(Q48946231)

English

Significance of the glutamic acid residues Glu334, Glu959, and Glu960 of the alpha subunits of Torpedo Na+, K+ pumps for transport activity and ouabain binding.

scientific article published in January 1998

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scholarly article

1 reference

Europe PubMed Central

17 February 2018

http://europepmc.org/abstract/MED/9459592

Significance of the glutamic acid residues Glu334, Glu959, and Glu960 of the alpha subunits of Torpedo Na+, K+ pumps for transport activity and ouabain binding. (English)

1 reference

Europe PubMed Central

17 February 2018

http://europepmc.org/abstract/MED/9459592

author name string

L A Vasilets

1

1 reference

Europe PubMed Central

17 February 2018

http://europepmc.org/abstract/MED/9459592

K Takeda

2

1 reference

Europe PubMed Central

17 February 2018

http://europepmc.org/abstract/MED/9459592

M Kawamura

3

1 reference

Europe PubMed Central

17 February 2018

http://europepmc.org/abstract/MED/9459592

W Schwarz

4

1 reference

Europe PubMed Central

17 February 2018

http://europepmc.org/abstract/MED/9459592

publication date

1 January 1998

1 reference

Europe PubMed Central

17 February 2018

http://europepmc.org/abstract/MED/9459592

Biochimica et Biophysica Acta

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Europe PubMed Central

17 February 2018

http://europepmc.org/abstract/MED/9459592

1368

1 reference

Europe PubMed Central

17 February 2018

http://europepmc.org/abstract/MED/9459592

1

1 reference

Europe PubMed Central

17 February 2018

http://europepmc.org/abstract/MED/9459592

137-149

1 reference

Europe PubMed Central

17 February 2018

http://europepmc.org/abstract/MED/9459592

Structure-function relationships of cation binding in the Na+/K(+)-ATPase.

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The influence of some cations on an adenosine triphosphatase from peripheral nerves

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The effect of membrane potential on the mammalian sodium-potassium pump reconstituted into phospholipid vesicles.

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Voltage dependence of the Na-K pump

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Chemical modification of Glu-953 of the alpha chain of Na+,K(+)-ATPase associated with inactivation of cation occlusion

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7 January 2021

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

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

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A Glu329-->Gln variant of the alpha-subunit of the rat kidney Na+,K(+)-ATPase can sustain active transport of Na+ and K+ and Na+,K(+)-activated ATP hydrolysis with normal turnover number

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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.

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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

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Structure-function relationships of Na+/K(+)-pumps expressed in Xenopus oocytes.

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Expression of functional (Na+ + K+)-ATPase from cloned cDNAs

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Activation of protein kinase C by phorbol ester induces downregulation of the Na+/K(+)-ATPase in oocytes of Xenopus laevis.

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A negative slope in the current-voltage relationship of the Na+/K+ pump in Xenopus oocytes produced by reduction of external [K+].

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Regulation of endogenous and expressed Na+/K+ pumps in Xenopus oocytes by membrane potential and stimulation of protein kinases

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Inward-directed current generated by the Na+,K+ pump in Na(+)- and K(+)-free medium.

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7 January 2021

Characteristics of Na+/K(+)-ATPase mediated proton current in Na(+)- and K(+)-free extracellular solutions. Indications for kinetic similarities between H+/K(+)-ATPase and Na+/K(+)-ATPase.

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7 January 2021

A conformation of Na(+)-K+ pump is permeable to proton.

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7 January 2021

Voltage-dependent stimulation of Na+/K+-pump current by external cations: selectivity of different K+ congeners

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7 January 2021

Voltage-dependent inhibition of the sodium pump by external sodium: species differences and possible role of the N-terminus of the alpha-subunit.

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7 January 2021

ICAM-1 directs migration and localization of interstitial leukocytes in experimental glomerulonephritis

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7 January 2021

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

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7 January 2021

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.

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7 January 2021

Location of high affinity Ca2+-binding sites within the predicted transmembrane domain of the sarcoplasmic reticulum Ca2+-ATPase

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7 January 2021

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

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7 January 2021

[Na] and [K] dependence of the Na/K pump current-voltage relationship in guinea pig ventricular myocytes

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7 January 2021

Extracellular access to the Na,K pump: pathway similar to ion channel

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7 January 2021

Charge movement by the Na/K pump in Xenopus oocytes

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7 January 2021

Channel-like function of the Na,K pump probed at microsecond resolution in giant membrane patches

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7 January 2021

Molecular model of the action potential sodium channel

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A structural motif for the voltage-gated potassium channel pore

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7 January 2021

Substitution of glutamic 779 with alanine in the Na,K-ATPase alpha subunit removes voltage dependence of ion transport.

1 reference

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

1 reference

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

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

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7 January 2021

Identifiers

10.1016/S0005-2736(97)00195-8

1 reference

Europe PubMed Central

17 February 2018

http://europepmc.org/abstract/MED/9459592

1 reference

Europe PubMed Central

17 February 2018

http://europepmc.org/abstract/MED/9459592

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