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- W2169373040 endingPage "717" @default.
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- W2169373040 abstract "Methylation of histone H3 on lysine 9 is critical for diverse biological processes including transcriptional repression, heterochromatin formation, and X inactivation. The biological effects of histone methylation are thought to be mediated by effector proteins that recognize and bind to specific patterns of methylation. Using an unbiased in vitro biochemical approach, we have identified ICBP90, a transcription and cell cycle regulator, as a novel methyl K9 H3-specific binding protein. ICBP90 and its murine homologue Np95 are enriched in pericentric heterochromatin of interphase nuclei, and this localization is dependent on H3K9 methylation. Specific binding of ICBP90 to methyl K9 H3 depends on two functional domains, a PHD (plant homeodomain) finger that defines the binding specificity and an SRA (SET- and RING-associated) domain that promotes binding activity. Furthermore, we present evidence that ICBP90 is required for proper heterochromatin formation in mammalian cells." @default.
- W2169373040 created "2016-06-24" @default.
- W2169373040 creator A5034097820 @default.
- W2169373040 creator A5054291041 @default.
- W2169373040 creator A5063718814 @default.
- W2169373040 creator A5081255056 @default.
- W2169373040 date "2008-01-01" @default.
- W2169373040 modified "2023-10-11" @default.
- W2169373040 title "ICBP90, a Novel Methyl K9 H3 Binding Protein Linking Protein Ubiquitination with Heterochromatin Formation" @default.
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- W2169373040 doi "https://doi.org/10.1128/mcb.01598-07" @default.
- W2169373040 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2223417" @default.
- W2169373040 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17967883" @default.
- W2169373040 hasPublicationYear "2008" @default.
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