(Q50467116)

English

Monomers of the NhaA Na+/H+ antiporter of Escherichia coli are fully functional yet dimers are beneficial under extreme stress conditions at alkaline pH in the presence of Na+ or Li+.

scientific article published on 17 July 2007

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scholarly article

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Europe PubMed Central

PubMed publication ID

14 March 2018

http://europepmc.org/abstract/MED/17635927

Monomers of the NhaA Na+/H+ antiporter of Escherichia coli are fully functional yet dimers are beneficial under extreme stress conditions at alkaline pH in the presence of Na+ or Li+. (English)

1 reference

Europe PubMed Central

PubMed publication ID

14 March 2018

http://europepmc.org/abstract/MED/17635927

Escherichia coli

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based on heuristic

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Abraham Rimon

1

1 reference

Europe PubMed Central

PubMed publication ID

14 March 2018

http://europepmc.org/abstract/MED/17635927

Tzvi Tzubery

2

1 reference

Europe PubMed Central

PubMed publication ID

14 March 2018

http://europepmc.org/abstract/MED/17635927

Etana Padan

3

1 reference

Europe PubMed Central

PubMed publication ID

14 March 2018

http://europepmc.org/abstract/MED/17635927

language of work or name

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publication date

17 July 2007

1 reference

Europe PubMed Central

PubMed publication ID

14 March 2018

http://europepmc.org/abstract/MED/17635927

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

14 March 2018

http://europepmc.org/abstract/MED/17635927

282

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Europe PubMed Central

PubMed publication ID

14 March 2018

http://europepmc.org/abstract/MED/17635927

37

1 reference

Europe PubMed Central

PubMed publication ID

14 March 2018

http://europepmc.org/abstract/MED/17635927

26810-26821

1 reference

Europe PubMed Central

PubMed publication ID

14 March 2018

http://europepmc.org/abstract/MED/17635927

NhaA of Escherichia coli, as a model of a pH-regulated Na+/H+antiporter

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Kinetic dissection of two distinct proton binding sites in Na+/H+ exchangers by measurement of reverse mode reaction

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Structural and functional analysis of the Na+/H+ exchanger

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Mutation E252C Increases Drastically the K Value for Na+ and Causes an Alkaline Shift of the pH Dependence of NhaA Na+/H+ Antiporter of Escherichia coli

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Oligomerization of NhaA, the Na+/H+ antiporter of Escherichia coli in the membrane and its functional and structural consequences.

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Three-dimensional structure of the ion-coupled transport protein NhaA.

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Crucial steps in the structure determination of the Na+/H+ antiporter NhaA in its native conformation

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Trans membrane domain IV is involved in ion transport activity and pH regulation of the NhaA-Na(+)/H(+) antiporter of Escherichia coli

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Functional and structural interactions of the transmembrane domain X of NhaA, Na+/H+ antiporter of Escherichia coli, at physiological pH.

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Site-directed mutagenesis by overlap extension using the polymerase chain reaction

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa

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Proximity of cytoplasmic and periplasmic loops in NhaA Na+/H+ antiporter of Escherichia coli as determined by site-directed thiol cross-linking

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21 January 2018

Characterization of a Na+/H+ antiporter gene of Escherichia coli

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Sodium-proton antiport in isolated membrane vesicles of Escherichia coli

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Identification of membrane domains of the Na+/H+ antiporter (NhaA) protein from Helicobacter pylori required for ion transport and pH sensing

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Unraveling functional and structural interactions between transmembrane domains IV and XI of NhaA Na+/H+ antiporter of Escherichia coli

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Histidine-226 is part of the pH sensor of NhaA, a Na+/H+ antiporter in Escherichia coli.

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Oligomeric state of membrane transport proteins analyzed with blue native electrophoresis and analytical ultracentrifugation

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The SecYEG preprotein translocation channel is a conformationally dynamic and dimeric structure

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Projection structure and oligomeric state of the osmoregulated sodium/glycine betaine symporter BetP of Corynebacterium glutamicum

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Identifiers

10.1074/JBC.M704469200

1 reference

Europe PubMed Central

PubMed publication ID

14 March 2018

http://europepmc.org/abstract/MED/17635927

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

14 March 2018

http://europepmc.org/abstract/MED/17635927

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