(Q57976571)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10594836%20AND%20SRC:MED&resulttype=core&format=json

2 November 2019

title

A molecular switch in SecA protein couples ATP hydrolysis to protein translocation (English)

1 reference

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2 November 2019

4

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2 November 2019

Anastassios Economou

8

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2 November 2019

author name string

S Karamanou

1

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2 November 2019

E Vrontou

2

1 reference

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2 November 2019

G Sianidis

3

1 reference

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2 November 2019

T Roos

5

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2 November 2019

A Kuhn

6

1 reference

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2 November 2019

A S Politou

7

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2 November 2019

language of work or name

English

0 references

publication date

1 December 1999

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2 November 2019

published in

Molecular Microbiology

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2 November 2019

volume

34

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2 November 2019

page(s)

1133-1145

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2 November 2019

issue

5

1 reference

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The C terminus of SecA is involved in both lipid binding and SecB binding.

2 November 2019

cites work

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01686.X

Crystal structure of RNA helicase from genotype 1b hepatitis C virus. A feasible mechanism of unwinding duplex RNA

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01686.X

Distinct catalytic roles of the SecYE, SecG and SecDFyajC subunits of preprotein translocase holoenzyme

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01686.X

The SecDFyajC domain of preprotein translocase controls preprotein movement by regulating SecA membrane cycling

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01686.X

Following the leader: bacterial protein export through the Sec pathway.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01686.X

SecA membrane cycling at SecYEG is driven by distinct ATP binding and hydrolysis events and is regulated by SecD and SecF.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01686.X

Both an N-terminal 65-kDa domain and a C-terminal 30-kDa domain of SecA cycle into the membrane at SecYEG during translocation

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01686.X

The molecular chaperone SecB is released from the carboxy-terminus of SecA during initiation of precursor protein translocation.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01686.X

The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01686.X

Autogenous translation regulation by Escherichia coli ATPase SecA may be mediated by an intrinsic RNA helicase activity of this protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01686.X

The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01686.X

SecY and SecA interact to allow SecA insertion and protein translocation across the Escherichia coli plasma membrane

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01686.X

Membrane deinsertion of SecA underlying proton motive force-dependent stimulation of protein translocation

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01686.X

RNA helicase activity of Escherichia coli SecA protein.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01686.X

Separable ATPase and Membrane Insertion Domains of the SecA Subunit of Preprotein Translocase

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01686.X

Topology of the integral membrane form of Escherichia coli SecA protein reveals multiple periplasmically exposed regions and modulation by ATP binding.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01686.X

Interaction of Diphtheria Toxin T Domain with Molten Globule-Like Proteins and Its Implications for Translocation

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01686.X

ΔμH+ and ATP function at different steps of the catalytic cycle of preprotein translocase

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01686.X

Escherichia coli SecA shape and dimensions

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01686.X

Identification of a region of interaction between Escherichia coli SecA and SecY proteins.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01686.X

Stability and solvent accessibility of SecA protein of Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01686.X

Stepwise movement of preproteins in the process of translocation across the cytoplasmic membrane of Escherichia coli.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01686.X

The catalytic cycle of the escherichia coli SecA ATPase comprises two distinct preprotein translocation events

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01686.X

Pro-OmpA derivatives with a His6 tag in their N-terminal "translocation initiation domains" are arrested by Ni2+ at an early post-targeting stage of translocation.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01686.X

Interaction of SecB with soluble SecA 1

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01686.X

Targeting and assembly of periplasmic and outer-membrane proteins in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01686.X

Preprotein transfer to the Escherichia coli translocase requires the co‐operative binding of SecB and the signal sequence to SecA

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01686.X

The carboxyl-terminal region is essential for Sec-A dimerization

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01686.X

The bacterial SecY/E translocation complex forms channel-like structures similar to those of the eukaryotic Sec61p complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01686.X

Synthetic signal peptides specifically recognize SecA and stimulate ATPase activity in the absence of preprotein

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.1999.01686.X

10.1046/J.1365-2958.1999.01686.X

21 January 2018

Identifiers

DOI

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10594836%20AND%20SRC:MED&resulttype=core&format=json

2 November 2019

1 reference