(Q34558712)

3 August 2017

title

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

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3 August 2017

Carola Hunte

5

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Hartmut Michel

series ordinal

4

object named as

Hartmut Michel

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3 August 2017

Emanuela Screpanti

1

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3 August 2017

Etana Padan

series ordinal

2

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3 August 2017

Abraham Rimon

series ordinal

3

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3 August 2017

language of work or name

English

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publication date

15 July 2006

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Journal of Molecular Biology

3 August 2017

published in

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3 August 2017

volume

362

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3 August 2017

issue

2

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3 August 2017

page(s)

192-202

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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

3 August 2017

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Structure of a Na+/H+ antiporter and insights into mechanism of action and regulation by pH.

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Projection structure of NhaA, a secondary transporter from Escherichia coli, at 4.0 A resolution

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11 October 2022

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Assessing oligomerization of membrane proteins by four-pulse DEER: pH-dependent dimerization of NhaA Na+/H+ antiporter of E. coli.

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Na(+)/H(+) antiporters.

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Diversity of the mammalian sodium/proton exchanger SLC9 gene family

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Evolutionary origins of eukaryotic sodium/proton exchangers

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Vacuolar cation/H+ exchange, ion homeostasis, and leaf development are altered in a T‐DNA insertional mutant of AtNHX1, the Arabidopsis vacuolar Na+/H+ antiporter

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Production and characterization of monoclonal antibodies directed against native epitopes of NhaA, the Na+ /H+ antiporter of Escherichia coli

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

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

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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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11 October 2022

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A pH-dependent conformational change of NhaA Na(+)/H(+) antiporter of Escherichia coli involves loop VIII-IX, plays a role in the pH response of the protein, and is maintained by the pure protein in dodecyl maltoside

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11 October 2022

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

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Lipids in membrane protein structures

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Electron-density map interpretation

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11 October 2022

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The expanding family of eucaryotic Na(+)/H(+) exchangers

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11 October 2022

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Kinetics of charge translocation in the passive downhill uptake mode of the Na+/H+ antiporter NhaA of Escherichia coli.

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11 October 2022

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Interaction of membrane proteins and lipids with solubilizing detergents

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11 October 2022

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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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11 October 2022

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Alkaline pH homeostasis in bacteria: new insights

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11 October 2022

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Functional analysis of amino acids of the Na+/H+ exchanger that are important for proton translocation

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11 October 2022

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Crystallisation of membrane proteins mediated by antibody fragments

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11 October 2022

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

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.JMB.2006.07.019

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

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.JMB.2006.07.019

[27] Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods.

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.JMB.2006.07.019

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

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.JMB.2006.07.019

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

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.JMB.2006.07.019

The Monoclonal Antibody 1F6 Identifies a pH-dependent Conformational Change in the Hydrophilic NH2Terminus of NhaA Na+/H+Antiporter ofEscherichia coli

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.JMB.2006.07.019

Identifiers

DOI

10.1016/J.JMB.2006.07.019

1 reference

3 August 2017

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