Functional role of polar amino acid residues in Na+/H+ exchangers (Q28367179)

TASK-3, a new member of the tandem pore K(+) channel family

Europe PubMed Central

title

Functional role of polar amino acid residues in Na+/H+ exchangers (English)

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author name string

C A Wiebe

series ordinal

1

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E R Dibattista

series ordinal

2

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L Fliegel

series ordinal

3

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language of work or name

English

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publication date

1 July 2001

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published in

Biochemical Journal

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volume

357

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issue

Pt 1

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page(s)

1-10

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cites work

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29 September 2017

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29 September 2017

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2 June 2018

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Glutamic acid 327 in the sheep alpha 1 isoform of Na+,K(+)-ATPase is a pivotal residue for cation-induced conformational changes

2 June 2018

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2 June 2018

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Metal-tetracycline/H+ antiporter of Escherichia coli encoded by a transposon Tn10. Histidine 257 plays an essential role in H+ translocation.

2 June 2018

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2 June 2018

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2 June 2018

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2 June 2018

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27 November 2018

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27 November 2018

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27 November 2018

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27 November 2018

1 reference

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27 November 2018

1 reference

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Glutamate 779, an intramembrane carboxyl, is essential for monovalent cation binding by the Na,K-ATPase.

27 November 2018

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Three aspartic residues in membrane-spanning regions of Na+/H+ antiporter from Vibrio alginolyticus play a role in the activity of the carrier.

27 November 2018

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Characterization of Na+/H(+)-antiporter gene closely related to the salt-tolerance of yeast Zygosaccharomyces rouxii

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1 reference

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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

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1 reference

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Functional consequences of substitutions of the carboxyl residue glutamate 779 of the Na,K-ATPase

1 reference

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1 reference

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