标题
Control of DNA Damage Bypass by Ubiquitylation of PCNA
作者
关键词
-
出版物
Genes
Volume 11, Issue 2, Pages 138
出版商
MDPI AG
发表日期
2020-01-29
DOI
10.3390/genes11020138
参考文献
相关参考文献
注意:仅列出部分参考文献,下载原文获取全部文献信息。- Conformational flexibility of fork-remodeling helicase Rad5 shown by full-ensemble hybrid methods
- (2019) Melissa S. Gildenberg et al. PLoS One
- Lesion Bypass and the Reactivation of Stalled Replication Forks
- (2018) Kenneth J. Marians Annual Review of Biochemistry
- The HIRAN domain of helicase-like transcription factor positions the DNA translocase motor to drive efficient DNA fork regression
- (2018) Diana A. Chavez et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- ATP Binding to Rad5 Initiates Replication Fork Reversal by Inducing the Unwinding of the Leading Arm and the Formation of the Holliday Junction
- (2018) Soochul Shin et al. Cell Reports
- Eukaryotic translesion synthesis: Choosing the right tool for the job
- (2018) Kyle T. Powers et al. DNA REPAIR
- Forging Ahead through Darkness: PCNA, Still the Principal Conductor at the Replication Fork
- (2017) Katherine N. Choe et al. MOLECULAR CELL
- Regulation of DNA damage tolerance in mammalian cells by post-translational modifications of PCNA
- (2017) Rie Kanao et al. MUTATION RESEARCH-FUNDAMENTAL AND MOLECULAR MECHANISMS OF MUTAGENESIS
- Solution NMR structure of the HLTF HIRAN domain: a conserved module in SWI2/SNF2 DNA damage tolerance proteins
- (2016) Dmitry M. Korzhnev et al. JOURNAL OF BIOMOLECULAR NMR
- Involvement of budding yeast Rad5 in translesion DNA synthesis through physical interaction with Rev1
- (2016) Xin Xu et al. NUCLEIC ACIDS RESEARCH
- PCNA tool belts and polymerase bridges form during translesion synthesis
- (2016) Elizabeth M. Boehm et al. NUCLEIC ACIDS RESEARCH
- The Regulation of DNA Damage Tolerance by Ubiquitin and Ubiquitin-Like Modifiers
- (2016) Lina Cipolla et al. Frontiers in Genetics
- Structure of a Novel DNA-binding Domain of Helicase-like Transcription Factor (HLTF) and Its Functional Implication in DNA Damage Tolerance
- (2015) Asami Hishiki et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- HLTF’s Ancient HIRAN Domain Binds 3′ DNA Ends to Drive Replication Fork Reversal
- (2015) Andrew C. Kile et al. MOLECULAR CELL
- Error-free DNA-damage tolerance in Saccharomyces cerevisiae
- (2015) Xin Xu et al. MUTATION RESEARCH-REVIEWS IN MUTATION RESEARCH
- Intrinsically Disordered Proteins and Intrinsically Disordered Protein Regions
- (2014) Christopher J. Oldfield et al. Annual Review of Biochemistry
- NMR Structure of the Human Rad18 Zinc Finger in Complex with Ubiquitin Defines a Class of UBZ Domains in Proteins Linked to the DNA Damage Response
- (2014) Alessandro A. Rizzo et al. BIOCHEMISTRY
- Readers of PCNA modifications
- (2013) Helle D. Ulrich et al. CHROMOSOMA
- DNA Repair Mechanisms and the Bypass of DNA Damage in Saccharomyces cerevisiae
- (2013) S. Boiteux et al. GENETICS
- A non-catalytic role of DNA polymerase η in recruiting Rad18 and promoting PCNA monoubiquitination at stalled replication forks
- (2013) Michael Durando et al. NUCLEIC ACIDS RESEARCH
- Regulation of the specialized DNA polymerase eta: Revisiting the biological relevance of its PCNA- and ubiquitin-binding motifs
- (2012) Emmanuelle Despras et al. ENVIRONMENTAL AND MOLECULAR MUTAGENESIS
- c-Jun N-terminal kinase–mediated Rad18 phosphorylation facilitates Polη recruitment to stalled replication forks
- (2012) Laura R. Barkley et al. MOLECULAR BIOLOGY OF THE CELL
- De novo mutations in human genetic disease
- (2012) Joris A. Veltman et al. NATURE REVIEWS GENETICS
- Y-family DNA polymerases and their role in tolerance of cellular DNA damage
- (2012) Julian E. Sale et al. NATURE REVIEWS MOLECULAR CELL BIOLOGY
- A SUMO-interacting motif activates budding yeast ubiquitin ligase Rad18 towards SUMO-modified PCNA
- (2012) Joanne L. Parker et al. NUCLEIC ACIDS RESEARCH
- Hallmarks of Cancer: The Next Generation
- (2011) Douglas Hanahan et al. CELL
- Pre-steady state kinetic studies show that an abasic site is a cognate lesion for the yeast Rev1 protein
- (2011) John M. Pryor et al. DNA REPAIR
- Symmetry and Asymmetry of the RING–RING Dimer of Rad18
- (2011) Anding Huang et al. JOURNAL OF MOLECULAR BIOLOGY
- Somatic mutations in aging, cancer and neurodegeneration
- (2011) Scott R. Kennedy et al. MECHANISMS OF AGEING AND DEVELOPMENT
- Asymmetric nature of two subunits of RAD18, a RING-type ubiquitin ligase E3, in the human RAD6A–RAD18 ternary complex
- (2011) Yuji Masuda et al. NUCLEIC ACIDS RESEARCH
- E3 ligase Rad18 promotes monoubiquitination rather than ubiquitin chain formation by E2 enzyme Rad6
- (2011) R. G. Hibbert et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Role of yeast Rad5 and its human orthologs, HLTF and SHPRH in DNA damage tolerance
- (2010) Ildiko Unk et al. DNA REPAIR
- Ubiquitin signalling in DNA replication and repair
- (2010) Helle D. Ulrich et al. NATURE REVIEWS MOLECULAR CELL BIOLOGY
- RING Domain E3 Ubiquitin Ligases
- (2009) Raymond J. Deshaies et al. Annual Review of Biochemistry
- Variations on a theme: Eukaryotic Y-family DNA polymerases
- (2009) M. Todd Washington et al. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
- Synthesis of Free and Proliferating Cell Nuclear Antigen-bound Polyubiquitin Chains by the RING E3 Ubiquitin Ligase Rad5
- (2009) Candice M. Carlile et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Eukaryotic Translesion Polymerases and Their Roles and Regulation in DNA Damage Tolerance
- (2009) L. S. Waters et al. MICROBIOLOGY AND MOLECULAR BIOLOGY REVIEWS
- Principles of ubiquitin and SUMO modifications in DNA repair
- (2009) Steven Bergink et al. NATURE
- Prediction of disordered regions in proteins based on the meta approach
- (2008) T. Ishida et al. BIOINFORMATICS
- Activation of Ubiquitin-Dependent DNA Damage Bypass Is Mediated by Replication Protein A
- (2008) Adelina A. Davies et al. MOLECULAR CELL
Create your own webinar
Interested in hosting your own webinar? Check the schedule and propose your idea to the Peeref Content Team.
Create NowAsk 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