in mouse oocytes modulate maternal-to-zygotic transition
Dahl, J. A., Jung, I., Aanes, H., Greggains, G. D., Manaf, A., Lerdrup, M., Li, G., Kuan, S., Li, B., Lee, A. Y., et al. (2016) · Nature · doi:10.1038/nature19360 · Cited by 628 · see citing works
Allelic reprogramming of the histone modification H3K4me3 in early mammalian development
Zhang, B., Zheng, H., Huang, B., Li, W., Xiang, Y.-L., Peng, X., Jia, M., Wu, X., Zhang, Y., Xu, Q.-H., et al. (2016) · Nature · doi:10.1038/nature19361 · Cited by 627 · see citing works
Step-wise methylation of histone H3K9 positions heterochromatin at the nuclear periphery
Towbin, B. D., González-Aguilera, C., Sack, R., Gaidatzis, D., Kalck, V., Meister, P., Askjaer, P., & Gasser, S. M. (2012) · Cell · doi:10.1016/j.cell.2012.06.051 · Cited by 597 · see citing works
Evaluating phase separation in live cells: diagnosis, caveats, and functional consequencesPreprint
McSwiggen, D. T., Mir, M., Darzacq, X., & Tjian, R. (2019) · Genes & Development · doi:10.1101/gad.331520.119 · Cited by 593 · see citing works
Lo, W., Trievel, R. C., Rojas, J. R., Duggan, L. J., Hsu, J.-Y., Allis, C. D., Marmorstein, R., & Berger, S. L. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80257-9 · Cited by 573 · see citing works
Eskeland, R., Leeb, M., Grimes, G. R., Kress, C., Boyle, S., Sproul, D., Gilbert, N., Fan, Y., Skoultchi, A. I., Wutz, A., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.02.032 · Cited by 553 · see citing works
Bannister, A. J., Schneider, R., & Kouzarides, T. (2002) · Cell · doi:10.1016/s0092-8674(02)00798-5 · Cited by 542 · see citing works
Self-citationH3K4me3 breadth is linked to cell identity and transcriptional consistency
Benayoun, B. A., Pollina, E. A., Ucar, D., Mahmoudi, S., Karra, K., Wong, E. D., Devarajan, K., Daugherty, A. C., Kundaje, A. B., Mancini, E., et al. (2014) · Cell · doi:10.1016/j.cell.2014.06.027 · Cited by 536 · see citing works
The histone mark H3K36me2 recruits DNMT3A and shapes the intergenic DNA methylation landscape
Weinberg, D. N., Papillon-Cavanagh, S., Chen, H., Yue, Y., Chen, X., Rajagopalan, K. N., Horth, C., McGuire, J. T., Xu, X., Nikbakht, H., et al. (2019) · Nature · doi:10.1038/s41586-019-1534-3 · Cited by 524 · see citing works
Disruption of histone methylation in developing sperm impairs offspring health transgenerationally
Siklenka, K., Erkek, S., Godmann, M., Lambrot, R., McGraw, S., Lafleur, C., Cohen, T., Xia, J., Suderman, M., Hallett, M., et al. (2015) · Science · doi:10.1126/science.aab2006 · Cited by 521 · see citing works
Kizer, K. O., Phatnani, H. P., Shibata, Y., Hall, H., Greenleaf, A. L., & Strahl, B. D. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.8.3305-3316.2005 · Cited by 511 · see citing works
Neumann, H., Hancock, S. M., Buning, R., Routh, A. L., Chapman, L., Somers, J., Owen‐Hughes, T., van Noort, J., Rhodes, D., & Chin, J. W. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.07.027 · Cited by 498 · see citing works
Understanding nucleosome dynamics and their links to gene expression and DNA replication
Lai, W. K. M., & Pugh, B. F. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.47 · Cited by 495 · see citing works
The evolving metabolic landscape of chromatin biology and epigenetics
Dai, Z., Ramesh, V., & Locasale, J. W. (2020) · Nature Reviews Genetics · doi:10.1038/s41576-020-0270-8 · Cited by 494 · see citing works
Histone modification: cause or cog?
Henikoff, S., & Shilatifard, A. (2011) · Trends in Genetics · doi:10.1016/j.tig.2011.06.006 · Cited by 482 · see citing works
Histone serotonylation is a permissive modification that enhances TFIID binding to H3K4me3
Farrelly, L. A., Thompson, R. E., Zhao, S., Lepack, A. E., Lyu, Y., Bhanu, N. V., Zhang, B., Loh, Y. E., Ramakrishnan, A., Vadodaria, K. C., et al. (2019) · Nature · doi:10.1038/s41586-019-1024-7 · Cited by 477 · see citing works
H3K4me3 Interactions with TAF3 Regulate Preinitiation Complex Assembly and Selective Gene Activation
Lauberth, S. M., Nakayama, T., Wu, X., Ferris, A. L., Tang, Z., Hughes, S. H., & Roeder, R. G. (2013) · Cell · doi:10.1016/j.cell.2013.01.052 · Cited by 473 · see citing works
Maternal H3K27me3 controls DNA methylation-independent imprinting
Inoue, A., Jiang, L., Lu, F., Suzuki, T., & Zhang, Y. (2017) · Nature · doi:10.1038/nature23262 · Cited by 467 · see citing works
Pfister, S. X., Ahrabi, S., Zalmas, L., Sarkar, S., Aymard, F., Bachrati, C. Z., Helleday, T., Legube, G., Thangue, N. B. L., Porter, A. C. G., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.05.026 · Cited by 465 · see citing works
Spatial Distribution of Di- and Tri-methyl Lysine 36 of Histone H3 at Active Genes
Bannister, A. J., Schneider, R., Myers, F. A., Thorne, A. W., Crane‐Robinson, C., & Kouzarides, T. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500796200 · Cited by 459 · see citing works
Self-citationResetting Epigenetic Memory by Reprogramming of Histone Modifications in Mammals
Zheng, H., Huang, B., Zhang, B., Xiang, Y., Du, Z., Xu, Q., Li, Y., Wang, Q., Ma, J., Xu, P., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.08.032 · Cited by 432 · see citing works
Reprogramming of H3K9me3-dependent heterochromatin during mammalian embryo development
Wang, C., Liu, X., Gao, Y., Yang, L., Li, C., Liu, W., Chen, C., Kou, X., Zhao, Y., Chen, J., et al. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0093-4 · Cited by 430 · see citing works
Recruitment of Polycomb group complexes and their role in the dynamic regulation of cell fate choice
Schuettengruber, B., & Cavalli, G. (2009) · Development · doi:10.1242/dev.033902 · Cited by 424 · see citing works
Regulated nucleosome mobility and the histone code
Cosgrove, M. S., Boeke, J. D., & Wolberger, C. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb851 · Cited by 421 · see citing works
Zippo, A., Serafini, R., Rocchigiani, M., Pennacchini, S., Křepelová, A., & Oliviero, S. (2009) · Cell · doi:10.1016/j.cell.2009.07.031 · Cited by 418 · see citing works
Histone H1 couples initiation and amplification of ubiquitin signalling after DNA damage
Thorslund, T., Ripplinger, A., Hoffmann, S., Wild, T., Uckelmann, M., Villumsen, B. H., Narita, T., Sixma, T. K., Choudhary, C., Bekker‐Jensen, S., et al. (2015) · Nature · doi:10.1038/nature15401 · Cited by 413 · see citing works
Profile of Histone Lysine Methylation across Transcribed Mammalian Chromatin
Vakoc, C. R., Sachdeva, M. M., Wang, H., & Blobel, G. A. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01529-06 · Cited by 406 · see citing works
Dorighi, K. M., Swigut, T., Henriques, T., Bhanu, N. V., Scruggs, B. S., Nady, N., Still, C. D., Garcia, B. A., Adelman, K., & Wysocka, J. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.04.018 · Cited by 403 · see citing works
Gene Silencing Triggers Polycomb Repressive Complex 2 Recruitment to CpG Islands Genome Wide
Riising, E. M., Comet, I. V., Leblanc, B., Wu, X., Johansen, J. V., & Helin, K. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.06.005 · Cited by 402 · see citing works
Spatial-CUT&Tag: Spatially resolved chromatin modification profiling at the cellular level
Deng, Y., Bartosovic, M., Kukanja, P., Zhang, D., Liu, Y., Su, G., Enninful, A., Bai, Z., Castelo-Branco, G., & Fan, R. (2022) · Science · doi:10.1126/science.abg7216 · Cited by 393 · see citing works
The roles of histone variants in fine-tuning chromatin organization and function
Martire, S., & Banaszynski, L. A. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0262-8 · Cited by 392 · see citing works
Ayrapetov, M. K., Gursoy-Yuzugullu, O., Xu, C., Xu, Y., & Price, B. D. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1403565111 · Cited by 391 · see citing works
The expanding landscape of ‘oncohistone’ mutations in human cancers
Nacev, B. A., Feng, L., Bagert, J. D., Lemiesz, A. E., Gao, J., Soshnev, A. A., Kundra, R., Schultz, N., Muir, T. W., & Allis, C. D. (2019) · Nature · doi:10.1038/s41586-019-1038-1 · Cited by 384 · see citing works
An ultra-low-input native ChIP-seq protocol for genome-wide profiling of rare cell populations
Brind’Amour, J., Liu, S., Hudson, M. B., Chen, C. C. L., Karimi, M. M., & Lorincz, M. C. (2015) · Nature Communications · doi:10.1038/ncomms7033 · Cited by 379 · see citing works
Chen, K., Chen, Z., Wu, D., Zhang, L., Lin, X., Su, J., Rodriguez, B., Xi, Y., Xia, Z., Chen, X., et al. (2015) · Nature Genetics · doi:10.1038/ng.3385 · Cited by 373 · see citing works
Wang, L., Gao, Y., Zheng, X., Liu, C., Dong, S., Li, R., Zhang, G., Wei, Y., Qu, H., Li, Y., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.08.019 · Cited by 372 · see citing works
Molecular determinants of nucleosome retention at CpG-rich sequences in mouse spermatozoa
Erkek, S., Hisano, M., Liang, C.-Y., Gill, M. E., Murr, R., Dieker, J. W. C., Schübeler, D., van der Vlag, J., Stadler, M. B., & Peters, A. H. F. M. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2599 · Cited by 371 · see citing works
Chromatin signature of embryonic pluripotency is established during genome activation
Vastenhouw, N. L., Zhang, Y., Woods, I. G., Imam, F. B., Regev, A., Liu, X. S., Rinn, J. L., & Schier, A. F. (2010) · Nature · doi:10.1038/nature08866 · Cited by 367 · see citing works
Turner, B. M. (1993) · Cell · doi:10.1016/s0092-8674(05)80078-9 · Cited by 349 · see citing works
The BAH domain of ORC1 links H4K20me2 to DNA replication licensing and Meier–Gorlin syndrome
Kuo, A. J., Song, J., Cheung, P., Ishibe-Murakami, S., Yamazoe, S., Chen, J., Patel, D. J., & Gozani, O. (2012) · Nature · doi:10.1038/nature10956 · Cited by 349 · see citing works
Histone H2AK119 Mono-Ubiquitination Is Essential for Polycomb-Mediated Transcriptional Repression
Tamburri, S., Lavarone, E., Fernández-Pérez, D., Conway, E., Zanotti, M., Manganaro, D., & Pasini, D. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.11.021 · Cited by 347 · see citing works
Phase separation of Polycomb-repressive complex 1 is governed by a charged disordered region of CBX2Preprint
Plys, A. J., Davis, C. P., Kim, J. J., Rizki, G., Keenen, M. M., Marr, S. K., & Kingston, R. E. (2019) · Genes & Development · doi:10.1101/gad.326488.119 · Cited by 346 · see citing works
Canzio, D., Chang, E. Y., Shankar, S., Kuchenbecker, K. M., Simon, M. D., Madhani, H. D., Narlikar, G. J., & Al‐Sady, B. (2011) · Molecular Cell · doi:10.1016/j.molcel.2010.12.016 · Cited by 341 · see citing works
Loop extrusion as a mechanism for formation of DNA damage repair foci
Arnould, C., Rocher, V., Finoux, A.-L., Clouaire, T., Li, K., Zhou, F., Caron, P., Mangeot, P. E., Ricci, E. P., Mourad, R., et al. (2021) · Nature · doi:10.1038/s41586-021-03193-z · Cited by 341 · see citing works
Yeast histone H4 N-terminal sequence is required for promoter activation in vivo
Durrin, L. K., Mann, R. K., Kayne, P. S., & Grunstein, M. R. (1991) · Cell · doi:10.1016/0092-8674(91)90554-c · Cited by 333 · see citing works
Kundu, S., Ji, F., Sunwoo, H., Jain, G., Lee, J. T., Sadreyev, R. I., Dekker, J., & Kingston, R. E. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.01.009 · Cited by 333 · see citing works
Regulation of gene transcription by Polycomb proteins
Aranda, S., Martín, G. M., & Croce, L. D. (2015) · Science Advances · doi:10.1126/sciadv.1500737 · Cited by 332 · see citing works
Zhang, W., Bone, J. R., Edmondson, D. G., Turner, B. M., & Dent, S. (1998) · The EMBO Journal · doi:10.1093/emboj/17.11.3155 · Cited by 322 · see citing works
Role of H3K9me3 heterochromatin in cell identity establishment and maintenance
Nicetto, D., & Zaret, K. S. (2019) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2019.04.013 · Cited by 312 · see citing works
Nuclear condensates of the Polycomb protein chromobox 2 (CBX2) assemble through phase separation
Tatavosian, R., Kent, S., Brown, K., Yao, T., Duc, H. N., Huynh, T., Zhen, C.-Y., Ma, B., Wang, H.-B., & Ren, X.-J. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.006620 · Cited by 308 · see citing works
A Histone Mutant Reproduces the Phenotype Caused by Loss of Histone-Modifying Factor Polycomb
Pengelly, A. R., Copur, Ö., Jäckle, H., Herzig, A., & Müller, J. (2013) · Science · doi:10.1126/science.1231382 · Cited by 297 · see citing works
Erdel, F., Rademacher, A., Vlijm, R., Tünnermann, J., Frank, L., Weinmann, R., Schweigert, E., Yserentant, K., Hummert, J., Bauer, C., et al. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.02.005 · Cited by 292 · see citing works
The histone H4 Lys 20 methyltransferase PR-Set7 regulates replication origins in mammalian cells
Tardat, M., Brustel, J., Kirsh, O., Lefevbre, C., Callanan, M. B., Sardet, C., & Julien, E. (2010) · Nature Cell Biology · doi:10.1038/ncb2113 · Cited by 289 · see citing works
Certain and Progressive Methylation of Histone H4 at Lysine 20 during the Cell Cycle
Pesavento, J. J., Yang, H., Kelleher, N. L., & Mizzen, C. A. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01517-07 · Cited by 288 · see citing works
Condensed Chromatin Behaves like a Solid on the Mesoscale In Vitro and in Living Cells
Strickfaden, H., Tolsma, T. O., Sharma, A. K., Underhill, D. A., Hansen, J. C., & Hendzel, M. J. (2020) · Cell · doi:10.1016/j.cell.2020.11.027 · Cited by 285 · see citing works
Molecular basis for the recognition of phosphorylated and phosphoacetylated histone h3 by 14-3-3.
Macdonald, N., Welburn, J., Noble, M., Nguyen, A., Yaffe, M., Clynes, D., Moggs, J., Orphanides, G., Thomson, S., Edmunds, J. W., et al. (2005) · Molecules and Cells · doi:10.1016/j.molcel.2005.08.032 · Cited by 282 · see citing works
Resetting histone modifications during human parental-to-zygotic transition
Xia, W., Xu, J., Yu, G., Yao, G., Xu, K., Ma, X., Zhang, N., Liu, B., Li, T., Lin, Z., et al. (2019) · Science · doi:10.1126/science.aaw5118 · Cited by 279 · see citing works
Writing of H3K4Me3 overcomes epigenetic silencing in a sustained but context-dependent manner
Cano-Rodríguez, D., Gjaltema, R. A. F., Jilderda, L. J., Jellema, P. G., Dokter‐Fokkens, J., Ruiters, M. H. J., & Rots, M. G. (2016) · Nature Communications · doi:10.1038/ncomms12284 · Cited by 276 · see citing works
Tropberger, P., Pott, S., Keller, C., Kamieniarz-Gdula, K., Caron, M. J., Richter, F. M., Li, G., Mittler, G., Liu, E. T., Bühler, M., et al. (2013) · Cell · doi:10.1016/j.cell.2013.01.032 · Cited by 272 · see citing works
Self-citationGene-Specific Targeting of H3K9 Methylation Is Sufficient for Initiating Repression In Vivo
Snowden, A. W., Gregory, P. D., Case, C. C., & Pabo, C. O. (2002) · Current Biology · doi:10.1016/s0960-9822(02)01391-x · Cited by 268 · see citing works
The acetyltransferase activity of CBP stimulates transcription
Martínez‐Balbás, M. A., Bannister, A. J., Martin, K., Haus‐Seuffert, P., Meisterernst, M., & Kouzarides, T. (1998) · The EMBO Journal · doi:10.1093/emboj/17.10.2886 · Cited by 266 · see citing works
Self-citationHistone H3K27 acetylation is dispensable for enhancer activity in mouse embryonic stem cells
Zhang, T., Zhang, Z., Dong, Q., Xiong, J., & Zhu, B. (2020) · Genome Biology · doi:10.1186/s13059-020-01957-w · Cited by 266 · see citing works
HBO1 Histone Acetylase Activity Is Essential for DNA Replication Licensing and Inhibited by Geminin
Miotto, B., & Struhl, K. (2010) · Molecular Cell · doi:10.1016/j.molcel.2009.12.012 · Cited by 259 · see citing works
Altered chromosomal topology drives oncogenic programs in SDH-deficient GISTs
Flavahan, W. A., Drier, Y., Johnstone, S. E., Hemming, M. L., Tarjan, D. R., Hegazi, E., Shareef, S. J., Javed, N. M., Raut, C. P., Eschle, B. K., et al. (2019) · Nature · doi:10.1038/s41586-019-1668-3 · Cited by 253 · see citing works
Locus-specific histone deacetylation using a synthetic CRISPR-Cas9-based HDAC
Kwon, D. Y., Zhao, Y.-T., Lamonica, J. M., & Zhou, Z. (2017) · Nature Communications · doi:10.1038/ncomms15315 · Cited by 246 · see citing works
A Hierarchy of H3K4me3 and H3K27me3 Acquisition in Spatial Gene Regulation in Xenopus Embryos
Akkers, R. C., van Heeringen, S. J., Jacobi, U. G., Janssen‐Megens, E. M., Françoijs, K., Stunnenberg, H. G., & Veenstra, G. J. C. (2009) · Developmental Cell · doi:10.1016/j.devcel.2009.08.005 · Cited by 244 · see citing works
Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated modification
Tessarz, P., Santos-Rosa, H., Robson, S. C., Sylvestersen, K. B., Nelson, C. J., Nielsen, M. L., & Kouzarides, T. (2014) · Nature · doi:10.1038/nature12819 · Cited by 243 · see citing works
PRC1 catalytic activity is central to polycomb system function
Blackledge, N. P., Fursova, N. A., Kelley, J. R., Huseyin, M. K., Feldmann, A., & Klose, R. J. (2020) · Molecular Cell · doi:10.1016/j.molcel.2019.12.001 · Cited by 243 · see citing works
O’Geen, H., Ren, C., Nicolet, C. M., Perez, A. A., Halmai, J. A. N. M., Le, V. M., Mackay, J. P., Farnham, P., & Segal, D. J. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx578 · Cited by 242 · see citing works
H3K9me3-heterochromatin loss at protein-coding genes enables developmental lineage specification
Nicetto, D., Donahue, G., Jain, T., Peng, T., Sidoli, S., Sheng, L., Montavon, T., Becker, J. S., Grindheim, J. M., Blahnik, K. R., et al. (2019) · Science · doi:10.1126/science.aau0583 · Cited by 241 · see citing works
Dopaminylation of histone H3 in ventral tegmental area regulates cocaine seeking
Lepack, A. E., Werner, C. T., Stewart, A. F., Fulton, S. L., Zhong, P., Farrelly, L. A., Smith, A. C. W., Ramakrishnan, A., Lyu, Y., Bastle, R. M., et al. (2020) · Science · doi:10.1126/science.aaw8806 · Cited by 241 · see citing works
Byvoet, P., Shepherd, G. R., Hardin, J. M., & Noland, B. J. (1972) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(72)90174-9 · Cited by 238 · see citing works
The effect of H3K79 dimethylation and H4K20 trimethylation on nucleosome and chromatin structure
Lu, X., Simon, M. D., Chodaparambil, J. V., Hansen, J. C., Shokat, K. M., & Luger, K. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1489 · Cited by 232 · see citing works
Causal role for inheritance of H3K27me3 in maintaining the OFF state of a <i>Drosophila</i> HOX gene
Coleman, R. T., & Struhl, G. (2017) · Science · doi:10.1126/science.aai8236 · Cited by 221 · see citing works
Germ line–inherited H3K27me3 restricts enhancer function during maternal-to-zygotic transition
Zenk, F. L., Loeser, E., Schiavo, R., Kilpert, F., Bogdanović, O., & Iovino, N. (2017) · Science · doi:10.1126/science.aam5339 · Cited by 221 · see citing works
Rickels, R., Herz, H.-M., Sze, C. C., Cao, K., Morgan, M. A., Collings, C. K., Gause, M., Takahashi, Y.-H., Wang, L., Rendleman, E. J., et al. (2017) · Nature Genetics · doi:10.1038/ng.3965 · Cited by 217 · see citing works
Black, J. C., Manning, A. L., Rechem, C. V., Kim, J., Ladd, B., Cho, J., Pineda, C. M., Murphy, N., Daniels, D. L., Montagna, C., et al. (2013) · Cell · doi:10.1016/j.cell.2013.06.051 · Cited by 214 · see citing works
Prepatterning of Developmental Gene Expression by Modified Histones before Zygotic Genome Activation
Lindeman, L. C., Andersen, I. S., Reiner, A. H., Li, N., Aanes, H., Østrup, O., Winata, C. L., Mathavan, S., Müller, F., Aleström, P., et al. (2011) · Developmental Cell · doi:10.1016/j.devcel.2011.10.008 · Cited by 209 · see citing works
Establishment of regions of genomic activity during the Drosophila maternal to zygotic transition
Li, X., Harrison, M. M., Villalta, J. E., Kaplan, T., & Eisen, M. B. (2014) · eLife · doi:10.7554/elife.03737 · Cited by 208 · see citing works
Trithorax and dCBP Acting in a Complex to Maintain Expression of a Homeotic Gene
Petruk, S., Sedkov, Y., Smith, S. T., Tillib, S. V., Kraevski, V., Nakamura, T., Canaani, E., Croce, C. M., & Mazo, A. (2001) · Science · doi:10.1126/science.1065683 · Cited by 204 · see citing works
Hake, S. B., Garcia, B. A., Kauer, M., Baker, S. P., Shabanowitz, J., Hunt, D. F., & Allis, C. D. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502413102 · Cited by 204 · see citing works
Transcriptional repression by PRC1 in the absence of H2A monoubiquitylationPreprint
Pengelly, A. R., Kalb, R., Finkl, K., & Müller, J. (2015) · Genes & Development · doi:10.1101/gad.265439.115 · Cited by 200 · see citing works
H4K20me0 recognition by BRCA1–BARD1 directs homologous recombination to sister chromatids
Nakamura, K., Saredi, G., Becker, J. R., Foster, B. M., Nguyen, N. V., Beyer, T. E., Cesa, L. C., Faull, P. A., Lukauskas, S., Frimurer, T. M., et al. (2019) · Nature Cell Biology · doi:10.1038/s41556-019-0282-9 · Cited by 192 · see citing works
Cohesin Disrupts Polycomb-Dependent Chromosome Interactions in Embryonic Stem Cells
Rhodes, J. D. P., Feldmann, A., Hernández-Rodríguez, B., Díaz, N., Brown, J. M., Fursova, N. A., Blackledge, N. P., Prathapan, P., Dobrinic, P., Huseyin, M. K., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2019.12.057 · Cited by 187 · see citing works
Gehani, S. S., Singh, S. A., Dietrich, N., Christophersen, N. S., Helin, K., & Hansen, K. H. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.08.020 · Cited by 186 · see citing works
Histone demethylase KDM5A regulates the ZMYND8–NuRD chromatin remodeler to promote DNA repair
Gong, F., Clouaire, T., Aguirrebengoa, M., Legube, G., & Miller, K. M. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201611135 · Cited by 182 · see citing works
Escobar, T. M., Oksuz, O., Saldaña-Meyer, R., Descostes, N., Bonasio, R., & Reinberg, D. (2019) · Cell · doi:10.1016/j.cell.2019.10.009 · Cited by 180 · see citing works
Histone dynamics mediate DNA unwrapping and sliding in nucleosomes
Armeev, G. A., Fedulova, A. S., Komarova, G. A., Kirpichnikov, M. P., & Shaytan, A. К. (2021) · Nature Communications · doi:10.1038/s41467-021-22636-9 · Cited by 179 · see citing works
Phosphorylation of histone H3.3 at serine 31 promotes p300 activity and enhancer acetylation
Martire, S., Gogate, A. A., Whitmill, A., Tafessu, A., Nguyen, J., Teng, Y., Tastemel, M., & Banaszynski, L. A. (2019) · Nature Genetics · doi:10.1038/s41588-019-0428-5 · Cited by 178 · see citing works
UFL1 promotes histone H4 ufmylation and ATM activation
Qin, B., Yu, J., Nowsheen, S., Wang, M., Tu, X., Liu, T., Li, H., Wang, L., & Lou, Z. (2019) · Nature Communications · doi:10.1038/s41467-019-09175-0 · Cited by 177 · see citing works
BARD1 reads H2A lysine 15 ubiquitination to direct homologous recombination
Becker, J. R., Clifford, G., Bonnet, C., Groth, A., Wilson, M. D., & Chapman, J. R. (2021) · Nature · doi:10.1038/s41586-021-03776-w · Cited by 175 · see citing works
Histone acylations and chromatin dynamics: concepts, challenges, and links to metabolism
Nitsch, S., Shahidian, L. Z., & Schneider, R. (2021) · EMBO Reports · doi:10.15252/embr.202152774 · Cited by 172 · see citing works
Self-citationH2A.Z facilitates licensing and activation of early replication origins
Long, H., Zhang, L., Lv, M., Wen, Z., Zhang, W., Chen, X., Zhang, P., Li, T., Chang, L., Jin, C., et al. (2019) · Nature · doi:10.1038/s41586-019-1877-9 · Cited by 170 · see citing works
Placeholder Nucleosomes Underlie Germline-to-Embryo DNA Methylation Reprogramming
Murphy, P. J., Wu, S. F., James, C. R., Wike, C. L., & Cairns, B. R. (2018) · Cell · doi:10.1016/j.cell.2018.01.022 · Cited by 167 · see citing works
Glutarylation of Histone H4 Lysine 91 Regulates Chromatin Dynamics
Bao, X., Liu, Z., Zhang, W., Gladysz, K., Fung, Y. M. E., Tian, G., Xiong, Y., Wong, J. W. H., Yuen, K. W. Y., & Li, X. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.08.018 · Cited by 164 · see citing works
The control of gene expression and cell identity by H3K9 trimethylation
Ninova, M., Tóth, K. F., & Aravin, A. A. (2019) · Development · doi:10.1242/dev.181180 · Cited by 162 · see citing works
Histone H3.3 phosphorylation amplifies stimulation-induced transcription
Armache, A., Yang, S., de Paz, A. M., Robbins, L., Durmaz, C., Cheong, J., Ravishankar, A., Daman, A. W., Ahimovic, D. J., Klevorn, T., et al. (2020) · Nature · doi:10.1038/s41586-020-2533-0 · Cited by 161 · see citing works
The Methylation of Histones during Regeneration of the Liver
Tidwell, T., Allfrey, V. G., & Mirsky, A. E. (1968) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)81723-4 · Cited by 159 · see citing works
Polycomb Group Proteins Regulate Chromatin Architecture in Mouse Oocytes and Early Embryos
Du, Z., Zheng, H., Kawamura, Y., Zhang, K., Gassler, J., Powell, S. T., Xu, Q., Lin, Z., Xu, K., Zhou, Q., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.11.011 · Cited by 158 · see citing works
MLL2 conveys transcription-independent H3K4 trimethylation in oocytes
Hanna, C., Taudt, A., Huang, J.-H., Gahurová, L., Kranz, A., Andrews, S. R., Dean, W., Stewart, A., Colomé-Tatché, M., & Kelsey, G. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-017-0013-5 · Cited by 156 · see citing works
A chromatin integration labelling method enables epigenomic profiling with lower input
Harada, A., Maehara, K., Handa, T., Arimura, Y., Nogami, J., Hayashi‐Takanaka, Y., Shirahige, K., Kurumizaka, H., Kimurâ, H., & Ohkawa, Y. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0248-3 · Cited by 155 · see citing works
A global change in RNA polymerase II pausing during the Drosophila midblastula transition
Chen, K., Johnston, J. J., Shao, W., Meier, S. R., Staber, C. J., & Zeitlinger, J. (2013) · eLife · doi:10.7554/elife.00861 · Cited by 153 · see citing works
Acetylation of histone H3 at lysine 64 regulates nucleosome dynamics and facilitates transcription
Cerbo, V. D., Mohn, F., Ryan, D., Montellier, E., Kacem, S., Tropberger, P., Kallis, E., Holzner, M., Hoerner, L., Feldmann, A., et al. (2014) · eLife · doi:10.7554/elife.01632 · Cited by 153 · see citing works
Self-citationDistinct dynamics and functions of H2AK119ub1 and H3K27me3 in mouse preimplantation embryos
Chen, Z., Djekidel, M. N., & Zhang, Y. (2021) · Nature Genetics · doi:10.1038/s41588-021-00821-2 · Cited by 153 · see citing works
Phase separation directs ubiquitination of gene-body nucleosomes
Gallego, L. D., Schneider, M., Mittal, C., Romanauska, A., Carrillo, R. M. G., Schubert, T., Pugh, B. F., & Köhler, A. (2020) · Nature · doi:10.1038/s41586-020-2097-z · Cited by 152 · see citing works
Replication timing maintains the global epigenetic state in human cells
Klein, K. N., Zhao, P. A., Lyu, X., Sasaki, T., Bartlett, D. A., Singh, A. M., Tasan, I., Zhang, M., Watts, L. P., Hiraga, S., et al. (2021) · Science · doi:10.1126/science.aba5545 · Cited by 151 · see citing works
Shimko, J. C., North, J. A., Bruns, A. N., Poirier, M. G., & Ottesen, J. J. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.01.003 · Cited by 148 · see citing works
Histone demethylase KDM5B is a key regulator of genome stability
Li, X., Liu, L., Yang, S., Song, N., Zhou, X., Gao, J., Yu, N., Shan, L., Wang, Q., Liang, J., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1324036111 · Cited by 148 · see citing works
Promoter bivalency favors an open chromatin architecture in embryonic stem cells
Martín, G. M., Blanco, E., Ballaré, C., Sansó, M., Spill, Y. G., Hu, D., Aoi, Y., Dily, F. L., Shilatifard, A., Martı́-Renom, M. A., et al. (2018) · Nature Genetics · doi:10.1038/s41588-018-0218-5 · Cited by 148 · see citing works
H2AK119ub1 guides maternal inheritance and zygotic deposition of H3K27me3 in mouse embryos
Mei, H., Kozuka, C., Hayashi, R., Kumon, M., Koseki, H., & Inoue, A. (2021) · Nature Genetics · doi:10.1038/s41588-021-00820-3 · Cited by 148 · see citing works
DOT1L inhibition reveals a distinct subset of enhancers dependent on H3K79 methylation
Godfrey, L., Crump, N. T., Thorne, R., Lau, I., Repapi, E., Dimou, D., Smith, A., Harman, J. R., Telenius, J. M., Oudelaar, A. M., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-10844-3 · Cited by 146 · see citing works
Burton, A., Brochard, V., Galan, C., Ruiz-Morales, E. R., Rovira, Q., Rodriguez‐Terrones, D., Kruse, K., Gras, S. L., Vishnu, U. S., Chin, H. G., et al. (2020) · Nature Cell Biology · doi:10.1038/s41556-020-0536-6 · Cited by 144 · see citing works
Self-citationThe influence of eukaryotic chromatin state on CRISPR–Cas9 editing efficiencies
Verkuijl, S. A. N., & Rots, M. G. (2018) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2018.07.005 · Cited by 143 · see citing works
Understanding the interplay between CpG island-associated gene promoters and H3K4 methylation
Hughes, A. L., Kelley, J. R., & Klose, R. J. (2020) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2020.194567 · Cited by 139 · see citing works
Poleshko, A. S., Smith, C. L., Nguyen, S. C., Sivaramakrishnan, P., Wong, K. G., Murray, J. I., Lakadamyali, M., Joyce, E. F., Jain, R., & Epstein, J. A. (2019) · eLife · doi:10.7554/elife.49278 · Cited by 138 · see citing works
RSC-Associated Subnucleosomes Define MNase-Sensitive Promoters in Yeast
Brahma, S., & Henikoff, S. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.10.046 · Cited by 137 · see citing works
Daujat, S., Weiss, T., Mohn, F., Lange, U. C., Ziegler-Birling, C., Zeißler, U., Lappé, M., Schübeler, D., Torres‐Padilla, M., & Schneider, R. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1629 · Cited by 134 · see citing works
Self-citationvan de Werken, C., van der Heijden, G. W., Eleveld, C., Teeuwssen, M., Albert, M., Baarends, W. M., Laven, J. S. E., Peters, A. H. F. M., & Baart, E. B. (2014) · Nature Communications · doi:10.1038/ncomms6868 · Cited by 128 · see citing works
Recognition of Histone Crotonylation by Taf14 Links Metabolic State to Gene Expression
Gowans, G. J., Bridgers, J. B., Zhang, J., Dronamraju, R., Burnetti, A., King, D. A., Thiengmany, A., Shinsky, S. A., Bhanu, N. V., Garcia, B. A., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.09.029 · Cited by 126 · see citing works
The role of PR-Set7 in replication licensing depends on Suv4-20hPreprint
Beck, D. B., Burton, A., Oda, H., Ziegler-Birling, C., Torres‐Padilla, M., & Reinberg, D. (2012) · Genes & Development · doi:10.1101/gad.195636.112 · Cited by 124 · see citing works
Self-citationHörmanseder, E., Simeone, A., Allen, G. E., Bradshaw, C. R., Figlmüller, M., Gurdon, J. B., & Jullien, J. (2017) · Cell stem cell · doi:10.1016/j.stem.2017.03.003 · Cited by 120 · see citing works
Regulation of the nucleosome unwrapping rate controls DNA accessibility
North, J. A., Shimko, J. C., Javaid, S., Mooney, A. M., Shoffner, M. A., Rose, S., Bundschuh, R. A., Fishel, R. A., Ottesen, J. J., & Poirier, M. G. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks747 · Cited by 117 · see citing works
High‐Resolution Chromatin Profiling Using CUT&RUN
Hainer, S. J., & Fazzio, T. G. (2019) · Current Protocols in Molecular Biology · doi:10.1002/cpmb.85 · Cited by 117 · see citing works
Two genomes, one cell: Mitochondrial-nuclear coordination via epigenetic pathways
Wiese, M., & Bannister, A. J. (2020) · Molecular Metabolism · doi:10.1016/j.molmet.2020.01.006 · Cited by 116 · see citing works
Self-citationEmbryonic transcription is controlled by maternally defined chromatin state
Hontelez, S., van Kruijsbergen, I., Γεωργίου, Γ., van Heeringen, S. J., Bogdanović, O., Lister, R., & Veenstra, G. J. C. (2015) · Nature Communications · doi:10.1038/ncomms10148 · Cited by 112 · see citing works
Complete loss of H3K9 methylation dissolves mouse heterochromatin organization
Montavon, T., Shukeir, N., Erikson, G. A., Engist, B., Onishi‐Seebacher, M., Ryan, D. P., Musa, Y., Mittler, G., Meyer, A. G., Genoud, C., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24532-8 · Cited by 111 · see citing works
Old cogs, new tricks: the evolution of gene expression in a chromatin context
Talbert, P. B., Meers, M. P., & Henikoff, S. (2019) · Nature Reviews Genetics · doi:10.1038/s41576-019-0105-7 · Cited by 110 · see citing works
A Snapshot on the Cis Chromatin Response to DNA Double-Strand Breaks
Clouaire, T., & Legube, G. (2019) · Trends in Genetics · doi:10.1016/j.tig.2019.02.003 · Cited by 107 · see citing works
Simultaneous profiling of multiple chromatin proteins in the same cells
Gopalan, S., Wang, Y., Harper, N. W., Garber, M. G., & Fazzio, T. G. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.09.019 · Cited by 107 · see citing works
Eeftens, J. M., Kapoor, M., Michieletto, D., & Brangwynne, C. P. (2021) · Nature Communications · doi:10.1038/s41467-021-26147-5 · Cited by 106 · see citing works
Lismer, A., Dumeaux, V., Lafleur, C., Lambrot, R., Brind’Amour, J., Lorincz, M., & Kimmins, S. (2021) · Developmental Cell · doi:10.1016/j.devcel.2021.01.014 · Cited by 100 · see citing works
TALEN outperforms Cas9 in editing heterochromatin target sites
Jain, S., Shukla, S., Che, Y., Zhang, M., Fatma, Z., Lingamaneni, M., Abesteh, S., Lane, S., Xiong, X., Wang, Y., et al. (2021) · Nature Communications · doi:10.1038/s41467-020-20672-5 · Cited by 96 · see citing works
Histone Core Phosphorylation Regulates DNA Accessibility
Brehove, M., Wang, T., North, J., Luo, Y., Dreher, S. J., Shimko, J. C., Ottesen, J. J., Luger, K., & Poirier, M. G. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.661363 · Cited by 93 · see citing works
Succinylation of H3K122 destabilizes nucleosomes and enhances transcription
Zorro Shahidian, L., Haas, M., Le Gras, S., Nitsch, S., Mourão, A., Geerlof, A., Margueron, R., Michaelis, J., Daujat, S., & Schneider, R. (2021) · The EMBO Reports · doi:10.15252/embr.202051009 · Cited by 92 · see citing works
Self-citationSeller, C. A., Cho, C.-Y., & O’Farrell, P. H. (2019) · Genes & Development · doi:10.1101/gad.321646.118 · Cited by 88 · see citing works
H3K9me selectively blocks transcription factor activity and ensures differentiated tissue integrity
Methot, S. P., Padeken, J., Brancati, G., Zeller, P. J., Delaney, C. E., Gaidatzis, D., Kohler, H., van Oudenaarden, A., Großhans, H., & Gasser, S. M. (2021) · Nature Cell Biology · doi:10.1038/s41556-021-00776-w · Cited by 87 · see citing works
Alagöz, M., Katsuki, Y., Ogiwara, H., Ogi, T., Shibata, A., Kakarougkas, A., & Jeggo, P. A. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv722 · Cited by 85 · see citing works
Direct Binding of INHAT to H3 Tails Disrupted by Modifications
Schneider, R., Bannister, A. J., Weise, C., & Kouzarides, T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.c400151200 · Cited by 84 · see citing works
Self-citationChiarella, A. M., Butler, K. V., Gryder, B. E., Lu, D., Wang, T. A., Yu, X., Pomella, S., Khan, J. I., Jin, J. J., & Hathaway, N. A. (2019) · Nature Biotechnology · doi:10.1038/s41587-019-0296-7 · Cited by 84 · see citing works
Bošković, A., Bender, A., Gall, L., Ziegler-Birling, C., Beaujean, N., & Torres‐Padilla, M. (2012) · Epigenetics · doi:10.4161/epi.20584 · Cited by 81 · see citing works
Dynamic Control of X-Chromosome Conformation and Repression by a Histone H4K20 Demethylase
Brejc, K., Bian, Q., Uzawa, S., Wheeler, B. S., Anderson, E., King, D. S., Kranzusch, P., Preston, C., & Meyer, B. J. (2017) · Cell · doi:10.1016/j.cell.2017.07.041 · Cited by 81 · see citing works
Widespread Enhancer Dememorization and Promoter Priming during Parental-to-Zygotic Transition
Zhang, B., Wu, X., Zhang, W., Shen, W., Sun, Q., Liu, K., Zhang, Y., Wang, Q., Li, Y., Meng, A., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.10.017 · Cited by 81 · see citing works
Laue, K., Rajshekar, S., Courtney, A. J., Lewis, Z., & Goll, M. G. (2019) · Nature Communications · doi:10.1038/s41467-019-09582-3 · Cited by 78 · see citing works
Phosphorylation of histone H3(T118) alters nucleosome dynamics and remodeling
North, J. A., Javaid, S., Ferdinand, M. B., Chatterjee, N., Picking, J. W., Shoffner, M. A., Nakkula, R. J., Bartholomew, B., Ottesen, J. J., Fishel, R. A., et al. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr304 · Cited by 77 · see citing works
Flagged first, then by citations
1 of the 238 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Lactate and lactylation in cancer
Chen, J., Huang, Z., Chen, Y., Tian, H., Chai, P., Shen, Y., Yao, Y., Xu, S., Ge, S., & Jia, R. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02082-x · Cited by 524 · see citing works
Zhong, Q., Xiao, X., Qiu, Y., Xu, Z., Chen, C., Chong, B., Zhao, X., Hai, S., Li, S., An, Z., et al. (2023) · MedComm · doi:10.1002/mco2.261 · Cited by 442 · see citing works
Signaling pathways and targeted therapies for psoriasis
Guo, J., Zhang, H., Lin, W., Lu, L., Su, J., & Chen, X. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01655-6 · Cited by 455 · see citing works
Epigenetic regulation in cardiovascular disease: mechanisms and advances in clinical trials
Shi, Y., Zhang, H., Huang, S., Yin, L., Wang, F., Luo, P., & Huang, H. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01055-2 · Cited by 366 · see citing works
Epigenetics-targeted drugs: current paradigms and future challenges
Dai, W., Qiao, X., Fang, Y., Guo, R., Bai, P., Liu, S., Li, T., Jiang, Y., Wei, S., Na, Z., et al. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02039-0 · Cited by 378 · see citing works
Redox regulation: mechanisms, biology and therapeutic targets in diseases
Li, B., Ming, H., Qin, S., Nice, E. C., Dong, J., Du, Z., & Huang, C. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02095-6 · Cited by 364 · see citing works
Ma, Z., Zuo, T., Frey, N., & Rangrez, A. Y. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01946-6 · Cited by 297 · see citing works
Nuclear GTPSCS functions as a lactyl-CoA synthetase to promote histone lactylation and gliomagenesis
Liu, R., Ren, X.-L., Park, Y., Feng, H., Sheng, X., Song, X.-H., AminiTabrizi, R., Shah, H., Li, L.-T., Zhang, Y., et al. (2024) · Cell Metabolism · doi:10.1016/j.cmet.2024.11.005 · Cited by 251 · see citing works
Xie, B., Lin, J., Chen, X., Zhou, X., Zhang, Y., Fan, M., Xiang, J., He, N., Hu, Z., & Wang, F. (2023) · Molecular Cancer · doi:10.1186/s12943-023-01856-1 · Cited by 221 · see citing works
Crossing epigenetic frontiers: the intersection of novel histone modifications and diseases
Yao, W., Hu, X., & Wang, X. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01918-w · Cited by 229 · see citing works
Histone lactylation drives CD8+ T cell metabolism and function
Raychaudhuri, D., Singh, P., Chakraborty, B., Hennessey, M., Tannir, A. J., Byregowda, S., Natarajan, S. M., Trujillo‐Ocampo, A., Im, J. S., & Goswami, S. (2024) · Nature Immunology · doi:10.1038/s41590-024-01985-9 · Cited by 217 · see citing works
Rheumatoid arthritis: pathogenesis and therapeutic advances
Gao, Y., Zhang, Y., & Liu, X. (2024) · MedComm · doi:10.1002/mco2.509 · Cited by 193 · see citing works
Nshanian, M., Gruber, J. J., Geller, B. S., Chleilat, F., Lancaster, S. M., White, S. M., Alexandrova, L. А., Camarillo, J. M., Kelleher, N. L., Zhao, Y., et al. (2025) · Nature Metabolism · doi:10.1038/s42255-024-01191-9 · Cited by 192 · see citing works
The Epigenetic Hallmarks of Cancer
Esteller, M., Dawson, M. A., Kadoch, C., Rassool, F. V., Jones, P. A., & Baylin, S. B. (2024) · Cancer Discovery · doi:10.1158/2159-8290.cd-24-0296 · Cited by 184 · see citing works
Histone lactylation couples cellular metabolism with developmental gene regulatory networks
Merkuri, F., Rothstein, M., & Simões-Costa, M. (2024) · Nature Communications · doi:10.1038/s41467-023-44121-1 · Cited by 171 · see citing works
Zhou, S., Liu, J., Wan, A., Zhang, Y., & Qi, X. (2024) · Journal of Hematology & Oncology · doi:10.1186/s13045-024-01545-6 · Cited by 168 · see citing works
Epigenetic regulation of early human embryo development
Wilkinson, A. L., Zorzan, I., & Rugg‐Gunn, P. J. (2023) · Cell stem cell · doi:10.1016/j.stem.2023.09.010 · Cited by 160 · see citing works
Policarpi, C., Munafò, M., Tsagkris, S., Carlini, V., & Hackett, J. A. (2024) · Nature Genetics · doi:10.1038/s41588-024-01706-w · Cited by 152 · see citing works
Qiao, J., Tan, Y., Liu, H., Yang, B., Zhang, Q., Liu, Q., Sun, W., Li, Z., Wang, Q., Feng, W., et al. (2024) · Advanced Science · doi:10.1002/advs.202307216 · Cited by 141 · see citing works
Targeting epigenetic regulators as a promising avenue to overcome cancer therapy resistance
Song, J., Yang, P. X., Chen, C., Ding, W., Tillement, O., Bai, H., & Zhang, S. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02266-z · Cited by 145 · see citing works
Altered glycosylation in cancer: molecular functions and therapeutic potential
Xu, X., Peng, Q., Jiang, X., Tan, S., Yang, W., Han, Y., Oyang, L., Lin, J., Shen, M., Wang, J., et al. (2024) · 癌症:英文版 · doi:10.1002/cac2.12610 · Cited by 131 · see citing works
Fan, W., Zeng, S., Wang, X., Wang, G., Liao, D., Li, R., He, S., Li, W., Huang, J., Li, X., et al. (2024) · Genome biology · doi:10.1186/s13059-024-03308-5 · Cited by 127 · see citing works
Epigenetic Dysregulation in Endometriosis: Implications for Pathophysiology and Therapeutics
Marquardt, R. M., Tran, D. N., Lessey, B. A., Rahman, M. S., & Jeong, J. (2023) · Endocrine Reviews · doi:10.1210/endrev/bnad020 · Cited by 130 · see citing works
Environmental exposures influence multigenerational epigenetic transmission
Klibaner-Schiff, E., Simonin, E. M., Akdiş, C. A., Cheong, A. W. Y., Johnson, M. M. D., Karagas, M. R., Kirsh, S., Kline, O., Mazumdar, M., Oken, E., et al. (2024) · Clinical Epigenetics · doi:10.1186/s13148-024-01762-3 · Cited by 128 · see citing works
Polyphenols as Potent Epigenetics Agents for Cancer
Rajendran, P., Abdelsalam, S. A., Renu, K., Veeraraghavan, V., Ammar, R. B., & Ahmed, E. A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231911712 · Cited by 115 · see citing works
The immune system in cardiovascular diseases: from basic mechanisms to therapeutic implications
Wang, X., Chen, L., Wei, J., Zheng, H., Zhou, N., Xu, X., Deng, X., Liu, T., & Zou, Y. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02220-z · Cited by 120 · see citing works
Molecular Spies in Action: Genetically Encoded Fluorescent Biosensors Light up Cellular Signals
Gest, A. M. M., Sahan, A. Z., Zhong, Y., Lin, W., Mehta, S., & Zhang, J. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00293 · Cited by 110 · see citing works
Epigenetic stress memory: A new approach to study cold and heat stress responses in plants
Ramakrishnan, M., Zhang, Z., Mullasseri, S., Kalendar, R. N., Ahmad, Z., Sharma, A., Liu, G., Zhou, M., & Wei, Q. (2022) · Frontiers in Plant Science · doi:10.3389/fpls.2022.1075279 · Cited by 106 · see citing works
Recycling of modified H2A-H2B provides short-term memory of chromatin states
Flury, V., Reverón-Gómez, N., Alcaraz, N., Stewart-Morgan, K. R., Wenger, A., Klose, R. J., & Groth, A. (2023) · Cell · doi:10.1016/j.cell.2023.01.007 · Cited by 97 · see citing works
Exosomes: A Promising Strategy for Repair, Regeneration and Treatment of Skin Disorders
Tienda-Vázquez, M. A., Hanel, J. M., Márquez-Arteaga, E. M., Salgado-Álvarez, A. P., Scheckhuber, C. Q., Alanís-Gómez, J. R., Espinoza-Silva, J. I., Ramos-Kuri, M., Hernández-Rosas, F., Melchor-Martínez, E. M., et al. (2023) · Cells · doi:10.3390/cells12121625 · Cited by 104 · see citing works
C/EBPβ: The structure, regulation, and its roles in inflammation-related diseases
Ren, Q., Liu, Z., Wu, L., Yin, G., Xie, X., Kong, W., Zhou, J., & Liu, S. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115938 · Cited by 104 · see citing works
Unlocking the multifaceted molecular functions and diverse disease implications of lactylation
Jing, F., Zhang, J., Zhang, H., & Li, T. (2024) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.13135 · Cited by 99 · see citing works
BET Bromodomain Inhibitors: Novel Design Strategies and Therapeutic Applications
To, K. K. W., Xing, E., Larue, R. C., & Li, P. (2023) · Molecules · doi:10.3390/molecules28073043 · Cited by 95 · see citing works
Single-cell sequencing technology applied to epigenetics for the study of tumor heterogeneity
Hu, Y., Shen, F., Yang, X., Han, T., Long, Z., Wen, J., Huang, J., Shen, J., & Guo, Q. (2023) · Clinical Epigenetics · doi:10.1186/s13148-023-01574-x · Cited by 95 · see citing works
Unveiling the link between chronic inflammation and cancer
Tripathi, S., Sharma, Y., & Kumar, D. (2025) · Metabolism Open · doi:10.1016/j.metop.2025.100347 · Cited by 91 · see citing works
Raza, A., Salehi, H., Bashir, S., Tabassum, J., Jamla, M., Charagh, S., Barmukh, R., Mir, R. A., Bhat, B. A., Javed, M. A., et al. (2024) · Plant Cell Reports · doi:10.1007/s00299-024-03153-7 · Cited by 88 · see citing works
Targeting epigenetic regulators for inflammation: Mechanisms and intervention therapy
Zhang, S., Meng, Y., Zhou, L., Qiu, L., Wang, H., Su, D., Zhang, B., Chan, K. M., & Han, J. (2022) · MedComm · doi:10.1002/mco2.173 · Cited by 82 · see citing works
Histone variants and modifications during abiotic stress response
Nunez-Vazquez, R., Desvoyes, B., & Gutiérrez, C. (2022) · Frontiers in Plant Science · doi:10.3389/fpls.2022.984702 · Cited by 80 · see citing works
Emerging epigenetic insights into aging mechanisms and interventions
Wu, Z., Zhang, W., Qu, J. T., & Liu, G. (2024) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2023.12.002 · Cited by 74 · see citing works
Decoding chromatin states by proteomic profiling of nucleosome readers
Lukauskas, S., Tvardovskiy, A., Nguyen, N. V., Stadler, M., Faull, P. A., Ravnsborg, T., Aygenli, B. Ö., Dornauer, S., Flynn, H. R., Lindeboom, R. G. H., et al. (2024) · Nature · doi:10.1038/s41586-024-07141-5 · Cited by 75 · see citing works
Self-citationThe complex role of MEG3: An emerging long non-coding RNA in breast cancer
Hussain, M. S., Majami, A. A., Ali, H., Gupta, G., Almalki, W. H., Alzarea, S. I., Kazmi, I. A., Syed, R. U., Khalifa, N. E., Break, M. K. B., et al. (2023) · Pathology - Research and Practice · doi:10.1016/j.prp.2023.154850 · Cited by 66 · see citing works
Metal Ion Signaling in Biomedicine
Rodriguez, R., Müller, S., Colombeau, L., Solier, S., Sindikubwabo, F., & Cañeque, T. (2025) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00577 · Cited by 66 · see citing works
Bidirectional histone monoaminylation dynamics regulate neural rhythmicity
Zheng, Q., Weekley, B. H., Vinson, D. A., Zhao, S., Bastle, R. M., Thompson, R. E., Stransky, S., Ramakrishnan, A., Cunningham, A. M., Dutta, S., et al. (2025) · Nature · doi:10.1038/s41586-024-08371-3 · Cited by 66 · see citing works
Therapeutic potential of natural molecules against Alzheimer's disease via SIRT1 modulation
Zhang, M., & Tang, Z. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.114474 · Cited by 66 · see citing works
Mind the gap: Epigenetic regulation of chromatin accessibility in plants
Candela-Ferre, J., Diego‐Martin, B., Pérez-Alemany, J., & Gallego‐Bartolomé, J. (2024) · PLANT PHYSIOLOGY · doi:10.1093/plphys/kiae024 · Cited by 65 · see citing works
Epigenetic control of plant abiotic stress responses
Ma, L., Xing, L., Li, Z., & Jiang, D. (2024) · Journal of genetics and genomics/Journal of Genetics and Genomics · doi:10.1016/j.jgg.2024.09.008 · Cited by 63 · see citing works
Zhang, C., Yu, R., Li, S., Yuan, M., Hu, T., Liu, J., Ke, H., Ye, S., Yun, J., Huang, J., et al. (2025) · Cell Death and Differentiation · doi:10.1038/s41418-025-01533-4 · Cited by 62 · see citing works
Cell-free DNA fragmentomics in cancer
Tsui, W., Jiang, P., & Lo, Y. M. D. (2025) · Cancer Cell · doi:10.1016/j.ccell.2025.09.006 · Cited by 63 · see citing works
Wang, X., Liu, Q., Yu, H., Xie, J., Zhao, J., Fang, Z.-T., Qu, M., Zhang, Y., Yang, Y., & Wang, J. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01812-5 · Cited by 60 · see citing works
Tubulin Post-Translational Modifications: The Elusive Roles of Acetylation
Carmona, B., Marinho, H. S., Matos, C. L., Nolasco, S., & Soares, H. (2023) · Biology · doi:10.3390/biology12040561 · Cited by 58 · see citing works
Integrated multi-omics with machine learning to uncover the intricacies of kidney disease
Liu, X., Shi, J., Jiao, Y., An, J., Tian, J., Yang, Y., & Zhuo, L. (2024) · Briefings in Bioinformatics · doi:10.1093/bib/bbae364 · Cited by 56 · see citing works
Mechanisms of DNA Methylation Regulatory Function and Crosstalk with Histone Lysine Methylation
Tibben, B. M., & Rothbart, S. B. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168394 · Cited by 55 · see citing works
Epigenetic regulation of cancer stemness
Galassi, C., Manic, G., Esteller, M., Galluzzi, L., & Vitale, I. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02340-6 · Cited by 57 · see citing works
Oxidative Stress, Endothelial Dysfunction, and N -Acetylcysteine in Type 2 Diabetes Mellitus
Li, X., Zou, J., Lin, A., Chi, J., Hao, H., Chen, H., & Liu, Z. (2024) · Antioxidants and Redox Signaling · doi:10.1089/ars.2023.0524 · Cited by 56 · see citing works
APP lysine 612 lactylation ameliorates amyloid pathology and memory decline in Alzheimer’s disease
Tian, Q., Li, J., Wu, B., Pang, Y., He, W., Xiao, Q., Wang, J., Yi, L., Tian, N., Shi, X., et al. (2025) · Journal of Clinical Investigation · doi:10.1172/jci184656 · Cited by 53 · see citing works
PROTACs: Novel tools for improving immunotherapy in cancer
Li, S., Chen, T., Liu, J., Zhang, H., Li, J., Wang, Z. P., & Shang, G. (2023) · Cancer Letters · doi:10.1016/j.canlet.2023.216128 · Cited by 52 · see citing works
Roth, G. V., Gengaro, I. R., & Qi, L. S. (2024) · Cell chemical biology · doi:10.1016/j.chembiol.2024.07.007 · Cited by 52 · see citing works
Epigenetic regulation of hematopoietic stem cell fate
Meng, Y., & Nerlov, C. (2024) · Trends in Cell Biology · doi:10.1016/j.tcb.2024.08.005 · Cited by 51 · see citing works
Zenk, F. L., Fleck, J. S., Jansen, S. M. J., Kashanian, B., Eisinger, B. N., Santel, M., Dupré, J.-S., Camp, J. G., & Treutlein, B. (2024) · Nature Neuroscience · doi:10.1038/s41593-024-01652-0 · Cited by 52 · see citing works
3D genome, on repeat: Higher-order folding principles of the heterochromatinized repetitive genome
Haws, S. A., Simándi, Z., Barnett, R. J., & Phillips‐Cremins, J. E. (2022) · Cell · doi:10.1016/j.cell.2022.06.052 · Cited by 51 · see citing works
Cut&tag: a powerful epigenetic tool for chromatin profiling
Fu, Z., Jiang, S., Sun, Y., zheng, S., Zong, L., & Li, P. (2023) · Epigenetics · doi:10.1080/15592294.2023.2293411 · Cited by 51 · see citing works
Natural antisense transcripts as versatile regulators of gene expression
Werner, A., Kanhere, A., Wahlestedt, C., & Mattick, J. S. (2024) · Nature Reviews Genetics · doi:10.1038/s41576-024-00723-z · Cited by 50 · see citing works
Griñán‐Ferré, C., Bellver‐Sanchís, A., Guerrero, A. T. G., & Pallàs, M. (2024) · Pharmacological Research · doi:10.1016/j.phrs.2024.107247 · Cited by 53 · see citing works
Lactate-mediated lactylation in human health and diseases: Progress and remaining challenges
Hu, X., Wu, X., Xu, J., & Xu, X. M. (2024) · Journal of Advanced Research · doi:10.1016/j.jare.2024.11.010 · Cited by 49 · see citing works
Deciphering the fibrotic process: mechanism of chronic radiation skin injury fibrosis
Wang, Y., Chen, S., Bao, S., Li, Y., Wen, Z., Xu, L., Chen, X., Guo, S., Pang, H., Zhou, Y., et al. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1338922 · Cited by 47 · see citing works
A two-way relationship between histone acetylation and metabolism
Charidemou, E., & Kirmizis, A. (2024) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2024.10.005 · Cited by 47 · see citing works
Acetylation of histone H3 in cancer progression and prognosis
Miziak, P., Baran, M., Borkiewicz, L., Trombik, T., & Stepulak, A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252010982 · Cited by 49 · see citing works
Epigenetic reprogramming during the maternal‐to‐zygotic transition
Chen, Y., Wang, L., Guo, F., Dai, X., & Zhang, X. (2023) · MedComm · doi:10.1002/mco2.331 · Cited by 47 · see citing works
Metabolite regulation of epigenetics in cancer
Wang, P., Chen, L., Xiong, Y., & Ye, D. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114815 · Cited by 48 · see citing works
Gut microbiota and epigenetic inheritance: implications for the development of IBD
Guo, X., Li, J.-H., Xu, J., Zhang, L., Huang, C., Nie, Y., & Zhou, Y.-L. (2025) · Gut microbes · doi:10.1080/19490976.2025.2490207 · Cited by 50 · see citing works
Gelléri, M., Chen, S., Szczurek, A., Hübner, B., Sterr, M., Neumann, J., Kröger, O., Sadlo, F., Imhoff, J., Markaki, Y., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2023.112567 · Cited by 44 · see citing works
Duan, X., Xing, Z., Qiao, L., Qin, S., Zhao, X., Gong, Y., & Li, X. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1495221 · Cited by 48 · see citing works
KMT2 Family of H3K4 Methyltransferases: Enzymatic Activity-dependent and -independent Functions
Van, H. T., Xie, G., Dong, P., Liu, Z. J., & Ge, K. (2024) · Journal of Molecular Biology · doi:10.1016/j.jmb.2024.168453 · Cited by 41 · see citing works
Epigenetic Mechanisms in Latent Epstein-Barr Virus Infection and Associated Cancers
Torne, A. S., & Robertson, E. S. (2024) · Cancers · doi:10.3390/cancers16050991 · Cited by 42 · see citing works
Genetic code expansion reveals site-specific lactylation in living cells reshapes protein functions
Shao, C., Tang, S., Yu, S., Liu, C., Zhang, Y., Wan, T., He, Z., Yuan, Q., Wu, S., Zhang, H., et al. (2025) · Nature Communications · doi:10.1038/s41467-024-55165-2 · Cited by 45 · see citing works
Hustmyer, C. M., & Landick, R. C. (2024) · Molecular Microbiology · doi:10.1111/mmi.15283 · Cited by 41 · see citing works
Histone Phosphorylation in DNA Damage Response
Gong, P., Guo, Z., Wang, S., Gao, S., & Cao, Q. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26062405 · Cited by 42 · see citing works
Epigenetic modulators provide a path to understanding disease and therapeutic opportunityPreprint
Honer, M. A., Ferman, B. I., Gray, Z. H., Bondarenko, E. A., & Whetstine, J. R. (2024) · Genes & Development · doi:10.1101/gad.351444.123 · Cited by 40 · see citing works
Epigenetic rejuvenation by partial reprogramming
Puri, D., & Wagner, W. (2023) · BioEssays · doi:10.1002/bies.202200208 · Cited by 42 · see citing works
Zhang, Z., & Zhang, Y. (2024) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-024-03021-y · Cited by 40 · see citing works
Dou, Y., Zhang, M., Zhang, H., Zhang, C., Feng, L., Hu, J., Gao, Y., Yuan, X.-Z., Zhao, Y., Zhao, H., et al. (2024) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2024.174972 · Cited by 40 · see citing works
Epithelial–mesenchymal plasticity in cancer: signaling pathways and therapeutic targets
Wang, X., Xue, X., Pang, M., Yu, L., Qian, J., Li, X., Tian, M., Lü, A., Lu, C. Y., & Liu, Y. (2024) · MedComm · doi:10.1002/mco2.659 · Cited by 40 · see citing works
Bakulski, K. M., Blostein, F., & London, S. J. (2023) · Environmental Health Perspectives · doi:10.1289/ehp12956 · Cited by 38 · see citing works
Real-time single-molecule imaging of transcriptional regulatory networks in living cells
Hwang, D.-W., Maekiniemi, A., Singer, R. H., & Sato, H. (2024) · Nature Reviews Genetics · doi:10.1038/s41576-023-00684-9 · Cited by 40 · see citing works
Epigenetic Regulation of Aging and its Rejuvenation
An, Y., Wang, Q., Gao, K., Zhang, C., Ouyang, Y., Li, R., Zhou, M., Wu, T., Zhou, L., Xie, Z., et al. (2025) · MedComm · doi:10.1002/mco2.70369 · Cited by 44 · see citing works
Zhang, X., Liu, Z., Zhang, Y., Xu, L., Chen, M., Zhou, Y.-F., Yu, J. Q., Li, X., & Zhang, N. (2023) · Cell & Bioscience · doi:10.1186/s13578-023-00996-7 · Cited by 37 · see citing works
Pereira, K. N. E., Shan, J., Licht, J. D., & Bennett, R. L. (2023) · Biochemical Society Transactions · doi:10.1042/bst20210567 · Cited by 38 · see citing works
The role of histone acetylation in transcriptional regulation and seed development
Chen, Y., Guo, P., & Dong, Z. (2023) · PLANT PHYSIOLOGY · doi:10.1093/plphys/kiad614 · Cited by 36 · see citing works
Epigenetic control of microglial immune responses
Scholz, R., Brösamle, D., Yuan, X., Beyer, M., & Neher, J. J. (2024) · Immunological Reviews · doi:10.1111/imr.13317 · Cited by 39 · see citing works
Lactate and lysine lactylation of histone regulate transcription in cancer
Yang, Y., Luo, N., Gong, Z., Zhou, W., Ku, Y., & Chen, Y. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e38426 · Cited by 37 · see citing works
Multi-omics based and AI-driven drug repositioning for epigenetic therapy in female malignancies
Salvati, A., Melone, V., Giordano, A., Lamberti, J., Palumbo, D., Palo, L., Rea, D., Memoli, D., Simonis, V., Alexandrova, E., et al. (2025) · Journal of Translational Medicine · doi:10.1186/s12967-025-06856-x · Cited by 40 · see citing works
EZH2: An Accomplice of Gastric Cancer
Yu, W., Liu, N., Song, X., Chen, L., Wang, M., Xiao, G., Li, T., Wang, Z., & Zhang, Y. (2023) · Cancers · doi:10.3390/cancers15020425 · Cited by 37 · see citing works
Targeting Homocysteine and Hydrogen Sulfide Balance as Future Therapeutics in Cancer Treatment
Majumder, A. (2023) · Antioxidants · doi:10.3390/antiox12081520 · Cited by 36 · see citing works
Regulatory roles of epigenetic modifications in plant-phytopathogen interactions
Zeng, T., Yan, F., Hahn, M., & Ma, Z. (2023) · Crop Health · doi:10.1007/s44297-023-00003-y · Cited by 36 · see citing works
HIRA vs. DAXX: the two axes shaping the histone H3.3 landscape
Choi, J., Kim, T., & Cho, E. (2024) · Experimental & Molecular Medicine · doi:10.1038/s12276-023-01145-3 · Cited by 36 · see citing works
Tang, J., Zhuang, Y., Zhang, Y., Hu, H., Wang, H., Xu, H., Li, Y., & Tu, C. (2025) · Journal of Hematology & Oncology · doi:10.1186/s13045-025-01726-x · Cited by 38 · see citing works
RNA modifications in gene regulation: Functions and pathways
Wei, J., & He, C. (2026) · Cell · doi:10.1016/j.cell.2026.01.006 · Cited by 36 · see citing works
Non-Cell-Autonomous Factors Implicated in Parvalbumin Interneuron Maturation and Critical Periods
Gibel-Russo, R., Benacom, D., & Nardo, A. A. D. (2022) · Frontiers in Neural Circuits · doi:10.3389/fncir.2022.875873 · Cited by 36 · see citing works
Epigenetics and Methylmercury-Induced Neurotoxicity, Evidence from Experimental Studies
Ke, T., Tinkov, A. A., Skalny, A. V., Santamarı́a, A., da Rocha, J. B. T., Bowman, A. B., Chen, W. L., & Aschner, M. (2023) · Toxics · doi:10.3390/toxics11010072 · Cited by 35 · see citing works
Epigenetic modification in diabetic kidney disease
Liu, Z., Liu, J., Wang, W., An, X., Luo, L., Yu, D., & Sun, W. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1133970 · Cited by 36 · see citing works
- 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