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

The hallmarks of cancer

Hanahan, D., & Weinberg, R. A. (2000) · Cell · doi:10.1016/s0092-8674(00)81683-9 · Cited by 29,219

Comprehensive Mapping of Long-Range Interactions Reveals Folding Principles of the Human Genome

Lieberman-Aiden, E., van Berkum, N. L., Williams, L., Imakaev, M., Ragoczy, T., Telling, A., Amit, I., Lajoie, B. R., Sabo, P. J., Dorschner, M. O., et al. (2009) · Science · doi:10.1126/science.1181369 · Cited by 8,898

High-Resolution Profiling of Histone Methylations in the Human Genome

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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

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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

Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins

Lachner, M., O'Carroll, D., Rea, S., Mechtler, K., & Jenuwein, T. (2001) · Nature · doi:10.1038/35065132 · Cited by 2,868

Histone methyltransferases MLL2 and SETD1A/B play distinct roles in H3K4me3 deposition during the transition from totipotency to pluripotency

Zhang, J., Sun, Q.-R., Liu, L., Yang, S., Zhang, X., Miao, Y., & Liu, X. (2024) · The EMBO Journal · doi:10.1038/s44318-024-00329-5 · Cited by 24

Kidney cancer: From tumor biology to innovative therapeutics

Rinaldi, L., Senatore, E., Feliciello, S., Chiuso, F., Insabato, L., & Feliciello, A. (2024) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2024.189240 · Cited by 21

Meta-epigenetic shifts in T cell aging and aging-related dysfunction

Rousseau, L., Hajdu, K. L., & Ho, P. (2025) · Journal of Biomedical Science · doi:10.1186/s12929-025-01146-6 · Cited by 21

Histones in neutrophil extracellular traps (NETs) contain oxidative post-translational modifications induced by the myeloperoxidase oxidant hypochlorous acid

Hemmling, H., Hallberg, L. A. E., Hägglund, P., & Hawkins, C. L. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103696 · Cited by 24

Microbiota-Derived Propionate Modulates Megakaryopoiesis and Platelet Function

Dürholz, K., Schmid, E., Frech, M., Azizov, V., Otterbein, N., Lucas, S., Rauh, M., Schett, G. A., Bruns, H., & Zaiss, M. M. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.908174 · Cited by 23

The pyruvate dehydrogenase complex at the epigenetic crossroads of acetylation and lactylation

Stacpoole, P. W., & Dirain, C. O. (2024) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2024.108540 · Cited by 21

Liver sinusoidal endothelial cells contribute to portal hypertension through collagen type IV–driven sinusoidal remodeling

Gan, C., Yaqoob, U., Lu, J., Xie, M., Anwar, A., Jalan-Sakrikar, N., Jerez, S., Sehrawat, T. S., Navarro-Corcuera, A., Kostallari, E., et al. (2024) · JCI Insight · doi:10.1172/jci.insight.174775 · Cited by 21

Epigenetic control during root development and symbiosis

Zanetti, M. E., Blanco, F. A., Ferrari, M., Ariel, F., Benoit, M., Niebel, A., & Crespi, M. D. (2024) · PLANT PHYSIOLOGY · doi:10.1093/plphys/kiae333 · Cited by 19

Histone H3.3 lysine 9 and 27 control repressive chromatin at cryptic enhancers and bivalent promoters

Trovato, M., Bunina, D., Yildiz, U., Marx, N. F.-N., Uckelmann, M., Levina, V., Perez, Y., Janeva, A., Garcia, B. A., Davidovich, C., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-51785-w · Cited by 20

Role of epigenetic regulation in diminished ovarian reserve

Chen, W. L., Dong, L., Wei, C., & Wu, H. (2024) · Journal of Assisted Reproduction and Genetics · doi:10.1007/s10815-024-03301-8 · Cited by 21

Nucleosome Structures Built from Highly Divergent Histones: Parasites and Giant DNA Viruses

Sato, S., Dacher, M., & Kurumizaka, H. (2022) · Epigenomes · doi:10.3390/epigenomes6030022 · Cited by 20

Remembering through the genome: the role of chromatin states in brain functions and diseases

Arzate‐Mejía, R. G., & Mansuy, I. M. (2023) · Translational Psychiatry · doi:10.1038/s41398-023-02415-4 · Cited by 22

The chromatin source-sink hypothesis: a shared mode of chromatin-mediated regulations

Murphy, P. J., & Berger, F. (2023) · Development · doi:10.1242/dev.201989 · Cited by 19

Epigenetic modifications in the development of bronchopulmonary dysplasia: a review

Wang, L., Xiao, J., Zhang, B., & Hou, A. (2024) · Pediatric Research · doi:10.1038/s41390-024-03167-7 · Cited by 20

Epigenetic control of immunoevasion in cancer stem cells

Galassi, C., Esteller, M., Vitale, I., & Galluzzi, L. (2024) · Trends in cancer · doi:10.1016/j.trecan.2024.08.004 · Cited by 20

Genetic and epigenetic control of the plant metabolome

Hayashi, K., Alseekh, S., & Fernie, A. R. (2023) · PROTEOMICS · doi:10.1002/pmic.202200104 · Cited by 19

Dynamic chromatin accessibility tuning by the long noncoding RNA ELDR accelerates chondrocyte senescence and osteoarthritis

Ji, M.-L., Li, Z., Hu, X. Y., Zhang, W. T., Zhang, H. X., & Lu, J. (2023) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2023.02.011 · Cited by 19

Intergenerational Perioperative Neurocognitive Disorder

Ju, L.-S., Morey, T. E., Seubert, C. N., & Martynyuk, A. E. (2023) · Biology · doi:10.3390/biology12040567 · Cited by 18

PAD2: A potential target for tumor therapy

Teng, Y., Chen, Y., Tang, X., Wang, S., & Yin, K. (2023) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2023.188931 · Cited by 19

Arsenic and Human Health: New Molecular Mechanisms For Arsenic-Induced Cancers

Nail, A. N., Xu, M., Bastick, J. C., Patel, D. P., Rogers, M. N., & States, J. C. (2023) · Current Pollution Reports · doi:10.1007/s40726-023-00278-3 · Cited by 18

Lysine acetylation regulates the AT-rich DNA possession ability of H-NS

Liu, Y., Zhou, M., Bu, Y., Qin, L., Zhang, Y., Shao, S., & Wang, Q. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad1172 · Cited by 18

Loops, crosstalk, and compartmentalization: it takes many layers to regulate DNA methylation

Xu, G., & Law, J. A. (2024) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2023.102147 · Cited by 18

Chromatin Transcription Elongation – A Structural Perspective

Farnung, L. (2024) · Journal of Molecular Biology · doi:10.1016/j.jmb.2024.168845 · Cited by 18

Acute multi-level response to defective de novo chromatin assembly in S-phase

Dreyer, J., Ricci, G., van den Berg, J., Bhardwaj, V., Funk, J., Armstrong, C., van Batenburg, V., Sine, C. C., VanInsberghe, M. A., Tjeerdsma, R. B., et al. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.10.023 · Cited by 18

Protein arginine methylation in transcription and epigenetic regulation

Pham, H. Q. H., Tao, X., & Yang, Y. (2023) · Frontiers in Epigenetics and Epigenomics · doi:10.3389/freae.2023.1245832 · Cited by 20

Unraveling the battle for lysine: A review of the competition among post-translational modifications

Shukri, A. H., Lukinović, V., Charih, F., & Biggar, K. K. (2023) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2023.194990 · Cited by 20

Heterogeneous enhancer states orchestrate β cell responses to metabolic stress

Wang, L., Wu, J., Sramek, M., Obayomi, S. M. B., Gao, P., Li, Y., Matveyenko, A. V., & Wei, Z. (2024) · Nature Communications · doi:10.1038/s41467-024-53717-0 · Cited by 18

Unlocking Wheat Drought Tolerance: The Synergy of Omics Data and Computational Intelligence

le Roux, M.-S. L., Kunert, K. J., Cullis, C. A., & Botha, A. (2024) · Food and Energy Security · doi:10.1002/fes3.70024 · Cited by 20

Integrated analyses of metabolome, leaf anatomy, epigenome, and transcriptome under different light intensities reveal dynamic regulation of histone modifications on the high light adaptation in Camellia sinensis

Zhang, H., Ge, Y., Hu, J., Wang, Y., Ni, D., Wang, P., & Guo, F. (2025) · The Plant Journal · doi:10.1111/tpj.70040 · Cited by 17

Glycolysis Induces Abnormal Transcription Through Histone Lactylation in T-cell Acute Lymphoblastic Leukemia

Wu, W., Zhang, J., Sun, H., Wu, X., Wang, H., Cui, B., Zhao, S., Wu, K., Pan, Y., Fan, R., et al. (2025) · Genomics Proteomics & Bioinformatics · doi:10.1093/gpbjnl/qzaf029 · Cited by 17

Nanoparticles with reprogramming of mitochondrial respiratory chain complex and epigenetic modifications functions for osteoporosis treatment

Liu, Y., Xin, L., Wang, S., Tan, J., Zhu, X., Chen, X., Song, J., Chen, T., & Zhai, Q. (2025) · Biomaterials · doi:10.1016/j.biomaterials.2025.123468 · Cited by 18

Single-cell omics sequencing technologies: the long-read generation

Wen, L., & Tang, F. (2025) · Trends in Genetics · doi:10.1016/j.tig.2025.07.012 · Cited by 18

Epi‐Immunotherapy in Cancer Treatment: Mechanisms, Clinical Progress, and Future Directions

Lu, N., Rong, G., & Han, W. (2025) · Cancer Innovation · doi:10.1002/cai2.70023 · Cited by 17

Recent Advances towards the Reversible Chemical Modification of Proteins

Wu, C.-S., & Cheng, L. (2022) · ChemBioChem · doi:10.1002/cbic.202200468 · Cited by 17

Top-Down Ion Mobility Separations of Isomeric Proteoforms

Berthias, F., Thurman, H. A., Wijegunawardena, G., Wu, H., Shvartsburg, A. A., & Jensen, O. N. (2022) · Analytical Chemistry · doi:10.1021/acs.analchem.2c02948 · Cited by 16

Leveraging histone glycation for cancer diagnostics and therapeutics

Knörlein, A., Xiao, Y. F., & David, Y. (2023) · Trends in cancer · doi:10.1016/j.trecan.2023.01.005 · Cited by 17

Systematic characterization of chromodomain proteins reveals an H3K9me1/2 reader regulating aging in C. elegans

Hou, X., Xu, M., Zhu, C., Gao, J., Li, M., Chen, X., Sun, C., Nashan, B., Zang, J., Zhou, Y., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36898-y · Cited by 16

Intrinsic catalytic properties of histone H3 lysine-9 methyltransferases preserve monomethylation levels under low S-adenosylmethionine

Haws, S. A., Miller, L. J., Luz, D. R. L., Kuznetsov, V. I., Trievel, R. C., Crăciun, G., & Denu, J. M. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104938 · Cited by 17

Chromatin control of human cytomegalovirus infection

Matthews, S. M., Groves, I. J., & O’Connor, C. M. (2023) · mBio · doi:10.1128/mbio.00326-23 · Cited by 17

Epigenetic Therapies in Triple-Negative Breast Cancer: Concepts, Visions, and Challenges

Lehmann, U. (2024) · Cancers · doi:10.3390/cancers16122164 · Cited by 17

Schlank orchestrates insect developmental transition by switching H3K27 acetylation to trimethylation in the prothoracic gland

Yuan, D., Zhang, X., Yang, Y., Wei, L., Li, H., Zhao, T., Guo, M., Li, Z., Huang, Z., Wang, M., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2401861121 · Cited by 17

USP3 promotes DNA damage response and chemotherapy resistance through stabilizing and deubiquitinating SMARCA5 in prostate cancer

Li, S., Li, S., Xiong, S., Li, Z., Yang, H., Yang, H., Xiong, Y., Zhan, X., Dong, Q., Hu, H., et al. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-07117-3 · Cited by 20

RNA Epigenetics in Cancer: Current Knowledge and Therapeutic Implications

Huang, S., Li, Z., Lin, W., Xie, R., & Huang, H. (2025) · MedComm · doi:10.1002/mco2.70322 · Cited by 19

Platelet-derived exosomal LINC00183 facilitate colorectal cancer malignant progression driven by histone lactylation through stabilizing ENO1

Su, G., Qian, J., Wang, Y., Zhu, Y., Chen, Y., Shen, J., Jiang, J., Cao, Y., Wang, N., Huang, X., et al. (2025) · Cell Death and Disease · doi:10.1038/s41419-025-07914-4 · Cited by 16

Cis-regulatory elements: systematic identification and horticultural applications

Li, T., Zeng, W., Zhu, F., & Lü, P. (2025) · aBIOTECH · doi:10.1007/s42994-025-00237-0 · Cited by 17

Epigenetic alterations facilitate transcriptional and translational programs in hypoxia

Watt, K., Dauber, B., Szkop, K. J., Lee, L. J., Jovanovic, P., Chen, S., Palia, R., Vassalakis, J. A., Cooper, T. T., Papadopoli, D. J., et al. (2025) · Nature Cell Biology · doi:10.1038/s41556-025-01786-8 · Cited by 21

Proprioceptors-enriched neuronal cultures from induced pluripotent stem cells from Friedreich ataxia patients show altered transcriptomic and proteomic profiles, abnormal neurite extension, and impaired electrophysiological properties

Dionisi, C., Chazalon, M., Rai, M., Keime, C., Imbault, V., Communi, D., Puccio, H. M., Schiffmann, S. N., & Pandolfo, M. (2022) · Brain Communications · doi:10.1093/braincomms/fcad007 · Cited by 18

Histone Modifications Represent a Key Epigenetic Feature of Epithelial-to-Mesenchyme Transition in Pancreatic Cancer

Xu, Y. X., & Zhu, Q. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24054820 · Cited by 17

High-Fat Diet Related Lung Fibrosis-Epigenetic Regulation Matters

Yang, J., Liang, C., Liu, L., Wang, L., & Yu, G. (2023) · Biomolecules · doi:10.3390/biom13030558 · Cited by 17

Histone modifications in embryo implantation and placentation: insights from mouse models

Bi, S., Tu, Z., Chen, D., & Zhang, S. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1229862 · Cited by 16

Updates in pathobiological aspects of anaplastic large cell lymphoma

Wu, R., & Lim, M. S. (2023) · Frontiers in Oncology · doi:10.3389/fonc.2023.1241532 · Cited by 16

An Optimized and High-Throughput Method for Histone Propionylation and Data-Independent Acquisition Analysis for the Identification and Quantification of Histone Post-translational Modifications

Searfoss, R. M., Karki, R., Lin, Z., Robison, F., & Garcia, B. A. (2023) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.3c00223 · Cited by 16

Diet as an epigenetic factor in inflammatory bowel disease

Marangoni, K., Dorneles, G. P., da Silva, D. M., Pinto, L. P., Rossoni, C., & Fernandes, S. A. (2023) · World Journal of Gastroenterology · doi:10.3748/wjg.v29.i41.5618 · Cited by 19

Zinc-Dependent Histone Deacetylases in Lung Endothelial Pathobiology

Patil, R. S., Maloney, M. E., Lucas, R., Fulton, D. J., Patel, V. S., Bagi, Z. A., Kovács‐Kása, A., Kovács, L., Su, Y., & Verin, A. D. (2024) · Biomolecules · doi:10.3390/biom14020140 · Cited by 15

Approaching the catalytic mechanism of protein lysine methyltransferases by biochemical and simulation techniques

Schnee, P., Pleiss, J., & Jeltsch, A. (2024) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2024.2318547 · Cited by 18

Multiplexed In Situ Imaging of Site-Specific m6A Methylation with Proximity Hybridization Followed by Primer Exchange Amplification (m6A-PHPEA)

Song, M., Wang, J., Hou, J., Fu, T., Feng, Y., Lv, W., Ge, F., Peng, R., Han, D., & Tan, W. (2024) · ACS Nano · doi:10.1021/acsnano.4c08407 · Cited by 16

The BAF complex enhances transcription through interaction with H3K56ac in the histone globular domain

Hyun, K., Ahn, J., Kim, H., Kim, Y., Kim, Y.-I., Park, H., Roeder, R. G., Lee, J. E., & Kim, J. (2024) · Nature Communications · doi:10.1038/s41467-024-53981-0 · Cited by 20

Protein posttranslational modifications in metabolic diseases: basic concepts and targeted therapies

Yang, Y., Wu, J., Zhou, W., Ji, G., & Dang, Y. (2024) · MedComm · doi:10.1002/mco2.752 · Cited by 17

Cold-induced nucleosome dynamics linked to silencing of Arabidopsis FLC

Montez, M., Zhu, D., Huertas, J., Maristany, M. J., Rutjens, B., Nielsen, M., Collepardo‐Guevara, R., & Dean, C. (2025) · Nature Communications · doi:10.1038/s41467-025-60735-z · Cited by 16

The epigenetic landscape of rheumatoid arthritis: Pathogenesis and drug therapeutic potentials

Huang, C., Liang, Y., Li, Y., Quan, W., Ouyang, L., & Zhang, J. (2025) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2025.08.022 · Cited by 20

Global proteomic analysis reveals lysine succinylation contributes to the pathogenesis of aortic aneurysm and dissection

Zhang, H., Zhang, Y., Wang, H., Yang, P., Chen, L., Liu, Y., Xu, Z., Wang, C., & Hu, J. (2023) · Journal of Proteomics · doi:10.1016/j.jprot.2023.104889 · Cited by 15

Radiotherapy and radio‐sensitization in H3K27M ‐mutated diffuse midline gliomas

Liu, C., Kuang, S., Wu, L., Cheng, Q., Gong, X., Wu, J., & Zhang, L. (2023) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.14225 · Cited by 16

Design, synthesis, and biological evaluation of HDAC6 inhibitors targeting L1 loop and serine 531 residue

Jha, S., Kim, J. H., Kim, M., Nguyen, A.-H., Ali, K. H., Gupta, S., Park, S. Y., Ha, E., & Seo, Y. H. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.116057 · Cited by 15

Epigenetic regulation in adult neural stem cells

Shi, J., Wang, Z., Wang, Z., Shao, G., & Li, X. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1331074 · Cited by 17

Gender-specific genetic and epigenetic signatures in cardiovascular disease

Bridges, J., Ramirez-Guerrero, J. A., & Rosa‐Garrido, M. (2024) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2024.1355980 · Cited by 15

[Role and Mechanism of Lactylation in Cancer].

Zhang, Q., Cao, L., & Xu, K. (2024) · PubMed Central · doi:10.3779/j.issn.1009-3419.2024.102.20 · Cited by 15

G9a an Epigenetic Therapeutic Strategy for Neurodegenerative Conditions: From Target Discovery to Clinical Trials

Bellver‐Sanchís, A., Ribalta‐Vilella, M., Irisarri, A., Gehlot, P., Choudhary, B. S., Jana, A., Vyas, V. K., Banerjee, D. R., Pallàs, M., Guerrero, A., et al. (2025) · Medicinal Research Reviews · doi:10.1002/med.22096 · Cited by 14

Histone post-translational modification and heterochromatin alterations in neurodegeneration: revealing novel disease pathways and potential therapeutics

Fisher, R. M. A., & Torrente, M. P. (2024) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2024.1456052 · Cited by 18

Proteomics in pancreatic cancer

Cai, F., Gu, Y., Ling, Y., Yi, G., Zang, S., Su, T., Liu, Y., Li, A., Wang, D., Zhao, W., et al. (2025) · Biomarker Research · doi:10.1186/s40364-025-00805-y · Cited by 19

The epigenetic landscape of tumor-associated macrophages: orchestrating immune evasion in the tumor microenvironment

Liu, X., Li, H., Yuan, M., Wan, J., Guo, J., Dong, X., Jin, X., Yang, C., & Wang, G. (2025) · Cancer Letters · doi:10.1016/j.canlet.2025.217972 · Cited by 14

Histone modification–mediated epigenetic regulation in AKI-to-CKD transition: a cell-type-specific perspective

Chai, S., Zeng, Z., Shang, J., Xu, Y., Han, X., Ma, B., Lv, Z., & Wang, R. (2025) · Journal of Translational Medicine · doi:10.1186/s12967-025-07350-0 · Cited by 14

Cross-Regulation Between Redox and Epigenetic Systems in Tumorigenesis: Molecular Mechanisms and Clinical Applications

Zhang, X., Ma, L., & Wang, J. (2023) · Antioxidants and Redox Signaling · doi:10.1089/ars.2023.0253 · Cited by 16

Oxidative stress-initiated one-carbon metabolism drives the generation of interleukin-10-producing B cells to resolve pneumonia

Fu, Y. L., Yu, B., Wang, Q., Lu, Z., Zhang, H., Zhang, D., Luo, F., Liu, R., Wang, L., & Chu, Y. (2023) · Cellular and Molecular Immunology · doi:10.1038/s41423-023-01109-7 · Cited by 14

The epigenome under pressure: On regulatory adaptation to chronic stress in the brain

Arzate‐Mejía, R. G., Carullo, N. V. N., & Mansuy, I. M. (2023) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2023.102832 · Cited by 15

Circulating nucleosomes as potential biomarkers for cancer diagnosis and treatment monitoring

Wang, H., Wang, Y., Zhang, D., & Li, P. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.130005 · Cited by 17

Identification of TMZ resistance‐associated histone post‐translational modifications in glioblastoma using multi‐omics data

Ye, L., Gu, L., Wang, Y., Xing, H., Li, P., Guo, X.-P., Wang, Y., & Ma, W. (2024) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.14649 · Cited by 14

Epigenetic control of dental stem cells: progress and prospects in multidirectional differentiation

Li, Y., Guo, X., Yao, H., Zhang, Z., & Zhao, H. (2024) · Epigenetics & Chromatin · doi:10.1186/s13072-024-00563-5 · Cited by 14

USP34 regulates PIN1-cGAS-STING axis-dependent ferroptosis in cervical cancer via SUMOylation

Liao, D., Cui, Y., Shi, L., Zeng, S., & Wang, H. (2025) · International Immunopharmacology · doi:10.1016/j.intimp.2024.113968 · Cited by 16

Three-color single-molecule localization microscopy in chromatin

Acosta, N., Gong, R., Su, Y., Frederick, J., Medina, K., Li, W. S., Mohammadian, K., Almassalha, L. M., Wang, G., & Backman, V. (2025) · Light Science & Applications · doi:10.1038/s41377-025-01786-1 · Cited by 14

Runt-related Transcription Factors and Gene Regulatory Mechanisms in Skeletal Development and Diseases

Hojo, H., & Ohba, S. (2023) · Current Osteoporosis Reports · doi:10.1007/s11914-023-00808-4 · Cited by 14

Histone monoaminylation dynamics are regulated by a single enzyme and promote neural rhythmicityPreprint

Zheng, Q., Bastle, R. M., Zhao, S., Kong, L., Vostal, L. E., Ramakrishnan, A., Shen, L., Fulton, S. L., Wang, H., Zhang, B., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.12.06.519310 · Cited by 13

Epigenetics: A link between toxicants and diseases

Romano, A. D. R. R., Pagiatakis, C., Gornati, R., Bernardini, G., & Papait, R. (2025) · iScience · doi:10.1016/j.isci.2025.112613 · Cited by 13

Liquid–Liquid Phase Separation in Major Hallmarks of Cancer

Xie, C., Wang, T., Liu, X. P., Wang, Y., Dang, Q., Ding, T., Xu, J., Yu, X., Lin, H. L., Xu, X., et al. (2025) · Cell Proliferation · doi:10.1111/cpr.70122 · Cited by 13

Transcription factor expression is the main determinant of variability in gene co‐activity

van Duin, L., Krautz, R., Rennie, S., & Andersson, R. (2023) · Molecular Systems Biology · doi:10.15252/msb.202211392 · Cited by 11

The role of histone H3 lysine demethylases in glioblastoma

Young, D. L., Guha, C., & Sidoli, S. (2023) · Cancer and Metastasis Reviews · doi:10.1007/s10555-023-10114-1 · Cited by 13

Casting histone variants during mammalian reproduction

Karam, G., & Molaro, A. (2023) · Chromosoma · doi:10.1007/s00412-023-00803-9 · Cited by 13

Histone H3 serine-57 is a CHK1 substrate whose phosphorylation affects DNA repair

Parisis, N., Dans, P. D., Jbara, M., Singh, B., Schausi, D., Molina‐Serrano, D., Heath, I. B., Hendrychová, D., Maity, S. K., Buitrago, D., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-40843-4 · Cited by 14

Emerging roles of interactions between ncRNAs and other epigenetic modifications in breast cancer

Xie, J., Gan, L., Xue, B., Wang, X., & Pei, X. (2023) · Frontiers in Oncology · doi:10.3389/fonc.2023.1264090 · Cited by 13

Histone demethylases in neurodevelopment and neurodegenerative diseases

Wang, H., Guo, B., & Guo, X. (2023) · International Journal of Neuroscience · doi:10.1080/00207454.2023.2276656 · Cited by 13

Crosstalk within and beyond the Polycomb repressive system

Shi, T., Sugishita, H., & Gotoh, Y. (2024) · The Journal of Cell Biology · doi:10.1083/jcb.202311021 · Cited by 12

Epigenetic Histone Modifications H3K36me3 and H4K5/8/12/16ac Induce Open Polynucleosome Conformations via Different Mechanisms

Lin, Y.-Y., Müller, P. K., Karagianni, E., Hepp, N., Mueller‐Planitz, F., Vanderlinden, W., & Lipfert, J. (2024) · Journal of Molecular Biology · doi:10.1016/j.jmb.2024.168671 · Cited by 13

Histone methylation modification and diabetic kidney disease: Potential molecular mechanisms and therapeutic approaches (Review)

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PHF8/KDM7B: A Versatile Histone Demethylase and Epigenetic Modifier in Nervous System Disease and Cancers

Fan, T., Xie, J., Huang, G. C., Li, L., Zeng, X., & Tao, Q. (2024) · Epigenomes · doi:10.3390/epigenomes8030036 · Cited by 13

Retrospective and multifactorial single-cell profiling reveals sequential chromatin reorganization during X inactivation

Kefalopoulou, S., Rullens, P. M. J., de Luca, K. L., de Vries, S. S., Korthout, T., van Oudenaarden, A., Zeller, P. J., & Kind, J. (2025) · Nature Cell Biology · doi:10.1038/s41556-025-01687-w · Cited by 12

Analog epigenetic memory revealed by targeted chromatin editing

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Analog epigenetic memory revealed by targeted chromatin editing

Palacios, S., Bruno, S., Weiss, R., Salibi, E., Kane, A., Ilia, K., & Del Vecchio, D. (2024) · doi:10.1101/2024.02.13.580200 · Cited by 13

PARylation promotes acute kidney injury via RACK1 dimerization-mediated HIF-1α degradation

Li, X., Shen, X., Mao, X., Wang, Y., Dong, Y., Sun, S., Zhang, M., Wei, J., Wang, J., Li, C., et al. (2025) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2025.07.019 · Cited by 12

TCA-cycle metabolites in the nucleus: drivers of chromatin and epigenetic control

Ghisletti, S., & Russo, M. (2025) · BMC Biology · doi:10.1186/s12915-025-02423-4 · Cited by 12

Interactions of Nucleosomes with Acidic Patch-Binding Peptides: A Combined Structural Bioinformatics, Molecular Modeling, Fluorescence Polarization, and Single-Molecule FRET Study

Oleinikov, P. D., Fedulova, A. S., Armeev, G. A., Motorin, N. A., Singh‐Palchevskaia, L., Sivkina, A. L., Feskin, P. G., Glukhov, G. S., Afonin, D. A., Komarova, G. A., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242015194 · Cited by 12

Preserving genome integrity: The vital role of SUMO-targeted ubiquitin ligases

Han, J., Mu, Y., & Huang, J. (2023) · Cell Insight · doi:10.1016/j.cellin.2023.100128 · Cited by 11

Histone variant-specific post-translational modifications

Joseph, F. M., & Young, N. L. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.02.012 · Cited by 44

Perceiving the epigenetic landscape through histone readers

Musselman, C. A., Lalonde, M., Côté, J., & Kutateladze, T. G. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2436 · Cited by 897

Nothing Is Yet Set in (Hi)stone: Novel Post-Translational Modifications Regulating Chromatin Function

Chan, J. C., & Maze, I. S. (2020) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2020.05.009 · Cited by 126

Genomic stability and epigenetic inheritance in holocentric Caenorhabditis elegans and insects

Yuen, K. W. Y. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.02.021

Beyond the tail: the consequence of context in histone post-translational modification and chromatin research

Weinzapfel, E. N., Fedder-Semmes, K. N., Sun, Z., & Keogh, M. (2024) · Biochemical Journal · doi:10.1042/bcj20230342 · Cited by 23