Loading dynamics of a sliding DNA clamp. - Wikidata - wikimedia - TriplyDB

Loading dynamics of a sliding DNA clamp.

Loading dynamics of a sliding DNA clamp.

http://www.wikidata.org/entity/Q35061085

about

Replisome Assembly at Bacterial Chromosomes and Iteron Plasmids Dynamics of Open DNA Sliding Clamps.New Structural Templates for Clinically Validated and Novel Targets in Antimicrobial Drug Research and Development.Watching cellular machinery in action, one molecule at a time.

P2860

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P2860

Loading dynamics of a sliding DNA clamp.

http://www.wikidata.org/entity/Q35061085

description

2014 nî lūn-bûn

@nan

2014 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2014年の論文

@ja

2014年論文

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2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

@wuu

name

Loading dynamics of a sliding DNA clamp.

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Loading dynamics of a sliding DNA clamp.

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type

label

Loading dynamics of a sliding DNA clamp.

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Loading dynamics of a sliding DNA clamp.

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prefLabel

Loading dynamics of a sliding DNA clamp.

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Loading dynamics of a sliding DNA clamp.

@en

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Angewandte Chemie International Edition

P1476

Loading dynamics of a sliding DNA clamp.

@en

P2093

Daehyung Kim

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Jong-Bong Lee

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

Slobodan Jergic

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

P2860

Crystal structure of the processivity clamp loader gamma (gamma) complex of E. coli DNA polymerase III

Three-dimensional structure of the beta subunit of E. coli DNA polymerase III holoenzyme: a sliding DNA clamp

The Mechanism of ATP-Dependent Primer-Template Recognition by a Clamp Loader Complex

How a DNA Polymerase Clamp Loader Opens a Sliding Clamp

Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex

The beta subunit of the Escherichia coli DNA polymerase III holoenzyme interacts functionally with the catalytic core in the absence of other subunits

Motion of a DNA sliding clamp observed by single molecule fluorescence spectroscopy

DNA polymerase III holoenzyme: structure and function of a chromosomal replicating machine.

Reverse-chaperoning activity of an AAA+ protein.

Escherichia coli DnaX product, the tau subunit of DNA polymerase III, is a multifunctional protein with single-stranded DNA-dependent ATPase activity

P304

6768-6771

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scholarly article

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10.1002/ANIE.201403063

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26

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53

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Nicholas E. Dixon

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2014-05-22T00:00:00Z

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262578517

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