(Q46084700)

19 December 2017

title

Mapping the interaction of DNA with the Escherichia coli DNA polymerase clamp loader complex (English)

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19 December 2017

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Eric R Goedken

1

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19 December 2017

Steven L Kazmirski

2

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19 December 2017

Gregory D Bowman

3

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19 December 2017

Mike O'Donnell

4

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19 December 2017

John Kuriyan

5

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19 December 2017

publication date

16 January 2005

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19 December 2017

Nature Structural & Molecular Biology

published in

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19 December 2017

volume

12

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19 December 2017

page(s)

183-190

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19 December 2017

issue

2

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19 December 2017

https://scigraph.springernature.com/pub.10.1038/nsmb889

exact match

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cites work

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Structural analysis of the inactive state of the Escherichia coli DNA polymerase clamp-loader complex

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Interplay of clamp loader subunits in opening the beta sliding clamp of Escherichia coli DNA polymerase III holoenzyme

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The internal workings of a DNA polymerase clamp-loading machine

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Fluorescence measurements on the E.coli DNA polymerase clamp loader: implications for conformational changes during ATP and clamp binding

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21 January 2018

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Mechanism of loading the Escherichia coli DNA polymerase III beta sliding clamp on DNA. Bona fide primer/templates preferentially trigger the gamma complex to hydrolyze ATP and load the clamp

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Ordered ATP hydrolysis in the gamma complex clamp loader AAA+ machine.

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Clamp loader structure predicts the architecture of DNA polymerase III holoenzyme and RFC.

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31 March 2020

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Characterization of pp60c-src tyrosine kinase activities using a continuous assay: autoactivation of the enzyme is an intermolecular autophosphorylation process

31 March 2020

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31 March 2020

Identifiers

DOI

10.1038/NSMB889

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19 December 2017

PubMed ID

15665871

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19 December 2017