Interplay between Ku and Replication Protein A in the Restriction of Exo1-mediated DNA Break End Resection

Sae2 promotes dsDNA endonuclease activity within Mre11–Rad50–Xrs2 to resect DNA breaks

(2014) Elda Cannavo et al.   NATURE

The Dissolution of Double Holliday Junctions

(2014) A. H. Bizard et al.   Cold Spring Harbor Perspectives in Biology

Holliday Junction Resolvases

(2014) H. D. M. Wyatt et al.   Cold Spring Harbor Perspectives in Biology

Phosphorylation of EXO1 by CDKs 1 and 2 regulates DNA end resection and repair pathway choice

(2014) Nozomi Tomimatsu et al.   Nature Communications

DNA-dependent Protein Kinase Regulates DNA End Resection in Concert with Mre11-Rad50-Nbs1 (MRN) and Ataxia Telangiectasia-mutated (ATM)

(2013) Yi Zhou et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

RPA Coordinates DNA End Resection and Prevents Formation of DNA Hairpins

(2013) Huan Chen et al.   MOLECULAR CELL

Nucleosome dynamics regulates DNA processing

(2013) Nicholas L Adkins et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

A new structural framework for integrating replication protein A into DNA processing machinery

(2013) Chris A. Brosey et al.   NUCLEIC ACIDS RESEARCH

Repair of Double-Strand Breaks by End Joining

(2013) K. K. Chiruvella et al.   Cold Spring Harbor Perspectives in Biology

The SOSS1 single-stranded DNA binding complex promotes DNA end resection in concert with Exo1

(2012) Soo-Hyun Yang et al.   EMBO JOURNAL

DNA breakage drives nuclear search

(2012) Grzegorz Ira et al.   NATURE CELL BIOLOGY

The dynamics of Ku70/80 and DNA-PKcs at DSBs induced by ionizing radiation is dependent on the complexity of damage

(2012) Pamela Reynolds et al.   NUCLEIC ACIDS RESEARCH

Structures of Human Exonuclease 1 DNA Complexes Suggest a Unified Mechanism for Nuclease Family

(2011) Jillian Orans et al.   CELL

Electron microscopy visualization of DNA–protein complexes formed by Ku and DNA ligase IV

(2011) Patricia Grob et al.   DNA REPAIR

Factors determining DNA double-strand break repair pathway choice in G2 phase

(2011) Atsushi Shibata et al.   EMBO JOURNAL

Functional Interplay of the Mre11 Nuclease and Ku in the Response to Replication-Associated DNA Damage

(2011) S. S. Foster et al.   MOLECULAR AND CELLULAR BIOLOGY

Release of Ku and MRN from DNA Ends by Mre11 Nuclease Activity and Ctp1 Is Required for Homologous Recombination Repair of Double-Strand Breaks

(2011) Petra Langerak et al.   PLoS Genetics

Ku Must Load Directly onto the Chromosome End in Order to Mediate Its Telomeric Functions

(2011) Christopher R. Lopez et al.   PLoS Genetics

Ku prevents Exo1 and Sgs1-dependent resection of DNA ends in the absence of a functional MRX complex or Sae2

(2010) Eleni P Mimitou et al.   EMBO JOURNAL

Saccharomyces cerevisiae Mre11/Rad50/Xrs2 and Ku proteins regulate association of Exo1 and Dna2 with DNA breaks

(2010) Eun Yong Shim et al.   EMBO JOURNAL

Telomere Maintenance and Survival in Saccharomyces cerevisiae in the Absence of Telomerase and RAD52

(2009) C. LeBel et al.   GENETICS

Sequential Loading ofSaccharomyces cerevisiaeKu and Cdc13p to Telomeres

(2009) Tzung-Ju Wu et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Sgs1 Helicase and Two Nucleases Dna2 and Exo1 Resect DNA Double-Strand Break Ends

(2008) Zhu Zhu et al.   CELL

Comparison of nonhomologous end joining and homologous recombination in human cells

(2008) Z MAO et al.   DNA REPAIR

Inhibition of DNA double-strand break repair by the Ku heterodimer in mrx mutants of Saccharomyces cerevisiae

(2008) Brian M. Wasko et al.   DNA REPAIR

The Yku70–Yku80 complex contributes to regulate double-strand break processing and checkpoint activation during the cell cycle

(2008) Michela Clerici et al.   EMBO REPORTS

Recruitment and Dissociation of Nonhomologous End Joining Proteins at a DNA Double-Strand Break in Saccharomyces cerevisiae

(2008) D. Wu et al.   GENETICS

Sae2, Exo1 and Sgs1 collaborate in DNA double-strand break processing

(2008) Eleni P. Mimitou et al.   NATURE

CDK targets Sae2 to control DNA-end resection and homologous recombination

(2008) Pablo Huertas et al.   NATURE