Methyl-cpG-binding domain proteins: readers of the epigenome

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The Methyl-CpG-binding Protein MeCP2 Links DNA Methylation to Histone Methylation

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Dynamic Readers for 5-(Hydroxy)Methylcytosine and Its Oxidized Derivatives

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MeCP2 binds to 5hmC enriched within active genes and accessible chromatin in the nervous system

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MBD2 is a transcriptional repressor belonging to the MeCP1 histone deacetylase complex

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REST and Its Corepressors Mediate Plasticity of Neuronal Gene Chromatin throughout Neurogenesis

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5-hmC–mediated epigenetic dynamics during postnatal neurodevelopment and aging

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Mi-2 complex couples DNA methylation to chromatin remodelling and histone deacetylation

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Thymine DNA glycosylase is essential for active DNA demethylation by linked deamination-base excision repair

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Methylation of Histone H4 at Arginine 3 Facilitating Transcriptional Activation by Nuclear Hormone Receptor

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Mice with Truncated MeCP2 Recapitulate Many Rett Syndrome Features and Display Hyperacetylation of Histone H3

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LSD1 Is a Subunit of the NuRD Complex and Targets the Metastasis Programs in Breast Cancer

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Replication-Dependent Marking of DNA by PCNA Facilitates CAF-1-Coupled Inheritance of Chromatin

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Neuronal MeCP2 Is Expressed at Near Histone-Octamer Levels and Globally Alters the Chromatin State

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Identification of a mammalian protein that binds specifically to DNA containing methylated CpGs

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DNA Demethylation in Zebrafish Involves the Coupling of a Deaminase, a Glycosylase, and Gadd45

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The thymine glycosylase MBD4 can bind to the product of deamination at methylated CpG sites

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Dissection of the methyl-CpG binding domain from the chromosomal protein MeCP2

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Enhancer decommissioning by LSD1 during embryonic stem cell differentiation

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Human SWI/SNF-Associated PRMT5 Methylates Histone H3 Arginine 8 and Negatively Regulates Expression of ST7 and NM23 Tumor Suppressor Genes

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Loss of silent-chromatin looping and impaired imprinting of DLX5 in Rett syndrome

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Three-dimensional genome architecture: players and mechanisms

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Disruption of DNA-methylation-dependent long gene repression in Rett syndrome

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Intragenic DNA methylation modulates alternative splicing by recruiting MeCP2 to promote exon recognition

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Insight into Rett syndrome: MeCP2 levels display tissue- and cell-specific differences and correlate with neuronal maturation

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PRMT5-mediated methylation of histone H4R3 recruits DNMT3A, coupling histone and DNA methylation in gene silencing

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The p120 catenin partner Kaiso is a DNA methylation-dependent transcriptional repressor

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Closely related proteins MBD2 and MBD3 play distinctive but interacting roles in mouse developmentPreprint

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Deterministic direct reprogramming of somatic cells to pluripotency

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Characterization of MeCP2, a vertebrate DNA binding protein with affinity for methylated DNA

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Histone arginine methylation

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Recognition and potential mechanisms for replication and erasure of cytosine hydroxymethylation

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DNA methylation and methyl-CpG binding proteins: developmental requirements and function

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Mbd3/NURD Complex Regulates Expression of 5-Hydroxymethylcytosine Marked Genes in Embryonic Stem Cells

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De Novo Mutations in Moderate or Severe Intellectual Disability

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Corepressor-Dependent Silencing of Chromosomal Regions Encoding Neuronal Genes

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Rett syndrome mutations abolish the interaction of MeCP2 with the NCoR/SMRT co-repressor

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Tissue type is a major modifier of the 5-hydroxymethylcytosine content of human genesPreprint

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Locally Disordered Methylation Forms the Basis of Intratumor Methylome Variation in Chronic Lymphocytic Leukemia

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Mice lacking methyl-CpG binding protein 1 have deficits in adult neurogenesis and hippocampal function

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The NuRD component Mbd3 is required for pluripotency of embryonic stem cells

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Methylation-Dependent and -Independent Genomic Targeting Principles of the MBD Protein Family

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A Family of Human Zinc Finger Proteins That Bind Methylated DNA and Repress Transcription

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Nucleosome Remodeling and Epigenetics

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Reduced meCP2 expression is frequent in autism frontal cortex and correlates with aberrant MECP2 promoter methylation

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MBD2/NuRD and MBD3/NuRD, Two Distinct Complexes with Different Biochemical and Functional Properties

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Methyl-CpG-binding Protein, MeCP2, Is a Target Molecule for Maintenance DNA Methyltransferase, Dnmt1

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Intergenic Transcripts Regulate the Epigenetic State of rRNA Genes

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Landscape of somatic single-nucleotide and copy-number mutations in uterine serous carcinoma

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ICBP90, an E2F-1 target, recruits HDAC1 and binds to methyl-CpG through its SRA domain

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Solution Structure of the Methyl-CpG Binding Domain of Human MBD1 in Complex with Methylated DNA

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NoRC—a novel member of mammalian ISWI‐containing chromatin remodeling machines

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Chromatin Compaction by Human MeCP2

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Brahma links the SWI/SNF chromatin-remodeling complex with MeCP2-dependent transcriptional silencing

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Autism and other neuropsychiatric symptoms are prevalent in individuals with MeCP2 duplication syndrome

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Methyl-CpG Binding Domain 1 (MBD1) Interacts with the Suv39h1-HP1 Heterochromatic Complex for DNA Methylation-based Transcriptional Repression

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Active Repression of Methylated Genes by the Chromosomal Protein MBD1

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Molecular genetics of Rett syndrome: when DNA methylation goes unrecognized

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Molecular Coupling of DNA Methylation and Histone Methylation

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MED1, a novel human methyl-CpG-binding endonuclease, interacts with DNA mismatch repair protein MLH1

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Expression of mRNA for DNA methyltransferases and methyl-CpG–binding proteins and DNA methylation status on CpG islands and pericentromeric satellite regions during human hepatocarcinogenesis

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Interaction between chromatin proteins MECP2 and ATRX is disrupted by mutations that cause inherited mental retardation

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NuRD‐mediated deacetylation of H3K27 facilitates recruitment of Polycomb Repressive Complex 2 to direct gene repression

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Assessment of 2q23.1 microdeletion syndrome implicates MBD5 as a single causal locus of intellectual disability, epilepsy, and autism spectrum disorder

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The HP1α–CAF1–SetDB1‐containing complex provides H3K9me1 for Suv39‐mediated K9me3 in pericentric heterochromatin

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Transcriptional Gene Silencing Promotes DNA Hypermethylation through a Sequential Change in Chromatin Modifications in Cancer Cells

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The affinity of different MBD proteins for a specific methylated locus depends on their intrinsic binding properties

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NuRD suppresses pluripotency gene expression to promote transcriptional heterogeneity and lineage commitment

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Identification of MeCP2 mutations in a series of females with autistic disorder

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A Novel Family of Bromodomain Genes

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Transcriptional Repression and Heterochromatin Formation by MBD1 and MCAF/AM Family Proteins

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c-Jun N-terminal phosphorylation antagonises recruitment of the Mbd3/NuRD repressor complex

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The NuRD complex cooperates with DNMTs to maintain silencing of key colorectal tumor suppressor genes

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Frequent alteration of DNA damage signalling and repair pathways in human colorectal cancers with microsatellite instability

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The Minimal Repression Domain of MBD2b Overlaps with the Methyl-CpG-binding Domain and Binds Directly to Sin3A

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MBD3 Localizes at Promoters, Gene Bodies and Enhancers of Active Genes

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The Human Proteins MBD5 and MBD6 Associate with Heterochromatin but They Do Not Bind Methylated DNA

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Alternative Splicing of MBD2 Supports Self-Renewal in Human Pluripotent Stem Cells

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The Thymine DNA Glycosylase MBD4 Represses Transcription and Is Associated with Methylated p16 INK4a and hMLH1 Genes

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The MBD protein family—Reading an epigenetic mark?

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MCAF Mediates MBD1-Dependent Transcriptional Repression

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Excision of thymine and 5-hydroxymethyluracil by the MBD4 DNA glycosylase domain: structural basis and implications for active DNA demethylation

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MBD5 and MBD6 interact with the human PR‐DUB complex through their methyl‐CpG‐binding domain

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Two Highly Related p66 Proteins Comprise a New Family of Potent Transcriptional Repressors Interacting with MBD2 and MBD3

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Involvement of SUMO Modification in MBD1- and MCAF1-mediated Heterochromatin Formation

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An intrinsically disordered region of methyl-CpG binding domain protein 2 (MBD2) recruits the histone deacetylase core of the NuRD complex

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Methyl-CpG-binding domain protein-2 mediates transcriptional repression associated with hypermethylated GSTP1 CpG islands in MCF-7 breast cancer cells.

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The Mbd1-Atf7ip-Setdb1 pathway contributes to the maintenance of X chromosome inactivation

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The Expanding Role of <scp>MBD</scp> Genes in Autism: Identification of a <i><scp>MECP2</scp></i> Duplication and Novel Alterations in <i><scp>MBD5</scp></i>, <i><scp>MBD6</scp></i>, and <i><scp>SETDB1</scp></i>

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Reciprocal deletion and duplication at 2q23.1 indicates a role for MBD5 in autism spectrum disorder

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Haploinsufficiency of MBD5 associated with a syndrome involving microcephaly, intellectual disabilities, severe speech impairment, and seizures

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Transcript overexpression of theMBD2andMBD4genes in CD4+ T cells from systemic lupus erythematosus patients

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CLLD8/KMT1F Is a Lysine Methyltransferase That Is Important for Chromosome Segregation

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Overexpression of MBD2 in Glioblastoma Maintains Epigenetic Silencing and Inhibits the Antiangiogenic Function of the Tumor Suppressor Gene BAI1

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TACC3 mediates the association of MBD2 with histone acetyltransferases and relieves transcriptional repression of methylated promoters

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Characterization of Dnmt3b:Thymine-DNA Glycosylase Interaction and Stimulation of Thymine Glycosylase-Mediated Repair by DNA Methyltransferase(s) and RNA

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Novel variants identified in methyl-CpG-binding domain genes in autistic individuals

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Control of the DNA Methylation System Component MBD2 by Protein Arginine Methylation

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p66 and p66 of the Mi-2/NuRD complex mediate MBD2 and histone interaction

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Analysis of neonatal brain lacking ATRX or MeCP2 reveals changes in nucleosome density, CTCF binding and chromatin looping

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MeCP2 is required for global heterochromatic and nucleolar changes during activity-dependent neuronal maturation

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MeCP2 and MBD2 expression in human neoplastic and non-neoplastic breast tissue and its association with oestrogen receptor status

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Disruption of MBD5 contributes to a spectrum of psychopathology and neurodevelopmental abnormalities

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Probing the Dynamic Distribution of Bound States for Methylcytosine-binding Domains on DNA

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Methyl‐CpG‐binding protein 2 polymorphisms and vulnerability to autism

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Antithetic Effects of MBD2a on Gene Regulation

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MBD2 and Multiple Domains of CHD4 Are Required for Transcriptional Repression by Mi-2/NuRD Complexes

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Involvement of a Novel Zinc Finger Protein, MIZF, in Transcriptional Repression by Interacting with a Methyl-CpG-binding Protein, MBD2

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MBD4 cooperates with DNMT1 to mediate methyl-DNA repression and protects mammalian cells from oxidative stress

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Up-Regulation of MBD1 Promotes Pancreatic Cancer Cell Epithelial-Mesenchymal Transition and Invasion by Epigenetic Down-Regulation of E-Cadherin

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Genome-wide profiling of DNA methylation in human cancer cells

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Methyl-CpG–DNA binding proteins in human prostate cancer: expression of CXXC sequence containing MBD1 and repression of MBD2 and MeCP2

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Frameshift mutations in the MBD4/MED1 gene in primary gastric cancer with high-frequency microsatellite instability

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Targeted manipulation of heterochromatin rescues MeCP2 Rett mutants and re-establishes higher order chromatin organization

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The proto-oncoprotein FBI-1 interacts with MBD3 to recruit the Mi-2/NuRD-HDAC complex and BCoR and to silence p21WAF/CDKN1A by DNA methylation

Choi, W., Jeon, B.-N., Yoon, J.-H., Koh, D.-I., Kim, M.-H., Yu, M.-Y., Lee, K., Kim, Y., Kim, K., Hur, S. S., et al. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt359 · Cited by 51 · see citing works

Unusual Characteristics of the DNA Binding Domain of Epigenetic Regulatory Protein MeCP2 Determine Its Binding Specificity

Khrapunov, S. N., Warren, C. L., Cheng, H., Berko, E. R., Greally, J. M., & Brenowitz, M. D. (2014) · Biochemistry · doi:10.1021/bi500424z · Cited by 51 · see citing works

Genome-Wide Binding of MBD2 Reveals Strong Preference for Highly Methylated Loci

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The RON Receptor Tyrosine Kinase Promotes Metastasis by Triggering MBD4-Dependent DNA Methylation Reprogramming

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MeCP2 Is an Epigenetic Factor That Links DNA Methylation with Brain Metabolism

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Chromatin Remodelers in the 3D Nuclear Compartment

Magaña‐Acosta, M., & Valadéz-Graham, V. (2020) · Frontiers in Genetics · doi:10.3389/fgene.2020.600615 · Cited by 52 · see citing works

Hoxa5 undergoes dynamic DNA methylation and transcriptional repression in the adipose tissue of mice exposed to high-fat diet

Parrillo, L., Costa, V., Raciti, G. A., Longo, M., Spinelli, R., Esposito, R., Nigro, C., Vastolo, V., Desiderio, A., Zatterale, F., et al. (2016) · International Journal of Obesity · doi:10.1038/ijo.2016.36 · Cited by 52 · see citing works

FOXK2 Transcription Factor and Its Emerging Roles in Cancer

de Moraes, G. N., Carneiro, L. D. T., Maia, R. C., Lam, E. W. ‐., & Sharrocks, A. D. (2019) · Cancers · doi:10.3390/cancers11030393 · Cited by 52 · see citing works

Epigenetic alterations in the gastrointestinal tract: Current and emerging use for biomarkers of cancer

Grady, W. M. (2021) · Advances in cancer research · doi:10.1016/bs.acr.2021.02.006 · Cited by 52 · see citing works

Oxysterols are potential physiological regulators of ageing

de Médina, P., Silvente‐Poirot, S., & Poirot, M. (2022) · Ageing Research Reviews · doi:10.1016/j.arr.2022.101615 · Cited by 51 · see citing works

Unraveling the epigenetic landscape of pulmonary arterial hypertension: implications for personalized medicine development

Dave, J. K., Jagana, V., Janoštiak, R., & Bisserier, M. (2023) · Journal of Translational Medicine · doi:10.1186/s12967-023-04339-5 · Cited by 50 · see citing works

DNA methylation in pulmonary fibrosis and lung cancer

Duan, J., Zhong, B., Fan, Z., Zhang, H., Xu, M., Zhang, X., & Sanders, Y. Y. (2022) · Expert Review of Respiratory Medicine · doi:10.1080/17476348.2022.2085091 · Cited by 49 · see citing works

Structural Basis of MeCP2 Distribution on Non-CpG Methylated and Hydroxymethylated DNA

Sperlazza, M. J., Bilinovich, S. M., Sinanan, L. M., Javier, F. R., & Williams, D. C. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.04.009 · Cited by 49 · see citing works

Protein Interactions at Oxidized 5-Methylcytosine Bases

Pfeifer, G. P., Szabó, P. E., & Song, J. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.07.039 · Cited by 49 · see citing works

Mapping the micro-proteome of the nuclear lamina and lamina-associated domains

Cutler, J. A., Wong, X., Hoskins, V. E., Gordon, M. R., Madugundu, A. K., Pandey, A., & Reddy, K. L. (2021) · Life Science Alliance · doi:10.26508/lsa.202000774 · Cited by 49 · see citing works

The Role of Oxidative Stress in Epigenetic Changes Underlying Autoimmunity

Zheng, X., & Sawalha, A. H. (2021) · Antioxidants and Redox Signaling · doi:10.1089/ars.2021.0066 · Cited by 47 · see citing works

Metabolic Regulation of Epigenetic Modifications and Cell Differentiation in Cancer

Saggese, P., Sellitto, A., Martinez, C. A., Giurato, G., Nassa, G., Rizzo, F. M., Tarallo, R., & Scafoglio, C. (2020) · Cancers · doi:10.3390/cancers12123788 · Cited by 46 · see citing works

Analysis of protein-DNA interactions in chromatin by UV induced cross-linking and mass spectrometry

Stützer, A., Welp, L. M., Raabe, M., Sachsenberg, T. T., Kappert, C., Wulf, A., Lau, A. M., David, S.-S., Chernev, A., Kramer, K., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-19047-7 · Cited by 45 · see citing works

Drug addiction and treatment: An epigenetic perspective

Koijam, A. S., Singh, K. D., Singh, N. B., Haobam, R., & Rajashekar, Y. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115951 · Cited by 43 · see citing works

Environmental Adaptation of Genetically Uniform Organisms with the Help of Epigenetic Mechanisms—An Insightful Perspective on Ecoepigenetics

Vogt, G. (2022) · Epigenomes · doi:10.3390/epigenomes7010001 · Cited by 42 · see citing works

The Methylation Status of the Epigenome: Its Emerging Role in the Regulation of Tumor Angiogenesis and Tumor Growth, and Potential for Drug Targeting

Pirola, L., Ciesielski, O., & Balcerczyk, A. (2018) · Cancers · doi:10.3390/cancers10080268 · Cited by 42 · see citing works

MBD2 acts as a repressor to maintain the homeostasis of the Th1 program in type 1 diabetes by regulating the STAT1-IFN-γ axis

Yue, T., Sun, F., Wang, F., Yang, C., Luo, J., Rong, S.-J., Zhou, H., Xiao, J., Wang, X., Zhou, Q., et al. (2021) · Cell Death and Differentiation · doi:10.1038/s41418-021-00852-6 · Cited by 42 · see citing works

A Tox21 Approach to Altered Epigenetic Landscapes: Assessing Epigenetic Toxicity Pathways Leading to Altered Gene Expression and Oncogenic Transformation In Vitro

Parfett, C. L. J., & Desaulniers, D. M. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18061179 · Cited by 41 · 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

Recent advances on gene-related DNA methylation in cancer diagnosis, prognosis, and treatment: a clinical perspective

Lavoro, A., Ricci, D., Gattuso, G., Longo, F., Spoto, G., Vitale, A. C. V., Giuliana, M. C., Falzone, L., Libra, M., & Candido, S. (2025) · Clinical Epigenetics · doi:10.1186/s13148-025-01884-2 · Cited by 39 · see citing works

Single-cell epigenetics – Chromatin modification atlas unveiled by mass cytometry

Cheung, P., Vallania, F., Dvorak, M., Chang, S. E., Schaffert, S. A., Donato, M., Rao, A., Mao, R., Utz, P. J., Khatri, P., et al. (2018) · Clinical Immunology · doi:10.1016/j.clim.2018.06.009 · Cited by 39 · see citing works

The Role of DNA Methylation in Gene Regulation

Bommarito, P. A., & Fry, R. C. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-812433-8.00005-8 · Cited by 39 · see citing works

DNA methylation: a cause and consequence of type 2 diabetes

Kim, M. (2019) · Genomics & Informatics · doi:10.5808/gi.2019.17.4.e38 · Cited by 39 · see citing works

Role of epigenetics and miRNAs in orofacial clefts

Garland, M. A., Sun, B. H., Zhang, S., Reynolds, K., Ji, Y., & Zhou, C. J. (2020) · Birth Defects Research · doi:10.1002/bdr2.1802 · Cited by 39 · see citing works

Epigenetic mechanisms and potential therapeutic targets in stroke

Morris-Blanco, K. C., Chokkalla, A. K., Arruri, V. K., Jeong, S., Probelsky, S. M., & Vemuganti, R. (2022) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x221116192 · Cited by 38 · see citing works

Antioxidative, Anti-Inflammatory, Anti-Obesogenic, and Antidiabetic Properties of Tea Polyphenols—The Positive Impact of Regular Tea Consumption as an Element of Prophylaxis and Pharmacotherapy Support in Endometrial Cancer

Olcha, P., Winiarska‐Mieczan, A., Kwiecień, M., Nowakowski, Ł., Miturski, A., Semczuk, A., Kiczorowska, B., & Gałczyński, K. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23126703 · Cited by 38 · see citing works

Capture of a functionally active methyl-CpG binding domain by an arthropod retrotransposon familyPreprint

de Mendoza, A., Pflueger, J., & Lister, R. (2019) · Genome Research · doi:10.1101/gr.243774.118 · Cited by 38 · see citing works

Epigenetics in the primary biliary cholangitis and primary sclerosing cholangitis

Cheung, A., LaRusso, N., Gores, G., & Lazaridis, K. (2017) · Seminars in Liver Disease · doi:10.1055/s-0037-1603324 · Cited by 37 · see citing works

Epigenetic Factors that Control Pericentric Heterochromatin Organization in Mammals

Fioriniello, S., Marano, D., Fiorillo, F., D’Esposito, M., & Ragione, F. D. (2020) · Genes · doi:10.3390/genes11060595 · Cited by 37 · see citing works

Targeting epigenetics: A novel promise for Alzheimer’s disease treatment

Jeremic, D., Jiménez‐Díaz, L., & Navarro‐López, J. D. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.102003 · Cited by 36 · see citing works

Tagging Methyl-CpG-Binding Domain Proteins Reveals Different Spatiotemporal Expression and Supports Distinct Functions

Wood, K. H., Johnson, B. S., Welsh, S. A., Lee, J. Y., Cui, Y., Krizman, E. N., Brodkin, E. S., Blendy, J. A., Robinson, M. B., Bartolomei, M. S., et al. (2016) · Epigenomics · doi:10.2217/epi-2015-0004 · Cited by 35 · see citing works

Are there specific readers of oxidized 5‐methylcytosine bases?

Song, J., & Pfeifer, G. P. (2016) · BioEssays · doi:10.1002/bies.201600126 · Cited by 35 · see citing works

MeCP2-mediated epigenetic regulation in senescent endothelial progenitor cells

Wang, C., Wang, F., Li, Z., Cao, Q., Huang, L., & Chen, S. (2018) · Stem Cell Research & Therapy · doi:10.1186/s13287-018-0828-y · Cited by 35 · see citing works

Methyl‐CpG‐Binding Protein (MBD) Family: Epigenomic Read‐Outs Functions and Roles in Tumorigenesis and Psychiatric Diseases

Gigek, C. O., Chen, E., & Smith, M. D. A. C. (2015) · Journal of Cellular Biochemistry · doi:10.1002/jcb.25281 · Cited by 36 · see citing works

Methylation-Dependent and -Independent Genomic Targeting Principles of the MBD Protein Family

Baubec, T., Ivánek, R., Lienert, F., & Schübeler, D. (2013) · Cell · doi:10.1016/j.cell.2013.03.011 · Cited by 365 · see citing works

Proteins that bind methylated DNA and human cancer: reading the wrong words

Lopez‐Serra, L., & Esteller, M. (2008) · British Journal of Cancer · doi:10.1038/sj.bjc.6604374 · Cited by 181 · see citing works

Reviewed by:

Menafra, R., Stunnenberg, H. G., Murgatroyd, C. A., & Stunnenberg, H. G. (2014)

MBD2 and MBD3: elusive functions and mechanisms

Menafra, R., & Stunnenberg, H. G. (2014) · Frontiers in Genetics · doi:10.3389/fgene.2014.00428 · Cited by 66 · see citing works