(Q28145111)

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

scientific article (publication date: 16 September 1999)

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

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B Hendrich

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Adrian Peter Bird

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A Bird

5

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U Hardeland

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H H Ng

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J Jiricny

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publication date

16 September 1999

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401

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6750

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301-4

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Mutagenic deamination of cytosine residues in DNA

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The expected equilibrium of the CpG dinucleotide in vertebrate genomes under a mutation model

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DNA methylation and the frequency of CpG in animal DNA.

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The CpG dinucleotide and human genetic disease

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Methylation, mutation and cancer

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An N -Glycosidase from Escherichia coli That Releases Free Uracil from DNA Containing Deaminated Cytosine Residues

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DNA excision repair pathways

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In vitro correction of G.T mispairs to G.C pairs in nuclear extracts from human cells

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Cloning and expression of human G/T mismatch-specific thymine-DNA glycosylase

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

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Identification and characterization of a family of mammalian methyl-CpG binding proteins

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MeCP2 is a transcriptional repressor with abundant binding sites in genomic chromatin

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Specific binding of a designed pyrrolidine abasic site analog to multiple DNA glycosylases

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Base analog and neighboring base effects on substrate specificity of recombinant human G:T mismatch-specific thymine DNA-glycosylase.

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

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Mismatch repair in replication fidelity, genetic recombination, and cancer biology

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