Identification of the site of inhibition by omeprazole of a alpha-beta fusion protein of the H,K-ATPase using site-directed mutagenesis. (Q41037593)

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11 November 2019

title

Identification of the site of inhibition by omeprazole of a alpha-beta fusion protein of the H,K-ATPase using site-directed mutagenesis (English)

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11 November 2019

1 reference

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11 November 2019

Z Corbett

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11 November 2019

D Bayle

series ordinal

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11 November 2019

S J Karlish

series ordinal

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11 November 2019

G Sachs

series ordinal

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11 November 2019

language of work or name

English

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publication date

1 May 1998

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Journal of Biological Chemistry

11 November 2019

published in

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11 November 2019

volume

273

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11 November 2019

issue

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11 November 2019

page(s)

13719-13728

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describes a project that uses

11 November 2019

site-directed mutagenesis

1 reference

based on heuristic

inferred from title

cites work

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

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Structure-function relationships in the Na,K-ATPase alpha subunit: site-directed mutagenesis of glutamine-111 to arginine and asparagine-122 to aspartic acid generates a ouabain-resistant enzyme

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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

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Expression of sodium pump activities in BALB/c 3T3 cells transfected with cDNA encoding alpha 3-subunits of rat brain Na+,K+-ATPase

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Amino Acid Replacement of Asp369 in the Sheep α1 Isoform Eliminates ATP and Phosphate Stimulation of [3]H Ouabain Binding to the Na+,K+-ATPase without Altering the Cation Binding Properties of the Enzyme

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Structure-function relationships of cation translocation by Ca(2+)- and Na+, K(+)-ATPases studied by site-directed mutagenesis.

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The site of action of pantoprazole in the gastric H+/K(+)-ATPase

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Characterization of a beta subunit of the gastric H+/K(+)-transporting ATPase

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The 60- to 90-kDa parietal cell autoantigen associated with autoimmune gastritis is a beta subunit of the gastric H+/K(+)-ATPase (proton pump).

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On the reversibility of binding of cardiotonic steroids to a partially purified (Na+K)-activated adenosinetriphosphatase from beef brain

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Role of negatively charged residues in the fifth and sixth transmembrane domains of the catalytic subunit of gastric H+,K+-ATPase

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Mutational Analysis of Putative SCH 28080 Binding Sites of the Gastric H+,K+-ATPase

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Location of the carbohydrates present in the HK-ATPase vesicles isolated from hog gastric mucosa

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21 January 2018

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21 January 2018

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Only the first and the last hydrophobic segments in the COOH-terminal third of Na,K-ATPase alpha subunit initiate and halt, respectively, membrane translocation of the newly synthesized polypeptide. Implications for the membrane topology

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