(Q46375266)

English

Thr-774 (transmembrane segment M5), Val-920 (M8), and Glu-954 (M9) are involved in Na+ transport, and Gln-923 (M8) is essential for Na,K-ATPase activity

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

21 December 2017

http://europepmc.org/abstract/MED/15764602

Thr-774 (transmembrane segment M5), Val-920 (M8), and Glu-954 (M9) are involved in Na+ transport, and Gln-923 (M8) is essential for Na,K-ATPase activity (English)

1 reference

Europe PubMed Central

PubMed publication ID

21 December 2017

http://europepmc.org/abstract/MED/15764602

transmembrane transport

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transmembrane protein

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author name string

Toshiaki Imagawa

1

1 reference

Europe PubMed Central

PubMed publication ID

21 December 2017

http://europepmc.org/abstract/MED/15764602

Tetsuya Yamamoto

2

1 reference

Europe PubMed Central

PubMed publication ID

21 December 2017

http://europepmc.org/abstract/MED/15764602

Shunji Kaya

3

1 reference

Europe PubMed Central

PubMed publication ID

21 December 2017

http://europepmc.org/abstract/MED/15764602

Kazuyasu Sakaguchi

4

1 reference

Europe PubMed Central

PubMed publication ID

21 December 2017

http://europepmc.org/abstract/MED/15764602

Kazuya Taniguchi

5

1 reference

Europe PubMed Central

PubMed publication ID

21 December 2017

http://europepmc.org/abstract/MED/15764602

language of work or name

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publication date

11 March 2005

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Europe PubMed Central

PubMed publication ID

21 December 2017

http://europepmc.org/abstract/MED/15764602

Journal of Biological Chemistry

1 reference

Europe PubMed Central

PubMed publication ID

21 December 2017

http://europepmc.org/abstract/MED/15764602

280

1 reference

Europe PubMed Central

PubMed publication ID

21 December 2017

http://europepmc.org/abstract/MED/15764602

19

1 reference

Europe PubMed Central

PubMed publication ID

21 December 2017

http://europepmc.org/abstract/MED/15764602

18736-18744

1 reference

Europe PubMed Central

PubMed publication ID

21 December 2017

http://europepmc.org/abstract/MED/15764602

Occluded cations in active transport

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

Biochemistry of Na,K-ATPase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

Structure and mechanism of Na,K-ATPase: functional sites and their interactions

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

Evolution of substrate specificities in the P-type ATPase superfamily.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

Structural similarities of Na,K-ATPase and SERCA, the Ca(2+)-ATPase of the sarcoplasmic reticulum

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

Structure-function relationships of Na(+), K(+), ATP, or Mg(2+) binding and energy transduction in Na,K-ATPase.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

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.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

Glutamic acid 327 in the sheep alpha 1 isoform of Na+,K(+)-ATPase stabilizes a K(+)-induced conformational change

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

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.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

Critical effects on catalytic function produced by amino acid substitutions at Asp804 and Asp808 of the alpha1 isoform of Na,K-ATPase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

Mutation to the glutamate in the fourth membrane segment of Na+,K+-ATPase and Ca2+-ATPase affects cation binding from both sides of the membrane and destabilizes the occluded enzyme forms

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

Structure-function relationships of E1-E2 transitions and cation binding in Na,K-pump protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

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.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

Alanine scanning mutagenesis of oxygen-containing amino acids in the transmembrane region of the Na,K-ATPase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

Residues of the fourth transmembrane segments of the Na,K-ATPase and the gastric H,K-ATPase contribute to cation selectivity

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

Mutation of aspartate 804 of Na(+),K(+)-ATPase modifies the cation binding pocket and thereby generates a high Na(+)-ATPase activity

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

Homology modeling of the cation binding sites of Na+K+-ATPase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

Two Ca2+ ATPase genes: homologies and mechanistic implications of deduced amino acid sequences

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

Molecular cloning of three distinct forms of the Na+,K+-ATPase alpha-subunit from rat brain

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

cDNA cloning and sequence determination of pig gastric (H+ + K+)-ATPase.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

Does binding of ouabain to human alpha1-subunit of Na+, K+-ATPase affect the ATPase activity of adjacent rat alpha1-subunit?

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

DNA sequencing with chain-terminating inhibitors

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

Replacement of several single amino acid side chains exposed to the inside of the ATP-binding pocket induces different extents of affinity change in the high and low affinity ATP-binding sites of rat Na/K-ATPase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

The Amino Acid Sequence 442GDASE446 in Na/K-ATPase Is an Important Motif in Forming the High and Low Affinity ATP Binding Pockets

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

The oligomeric nature of Na/K-transport ATPase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

The M4M5 cytoplasmic loop of the Na,K-ATPase, overexpressed in Escherichia coli, binds nucleoside triphosphates with the same selectivity as the intact native protein.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500137200

21 January 2018

Identifiers

10.1074/JBC.M500137200

1 reference

Europe PubMed Central

PubMed publication ID

21 December 2017

http://europepmc.org/abstract/MED/15764602

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

21 December 2017

http://europepmc.org/abstract/MED/15764602

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