Structure of the polymerase ε holoenzyme and atomic model of the leading strand replisome
Published 2020 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
Structure of the polymerase ε holoenzyme and atomic model of the leading strand replisome
Authors
Keywords
-
Journal
Nature Communications
Volume 11, Issue 1, Pages -
Publisher
Springer Science and Business Media LLC
Online
2020-06-22
DOI
10.1038/s41467-020-16910-5
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- DNA unwinding mechanism of a eukaryotic replicative CMG helicase
- (2020) Zuanning Yuan et al. Nature Communications
- Structure of the processive human Pol δ holoenzyme
- (2020) Claudia Lancey et al. Nature Communications
- Structures and operating principles of the replisome
- (2019) Yang Gao et al. SCIENCE
- Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix
- (2019) Dorothee Liebschner et al. Acta Crystallographica Section D-Structural Biology
- The ring-shaped hexameric helicases that function at DNA replication forks
- (2018) Michael E. O’Donnell et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- The ring-shaped hexameric helicases that function at DNA replication forks
- (2018) Michael E. O’Donnell et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- POLE3-POLE4 Is a Histone H3-H4 Chaperone that Maintains Chromatin Integrity during DNA Replication
- (2018) Roberto Bellelli et al. MOLECULAR CELL
- A mechanism for preventing asymmetric histone segregation onto replicating DNA strands
- (2018) Chuanhe Yu et al. SCIENCE
- Structure of DNA-CMG-Pol epsilon elucidates the roles of the non-catalytic polymerase modules in the eukaryotic replisome
- (2018) Panchali Goswami et al. Nature Communications
- Crystal structure of the human Polϵ B-subunit in complex with the C-terminal domain of the catalytic subunit
- (2017) Andrey G. Baranovskiy et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy
- (2017) Shawn Q Zheng et al. NATURE METHODS
- Coordinated regulation of heterochromatin inheritance by Dpb3–Dpb4 complex
- (2017) Haijin He et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Quality control mechanisms exclude incorrect polymerases from the eukaryotic replication fork
- (2017) Grant D. Schauer et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Mcm10 promotes rapid isomerization of CMG-DNA for replisome bypass of lagging strand DNA blocks
- (2017) Lance D Langston et al. eLife
- New Insights into the Mechanism of DNA Duplication by the Eukaryotic Replisome
- (2016) Luca Pellegrini et al. TRENDS IN BIOCHEMICAL SCIENCES
- Cryo-EM structures of the eukaryotic replicative helicase bound to a translocation substrate
- (2016) Ferdos Abid Ali et al. Nature Communications
- Accelerated cryo-EM structure determination with parallelisation using GPUs in RELION-2
- (2016) Dari Kimanius et al. eLife
- CTFFIND4: Fast and accurate defocus estimation from electron micrographs
- (2015) Alexis Rohou et al. JOURNAL OF STRUCTURAL BIOLOGY
- The architecture of a eukaryotic replisome
- (2015) Jingchuan Sun et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- The architecture of a eukaryotic replisome
- (2015) Jingchuan Sun et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Mechanism of asymmetric polymerase assembly at the eukaryotic replication fork
- (2014) Roxana E Georgescu et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- CMG helicase and DNA polymerase form a functional 15-subunit holoenzyme for eukaryotic leading-strand DNA replication
- (2014) L. D. Langston et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Dpb2 Integrates the Leading-Strand DNA Polymerase into the Eukaryotic Replisome
- (2013) Sugopa Sengupta et al. CURRENT BIOLOGY
- Quantifying the local resolution of cryo-EM density maps
- (2013) Alp Kucukelbir et al. NATURE METHODS
- Structural basis for processive DNA synthesis by yeast DNA polymerase ɛ
- (2013) Matthew Hogg et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Replicative DNA Polymerases
- (2013) E. Johansson et al. Cold Spring Harbor Perspectives in Biology
- DNA polymerization-independent functions of DNA polymerase epsilon in assembly and progression of the replisome in fission yeast
- (2012) Tetsuya Handa et al. MOLECULAR BIOLOGY OF THE CELL
- The C-terminus of Dpb2 is required for interaction with Pol2 and for cell viability
- (2012) Isabelle Isoz et al. NUCLEIC ACIDS RESEARCH
- Studies on Human DNA Polymerase ϵ and GINS Complex and Their Role in DNA Replication
- (2011) Vladimir P. Bermudez et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Features and development ofCoot
- (2010) P. Emsley et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- CDK-dependent complex formation between replication proteins Dpb11, Sld2, Pol , and GINS in budding yeast
- (2010) S. Muramatsu et al. GENES & DEVELOPMENT
- Mismatch Repair–Independent Increase in Spontaneous Mutagenesis in Yeast Lacking Non-Essential Subunits of DNA Polymerase ε
- (2010) Anna Aksenova et al. PLoS Genetics
- MolProbity: all-atom structure validation for macromolecular crystallography
- (2009) Vincent B. Chen et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- Evolution of DNA polymerases: an inactivated polymerase-exonuclease module in Pol ε and a chimeric origin of eukaryotic polymerases from two classes of archaeal ancestors
- (2009) Tahir H Tahirov et al. Biology Direct
- Structure of a Sliding Clamp on DNA
- (2008) Roxana E. Georgescu et al. CELL
- The solution structure of the amino-terminal domain of human DNA polymerase ε subunit B is homologous to C-domains of AAA+ proteins
- (2008) Tarmo Nuutinen et al. NUCLEIC ACIDS RESEARCH
Become a Peeref-certified reviewer
The Peeref Institute provides free reviewer training that teaches the core competencies of the academic peer review process.
Get StartedAsk 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