Tyrosine phosphorylation enhances RAD52-mediated annealing by modulating its DNA binding
Published 2011 View Full Article
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Title
Tyrosine phosphorylation enhances RAD52-mediated annealing by modulating its DNA binding
Authors
Keywords
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Journal
EMBO JOURNAL
Volume 30, Issue 16, Pages 3368-3382
Publisher
Wiley
Online
2011-07-29
DOI
10.1038/emboj.2011.238
References
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- Human BRCA2 protein promotes RAD51 filament formation on RPA-covered single-stranded DNA
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- Human Rad52 binds and wraps single-stranded DNA and mediates annealing via two hRad52–ssDNA complexes
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- Rad52 inactivation is synthetically lethal with BRCA2 deficiency
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- (2009) Hiroko Shimizu et al. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- Human Replication Protein A−Rad52−Single-Stranded DNA Complex: Stoichiometry and Evidence for Strand Transfer Regulation by Phosphorylation
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- BCR-ABL promotes the frequency of mutagenic single-strand annealing DNA repair
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- Rad52 recruitment is DNA replication independent and regulated by Cdc28 and the Mec1 kinase
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- SSB protein diffusion on single-stranded DNA stimulates RecA filament formation
- (2009) Rahul Roy et al. NATURE
- BCR/ABL and Other Kinases from Chronic Myeloproliferative Disorders Stimulate Single-Strand Annealing, an Unfaithful DNA Double-Strand Break Repair
- (2008) K. Cramer et al. CANCER RESEARCH
- Distinct RAD51 Associations with RAD52 and BCCIP in Response to DNA Damage and Replication Stress
- (2008) J. Wray et al. CANCER RESEARCH
- Identification of a Second DNA Binding Site in the Human Rad52 Protein
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- Human Rad52-mediated homology search and annealing occurs by continuous interactions between overlapping nucleoprotein complexes
- (2008) E. Rothenberg et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
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