The Ku subunit of telomerase binds Sir4 to recruit telomerase to lengthen telomeres in S. cerevisiae | eLife
Rap1–Sir4 binding independent of other Sir, yKu, or histone interactions initiates the assembly of telomeric heterochromatin in yeast
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
Sir4
Figure 1 | PLOS Genetics
Discovery and Evolution of New Domains in Yeast Heterochromatin Factor Sir4 and Its Partner Esc1
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
The Ku subunit of telomerase binds Sir4 to recruit telomerase to lengthen telomeres in S. cerevisiae | eLife
Sir4 foci-Esc1 colocalization increases with increased TPE. (A)... | Download Scientific Diagram
RCSB PDB - 1NYH: Crystal Structure of the Coiled-coil Dimerization Motif of Sir4
40620-30 Micro Switch SIR4 Precision Limit Switch 10A-120,240 or 480 VAC,600 VAC | eBay
SIR4 180 - High Frequency Power Supplies for Electrostatic Precipitators
The Sir4 H‐BRCT domain interacts with phospho‐proteins to sequester and repress yeast heterochromatin | The EMBO Journal
Le contrôleur d'entretien SIR 4 - BMW Z3 / Z4 Club France
Figure 6 from Saccharomyces cerevisiae Epigenetics in | Semantic Scholar
Cells | Free Full-Text | Sir4 Deficiency Reverses Cell Senescence by Sub-Telomere Recombination
ALSTOM SIR4 HIGH VOLTAGE UNIT 480V 85KV/1200Ma | eBay
RCSB PDB - 1NYH: Crystal Structure of the Coiled-coil Dimerization Motif of Sir4
Cells | Free Full-Text | Sir4 Deficiency Reverses Cell Senescence by Sub-Telomere Recombination
ELESTA relays - SIR312 - ELESTA product overview - Standard products 12/24 VDC
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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
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
