Stability of the human polymerase δ holoenzyme and its implications in lagging strand DNA synthesis
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Title
Stability of the human polymerase δ holoenzyme and its implications in lagging strand DNA synthesis
Authors
Keywords
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Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 113, Issue 13, Pages E1777-E1786
Publisher
Proceedings of the National Academy of Sciences
Online
2016-03-15
DOI
10.1073/pnas.1523653113
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Note: Only part of the references are listed.- Regulation of Rad6/Rad18 Activity During DNA Damage Tolerance
- (2015) Mark Hedglin et al. Annual Review of Biophysics
- Replication-Coupled PCNA Unloading by the Elg1 Complex Occurs Genome-wide and Requires Okazaki Fragment Ligation
- (2015) Takashi Kubota et al. Cell Reports
- The C-terminal Domain of the DNA Polymerase Catalytic Subunit Regulates the Primase and Polymerase Activities of the Human DNA Polymerase α-Primase Complex
- (2014) Yinbo Zhang et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Diffusion of Human Replication Protein A along Single-Stranded DNA
- (2014) Binh Nguyen et al. JOURNAL OF MOLECULAR BIOLOGY
- Mechanism of asymmetric polymerase assembly at the eukaryotic replication fork
- (2014) Roxana E Georgescu et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- DNA synthesis by Pol η promotes fragile site stability by preventing under-replicated DNA in mitosis
- (2013) Valérie Bergoglio et al. JOURNAL OF CELL BIOLOGY
- 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
- Replication Clamps and Clamp Loaders
- (2013) M. Hedglin et al. Cold Spring Harbor Perspectives in Biology
- Okazaki Fragment Metabolism
- (2013) L. Balakrishnan et al. Cold Spring Harbor Perspectives in Biology
- Stepwise assembly of the human replicative polymerase holoenzyme
- (2013) Mark Hedglin et al. eLife
- Temporally distinct translesion synthesis pathways for ultraviolet light-induced photoproducts in the mammalian genome
- (2012) Piya Temviriyanukul et al. DNA REPAIR
- Ribonucleotide incorporation, proofreading and bypass by human DNA polymerase δ
- (2012) Anders R. Clausen et al. DNA REPAIR
- The Human Lagging Strand DNA Polymerase δ Holoenzyme Is Distributive
- (2012) Zhenxin Hu et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Intrinsic Flexibility of Ubiquitin on Proliferating Cell Nuclear Antigen (PCNA) in Translesion Synthesis
- (2012) Richard G. Hibbert et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Y-family DNA polymerases and their role in tolerance of cellular DNA damage
- (2012) Julian E. Sale et al. NATURE REVIEWS MOLECULAR CELL BIOLOGY
- Characterization of Human DNA Polymerase Delta and Its Subassemblies Reconstituted by Expression in the Multibac System
- (2012) Yajing Zhou et al. PLoS One
- Phosphorylation of the p68 Subunit of Pol δ Acts as a Molecular Switch To Regulate Its Interaction with PCNA
- (2011) Amal A. Rahmeh et al. BIOCHEMISTRY
- The quantitative proteome of a human cell line
- (2011) M. Beck et al. Molecular Systems Biology
- PCNA binding domains in all three subunits of yeast DNA polymerase modulate its function in DNA replication
- (2011) N. Acharya et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- PCNA Ubiquitination Is Important, But Not Essential for Translesion DNA Synthesis in Mammalian Cells
- (2011) Ayal Hendel et al. PLoS Genetics
- The p12 Subunit of Human Polymerase δ Modulates the Rate and Fidelity of DNA Synthesis
- (2010) Xiao Meng et al. BIOCHEMISTRY
- Human replicative DNA polymerase δ can bypass T-T (6-4) ultraviolet photoproducts on template strands
- (2010) Takeo Narita et al. GENES TO CELLS
- Role of the ubiquitin-binding domain of Polη in Rad18-independent translesion DNA synthesis in human cell extracts
- (2010) Valérie Schmutz et al. NUCLEIC ACIDS RESEARCH
- DNA polymerase lacking the ubiquitin-binding domain promotes replicative lesion bypass in humans cells
- (2010) N. Acharya et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Variations on a theme: Eukaryotic Y-family DNA polymerases
- (2009) M. Todd Washington et al. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
- High fidelity and lesion bypass capability of human DNA polymerase δ
- (2009) Michael W. Schmitt et al. BIOCHIMIE
- Proliferating Cell Nuclear Antigen Uses Two Distinct Modes to Move along DNA
- (2009) Anna B. Kochaniak et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Structural Basis for Novel Interactions between Human Translesion Synthesis Polymerases and Proliferating Cell Nuclear Antigen
- (2009) Asami Hishiki et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Human DNA Polymerase Is Required for Common Fragile Site Stability during Unperturbed DNA Replication
- (2009) L. Rey et al. MOLECULAR AND CELLULAR BIOLOGY
- Cohesin acetylation speeds the replication fork
- (2009) Marie-Emilie Terret et al. NATURE
- Highly error-free role of DNA polymerase in the replicative bypass of UV-induced pyrimidine dimers in mouse and human cells
- (2009) J.-H. Yoon et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- DNA Polymerase δ Is Highly Processive with Proliferating Cell Nuclear Antigen and Undergoes Collision Release upon Completing DNA
- (2008) Lance D. Langston et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- PCNA Ubiquitination and REV1 Define Temporally Distinct Mechanisms for Controlling Translesion Synthesis in the Avian Cell Line DT40
- (2008) Charlotte E. Edmunds et al. MOLECULAR CELL
- Regulation of polymerase exchange between Pol and Pol by monoubiquitination of PCNA and the movement of DNA polymerase holoenzyme
- (2008) Z. Zhuang et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
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