The SRA domain of UHRF1 flips 5-methylcytosine out of the DNA helix - Wikidata - awgldk - TriplyDB

The SRA domain of UHRF1 flips 5-methylcytosine out of the DNA helix

The SRA domain of UHRF1 flips 5-methylcytosine out of the DNA helix

http://www.wikidata.org/entity/Q27651993

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The epigenetic regulator UHRF1 promotes ubiquitination-mediated degradation of the tumor-suppressor protein promyelocytic leukemia protein Np95 interacts with de novo DNA methyltransferases, Dnmt3a and Dnmt3b, and mediates epigenetic silencing of the viral CMV promoter in embryonic stem cells The replication focus targeting sequence (RFTS) domain is a DNA-competitive inhibitor of Dnmt1 Establishing, maintaining and modifying DNA methylation patterns in plants and animals Modifiers and Readers of DNA Modifications and Their Impact on Genome Structure, Expression, and Stability in Disease Cellular response to DNA interstrand crosslinks: the Fanconi anemia pathway Functions of TET Proteins in Hematopoietic Transformation DNA methylation pathways and their crosstalk with histone methylation NIRF/UHRF2 occupies a central position in the cell cycle network and allows coupling with the epigenetic landscape Unlocking epigenetic codes in neurogenesis UHRF1, a modular multi-domain protein, regulates replication-coupled crosstalk between DNA methylation and histone modifications A dual flip-out mechanism for 5mC recognition by the Arabidopsis SUVH5 SRA domain and its impact on DNA methylation and H3K9 dimethylation in vivo The structural basis for selective binding of non-methylated CpG islands by the CFP1 CXXC domain Recognition of modification status on a histone H3 tail by linked histone reader modules of the epigenetic regulator UHRF1 Structure and cleavage activity of the tetrameric MspJI DNA modification-dependent restriction endonuclease Molecular basis for recognition of methylated and specific DNA sequences by the zinc finger protein Kaiso An atomic model of Zfp57 recognition of CpG methylation within a specific DNA sequence The PHD Finger of Human UHRF1 Reveals a New Subgroup of Unmethylated Histone H3 Tail Readers The recognition domain of the methyl-specific endonuclease McrBC flips out 5-methylcytosine SRA- and SET-domain-containing proteins link RNA polymerase V occupancy to DNA methylation Structure and mutagenesis of the DNA modification-dependent restriction endonuclease AspBHI Crystal structure of the 5hmC specific endonuclease PvuRts1I Structure of 5-hydroxymethylcytosine-specific restriction enzyme, AbaSI, in complex with DNA Structure of the N -glycosidase MilB in complex with hydroxymethyl CMP reveals its Arg23 specifically recognizes the substrate and controls its entry Mechanism of DNA Methylation-Directed Histone Methylation by KRYPTONITE Structural basis of CpG and inhibitory DNA recognition by Toll-like receptor 9 Signalling pathways in UHRF1-dependent regulation of tumor suppressor genes in cancer DNA methylation, its mediators and genome integrity Conserved linker regions and their regulation determine multiple chromatin-binding modes of UHRF1 Disruption of Dnmt1/PCNA/UHRF1 interactions promotes tumorigenesis from human and mice glial cells Cooperative DNA and histone binding by Uhrf2 links the two major repressive epigenetic pathways Chemical display of pyrimidine bases flipped out by modification-dependent restriction endonucleases of MspJI and PvuRts1I families Prostate cancer epigenetics and its clinical implications Hemi-methylated DNA regulates DNA methylation inheritance through allosteric activation of H3 ubiquitylation by UHRF1 On how mammalian transcription factors recognize methylated DNA.Recognition of 5-hydroxymethylcytosine by the Uhrf1 SRA domain.A SILAC-based screen for Methyl-CpG binding proteins identifies RBP-J as a DNA methylation and sequence-specific binding protein Introduction--Epiphanies in epigenetics.Dissecting the precise role of H3K9 methylation in crosstalk with DNA maintenance methylation in mammals.Differential binding of Escherichia coli McrA protein to DNA sequences that contain the dinucleotide m5CpG

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The SRA domain of UHRF1 flips 5-methylcytosine out of the DNA helix

http://www.wikidata.org/entity/Q27651993

description

2008 nî lūn-bûn

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2008 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

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2008 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

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2008年論文

@zh-tw

2008年论文

@wuu

name

The SRA domain of UHRF1 flips 5-methylcytosine out of the DNA helix

@ast

The SRA domain of UHRF1 flips 5-methylcytosine out of the DNA helix

@en

The SRA domain of UHRF1 flips 5-methylcytosine out of the DNA helix

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type

label

The SRA domain of UHRF1 flips 5-methylcytosine out of the DNA helix

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The SRA domain of UHRF1 flips 5-methylcytosine out of the DNA helix

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The SRA domain of UHRF1 flips 5-methylcytosine out of the DNA helix

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prefLabel

The SRA domain of UHRF1 flips 5-methylcytosine out of the DNA helix

@ast

The SRA domain of UHRF1 flips 5-methylcytosine out of the DNA helix

@en

The SRA domain of UHRF1 flips 5-methylcytosine out of the DNA helix

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The SRA domain of UHRF1 flips 5-methylcytosine out of the DNA helix

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Magnolia Bostick

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Steven E Jacobsen

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Xiaodong Cheng

http://www.w3.org/2001/XMLSchema#string

Xing Zhang

http://www.w3.org/2001/XMLSchema#string

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EUKARYOTIC CYTOSINE METHYLTRANSFERASES

Solution structure of the methyl-CpG binding domain of human MBD1 in complex with methylated DNA

The interaction of the SRA domain of ICBP90 with a novel domain of DNMT1 is involved in the regulation of VEGF gene expression

Crystal structures of DNA/RNA repair enzymes AlkB and ABH2 bound to dsDNA

UHRF1 plays a role in maintaining DNA methylation in mammalian cells

ICBP90 belongs to a new family of proteins with an expression that is deregulated in cancer cells

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Stressing-out DNA? The contribution of serine-phosphodiester interactions in catalysis by uracil DNA glycosylase

Structure of the bacteriophage T4 DNA adenine methyltransferase

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826-829

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644659

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10.1038/NATURE07280

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7214

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455

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Hideharu Hashimoto

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2008-09-03T00:00:00Z

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23238974

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1004378663

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18772888

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2602803

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