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The macro domain is an ADP-ribose binding module

Published:2005-05-19 Issue:11 Volume:24 Page:1911-1920
ISSN:0261-4189
Container-title:The EMBO Journal
language:
Short-container-title:EMBO J

Author:

Karras Georgios I,Kustatscher Georg,Buhecha Heeran R,Allen Mark D,Pugieux Céline,Sait Fiona,Bycroft Mark,Ladurner Andreas G

Publisher

Wiley

Subject

General Immunology and Microbiology,General Biochemistry, Genetics and Molecular Biology,Molecular Biology,General Neuroscience

Reference71 articles.

1. Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria

2. ADP-ribosylation of nuclear proteins in vivo. Identification of histone H2B as a major acceptor for mono- and poly(ADP-ribose) in dimethyl sulfate-treated hepatoma AH 7974 cells.

3. BAL is a novel risk-related gene in diffuse large B-cell lymphomas that enhances cellular migration

4. The Crystal Structure of AF1521 a Protein from Archaeoglobus fulgidus with Homology to the Non-histone Domain of MacroH2A

5. The PARP superfamily

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1. Mono‐ADP‐Ribosylation of Peptides: An Overview of Synthetic and Chemoenzymatic Methodologies;ChemBioChem;2024-09-05

2. Poly‐ADP‐ribosylation dynamics, signaling, and analysis;Environmental and Molecular Mutagenesis;2024-09-02

3. Evolutionary and molecular basis of ADP-ribosylation reversal by zinc-dependent macrodomains;Journal of Biological Chemistry;2024-09

4. Histone H2A variants play a key role at DNA double-strand breaks during repair pathway choice;Frontiers in Epigenetics and Epigenomics;2024-08-22

5. The Function of H2A Histone Variants and Their Roles in Diseases;Biomolecules;2024-08-12

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