A point mutation (G338S) and its suppressor mutations affect both the pH response of the NhaA-Na+/H+ antiporter as well as the growth phenotype of Escherichia coli (Q77359753)

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scientific article published on 01 October 1998

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English	A point mutation (G338S) and its suppressor mutations affect both the pH response of the NhaA-Na+/H+ antiporter as well as the growth phenotype of Escherichia coli	scientific article published on 01 October 1998

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scholarly article

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9756882%20AND%20SRC:MED&resulttype=core&format=json

5 December 2019

A point mutation (G338S) and its suppressor mutations affect both the pH response of the NhaA-Na+/H+ antiporter as well as the growth phenotype of Escherichia coli (English)

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9756882%20AND%20SRC:MED&resulttype=core&format=json

5 December 2019

Escherichia coli

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inferred from title

2

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5 December 2019

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A Rimon

1

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5 December 2019

Z Kariv

3

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9756882%20AND%20SRC:MED&resulttype=core&format=json

5 December 2019

E Padan

4

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5 December 2019

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publication date

1 October 1998

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5 December 2019

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7

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Journal of Biological Chemistry

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5 December 2019

273

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5 December 2019

41

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5 December 2019

26470-26476

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5 December 2019

Molecular physiology of Na+/H+ antiporters, key transporters in circulation of Na+ and H+ in cells

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.41.26470

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.41.26470

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.41.26470

21 January 2018

Replacements of histidine 226 of NhaA-Na+/H+ antiporter of Escherichia coli. Cysteine (H226C) or serine (H226S) retain both normal activity and pH sensitivity, aspartate (H226D) shifts the pH profile toward basic pH, and alanine (H226A) inactivates

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.41.26470

21 January 2018

An Early Step in Pseudomonas Exotoxin Action Is Removal of the Terminal Lysine Residue, Which Allows Binding to the KDEL Receptor

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.41.26470

21 January 2018

A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.41.26470

21 January 2018

Histidine 225, a residue of the NhaA-Na+/H+ antiporter of Escherichia coli is exposed and faces the cell exterior

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.41.26470

21 January 2018

Ion extrusion systems in Escherichia coli

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.41.26470

21 January 2018

Sodium-proton antiport in isolated membrane vesicles of Escherichia coli

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.41.26470

21 January 2018

Linearization of the Bradford protein assay increases its sensitivity: theoretical and experimental studies

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.41.26470

21 January 2018

The Proton Electrochemical Gradient in Escherichia coli Cells

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.41.26470

21 January 2018

The Na+-specific interaction between the LysR-type regulator, NhaR, and the nhaA gene encoding the Na+/H+ antiporter of Escherichia coli

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.41.26470

21 January 2018

Identification and characterization of functional residues in a Na+/H+ antiporter (NhaA) from Escherichia coli by random mutagenesis.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.41.26470

21 January 2018

Topological analysis of NhaA, a Na+/H+ antiporter from Escherichia coli.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.41.26470

21 January 2018

Essential aspartic acid residues, Asp-133, Asp-163 and Asp-164, in the transmembrane helices of a Na+/H+ antiporter (NhaA) from Escherichia coli

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.41.26470

21 January 2018

Identifiers

10.1074/JBC.273.41.26470

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9756882%20AND%20SRC:MED&resulttype=core&format=json

5 December 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9756882%20AND%20SRC:MED&resulttype=core&format=json

5 December 2019

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