(PDF) MLL Repression Domain Interacts With Histone

MLL Repression Domain Interacts With Histone Deacetylases, the Polycomb Group Proteins HPC2 and BMI-1, and the Corepressor C-Terminal-Binding Protein

Proceedings of the National Academy of Sciences of the United States of America - United States

doi 10.1073/pnas.1436338100

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June 26, 2003

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Proceedings of the National Academy of Sciences

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MLL Repression Domain Interacts With Histone Deacetylases, the Polycomb Group Proteins HPC2 and BMI-1, and the Corepressor C-Terminal-Binding Protein

Proceedings of the National Academy of Sciences of the United States of America - United States

doi 10.1073/pnas.1436338100

Full Text

Abstract

Categories

Date

Authors

Publisher

Related search

WDR5 Interacts With Mixed Lineage Leukemia (MLL) Protein via the Histone H3-Binding Pocket

Ssn6-Tup1 Interacts With Class I Histone Deacetylases Required for Repression

Transcriptional Corepressor TOPLESS Complexes With Pseudoresponse Regulator Proteins and Histone Deacetylases to Regulate Circadian Transcription

Structural Transitions of the RING1B C-Terminal Region Upon Binding the Polycomb Cbox Domain†

Interaction Between FOG-1 and the Corepressor C-Terminal Binding Protein Is Dispensable for Normal Erythropoiesis in Vivo

Role of the C-Terminal Binding Protein PXDLS Motif Binding Cleft in Protein Interactions and Transcriptional Repression

The Trithorax Group Proteins Kismet and ASH1 Promote H3K36 Dimethylation to Counteract Polycomb Group Repression in Drosophila

MYC Interacts With the G9a Histone Methyltransferase to Drive Transcriptional Repression and Tumorigenesis

The 18-Kilodalton Chlamydia Trachomatis Histone H1-Like Protein (Hc1) Contains a Potential N-Terminal Dimerization Site and a C-Terminal Nucleic Acid-Binding Domain.