(Q46035863)

18 December 2017

title

Na+-K+-ATPase alpha-subunit containing Q905-V930 of gastric H+-K+-ATPase alpha preferentially assembles with H+-K+-ATPase beta. (English)

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18 December 2017

author name string

S G Wang

1

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18 December 2017

K A Eakle

2

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18 December 2017

R Levenson

3

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18 December 2017

R A Farley

4

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18 December 2017

language of work or name

English

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publication date

1 March 1997

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18 December 2017

American Journal of Physiology

published in

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18 December 2017

volume

272

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18 December 2017

issue

3 Pt 1

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18 December 2017

page(s)

C923-30

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18 December 2017

Topology of the Na,K-ATPase. Evidence for externalization of a labile transmembrane structure during heating.

cites work

1 reference

https://api.crossref.org/works/10.1152%2FAJPCELL.1997.272.3.C923

Functional expression of gastric H+,K(+)-ATPase and site-directed mutagenesis of the putative cation binding site and catalytic center

21 January 2018

1 reference

https://api.crossref.org/works/10.1152%2FAJPCELL.1997.272.3.C923

Hydrophobic C-terminal amino acids in the beta-subunit are involved in assembly with the alpha-subunit of Na,K-ATPase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1152%2FAJPCELL.1997.272.3.C923

Kinetic properties of the alpha 2 beta 1 and alpha 2 beta 2 isozymes of the Na,K-ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1152%2FAJPCELL.1997.272.3.C923

Comparison of the enzymatic properties of the Na,K-ATPase alpha 3 beta 1 and alpha 3 beta 2 isozymes

21 January 2018

1 reference

https://api.crossref.org/works/10.1152%2FAJPCELL.1997.272.3.C923

The rat distal colon P-ATPase alpha subunit encodes a ouabain-sensitive H+, K+-ATPase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1152%2FAJPCELL.1997.272.3.C923

High-affinity ouabain binding by yeast cells expressing Na+, K(+)-ATPase alpha subunits and the gastric H+, K(+)-ATPase beta subunit

21 January 2018

1 reference

https://api.crossref.org/works/10.1152%2FAJPCELL.1997.272.3.C923

The influence of beta subunit structure on the interaction of Na+/K(+)-ATPase complexes with Na+. A chimeric beta subunit reduces the Na+ dependence of phosphoenzyme formation from ATP.

21 January 2018

1 reference

https://api.crossref.org/works/10.1152%2FAJPCELL.1997.272.3.C923

Maturation of the catalytic alpha-subunit of Na,K-ATPase during intracellular transport

21 January 2018

1 reference

https://api.crossref.org/works/10.1152%2FAJPCELL.1997.272.3.C923

An ion-transporting ATPase encodes multiple apical localization signals

21 January 2018

1 reference

https://api.crossref.org/works/10.1152%2FAJPCELL.1997.272.3.C923

The beta subunit modulates potassium activation of the Na-K pump.

21 January 2018

1 reference

https://api.crossref.org/works/10.1152%2FAJPCELL.1997.272.3.C923

Modulation of the Na,K-pump function by beta subunit isoforms

21 January 2018

1 reference

https://api.crossref.org/works/10.1152%2FAJPCELL.1997.272.3.C923

Comparison of the effects of potassium on ouabain binding to native and site-directed mutants of Na,K-ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1152%2FAJPCELL.1997.272.3.C923

Purification and characterization of (Na+ plus K+ )-ATPase. 3. Purification from the outer medulla of mammalian kidney after selective removal of membrane components by sodium dodecylsulphate

21 January 2018

1 reference

https://api.crossref.org/works/10.1152%2FAJPCELL.1997.272.3.C923

Membrane disposition of the M5-M6 hairpin of Na+,K(+)-ATPase alpha subunit is ligand dependent.

21 January 2018

1 reference

https://api.crossref.org/works/10.1152%2FAJPCELL.1997.272.3.C923

10.1152/AJPCELL.1997.272.3.C923

21 January 2018

Identifiers

DOI

0 references

PubMed ID

9124528

1 reference

18 December 2017