Collaborative coupling between polymerase and helicase for leading-strand synthesis. - Test2 - elhamkhani - TriplyDB

Collaborative coupling between polymerase and helicase for leading-strand synthesis.

Collaborative coupling between polymerase and helicase for leading-strand synthesis.

http://www.wikidata.org/entity/Q30521445

about

Stimulation of gross chromosomal rearrangements by the human CEB1 and CEB25 minisatellites in Saccharomyces cerevisiae depends on G-quadruplexes or Cdc13 Methods to study the coupling between replicative helicase and leading-strand DNA polymerase at the replication fork Coordinated DNA Replication by the Bacteriophage T4 Replisome High Spatiotemporal-Resolution Magnetic Tweezers: Calibration and Applications for DNA Dynamics.Lab-on-a-chip technologies for single-molecule studies Mechanism of strand displacement synthesis by DNA replicative polymerases Replisome mechanics: lagging strand events that influence speed and processivity CMG helicase and DNA polymerase ε form a functional 15-subunit holoenzyme for eukaryotic leading-strand DNA replication.Cooperative base pair melting by helicase and polymerase positioned one nucleotide from each other.Helicase processivity and not the unwinding velocity exhibits universal increase with force.Strand displacement synthesis by yeast DNA polymerase ε.Direct observation of stalled fork restart via fork regression in the T4 replication system.Studying genomic processes at the single-molecule level: introducing the tools and applications.Single-molecule perspectives on helicase mechanisms and functions.Watching cellular machinery in action, one molecule at a time.Helicase and polymerase move together close to the fork junction and copy DNA in one-nucleotide steps.A mechanistic study of helicases with magnetic traps.Manipulation of single polymerase-DNA complexes: a mechanical view of DNA unwinding during replication.Understanding DNA replication by the bacteriophage T4 replisome.The human papillomavirus DNA helicase E1 binds, stimulates, and confers processivity to cellular DNA polymerase epsilon.Bacterial DnaB helicase interacts with the excluded strand to regulate unwinding.Correction-free force calibration for magnetic tweezers experiments

P2860

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P2860

Collaborative coupling between polymerase and helicase for leading-strand synthesis.

http://www.wikidata.org/entity/Q30521445

description

2012 nî lūn-bûn

@nan

2012 թուականի Մարտին հրատարակուած գիտական յօդուած

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2012 թվականի մարտին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

@zh-hk

2012年論文

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2012年論文

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2012年论文

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name

Collaborative coupling between polymerase and helicase for leading-strand synthesis.

@ast

Collaborative coupling between polymerase and helicase for leading-strand synthesis.

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type

label

Collaborative coupling between polymerase and helicase for leading-strand synthesis.

@ast

Collaborative coupling between polymerase and helicase for leading-strand synthesis.

@en

prefLabel

Collaborative coupling between polymerase and helicase for leading-strand synthesis.

@ast

Collaborative coupling between polymerase and helicase for leading-strand synthesis.

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Nucleic Acids Research

P1476

Collaborative coupling between polymerase and helicase for leading-strand synthesis.

@en

P2093

Fangyuan Ding

http://www.w3.org/2001/XMLSchema#string

Maria Manosas

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Michelle M Spiering

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Stephen J Benkovic

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Vincent Croquette

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P2860

Magnetic tweezers: micromanipulation and force measurement at the molecular level

Active and passive mechanisms of helicases

Single-molecule studies reveal dynamics of DNA unwinding by the ring-shaped T7 helicase

Real-time observation of bacteriophage T4 gp41 helicase reveals an unwinding mechanism

DINAMelt web server for nucleic acid melting prediction.

Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 A resolution

Coupling DNA unwinding activity with primer synthesis in the bacteriophage T4 primosome

Mechanism of strand displacement synthesis by DNA replicative polymerases

A general model for nucleic acid helicases and their "coupling" within macromolecular machines.

Strand displacement by DNA polymerase III occurs through a tau-psi-chi link to single-stranded DNA-binding protein coating the lagging strand template

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6187-6198

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scholarly article

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10.1093/NAR/GKS254

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13

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40

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22434886

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3401439

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