Rap1–Sir4 binding independent of other Sir, yKu, or histone interactions initiates the assembly of telomeric heterochromatin in yeast
RCSB PDB - 1NYH: Crystal Structure of the Coiled-coil Dimerization Motif of Sir4
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Figure 1 | PLOS Genetics
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Figure 6 from Saccharomyces cerevisiae Epigenetics in | Semantic Scholar
The Sir4 H‐BRCT domain interacts with phospho‐proteins to sequester and repress yeast heterochromatin | The EMBO Journal
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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 Ku subunit of telomerase binds Sir4 to recruit telomerase to lengthen telomeres in S. cerevisiae | eLife
Sir4
File:SIR2 heterodimer in complex with SIR4 SID black background.png - Wikimedia Commons
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
Discovery and Evolution of New Domains in Yeast Heterochromatin Factor Sir4 and Its Partner Esc1
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SIR4 Rabbit Polyclonal Antibody | ARP American Research Products, Inc.
Sir4 foci-Esc1 colocalization increases with increased TPE. (A)... | Download Scientific Diagram
Assembly of the SIR Complex and Its Regulation by O-Acetyl-ADP-Ribose, a Product of NAD-Dependent Histone Deacetylation - ScienceDirect
The Sir4 H‐BRCT domain interacts with phospho‐proteins to sequester and repress yeast heterochromatin | The EMBO Journal
A Deubiquitinating Enzyme Interacts with SIR4 and Regulates Silencing in S. cerevisiae: Cell
