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Structure, ISSN 0969-2126, 01/2018, Volume 26, Issue 1, pp. 85 - 95.e3
The CXXC domain, first identified as the reader of unmodified CpG dinucleotide, plays important roles in epigenetic regulation by targeting various activities... 
histone methylation | DNMT1 | KDM2A | DNA methylation | TET1 | CFP1 | CpG island | MLL | CXXC domain | epigenetics | HOMEODOMAIN | METHYLATION | METHYLTRANSFERASE | CHROMATIN-STRUCTURE | 5-METHYLCYTOSINE | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRANSCRIPTION | BINDING DOMAIN | CELL BIOLOGY | BIOPHYSICS | GENES | DIOXYGENASE | CPG ISLANDS | Epigenesis, Genetic | Humans | Crystallography, X-Ray | Mixed Function Oxygenases - metabolism | Mixed Function Oxygenases - chemistry | Proto-Oncogene Proteins - chemistry | Neoplasm Proteins - metabolism | DNA-Binding Proteins - metabolism | Protein Isoforms - metabolism | Protein Isoforms - chemistry | Cloning, Molecular | Escherichia coli - metabolism | Jumonji Domain-Containing Histone Demethylases - chemistry | Protein Interaction Domains and Motifs | Neoplasm Proteins - genetics | Binding Sites | Proto-Oncogene Proteins - metabolism | Recombinant Proteins - metabolism | Amino Acid Sequence | Protein Conformation, alpha-Helical | Gene Expression | Genetic Vectors - chemistry | F-Box Proteins - metabolism | F-Box Proteins - chemistry | Genetic Vectors - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Neoplasm Proteins - chemistry | Proto-Oncogene Proteins - genetics | Recombinant Proteins - genetics | DNA - metabolism | DNA-Binding Proteins - genetics | DNA-Binding Proteins - chemistry | Jumonji Domain-Containing Histone Demethylases - genetics | DNA - genetics | Sequence Homology, Amino Acid | DNA - chemistry | Sequence Alignment | Protein Conformation, beta-Strand | Escherichia coli - genetics | CpG Islands | Protein Binding | Mixed Function Oxygenases - genetics | F-Box Proteins - genetics | Jumonji Domain-Containing Histone Demethylases - metabolism | Protein Isoforms - genetics | Epigenetic inheritance | Chromatin | Methyltransferases | DNA | Crystals | Physiological aspects | Genetic research | Nucleotide sequencing | Methylation | Structure | Protein binding | DNA sequencing
Journal Article
International Journal of Molecular Sciences, ISSN 1661-6596, 09/2017, Volume 18, Issue 9, p. 1898
Journal Article
Biochemical Society Symposium, ISSN 0067-8694, 06/2013, Volume 41, Issue 3, pp. 727 - 740
Vertebrate DNA can be chemically modified by methylation of the 5 position of the cytosine base in the context of CpG dinucleotides. This modification creates... 
DNA methylation | Epigenetics | DNA demethylation | Chromatin | Transcription | CpG island | transcription | BIOCHEMISTRY & MOLECULAR BIOLOGY | BINDING-PROTEIN | TRANSCRIPTIONAL REPRESSION | chromatin | H3-LYS METHYLTRANSFERASE COMPLEX | epigenetics | FINGER PROTEIN-1 | EMBRYONIC STEM-CELLS | MIXED-LINEAGE-LEUKEMIA | GENOME-WIDE ANALYSIS | POSTNATAL-DEVELOPMENT | HISTONE H3 ACETYLATION | Amino Acid Sequence | Chromatin - metabolism | DNA-Binding Proteins - physiology | Humans | Models, Molecular | Molecular Sequence Data | DNA Methylation - genetics | Protein Structure, Tertiary - genetics | DNA - metabolism | CpG Islands - physiology | DNA-Binding Proteins - genetics | DNA-Binding Proteins - chemistry | CpG Islands - genetics | Zinc Fingers - genetics | DNA Methylation - physiology | Protein Binding - physiology | MBD, methyl-CpG-binding domain | PRC, polycomb group repressive complex | IDAX, inhibition of the Dvl and axin complex protein | ESC, embryonic stem cell | RING, really interesting new gene | CFP1, CxxC finger protein 1 | JmjC, Jumonji C | PHD, plant homeodomain | Biochemical Society Annual Symposium No. 80 | 5mC, 5-methylcytosine | CGBP, CpG-binding protein | 5hmC, 5-hydroxymethylcytosine | DNMT1, DNA methyltransferase 1 | FBXL19, F-box and leucine-rich repeat protein 19 | RFTS, replication foci-targeting sequence | WDR, WD40 repeat | DPY-30, dosage compensation protein 30 | AF9, ALL1–fused gene from chromosome 9 protein | ChIP-seq, chromatin immunoprecipitation sequencing | HDAC, histone deacetylase | YY1, Yin and Yang 1 | RbBP5, retinoblastoma-binding protein 5 | ZF-CxxC, zinc finger-CxxC | BAH, bromo-adjacent homology | ASH2L, absent, small or homeotic 2-like | SETD1, SET domain 1 | TET, ten-eleven translocation | SEC, super-elongation complex | MLL, mixed lineage leukaemia protein | CGI, CpG island | ENL, eleven-nineteen leukaemia | shRNA, short hairpin RNA | KDM, lysine demethylase | RNAPII, RNA polymerase II
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2018, Volume 293, Issue 10, pp. 3663 - 3674
The pluripotency-controlling stem-cell protein SRY-box 2 (SOX2) plays a pivotal role in maintaining the self-renewal and pluripotency of embryonic stem cells... 
CANCER-CELLS | 20-LIKE 1 PHF20L1 | REGULATES PLURIPOTENCY | LYSINE METHYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | PHOSPHORYLATION SWITCH | GENOMIC ANALYSIS | DNMT1 STABILITY | DIFFERENTIATION | HISTONE METHYLATION | EXPRESSION | Embryonic Stem Cells - metabolism | Embryonic Stem Cells - cytology | Histone Demethylases - antagonists & inhibitors | Humans | Ovarian Neoplasms - pathology | Neoplasm Proteins - antagonists & inhibitors | Neoplasm Proteins - metabolism | Histone Demethylases - genetics | Recombinant Fusion Proteins - metabolism | SOXB1 Transcription Factors - metabolism | Chromosomal Proteins, Non-Histone - antagonists & inhibitors | Histone-Lysine N-Methyltransferase - antagonists & inhibitors | RNA Interference | SOXB1 Transcription Factors - genetics | Proteolysis | HEK293 Cells | SOXB1 Transcription Factors - chemistry | Female | Ovarian Neoplasms - metabolism | Protein Stability | Neoplasm Proteins - genetics | Histone-Lysine N-Methyltransferase - genetics | Teratocarcinoma - metabolism | Chromosomal Proteins, Non-Histone - metabolism | Histone Demethylases - chemistry | Mice, Inbred C57BL | Cells, Cultured | Neoplasm Proteins - chemistry | Recombinant Fusion Proteins - chemistry | Teratocarcinoma - pathology | Ovarian Neoplasms - enzymology | Chromosomal Proteins, Non-Histone - genetics | Histone-Lysine N-Methyltransferase - chemistry | Histone Demethylases - metabolism | Animals | Histone-Lysine N-Methyltransferase - metabolism | Teratocarcinoma - enzymology | Cell Line, Tumor | Protein Processing, Post-Translational | Mutation | Methylation | Chromosomal Proteins, Non-Histone - chemistry | Amino Acid Substitution | Index Medicus | post-translational modification (PTM) | PHF20L1 | SOX2 | stem cells | SET7 | LSD1 | ubiquitin-dependent protease | cancer stem cells | pluripotency | Cell Biology
Journal Article
PLoS ONE, ISSN 1932-6203, 2011, Volume 6, Issue 2, p. e16627
Several mammalian proteins involved in chromatin and DNA modification contain CXXC zinc finger domains. We compared the structure and function of the CXXC... 
MAINTENANCE | METHYLATION | DNA CYTOSINE-5 METHYLTRANSFERASE | PROTEIN | REPLICATION | MAMMALIAN DNA | GENE | MULTIDISCIPLINARY SCIENCES | CATALYTIC DOMAIN | ACUTE MYELOID-LEUKEMIA | MLL | DNA (Cytosine-5-)-Methyltransferases - physiology | Protein Binding - genetics | Humans | Molecular Sequence Data | Proto-Oncogene Proteins - chemistry | DNA (Cytosine-5-)-Methyltransferases - chemistry | DNA (Cytosine-5-)-Methyltransferases - metabolism | DNA-Binding Proteins - metabolism | Mixed Function Oxygenases | DNA Methylation - physiology | Proto-Oncogene Proteins - metabolism | DNA-Binding Proteins - physiology | Mutagenesis, Site-Directed | Sequence Deletion - physiology | DNA (Cytosine-5-)-Methyltransferase 1 | Cells, Cultured | Models, Molecular | Proto-Oncogene Proteins - genetics | Amino Acid Sequence - physiology | Protein Structure, Tertiary - genetics | DNA-Binding Proteins - genetics | DNA-Binding Proteins - chemistry | Sequence Homology, Amino Acid | DNA (Cytosine-5-)-Methyltransferases - genetics | Animals | Proto-Oncogene Proteins - physiology | CpG Islands - genetics | Zinc Fingers - genetics | Mice | Zinc Fingers - physiology | Enzyme Activation - genetics | Enzyme Activation - physiology | Protein Binding - physiology | Protein Structure, Tertiary - physiology | Pyrimidines | Methyltransferases | Analysis | DNA | DNA binding proteins | Methylation | Embryonic stem cells | DNA-ligand interactions | Chromatin | Genes | Embryo cells | Science | Homology | Genomes | Biology | Catalytic activity | Proteins | DNA methylation | Physiology | Cytosine | Zinc finger proteins | Catalysis | Coordination compounds | Deoxyribonucleic acid--DNA | CpG islands | Binding | Dioxygenase | Enzymes | Construction | Nucleotide sequence | DNMT1 protein | Mammals | Substrates | Zinc | Algorithms | Mutagenesis | Stem cells | Epigenetics | DNA methyltransferase | Mutation | Structure-function relationships | Deoxyribonucleic acid
Journal Article
Genes, Chromosomes and Cancer, ISSN 1045-2257, 11/2017, Volume 56, Issue 11, pp. 769 - 787
Journal Article
Molecular Oncology, ISSN 1574-7891, 02/2016, Volume 10, Issue 2, pp. 292 - 302
Tudor domain–containing proteins (TDRDs), which recognize and bind to methyl-lysine/arginine residues on histones and non-histone proteins, play critical roles... 
PHF20L1 | Copy number alteration | Breast cancer | Tudor domain | Methylation | READERS | LANDSCAPE | CELL-LINES | HISTONE METHYLATION | TUMORS | ONCOLOGY | LYSINE METHYLATION | GENES | ARGININE METHYLATION | EXPRESSION | DRIVER MUTATIONS | Protein Structure, Tertiary | RNA, Small Interfering - genetics | Cell Proliferation | Datasets as Topic | Prognosis | Chromosomal Proteins, Non-Histone - metabolism | DNA (Cytosine-5-)-Methyltransferase 1 | Genomics | Humans | Gene Expression Profiling | Chromosomal Proteins, Non-Histone - genetics | Gene Knockdown Techniques | DNA (Cytosine-5-)-Methyltransferases - metabolism | DNA Methylation | Breast Neoplasms - genetics | Gene Amplification | Cell Line, Tumor | Female | Histones - metabolism | Oncogenes | Chromatin | RNA | Genes | Plant genetics | DNA binding proteins | Genetic transcription | Methyltransferases | Analysis | Physiological aspects | Genetic research | Histones | Genetic aspects | Protein binding | Cancer | Cell proliferation | Transcription | Copy number | Taxonomy | Genomes | Datasets | Homeobox | Proteins | Consortia | Cell growth | Arginine | DNA methylation | Deoxyribonucleic acid--DNA | Medical research | Cell survival | Genomic analysis | DNMT1 protein | Tumor cell lines | Ribonucleic acid--RNA | Metabolism | Gene amplification | Womens health | Lysine | Cell lines | Epigenetics | DNA methyltransferase | Mutation | Tumors
Journal Article
PLoS ONE, ISSN 1932-6203, 2011, Volume 6, Issue 5, p. e19503
Epigenetic regulation of gene expression is well known mechanism that regulates cellular senescence of cancer cells. Here we show that inhibition of DNA... 
BREAST-CANCER | LUNG-CANCER | IN-VITRO | METHYLATION | GENE | MULTIDISCIPLINARY SCIENCES | PROSTATE-CANCER | HUMAN FIBROBLASTS | HUMAN CANCER-CELLS | DIFFERENTIATION | HISTONE DEACETYLASE | Immunohistochemistry | Cell Cycle - genetics | Humans | Multipotent Stem Cells - metabolism | Cellular Senescence - drug effects | DNA (Cytosine-5-)-Methyltransferases - antagonists & inhibitors | DNA (Cytosine-5-)-Methyltransferases - metabolism | DNA-Binding Proteins - metabolism | Flow Cytometry | Chromatin Immunoprecipitation | Nuclear Proteins - genetics | Repressor Proteins - metabolism | Proto-Oncogene Proteins - metabolism | Cellular Senescence - genetics | DNA (Cytosine-5-)-Methyltransferase 1 | Cells, Cultured | Enzyme Inhibitors - pharmacology | Repressor Proteins - genetics | Nuclear Proteins - metabolism | Proto-Oncogene Proteins - genetics | Transcription Factors - genetics | DNA-Binding Proteins - genetics | Reverse Transcriptase Polymerase Chain Reaction | Blotting, Western | Enhancer of Zeste Homolog 2 Protein | Transcription Factors - metabolism | Azacitidine - pharmacology | Polycomb Repressive Complex 2 | Polycomb Repressive Complex 1 | Multipotent Stem Cells - cytology | CpG Islands - genetics | Cell Proliferation - drug effects | MicroRNAs - genetics | Cell Cycle - drug effects | Proteins | Epigenetic inheritance | MicroRNA | Methyltransferases | Genes | DNA | Stem cells | Methylation | Gene expression | Azacytidine | Veterinary colleges | Senescence | INK4a protein | Kinases | Cord blood | DNA methylation | Aging | Inhibition | Active control | Deoxyribonucleic acid--DNA | CpG islands | p16 Protein | DNMT1 protein | MiRNA | Aging (artificial) | siRNA | Ribonucleic acid--RNA | Polycomb group proteins | Cyclin-dependent kinase inhibitor p21 | Lysine | Epigenetics | DNA methyltransferase | Umbilical cord | Histone H3 | Cancer | RNA | Deoxyribonucleic acid | Ribonucleic acid
Journal Article
Biochemical and Biophysical Research Communications, ISSN 0006-291X, 04/2013, Volume 433, Issue 4, pp. 415 - 419
-methylpurine DNA glycosylase (MPG), a DNA repair enzyme, functions in the DNA base excision repair (BER) pathway. Aberrant over-expression of MPG in various... 
UHRF2 | Protein interaction | MPG | UHRF1 | IP/MS | TARGET | METHYLATION | DNMT1 | BIOCHEMISTRY & MOLECULAR BIOLOGY | SENSITIVITY | LINKS | CELL-CYCLE ARREST | CANCER | BIOPHYSICS | BASE EXCISION-REPAIR | ALKYLATING-AGENTS | ICBP90 | Neoplasms - metabolism | RNA-Binding Proteins - genetics | Immunoprecipitation | CCAAT-Enhancer-Binding Proteins - isolation & purification | Nuclear Proteins - isolation & purification | Humans | Neoplasm Proteins - metabolism | RNA-Binding Proteins - isolation & purification | Tumor Suppressor Protein p53 - genetics | Cell Nucleus - metabolism | Transfection | MCF-7 Cells | HEK293 Cells | Membrane Proteins - metabolism | CCAAT-Enhancer-Binding Proteins - genetics | Neoplasm Proteins - genetics | Nuclear Proteins - genetics | DNA Glycosylases - metabolism | CCAAT-Enhancer-Binding Proteins - metabolism | Membrane Proteins - genetics | Electrophoresis, Polyacrylamide Gel | HCT116 Cells | DNA Glycosylases - genetics | Tumor Suppressor Protein p53 - metabolism | Ubiquitin-Protein Ligases - metabolism | Nuclear Proteins - metabolism | Thyroid Hormones - genetics | Protein Interaction Mapping | Carrier Proteins - genetics | Microscopy, Confocal | Carrier Proteins - metabolism | Cell Nucleus - genetics | Thyroid Hormones - metabolism | Serine-Arginine Splicing Factors | Protein Binding | HeLa Cells | Neoplasms - pathology | Ubiquitin-Protein Ligases - genetics | Mass Spectrometry - methods | RNA-Binding Proteins - metabolism | Tumor proteins | DNA
Journal Article
细胞研究:英文版, ISSN 1001-0602, 2010, Volume 20, Issue 11, pp. 1201 - 1215
Global DNA hypomethylation at CpG islands coupled with local hypermethylation is a hallmark for breast cancer, yet the mechanism underlying this change remains... 
乳腺上皮细胞 | 小鼠模型 | CpG岛 | DNA甲基化 | 表达调控 | 基因转录 | 机制转变 | BRCA1 | FULL-LENGTH ISOFORM | DNMT1 | histone modification | CHROMOSOME TERRITORIES | TUMOR-FORMATION | genomic imprinting | MAMMALIAN-CELLS | CELL BIOLOGY | BREAST-CANCER | DAMAGE REPAIR | NUCLEAR ARCHITECTURE | EMBRYONIC STEM-CELLS | DNA methylation | tumor formation | MICE | GENETIC INTERACTIONS | Genomic Imprinting | Proto-Oncogene Proteins p21(ras) - genetics | Humans | Transcriptional Activation | Gene Expression Regulation, Neoplastic | Breast Neoplasms - metabolism | DNA (Cytosine-5-)-Methyltransferases - metabolism | Breast Neoplasms - enzymology | DNA Methylation | BRCA1 Protein - metabolism | Female | Proto-Oncogene Proteins p21(ras) - metabolism | Promoter Regions, Genetic | DNA (Cytosine-5-)-Methyltransferase 1 | Proto-Oncogene Proteins c-fos - metabolism | BRCA1 Protein - physiology | Proto-Oncogene Proteins c-myc - metabolism | Mammary Glands, Animal - cytology | BRCA1 Protein - genetics | DNA (Cytosine-5-)-Methyltransferases - genetics | Animals | Mammary Glands, Animal - metabolism | Cell Line, Tumor | CpG Islands | Protein Binding | Proto-Oncogene Proteins c-fos - genetics | Mice | Proto-Oncogene Proteins c-myc - genetics | Histones - metabolism | Octamer Transcription Factor-1 - metabolism | Enzymes | Animal models | Chromatin | BRCA1 protein | Transcription | Epithelial cells | DNMT1 protein | c-Myc protein | Breast cancer | Promoters