Cited by 6,012Genomics and Chromatin DynamicsEpigenetics and DNA MethylationChromatin Remodeling and Cancer

The DOI matches its Crossref record; 128 of the 130 references it cites were found in a registry or an index.

Regulation of chromatin by histone modifications

Open access

Bannister, Andrew J, Kouzarides, Tony·2011·Cell Research

DOI 10.1038/cr.2011.22PMC PMC3193420

Open this paper in CoChat — free account Open PDF

Abstract

Chromatin is not an inert structure, but rather an instructive DNA scaffold that can respond to external cues to regulate the many uses of DNA. A principle component of chromatin that plays a key role in this regulation is the modification of histones. There is an ever-growing list of these modifications and the complexity of their action is only just beginning to be understood. However, it is clear that histone modifications play fundamental roles in most biological processes that are involved in the manipulation and expression of DNA. Here, we describe the known histone modifications, define where they are found genomically and discuss some of their functional consequences, concentrating mostly on transcription where the majority of characterisation has taken place.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1038/cr.2011.22

Cites

128 of 128 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Chromatin modifications and their function
Kouzarides, T. (2007) · Cell · doi:10.1016/j.cell.2007.02.005 · Cited by 10,883
Self-citation
Crystal structure of the nucleosome core particle at 2.8 Å resolution
Luger, K., Mäder, A. W., Richmond, R. K., Sargent, D. F., & Richmond, T. J. (1997) · Nature · doi:10.1038/38444 · Cited by 9,466
THE UBIQUITIN SYSTEM
Hershko, A., & Ciechanover, A. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.425 · Cited by 8,840
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
Functional Demarcation of Active and Silent Chromatin Domains in Human HOX Loci by Noncoding RNAs
Rinn, J. L., Kertesz, M., Wang, J. K., Squazzo, S. L., Xu, X. H., Brugmann, S. A., Goodnough, L. H., Helms, J. A., Farnham, P., Segal, E., et al. (2007) · Cell · doi:10.1016/j.cell.2007.05.022 · Cited by 4,246
Histone demethylation mediated by the nuclear amine oxidase homolog LSD1
Shi, Y., Lan, F., Matson, C., Mulligan, P., Whetstine, J. R., Cole, P. A., Casero, R. A., & Shi, Y. (2004) · Cell · doi:10.1016/j.cell.2004.12.012 · Cited by 4,051
Long Noncoding RNA as Modular Scaffold of Histone Modification Complexes
Tsai, M.-C., Manor, O., Wan, Y., Mosammaparast, N., Wang, J. K., Lan, F., Shi, Y., Segal, E., & Chang, H. Y. (2010) · Science · doi:10.1126/science.1192002 · Cited by 3,290
Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain
Bannister, A. J., Zegerman, P., Partridge, J. F., Miska, E. A., Thomas, J. O., Allshire, R. C., & Kouzarides, T. (2001) · Nature · doi:10.1038/35065138 · Cited by 2,903
Self-citation
Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins
Lachner, M., O'Carroll, D., Rea, S., Mechtler, K., & Jenuwein, T. (2001) · Nature · doi:10.1038/35065132 · Cited by 2,868
Regulation of chromatin structure by site-specific histone H3 methyltransferases
Rea, S., Eisenhaber, F., O'Carroll, D., Strahl, B. D., Sun, Z.-W., Schmid, M., Opravil, S., Mechtler, K., Ponting, C. P., Allis, C. D., et al. (2000) · Nature · doi:10.1038/35020506 · Cited by 2,845

Flagged first, then by citations

Show all 130 references

2 of the 130 references couldn’t be matched to a known paper.

Research works printed but not linked: 1

Kouzarides T, Berger SL . Chromatin modifications and their mechanism of action. In: Allis CD, Jenuwein T, Reinberg D, eds. Epigenetics, New York: Cold Spring Harbor Laboratory Press, 2007:191–210.

Sorted by citations

Items 901–1,000 of 1,026

Low dose carbendazim disrupts mouse spermatogenesis might Be through estrogen receptor related histone and DNA methylation
Liu, J., Zhang, P., Zhao, Y. M., & Zhang, H. (2019) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2019.03.103 · Cited by 62
Bacterial Factors Targeting the Nucleus: The Growing Family of Nucleomodulins
Bierne, H., & Pourpre, R. (2020) · Toxins · doi:10.3390/toxins12040220 · Cited by 70
Detailed Review Paper on the State of the Science on Novel In Vitro and In Vivo Screening and Testing Methods and Endpoints for Evaluating Endocrine Disruptors
OECD (2012) · OECD series on testing and assessment · doi:10.1787/9789264221352-en · Cited by 63
One minute analysis of 200 histone posttranslational modifications by direct injection mass spectrometryPreprint
Sidoli, S., Kori, Y., Lopes, M. D. C., Yuan, Z., Kim, H. J., Kulej, K., Janssen, K. A., Agosto, L. M., da Cunha, J. P. C., Andrews, A. J., et al. (2019) · Genome Research · doi:10.1101/gr.247353.118 · Cited by 63
Alcohol effects on the epigenome in the germline: Role in the inheritance of alcohol-related pathology
Chastain, L. G., & Sarkar, D. K. (2017) · Alcohol · doi:10.1016/j.alcohol.2016.12.007 · Cited by 66
Activation of stress response axis as a key process in environment-induced sex plasticity in fish
Hattori, R. S., Castañeda-Cortés, D. C., Padilla, L. F. A., Strobl‐Mazzulla, P. H., & Fernandino, J. I. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03532-9 · Cited by 65
Histone Deacetylases and Histone Deacetylase Inhibitors in Neuroblastoma
Phimmachanh, M., Han, J. Z. R., O’Donnell, Y. E. I., Latham, S. L., & Croucher, D. R. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.578770 · Cited by 61
Decoding the protein composition of whole nucleosomes with Nuc-MS
Schachner, L. F., Jooß, K., Morgan, M. A., Piunti, A., Meiners, M. J., Kafader, J. O., Lee, A. S., Iwanaszko, M., Cheek, M. A., Burg, J. M., et al. (2021) · Nature Methods · doi:10.1038/s41592-020-01052-9 · Cited by 67
Identification of permissive amber suppression sites for efficient non-canonical amino acid incorporation in mammalian cells
Bartoschek, M. D., Ugur, E., Nguyen, T., Rodschinka, G., Wierer, M., Lang, K., & Bultmann, S. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab132 · Cited by 60
Role of Epigenetic Regulation in Plasticity of Tumor Immune Microenvironment
Yang, Y., & Wang, Y. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.640369 · Cited by 64
Epigenetic Modification of the von Willebrand Factor Promoter Drives Platelet Aggregation on the Pulmonary Endothelium in Chronic Thromboembolic Pulmonary Hypertension
Manz, X. D., Szulcek, R., Pan, X., Symersky, P., Dickhoff, C., Majolée, J., Kremer, V., Michielon, E., Jordanova, E. S., Radonic, T. R., et al. (2022) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.202109-2075oc · Cited by 61
Role of Epigenetic Mechanisms in Chronic Pain
Mauceri, D. (2022) · Cells · doi:10.3390/cells11162613 · Cited by 63
Epigenetic therapy as a novel approach in hepatocellular carcinoma
Anestopoulos, I., Voulgaridou, G.-P., Georgakilas, A. G., Franco, R., Pappa, A., & Panayiotidis, M. I. (2014) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2014.09.005 · Cited by 63
Chromatin Proteomics Reveals Variable Histone Modifications during the Life Cycle of Trypanosoma cruzi
de Jesus, T. C. L., Nunes, V. S., Lopes, M. D. C., Martil, D. E., Iwai, L. K., Moretti, N. S., Machado, F. C., de Lima-Stein, M. L., Thiemann, O. H., Elias, M. C., et al. (2016) · Journal of Proteome Research · doi:10.1021/acs.jproteome.6b00208 · Cited by 58
Modulating epigenetic HAT activity for reinstating acetylation homeostasis: A promising therapeutic strategy for neurological disorders
Ganai, S. A., Banday, S., Farooq, Z., & Altaf, M. (2016) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2016.07.001 · Cited by 60
Epigenetic regulation of active Chinese herbal components for cancer prevention and treatment: A follow-up review
Huang, Z., Huang, Q., Ji, L., Wang, Y., Qi, X., Liu, L., Liu, Z., & Lu, L. (2016) · Pharmacological Research · doi:10.1016/j.phrs.2016.09.023 · Cited by 62
Epigenetic Crosstalk between the Tumor Microenvironment and Ovarian Cancer Cells: A Therapeutic Road Less Traveled
Klymenko, Y., & Nephew, K. P. (2018) · Cancers · doi:10.3390/cancers10090295 · Cited by 63
Epigenetic Mechanisms of Abiotic Stress Response and Memory in Plants
Mozgová, I., Mikulski, P., Pečinka, A., & Farrona, S. (2019) · Springer eBooks · doi:10.1007/978-3-030-14760-0_1 · Cited by 63
Epigenetic Gene Regulation by Dietary Compounds in Cancer Prevention
Montgomery, M. R., & Srinivasan, A. (2019) · Advances in Nutrition · doi:10.1093/advances/nmz046 · Cited by 66
Developmental exposure to 50 parts-per-billion arsenic influences histone modifications and associated epigenetic machinery in a region- and sex-specific manner in the adult mouse brain
Tyler, C. R., Hafez, A. K., Solomon, E. R., & Allan, A. M. (2015) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2015.07.013 · Cited by 60
Mechanisms underlying aberrant expression of miR-29c in uterine leiomyoma
Chuang, T., & Khorram, O. (2015) · Fertility and Sterility · doi:10.1016/j.fertnstert.2015.09.020 · Cited by 62
Epigenetic Landscape of Liquid Biopsy in Colorectal Cancer
Rodríguez‐Casanova, A., Costa‐Fraga, N., Bao‐Caamano, A., López‐López, R., Muinelo‐Romay, L., & Díaz‐Lagares, Á. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.622459 · Cited by 60
Genome information processing by the INO80 chromatin remodeler positions nucleosomes
Oberbeckmann, E., Krietenstein, N., Niebauer, V., Wang, Y., Schall, K., Moldt, M., Straub, T., Rohs, R., Hopfner, K., Korber, P., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-23016-z · Cited by 60
Parallel Profiling of the Transcriptome, Cistrome, and Epigenome in the Cellular Response to Ionizing Radiation
Rashi‐Elkeles, S., Warnatz, H.-J., Elkon, R., Kupershtein, A., Chobod, Y., Paz, A., Amstislavskiy, V. S., Sultan, M., Safer, H. M., Nietfeld, W., et al. (2014) · Science Signaling · doi:10.1126/scisignal.2005032 · Cited by 57
Influence of Arsenic on Global Levels of Histone Posttranslational Modifications: a Review of the Literature and Challenges in the Field
Howe, C. G., & Gamble, M. V. (2016) · Current Environmental Health Reports · doi:10.1007/s40572-016-0104-1 · Cited by 61
Lack of the COMPASS Component Ccl1 Reduces H3K4 Trimethylation Levels and Affects Transcription of Secondary Metabolite Genes in Two Plant–Pathogenic Fusarium Species
Studt, L., Janevska, S., Arndt, B., Boedi, S., Sulyok, M., Humpf, H., Tudzynski, B., & Strauss, J. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2016.02144 · Cited by 60
Epigenetic regulation of long non-coding RNAs in gastric cancer
Zhou, Z., Lin, Z., Pang, X., Tariq, M., Ao, X., Li, P., & Wang, J. (2017) · Oncotarget · doi:10.18632/oncotarget.23821 · Cited by 60
Entanglement of Genetics and Epigenetics in Parkinson’s Disease
van Heesbeen, H. J., & Smidt, M. P. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00277 · Cited by 60
Acute Myeloid Leukemia: Aging and Epigenetics
Zjablovskaja, P., & Florian, M. C. (2019) · Cancers · doi:10.3390/cancers12010103 · Cited by 61
The SUMO Ligase Su(var)2-10 Controls Hetero- and Euchromatic Gene Expression via Establishing H3K9 Trimethylation and Negative Feedback Regulation
Ninova, M., Godneeva, B. K., Chen, Y.-C. A., Luo, Y., Prakash, S. J., Jankovics, F., Erdélyi, M., Aravin, A. A., & Tóth, K. F. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.09.033 · Cited by 59
Epigenetic mechanisms in irritable bowel syndrome
Mahurkar-Joshi, S., & Chang, L. (2020) · Frontiers in Psychiatry · doi:10.3389/fpsyt.2020.00805 · Cited by 59
“In general, acetylation of core histone tails leads to open chromatin structure to allow transcription and the histone deacetylases (HDACs) oppose the effects of histone acetylases and are predominantly transcriptional repressors (120).”
Background
HDAC2 hyperexpression alters hippocampal neuronal transcription and microglial activity in neuroinflammation-induced cognitive dysfunction
Sun, X.-Y., Zheng, T., Yang, X., Liu, L., Gao, S.-S., Xu, H.-B., Song, Y.-T., Tong, K., Yang, L., Gao, Y., et al. (2019) · Journal of Neuroinflammation · doi:10.1186/s12974-019-1640-z · Cited by 59
H3K4 methylation at active genes mitigates transcription-replication conflicts during replication stress
Chong, S. Y., Cutler, S., Lin, J., Tsai, C.-H., Tsai, H., Biggins, S., Tsukiyama, T., Lo, Y., & Kao, C.-F. (2020) · Nature Communications · doi:10.1038/s41467-020-14595-4 · Cited by 60
Understanding the Interplay Between Health Disparities and Epigenomics
Mancilla, V. J., Peeri, N. C., Silzer, T. K., Basha, R. M., Felini, M., Jones, H. P., Phillips, N., Tao, M., Thyagarajan, S., & Vishwanatha, J. K. (2020) · Frontiers in Genetics · doi:10.3389/fgene.2020.00903 · Cited by 63
Clinical epigenetics and acute/chronic rejection in solid organ transplantation: An update
Vasco, M., Benincasa, G., Fiorito, C., Faenza, M., Rosa, P. D., Maiello, C., Santangelo, M. L., Vennarecci, G., & Claudio Napoli, A. (2021) · Transplantation Reviews · doi:10.1016/j.trre.2021.100609 · Cited by 65
Endothelial-to-Mesenchymal Transition in Cardiovascular Pathophysiology
Singh, A. D., Bhatt, K. S., Nguyen, H. C., Frisbee, J. C., & Singh, K. K. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25116180 · Cited by 62
Unveiling the role of histone deacetylases in neurological diseases: focus on epilepsy
Cao, D., Zhou, X., Guo, Q., Xiang, M.-Y., Bao, M., He, B., & Mao, X. (2024) · Biomarker Research · doi:10.1186/s40364-024-00687-6 · Cited by 61
Top-down and Middle-down Protein Analysis Reveals that Intact and Clipped Human Histones Differ in Post-translational Modification Patterns*
Tvardovskiy, A., Wrzesinski, K., Sidoli, S., Fey, S. J., Rogowska-Wrzesińska, A., & Jensen, O. N. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m115.048975 · Cited by 61
Depletion of the chromatin remodeler CHD4 sensitizes AML blasts to genotoxic agents and reduces tumor formation
Sperlazza, J. R., Rahmani, M., Beckta, J. M., Aust, M. M., Hawkins, E., Wang, S. Z., Zhu, S. Z., Podder, S., Dumur, C. I., Archer, K. J., et al. (2015) · Blood · doi:10.1182/blood-2015-03-631606 · Cited by 59
Eaf5/7/3 form a functionally independent NuA4 submodule linked to RNA polymerase II‐coupled nucleosome recycling
Rossetto, D., Cramet, M., Wang, A. Y., Steunou, A., Lacoste, N., Schulze-Hentrich, J. M., Côté, V., Saksouk, J., Piquet, S., Nourani, A., et al. (2014) · The EMBO Journal · doi:10.15252/embj.201386433 · Cited by 57
Crafting the Brain – Role of Histone Acetyltransferases in Neural Development and Disease
Sheikh, B. N. (2014) · Cell and Tissue Research · doi:10.1007/s00441-014-1835-7 · Cited by 59
PIP4K and the role of nuclear phosphoinositides in tumour suppression
Fiume, R., Bultsma, Y., Shah, Z. H., Keune, W., Jones, D. R., Jude, J., & Divecha, N. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2015.02.014 · Cited by 61
Distinct Amino Acids of Histone H3 Control Secondary Metabolism in Aspergillus nidulans
Nützmann, H., Fischer, J., Scherlach, K., Hertweck, C., & Brakhage, A. A. (2013) · Applied and Environmental Microbiology · doi:10.1128/aem.01578-13 · Cited by 59
Closing the genotype–phenotype gap: Emerging technologies for evolutionary genetics in ecological model vertebrate systems
Kratochwil, C. F., & Meyer, A. (2014) · BioEssays · doi:10.1002/bies.201400142 · Cited by 59
Enrichment of HP1a on Drosophila Chromosome 4 Genes Creates an Alternate Chromatin Structure Critical for Regulation in this Heterochromatic Domain
Riddle, N. C., Jung, Y. L., Gu, T., Alekseyenko, A. A., Asker, D., Gui, H., Kharchenko, P. V., Minoda, A., Plachetka, A., Schwartz, Y. B., et al. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002954 · Cited by 58
Epigenetic alterations in chronic disease focusing on Behçet’s disease: Review
Alipour, S., Nouri, M., Sakhinia, E., Samadi, N., Roshanravan, N., Ghavami, A., & Khabbazi, A. (2017) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2017.04.106 · Cited by 60
The Cell Wall Integrity Signaling Pathway and Its Involvement in Secondary Metabolite Production
Valiante, V. (2017) · Journal of Fungi · doi:10.3390/jof3040068 · Cited by 62
Sulforaphane epigenetically demethylates the CpG sites of the miR-9-3 promoter and reactivates miR-9-3 expression in human lung cancer A549 cells
Gao, L., Cheng, D., Yang, J., Wu, R., Li, W., & Kong, A. T. (2018) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2018.01.015 · Cited by 59
Pathogenesis of follicular lymphoma
Lackraj, T., Goswami, R. S., & Kridel, R. (2017) · Best Practice & Research Clinical Haematology · doi:10.1016/j.beha.2017.10.006 · Cited by 65
LncRNA regulation: New frontiers in epigenetic solutions to drug chemoresistance
Zhou, Y., Sun, W. C., Qin, Z., Guo, S., Kang, Y., Zeng, S., & Yu, L. (2020) · Biochemical Pharmacology · doi:10.1016/j.bcp.2020.114228 · Cited by 58
The Role of Solute Carrier Transporters in Efficient Anticancer Drug Delivery and Therapy
Puris, E., Fricker, G., & Gynther, M. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15020364 · Cited by 58
Chromatin, DNA structure and alternative splicing
Moreno, N. N., Giono, L. E., Botto, A. E. C., Muñoz, M. J., & Kornblihtt, A. R. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.08.002 · Cited by 62
NAA40 contributes to colorectal cancer growth by controlling PRMT5 expression
Demetriadou, C., Pavlou, D., Mpekris, F., Achilleos, C., Stylianopoulos, T., Zaravinos, A., Papageorgis, P., & Kirmizis, A. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1487-3 · Cited by 58
DNA methylation and chromatin modifiers in colorectal cancer
Vymetalkova, V. P., Vodička, P., Vodenková, S., Alonso, S., & Schneider‐Stock, R. (2019) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2019.04.002 · Cited by 58
Targeting EZH2 as cancer therapy
Hanaki, S., & Shimada, M. (2021) · The Journal of Biochemistry · doi:10.1093/jb/mvab007 · Cited by 56
Germline modifiers of the tumor immune microenvironment implicate drivers of cancer risk and immunotherapy response
Pagadala, M. S., Sears, T. J., Wu, V. H., Pérez‐Guijarro, E., Kim, H., Castro, A., Talwar, J. V., González-Colín, C., Cao, S., Schmiedel, B. J., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-38271-5 · Cited by 54
Long-Term Pancreatic Beta Cell Exposure to High Levels of Glucose but Not Palmitate Induces DNA Methylation within the Insulin Gene Promoter and Represses Transcriptional Activity
Ishikawa, K., Tsunekawa, S., Ikeniwa, M., Izumoto, T., Iida, A., Ogata, H., Uenishi, E., Seino, Y., Ozaki, N., Sugimura, Y., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0115350 · Cited by 58
Comparison of trichostatin A and valproic acid treatment regimens in a mouse model of kidney fibrosis
Beneden, K. V., Geers, C., Pauwels, M., Mannaerts, I., Wissing, K. M., Branden, C. V. D., & van Grunsven, L. A. (2013) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2013.05.013 · Cited by 58
Intrinsically disordered proteins in the nucleus of human cells
Frege, T., & Uversky, V. N. (2015) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2015.03.003 · Cited by 58
Histone modifications and a choice of variant: a language that helps the genome express itself
Gurard‐Levin, Z. A., & Almouzni, G. (2014) · F1000Prime Reports · doi:10.12703/p6-76 · Cited by 65
Next-Generation Sequencing and Epigenomics Research: A Hammer in Search of Nails
Sarda, S., & Hannenhalli, S. S. (2014) · Genomics & Informatics · doi:10.5808/gi.2014.12.1.2 · Cited by 58
Natural compounds: Role in reversal of epigenetic changes
Aggarwal, R., Jha, M., Shrivastava, A., & Jha, A. K. (2015) · Biochemistry (Moscow) · doi:10.1134/s0006297915080027 · Cited by 58
Alteration of Gene Expression, DNA Methylation, and Histone Methylation in Free Radical Scavenging Networks in Adult Mouse Hippocampus following Fetal Alcohol Exposure
Chater‐Diehl, E., Laufer, B. I., Castellani, C. A., Alberry, B., & Singh, S. M. (2016) · PLoS ONE · doi:10.1371/journal.pone.0154836 · Cited by 57
A drive in SUVs: From development to disease
Rao, V. K., Pal, A., & Taneja, R. (2017) · Epigenetics · doi:10.1080/15592294.2017.1281502 · Cited by 62
Reading chromatin signatures after DNA double-strand breaks
Wilson, M. D., & Durocher, D. (2017) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2016.0280 · Cited by 60
Role of Histone Deacetylases (HDACs) in Epilepsy and Epileptogenesis
Citraro, R., Leo, A., Santoro, M., D’Agostino, G., Constanti, A., & Russo, E. (2018) · Current Pharmaceutical Design · doi:10.2174/1381612823666171024130001 · Cited by 58
Histone tail cleavage as a novel epigenetic regulatory mechanism for gene expression
Yi, S.-J., & Kim, K. (2018) · BMB Reports · doi:10.5483/bmbrep.2018.51.5.053 · Cited by 59
How alcohol drinking affects our genes: an epigenetic point of view
Ciafrè, S., Carito, V., Ferraguti, G., Greco, A., Chaldakov, G. N., Fiore, M., & Ceccanti, M. (2018) · Biochemistry and Cell Biology · doi:10.1139/bcb-2018-0248 · Cited by 64
Novel triazolophthalazine-hydrazone hybrids as potential PCAF inhibitors: Design, synthesis, in vitro anticancer evaluation, apoptosis, and molecular docking studies
Abulkhair, H. S., Turky, A., Ghiaty, A. H., Ahmed, H. E. A., & Bayoumi, A. H. (2020) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2020.103899 · Cited by 58
Trimethyllysine: From Carnitine Biosynthesis to Epigenetics
Maas, M. N., Hintzen, J. C. J., Porzberg, M. R. B., & Mecinović, J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21249451 · Cited by 58
Plant 3D genomics: the exploration and application of chromatin organization
Pei, L., Li, G., Lindsey, K., Zhang, X., & Wang, M. (2021) · New Phytologist · doi:10.1111/nph.17262 · Cited by 61
Epigenetics in kidney diseases
Ding, H., Zhang, L., Yang, Q., Zhang, X., & Li, X. (2020) · Advances in clinical chemistry · doi:10.1016/bs.acc.2020.09.005 · Cited by 60
Environmental pollutants exposure and male reproductive toxicity: The role of epigenetic modifications
Han, X., & Huang, Q. (2021) · Toxicology · doi:10.1016/j.tox.2021.152780 · Cited by 61
Epigenetic modifications in neuropathic pain
Luo, D., Li, X., Tang, S., Song, F., Li, W., Xie, G., Liang, J., & Zhou, J. (2021) · Molecular Pain · doi:10.1177/17448069211056767 · Cited by 57
Epigenetic Therapies and Biomarkers in Breast Cancer
Brown, L. J., Achinger-Kawecka, J., Portman, N., Clark, S. J., Stirzaker, C., & Lim, E. (2022) · Cancers · doi:10.3390/cancers14030474 · Cited by 64
Mechanisms of DNA methylation and histone modifications
Acharjee, S., Chauhan, S. K., Pal, R., & Tomar, R. S. (2023) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2023.01.001 · Cited by 61
Modulating glucocorticoid receptor actions in physiology and pathology: Insights from coregulators
Fadel, L., Dacic, M., Fonda, V., Sokolsky, B. A., Quagliarini, F., Rogatsky, I., & Uhlenhaut, N. H. (2023) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2023.108531 · Cited by 63
The “early life” origins of obesity‐related health disorders: New discoveries regarding the intergenerational transmission of developmentally programmed traits in the global cardiometabolic health crisis
Benyshek, D. C. (2013) · American Journal of Physical Anthropology · doi:10.1002/ajpa.22393 · Cited by 59
Generation of a synthetic GlcNAcylated nucleosome reveals regulation of stability by H2A-Thr101 GlcNAcylation
Lercher, L., Raj, R., Patel, N. A., Price, J., Mohammed, S., Robinson, C. V., Schofield, C. J., & Davis, B. G. (2015) · Nature Communications · doi:10.1038/ncomms8978 · Cited by 59
Genes Are Often Sheltered from the Global Histone Hyperacetylation Induced by HDAC Inhibitors
Halsall, J., Gupta, V., O'Neill, L. P., Turner, B. M., & Nightingale, K. P. (2012) · PLoS ONE · doi:10.1371/journal.pone.0033453 · Cited by 57
“The post-translational modification of core histones plays a central role in epigenetic gene regulation [1].”
Background
Histone Cleavage as a Mechanism for Epigenetic Regulation: Current Insights and Perspectives
Zhou, P., Wu, E., Alam, H. B., & Li, Y. (2014) · Current Molecular Medicine · doi:10.2174/1566524014666141015155630 · Cited by 57
Histone Deacetylase Inhibition Activates Transgene Expression from Integration-Defective Lentiviral Vectors in Dividing and Non-Dividing Cells
Pelascini, L. P. L., Janssen, J. M., & Gonçalves, M. A. F. V. (2012) · Human Gene Therapy · doi:10.1089/hum.2012.069 · Cited by 59
Epigenetic regulation in the inner ear and its potential roles in development, protection, and regeneration
Layman, W. S., & Zuo, J. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00446 · Cited by 61
Histone Methyltransferase Inhibitors: Novel Epigenetic Agents for Cancer Treatment
Zagni, C., Chiacchio, U., & Rescifina, A. (2012) · Current Medicinal Chemistry · doi:10.2174/092986713804806667 · Cited by 59
Mechanisms of epigenetic memory and addiction
Tuesta, L. M., & Zhang, Y. (2014) · The EMBO Journal · doi:10.1002/embj.201488106 · Cited by 58
Is Glioblastoma an Epigenetic Malignancy?
Maleszewska, M., & Kaminska, B. (2013) · Cancers · doi:10.3390/cancers5031120 · Cited by 63
Chromatin without the 30-nm fiber
Razin, S. V., & Gavrilov, A. A. (2014) · Epigenetics · doi:10.4161/epi.28297 · Cited by 56
Jmjd3 mediates blood–spinal cord barrier disruption after spinal cord injury by regulating MMP-3 and MMP-9 expressions
Lee, J. Y., Na, W. H., Choi, H. Y., Lee, K. H., Ju, B. G., & Yune, T. Y. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2016.07.015 · Cited by 57
Histone peptide microarray screen of chromo and Tudor domains defines new histone lysine methylation interactions
Shanle, E. K., Shinsky, S. A., Bridgers, J. B., Bae, N., Sagum, C. A., Krajewski, K., Rothbart, S. B., Bedford, M. T., & Strahl, B. D. (2017) · Epigenetics & Chromatin · doi:10.1186/s13072-017-0117-5 · Cited by 61
Setd1b, encoding a histone 3 lysine 4 methyltransferase, is a maternal effect gene required for the oogenic gene expression program
Brici, D., Zhang, Q., Reinhardt, S., Dahl, A., Hartmann, H., Schmidt, K., Goveas, N., Huang, J., Gahurová, L., Kelsey, G., et al. (2017) · Development · doi:10.1242/dev.143347 · Cited by 54
Structural basis for activation of SAGA histone acetyltransferase Gcn5 by partner subunit Ada2
Sun, J. G., Paduch, M., Kim, S.-A., Kramer, R. M., Barrios, A. F., Lu, V., Luke, J., Usatyuk, S., Kossiakoff, A. A., & Tan, S. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1805343115 · Cited by 58
Function and Transcriptional Regulation of Bovine TORC2 Gene in Adipocytes: Roles of C/EBPγ, XBP1, INSM1 and ZNF263
Khan, R., Raza, S. H. A., Junjvlieke, Z., Xiaoyu, W., Garcia, M., Elnour, I. E., Hongbao, W., & Linsen, Z. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20184338 · Cited by 56
Epigenetic Mechanisms Governing Innate Inflammatory Responses
Perkins, D. J., Patel, M. C., Blanco, J. C. G., & Vogel, S. N. (2016) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.2016.0003 · Cited by 51
Extracellular Vesicles and Epigenetic Modifications Are Hallmarks of Melanoma Progression
Mannavola, F., D’Oronzo, S., Cives, M., Stucci, L. S., Ranieri, G., Silvestris, F., & Tucci, M. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms21010052 · Cited by 57
TRPA1 regulates macrophages phenotype plasticity and atherosclerosis progression
Wang, Q., Chen, K., Zhang, F., Peng, K., Wang, Z., Yang, D., & Yang, Y. (2020) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2020.04.004 · Cited by 56
Epigenetic Alteration Shaped by the Environmental Chemical Bisphenol A
Qin, T., Zhang, X., Guo, T., Yang, T., Gao, Y., Hao, W., & Xiao, X. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2020.618966 · Cited by 56
Leveraging clinical epigenetics in heart failure with preserved ejection fraction: a call for individualized therapies
Hamdani, N., Costantino, S., Mügge, A., Lebeche, D., Tschöpe, C., Thum, T., & Paneni, F. (2021) · European Heart Journal · doi:10.1093/eurheartj/ehab197 · Cited by 56
Balancing DNA repair to prevent ageing and cancer
Stead, E. R., & Bjedov, I. (2021) · Experimental Cell Research · doi:10.1016/j.yexcr.2021.112679 · Cited by 62
The epigenetic correlation among ovarian cancer, endometriosis and PCOS: A review
Throwba, H., Unnikrishnan, L., Pangath, M., Vasudevan, K., Jayaraman, S., Li, M., Iyaswamy, A., Palaniyandi, K., & Gnanasampanthapandian, D. (2022) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2022.103852 · Cited by 56
Discovering and mapping chromatin states using a tree hidden Markov model
Biesinger, J., Wang, Y., & Xie, X. S. (2013) · BMC Bioinformatics · doi:10.1186/1471-2105-14-s5-s4 · Cited by 54

Authors: Bannister, A. J., & Kouzarides, T.
Affiliations: University of Cambridge (GB)
Corresponding author: Kouzarides, Tony
ORCID: Bannister, Andrew J
Kouzarides, Tony
Venue: Cell Research
Publisher: Springer Science and Business Media LLC
Published: 2011-02-15
Volume: 21
Issue: 3
Pages: 381-395
ISSN: 1001-0602 (ISSN-L)
1748-7838
DOI: 10.1038/cr.2011.22
PMC: PMC3193420
OpenAlex: W2147524392
Cited by: 6,012
References: 130
Citations by year: 2026: 322 · 2025: 536 · 2024: 558 · 2023: 510 · 2022: 523 · 2021: 490 · 2020: 502 · 2019: 427 · 2018: 404 · 2017: 383 · 2016: 348 · 2015: 283 · 2014: 253 · 2013: 219 · 2012: 176
FWCI: 20.90
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.springer.com/tdm (tdm)
Locations: Cell Research (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
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: chromatin regulation, histone modifications, transcriptional regulation, epigenetics
MeSH terms: Chromatin, Heterochromatin, Histones, Protein Processing, Post-Translational, Histone Demethylases

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

Regulation of chromatin by histone modifications

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks