![The Sir4 H‐BRCT domain interacts with phospho‐proteins to sequester and repress yeast heterochromatin | The EMBO Journal The Sir4 H‐BRCT domain interacts with phospho‐proteins to sequester and repress yeast heterochromatin | The EMBO Journal](https://www.embopress.org/cms/asset/97ddd880-913f-460b-b533-6583691ab71d/embj2019101744-abs-0001-m.jpg)
The Sir4 H‐BRCT domain interacts with phospho‐proteins to sequester and repress yeast heterochromatin | The EMBO Journal
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Assembly of the SIR Complex and Its Regulation by O-Acetyl-ADP-Ribose, a Product of NAD-Dependent Histone Deacetylation - ScienceDirect
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Schematic view of the structural and functional domains identified in... | Download Scientific Diagram
![Assembly of the SIR Complex and Its Regulation by O-Acetyl-ADP-Ribose, a Product of NAD-Dependent Histone Deacetylation - ScienceDirect Assembly of the SIR Complex and Its Regulation by O-Acetyl-ADP-Ribose, a Product of NAD-Dependent Histone Deacetylation - ScienceDirect](https://ars.els-cdn.com/content/image/1-s2.0-S0092867405003545-gr4.jpg)
Assembly of the SIR Complex and Its Regulation by O-Acetyl-ADP-Ribose, a Product of NAD-Dependent Histone Deacetylation - ScienceDirect
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Silent information regulator protein complexes in Saccharomyces cerevisiae: A SIR2/SIR4 complex and evidence for a regulatory domain in SIR4 that inhibits its interaction with SIR3 | PNAS
![The Sir4 H‐BRCT domain interacts with phospho‐proteins to sequester and repress yeast heterochromatin | The EMBO Journal The Sir4 H‐BRCT domain interacts with phospho‐proteins to sequester and repress yeast heterochromatin | The EMBO Journal](https://www.embopress.org/cms/asset/5d0fc1ad-7664-407d-bb5a-cfa31e9aa4ad/embj2019101744-fig-0002-m.jpg)