(Q38364012)

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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

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Europe PubMed Central

PubMed publication ID

2 September 2017

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 (English)

1 reference

Europe PubMed Central

PubMed publication ID

2 September 2017

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Satomi Teramachi

1

1 reference

Europe PubMed Central

PubMed publication ID

2 September 2017

Toshiaki Imagawa

2

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Europe PubMed Central

PubMed publication ID

2 September 2017

Shunji Kaya

3

1 reference

Europe PubMed Central

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2 September 2017

Kazuya Taniguchi

4

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Europe PubMed Central

PubMed publication ID

2 September 2017

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publication date

22 July 2002

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Europe PubMed Central

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2 September 2017

Journal of Biological Chemistry

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Europe PubMed Central

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2 September 2017

277

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Europe PubMed Central

PubMed publication ID

2 September 2017

40

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Europe PubMed Central

PubMed publication ID

2 September 2017

37394-37400

1 reference

Europe PubMed Central

PubMed publication ID

2 September 2017

Occluded cations in active transport

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204772200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204772200

21 January 2018

The oligomeric nature of Na/K-transport ATPase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204772200

21 January 2018

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

1 reference

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21 January 2018

Chemical modification as an approach to elucidation of sodium pump structure-function relations

1 reference

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21 January 2018

Identification of an amino acid in the ATP binding site of Na+/K(+)-ATPase after photochemical labeling with 8-azido-ATP.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204772200

21 January 2018

Site-directed mutagenesis of the sodium pump: analysis of mutations to amino acids in the proposed nucleotide binding site by stable oxygen isotope exchange

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204772200

21 January 2018

Differential effects of reduced glycoprotein VI levels on activation of murine platelets by glycoprotein VI ligands

1 reference

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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.M204772200

21 January 2018

DNA sequencing with chain-terminating inhibitors

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204772200

21 January 2018

Selective coupling with K+ currents of muscarinic acetylcholine receptor subtypes in NG108-15 cells.

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21 January 2018

A new technique for the assay of infectivity of human adenovirus 5 DNA

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21 January 2018

Molecular cloning and sequence analysis of human Na,K-ATPase beta-subunit

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204772200

21 January 2018

Purification and characteristics of (Na+,K+)-ATPase from canine kidney by zonal centrifugation in sucrose density gradient

1 reference

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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

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21 January 2018

Importance of Na,K-ATPase residue alpha 1-Arg544 in the segment Arg544-Asp567 for high-affinity binding of ATP, ADP, or MgATP.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204772200

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.M204772200

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

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21 January 2018

Gastric H/K-ATPase liberates two moles of Pi from one mole of phosphoenzyme formed from a high-affinity ATP binding site and one mole of enzyme-bound ATP at the low-affinity site during cross-talk between catalytic subunits.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204772200

21 January 2018

Thermal denaturation of the Na,K-ATPase provides evidence for alpha-alpha oligomeric interaction and gamma subunit association with the C-terminal domain

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204772200

21 January 2018

Substrate regulation of calcium binding in Ca2+-ATPase molecules of the sarcoplasmic reticulum. I. Effect of ATP.

1 reference

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21 January 2018

Identifiers

10.1074/JBC.M204772200

1 reference

Europe PubMed Central

PubMed publication ID

2 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

2 September 2017

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