Impact of macromolecular crowding on DNA replication. - Wikidata - wikimedia - TriplyDB

Impact of macromolecular crowding on DNA replication.

Impact of macromolecular crowding on DNA replication.

http://www.wikidata.org/entity/Q30428470

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DNA replication at the single-molecule level Connecting the dots: the effects of macromolecular crowding on cell physiology.DNA binding proteins explore multiple local configurations during docking via rapid rebinding.Improved cell-free RNA and protein synthesis system.Calcineurin in a Crowded World.Molecular crowding enhanced ATPase activity of the RNA helicase eIF4A correlates with compaction of its quaternary structure and association with eIF4G.The interaction between eukaryotic initiation factor 1A and eIF5 retains eIF1 within scanning preinitiation complexes.Cell-free synthetic biology for in vitro prototype engineering.Examining weak protein-protein interactions in start codon recognition via NMR spectroscopy.Emerging applications of small angle solution scattering in structural biology.Artificial cell mimics as simplified models for the study of cell biology.Quantitative computational models of molecular self-assembly in systems biology.Molecular crowding impacts the structure of apolipoprotein A-I with potential implications on in vivo metabolism and function.Making microenvironments: A look into incorporating macromolecular crowding into in vitro experiments, to generate biomimetic microenvironments which are capable of directing cell function for tissue engineering applications.Kinetics of T3-DNA Ligase-Catalyzed Phosphodiester Bond Formation Measured Using the α-Hemolysin Nanopore.Intersegmental transfer of proteins between DNA regions in the presence of crowding.Role of Macromolecular Crowding on the Intracellular Diffusion of DNA Binding Proteins.Direct observation of Ca(2+) -induced calmodulin conformational transitions in intact Xenopus laevis oocytes by (19) F NMR spectroscopy.Visualizing an ultra-weak protein-protein interaction in phosphorylation signaling.The growth of filaments under macromolecular confinement using scaling theory.Site accessibility tailors DNA cleavage by restriction enzymes in DNA confined monolayers.A single-molecule approach to DNA replication in Escherichia coli cells demonstrated that DNA polymerase III is a major determinant of fork speed.Denaturation and renaturation behaviors of short DNA in a confined space.Dynamics of highly polydisperse colloidal suspensions as a model system for bacterial cytoplasm.

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Impact of macromolecular crowding on DNA replication.

http://www.wikidata.org/entity/Q30428470

description

2013 nî lūn-bûn

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2013 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2013年の論文

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2013年論文

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name

Impact of macromolecular crowding on DNA replication.

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Impact of macromolecular crowding on DNA replication.

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Impact of macromolecular crowding on DNA replication.

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Impact of macromolecular crowding on DNA replication.

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Nature Communications

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Impact of macromolecular crowding on DNA replication.

@en

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Barak Akabayov

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

Charles C Richardson

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

Gerhard Wagner

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Sabine R Akabayov

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Seung-Joo Lee

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P2860

Macromolecular crowding perturbs protein refolding kinetics: implications for folding inside the cell

Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides

Modular architecture of the bacteriophage T7 primase couples RNA primer synthesis to DNA synthesis

The crystal structure of the bifunctional primase-helicase of bacteriophage T7

Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase

The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media

CRYSOL– a Program to Evaluate X-ray Solution Scattering of Biological Macromolecules from Atomic Coordinates

A unique loop in T7 DNA polymerase mediates the binding of helicase-primase, DNA binding protein, and processivity factor

The effect of macromolecular crowding, ionic strength and calcium binding on calmodulin dynamics.

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10.1038/NCOMMS2620

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4

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2013-01-01T00:00:00Z

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236063753

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1020205007

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23511479

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3666333

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