(Q54441934)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:17483094%20AND%20SRC:MED&resulttype=core&format=json

30 December 2019

title

Escherichia coli PriA protein, two modes of DNA binding and activation of ATP hydrolysis (English)

1 reference

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30 December 2019

1 reference

4

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30 December 2019

author name string

Taku Tanaka

1

1 reference

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30 December 2019

Toshimi Mizukoshi

2

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30 December 2019

Kaori Sasaki

3

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30 December 2019

Hisao Masai

5

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30 December 2019

language of work or name

English

0 references

publication date

4 May 2007

1 reference

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Journal of Biological Chemistry

30 December 2019

published in

1 reference

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30 December 2019

volume

282

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30 December 2019

page(s)

19917-19927

1 reference

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30 December 2019

issue

27

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DNA replication checkpoint

30 December 2019

cites work

1 reference

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Checking on the fork: the DNA-replication stress-response pathway

21 January 2018

1 reference

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Recombinational repair and restart of damaged replication forks.

21 January 2018

1 reference

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Swi1 prevents replication fork collapse and controls checkpoint kinase Cds1.

21 January 2018

1 reference

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Swi1 and Swi3 are components of a replication fork protection complex in fission yeast.

21 January 2018

1 reference

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An Escherichia coli replication protein that recognizes a unique sequence within a hairpin region in phi X174 DNA.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M701848200

Replication deficiencies in priA mutants of Escherichia coli lacking the primosomal replication n' protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M701848200

The DNA replication priming protein, PriA, is required for homologous recombination and double-strand break repair

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M701848200

The DNA replication protein PriA and the recombination protein RecG bind D-loops.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M701848200

Two modes of PriA binding to DNA.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M701848200

Duplex opening by primosome protein PriA for replisome assembly on a recombination intermediate

21 January 2018

1 reference

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Replication fork assembly at recombination intermediates is required for bacterial growth

21 January 2018

1 reference

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Association of phiX174 DNA-dependent ATPase activity with an Escherichia coli protein, replication factor Y, required for in vitro synthesis of phiX174 DNA

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M701848200

Escherichia coli replication factor Y, a component of the primosome, can act as a DNA helicase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M701848200

Bacterial DNA replication initiation factor priA is related to proteins belonging to the 'DEAD-box' family

21 January 2018

1 reference

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DNA binding of PriA protein requires cooperation of the N-terminal D-loop/arrested-fork binding and C-terminal helicase domains.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M701848200

Properties of the PriA helicase domain and its role in binding PriA to specific DNA structures

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M701848200

A critical role of the 3' terminus of nascent DNA chains in recognition of stalled replication forks.

21 January 2018

1 reference

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Stabilization of a stalled replication fork by concerted actions of two helicases

21 January 2018

1 reference

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Escherichia coli and Bacillus subtilis PriA proteins essential for recombination-dependent DNA replication: involvement of ATPase/helicase activity of PriA for inducible stable DNA replication.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M701848200

ATPase/helicase motif mutants of Escherichia coli PriA protein essential for recombination-dependent DNA replication.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M701848200

Crystallization and preliminary crystallographic analysis of the N-terminal domain of PriA from Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M701848200

Escherichia coli PriA helicase: fork binding orients the helicase to unwind the lagging strand side of arrested replication forks

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M701848200

Direct rescue of stalled DNA replication forks via the combined action of PriA and RecG helicase activities.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M701848200

21 January 2018

Identifiers

DOI

10.1074/JBC.M701848200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:17483094%20AND%20SRC:MED&resulttype=core&format=json

30 December 2019

1 reference