MBD2 is a transcriptional repressor belonging to the MeCP1 histone deacetylase complex (Q28143627)

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scientific article (publication date: September 1999)

Language	Label	Description	Also known as
English	MBD2 is a transcriptional repressor belonging to the MeCP1 histone deacetylase complex	scientific article (publication date: September 1999)

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scholarly article

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

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Hediye Erdjument-Bromage

6

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H Erdjument-Bromage

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B Hendrich

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Adrian Peter Bird

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A Bird

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Y Zhang

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author name string

H H Ng

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C A Johnson

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B M Turner

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P Tempst

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D Reinberg

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language of work or name

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publication date

September 1999

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Nature Genetics

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23

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1

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58-61

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

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Purification, sequence, and cellular localization of a novel chromosomal protein that binds to methylated DNA

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A component of the transcriptional repressor MeCP1 shares a motif with DNA methyltransferase and HRX proteins

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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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Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves a histone deacetylase complex

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Methylated DNA and MeCP2 recruit histone deacetylase to repress transcription

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A mammalian protein with specific demethylase activity for mCpG DNA.

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DNA methylation inhibits transcription indirectly via a methyl-CpG binding protein

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Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex

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SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex

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Trichostatin A and trapoxin: novel chemical probes for the role of histone acetylation in chromatin structure and function

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Synergy of demethylation and histone deacetylase inhibition in the re-expression of genes silenced in cancer

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DNA methylation models histone acetylation

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DNA methylation and chromatin modification.

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Trichostatin A causes selective loss of DNA methylation in Neurospora

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Retinoblastoma protein recruits histone deacetylase to repress transcription

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Retinoblastoma protein represses transcription by recruiting a histone deacetylase

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Rb interacts with histone deacetylase to repress transcription

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DNA methylation specifies chromosomal localization of MeCP2.

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

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Structure-function analysis of the TBP-binding protein Dr1 reveals a mechanism for repression of class II gene transcription

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Preparation of site-specific antibodies to acetylated histones

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