Dual roles of the SUMO-interacting motif in the regulation of Srs2 sumoylation
Published 2012 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
Dual roles of the SUMO-interacting motif in the regulation of Srs2 sumoylation
Authors
Keywords
-
Journal
NUCLEIC ACIDS RESEARCH
Volume 40, Issue 16, Pages 7831-7843
Publisher
Oxford University Press (OUP)
Online
2012-06-18
DOI
10.1093/nar/gks484
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- Unwinding of synthetic replication and recombination substrates by Srs2
- (2012) Victoria Marini et al. DNA REPAIR
- Recognition of SUMO-modified PCNA requires tandem receptor motifs in Srs2
- (2012) Anthony A. Armstrong et al. NATURE
- Homologous recombination and its regulation
- (2012) L. Krejci et al. NUCLEIC ACIDS RESEARCH
- Srs2 overexpression reveals a helicase-independent role at replication forks that requires diverse cell functions
- (2011) Ana María León Ortiz et al. DNA REPAIR
- SUMOylation and de-SUMOylation in response to DNA damage
- (2011) Hong Dou et al. FEBS LETTERS
- UBC9 Autosumoylation Negatively Regulates Sumoylation of Septins inSaccharomyces cerevisiae
- (2011) Chia-Wen Ho et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Inhibition of Homologous Recombination by the PCNA-Interacting Protein PARI
- (2011) George-Lucian Moldovan et al. MOLECULAR CELL
- SUMOylation regulates telomere length homeostasis by targeting Cdc13
- (2011) Lisa E Hang et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Overcoming natural replication barriers: differential helicase requirements
- (2011) Ranjith P. Anand et al. NUCLEIC ACIDS RESEARCH
- Srs2: The “Odd-Job Man” in DNA repair
- (2010) Victoria Marini et al. DNA REPAIR
- Rad52 SUMOylation affects the efficiency of the DNA repair
- (2010) Veronika Altmannova et al. NUCLEIC ACIDS RESEARCH
- Cdk1 Targets Srs2 to Complete Synthesis-Dependent Strand Annealing and to Promote Recombinational Repair
- (2010) Marco Saponaro et al. PLoS Genetics
- Localization of recombination proteins and Srs2 reveals anti-recombinase function in vivo
- (2009) Rebecca C. Burgess et al. JOURNAL OF CELL BIOLOGY
- Human Fbh1 helicase contributes to genome maintenance via pro- and anti-recombinase activities
- (2009) Kasper Fugger et al. JOURNAL OF CELL BIOLOGY
- Structural and Functional Insights into the Roles of the Mms21 Subunit of the Smc5/6 Complex
- (2009) Xinyuan Duan et al. MOLECULAR CELL
- Structure of the Siz/PIAS SUMO E3 Ligase Siz1 and Determinants Required for SUMO Modification of PCNA
- (2009) Ali A. Yunus et al. MOLECULAR CELL
- Principles of ubiquitin and SUMO modifications in DNA repair
- (2009) Steven Bergink et al. NATURE
- SRS2 and SGS1 prevent chromosomal breaks and stabilize triplet repeats by restraining recombination
- (2009) Alix Kerrest et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Functional significance of the Rad51-Srs2 complex in Rad51 presynaptic filament disruption
- (2009) S. Colavito et al. NUCLEIC ACIDS RESEARCH
- Mechanisms of Dealing with DNA Damage-Induced Replication Problems
- (2008) Magda Budzowska et al. CELL BIOCHEMISTRY AND BIOPHYSICS
- Homologous recombination in DNA repair and DNA damage tolerance
- (2008) Xuan Li et al. CELL RESEARCH
- Small Ubiquitin-related Modifier (SUMO) Binding Determines Substrate Recognition and Paralog-selective SUMO Modification
- (2008) Jianmei Zhu et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Mechanism and Consequences for Paralog-Specific Sumoylation of Ubiquitin-Specific Protease 25
- (2008) Erik Meulmeester et al. MOLECULAR CELL
- Ubc9 Sumoylation Regulates SUMO Target Discrimination
- (2008) Puck Knipscheer et al. MOLECULAR CELL
- Srs2 removes deadly recombination intermediates independently of its interaction with SUMO-modified PCNA
- (2008) C. Le Breton et al. NUCLEIC ACIDS RESEARCH
- Rapid unwinding of triplet repeat hairpins by Srs2 helicase of Saccharomyces cerevisiae
- (2008) Alok Dhar et al. NUCLEIC ACIDS RESEARCH
Discover Peeref hubs
Discuss science. Find collaborators. Network.
Join a conversationAsk a Question. Answer a Question.
Quickly pose questions to the entire community. Debate answers and get clarity on the most important issues facing researchers.
Get Started