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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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The Sir4 H‐BRCT domain interacts with phospho‐proteins to sequester and repress yeast heterochromatin | The EMBO Journal
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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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The Ku subunit of telomerase binds Sir4 to recruit telomerase to lengthen telomeres in S. cerevisiae | eLife
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The Ku subunit of telomerase binds Sir4 to recruit telomerase to lengthen telomeres in S. cerevisiae | eLife
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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. - Abstract - Europe PMC
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