Evidence that Ser775 in the alpha subunit of the Na,K-ATPase is a residue in the cation binding pocket (Q73735513)

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6 November 2019

title

Evidence that Ser775 in the alpha subunit of the Na,K-ATPase is a residue in the cation binding pocket (English)

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6 November 2019

4

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6 November 2019

author name string

R Blostein

1

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6 November 2019

A Wilczynska

2

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6 November 2019

S J Karlish

3

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6 November 2019

J B Lingrel

5

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6 November 2019

language of work or name

English

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publication date

1 October 1997

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Journal of Biological Chemistry

6 November 2019

published in

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6 November 2019

volume

272

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6 November 2019

issue

40

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6 November 2019

page(s)

24987-24993

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Structural organization, ion transport, and energy transduction of P-type ATPases

6 November 2019

cites work

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https://api.crossref.org/works/10.1074%2FJBC.272.40.24987

Occluded cations in active transport

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.272.40.24987

The order of release of sodium and addition of potassium in the sodium-potassium pump reaction mechanism

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.40.24987

Functional consequences of mutation Asn326-->Leu in the 4th transmembrane segment of the alpha-subunit of the rat kidney Na+, K(+)-ATPase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.40.24987

Site-directed mutagenesis of the Na,K-ATPase: consequences of substitutions of negatively-charged amino acids localized in the transmembrane domains.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.40.24987

Glutamate 329 located in the fourth transmembrane segment of the alpha-subunit of the rat kidney Na+,K+-ATPase is not an essential residue for active transport of sodium and potassium ions.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.40.24987

Amino acid replacement of Asp369 in the sheep alpha 1 isoform eliminates ATP and phosphate stimulation of [3H]ouabain binding to the Na+, K(+)-ATPase without altering the cation binding properties of the enzyme

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.40.24987

Mutant Glu781-->Ala of the rat kidney Na+,K(+)-ATPase displays low cation affinity and catalyzes ATP hydrolysis at a high rate in the absence of potassium ions.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.40.24987

Substitutions of glutamate 781 in the Na,K-ATPase alpha subunit demonstrate reduced cation selectivity and an increased affinity for ATP.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.40.24987

Site-directed mutagenesis of a predicted cation binding site of Na, K-ATPase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.40.24987

Asp804 and Asp808 in the transmembrane domain of the Na,K-ATPase alpha subunit are cation coordinating residues

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.40.24987

Identification of Asp804 and Asp808 as Na+ and K+ coordinating residues in alpha-subunit of renal Na,K-ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.40.24987

Substitutions of serine 775 in the alpha subunit of the Na,K-ATPase selectively disrupt K+ high affinity activation without affecting Na+ interaction.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.40.24987

Structure/function analysis of the amino-terminal region of the 1 and 2 subunits of Na,K-ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.40.24987

A simple method for the preparation of 32P-labelled adenosine triphosphate of high specific activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.40.24987

The amino-terminal segment of the catalytic subunit of kidney Na,K-ATPase regulates the potassium deocclusion pathway of the reaction cycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.40.24987

Novel aromatic isothiouronium derivatives which act as high affinity competitive antagonists of alkali metal cations on Na/K-ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.40.24987

ATP hydrolysis associated with an uncoupled sodium flux through the sodium pump: evidence for allosteric effects of intracellular ATP and extracellular sodium

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.40.24987

Sodium ions, acting at high-affinity extracellular sites, inhibit sodium-ATPase activity of the sodium pump by slowing dephosphorylation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.40.24987

Sodium pump-mediated ATP:ADP exchange. The sided effects of sodium and potassium ions

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.40.24987

Red cell sodium fluxes catalysed by the sodium pump in the absence of K+ and ADP

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.40.24987

The interaction of potassium ions and ATP on the sodium pump of resealed red cell ghosts.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.40.24987

Comparison of rates of cation release and of conformational change in dog kidney Na, K-ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.40.24987

Dialkylglycine decarboxylase structure: bifunctional active site and alkali metal sites

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.40.24987

21 January 2018

Identifiers

DOI

10.1074/JBC.272.40.24987

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9312104%20AND%20SRC:MED&resulttype=core&format=json

6 November 2019

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