Resolving individual steps of Okazaki-fragment maturation at a millisecond timescale. - Wikidata - wikimedia - TriplyDB

Resolving individual steps of Okazaki-fragment maturation at a millisecond timescale.

Resolving individual steps of Okazaki-fragment maturation at a millisecond timescale.

http://www.wikidata.org/entity/Q36873034

about

Yeast DNA polymerase ζ maintains consistent activity and mutagenicity across a wide range of physiological dNTP concentrations Deoxynucleoside Salvage in Fission Yeast Allows Rescue of Ribonucleotide Reductase Deficiency but Not Spd1-Mediated Inhibition of Replication.PCNA ubiquitylation ensures timely completion of unperturbed DNA replication in fission yeast.Small molecule inhibitors uncover synthetic genetic interactions of human flap endonuclease 1 (FEN1) with DNA damage response genes.Proficient Replication of the Yeast Genome by a Viral DNA Polymerase Reconstitution of a eukaryotic replisome reveals the mechanism of asymmetric distribution of DNA polymerases Quality control mechanisms exclude incorrect polymerases from the eukaryotic replication fork.Single-molecule FRET unveils induced-fit mechanism for substrate selectivity in flap endonuclease 1.A Critical Balance: dNTPs and the Maintenance of Genome Stability Forging Ahead through Darkness: PCNA, Still the Principal Conductor at the Replication Fork.Eukaryotic DNA Replication Fork.In vitro Assays for Eukaryotic Leading/Lagging Strand DNA Replication.A Redox Role for the [4Fe4S] Cluster of Yeast DNA Polymerase δ.The dark side of the ring: role of the DNA sliding surface of PCNA.Direct Visualization of RNA-DNA Primer Removal from Okazaki Fragments Provides Support for Flap Cleavage and Exonucleolytic Pathways in Eukaryotic Cells.Characterization of a coupled DNA replication and translesion synthesis polymerase supraholoenzyme from archaea.Positioning the 5'-flap junction in the active site controls the rate of flap endonuclease-1-catalyzed DNA cleavage.Missed cleavage opportunities by FEN1 lead to Okazaki fragment maturation via the long-flap pathway.Not just for coding: a new role for histone tails in replication enzyme activation.Flap endonuclease overexpression drives genome instability and DNA damage hypersensitivity in a PCNA-dependent manner.Ubiquitylation at the Fork: Making and Breaking Chains to Complete DNA Replication

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Resolving individual steps of Okazaki-fragment maturation at a millisecond timescale.

http://www.wikidata.org/entity/Q36873034

description

2016 nî lūn-bûn

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2016年の論文

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2016年論文

@yue

2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

@zh-mo

2016年論文

@zh-tw

2016年论文

@wuu

2016年论文

@zh

2016年论文

@zh-cn

name

Resolving individual steps of Okazaki-fragment maturation at a millisecond timescale.

@en

type

label

Resolving individual steps of Okazaki-fragment maturation at a millisecond timescale.

@en

prefLabel

Resolving individual steps of Okazaki-fragment maturation at a millisecond timescale.

@en

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Nature Structural & Molecular Biology

P1476

Resolving individual steps of Okazaki-fragment maturation at a millisecond timescale.

@en

P2093

Joseph L Stodola

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Peter M Burgers

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P2860

Idling by DNA polymerase delta maintains a ligatable nick during lagging-strand DNA replication

The 3'-->5' exonuclease of DNA polymerase delta can substitute for the 5' flap endonuclease Rad27/Fen1 in processing Okazaki fragments and preventing genome instability

Structural basis for FEN-1 substrate specificity and PCNA-mediated activation in DNA replication and repair

The C-terminal domain of yeast PCNA is required for physical and functional interactions with Cdc9 DNA ligase

Human Flap Endonuclease Structures, DNA Double-Base Flipping, and a Unified Understanding of the FEN1 Superfamily

Mechanism for priming DNA synthesis by yeast DNA Polymerase α

The multiple biological roles of the 3'-->5' exonuclease of Saccharomyces cerevisiae DNA polymerase delta require switching between the polymerase and exonuclease domains

Cleavage specificity of Saccharomyces cerevisiae flap endonuclease 1 suggests a double-flap structure as the cellular substrate.

DNA polymerase delta is highly processive with proliferating cell nuclear antigen and undergoes collision release upon completing DNA.

Direct interaction of proliferating cell nuclear antigen with the small subunit of DNA polymerase delta

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402-408

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scholarly article

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10.1038/NSMB.3207

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5

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23

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2016-04-11T00:00:00Z

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1038042511

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27065195

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4857878

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