Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Residues within transmembrane domains 4 and 6 of the Na,K-ATPase alpha subunit are important for Na+ selectivity.

Biochemistry - 20 Jul 2004

Sánchez Gladis, Blanco Gustavo

Abstract excerpt

The Na,K- and H,K-ATPases are plasma membrane enzymes responsible for the active exchange of extracellular K(+) for cytoplasmic Na(+) or H(+), respectively. At present, the structural determinants for the specific function of these ATPases remain poorly understood. To investigate the cation selectivity of these ATPases, we constructed a series of Na,K-ATPase mutants in which residues in the membrane spanning...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Adenosine Triphosphate
Share to Amino Acids
Share to Cloning, Molecular

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Mutagenesis, Site-Directed

Share to Protein Conformation

Share to Protein Subunits

Share to Sodium

Share to Sodium-Potassium-Exchanging ATPase

Source

Identifiers

PMID: 15248763
DOI: 10.1021/bi049484s

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Residues within transmembrane domains 4 and 6 of the Na,K-ATPase alpha subunit are important for Na+ selectivity.PMID 15248763Read ↗

Residues of the fourth transmembrane segments of the Na,K-ATPase and the gastric H,K-ATPase contribute to cation selectivity.Semantic proximity Read ↗

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

Deceleration of the E1P-E2P transition and ion transport by mutation of potentially salt bridge-forming residues Lys-791 and Glu-820 in gastric H+/K+-ATPase.Semantic proximity Read ↗

Structural and functional interaction sites between Na,K-ATPase and FXYD proteins.Semantic proximity Read ↗

The V-type H+ ATPase: molecular structure and function, physiological roles and regulation.Semantic proximity Read ↗

Role of the transmembrane domain of FXYD7 in structural and functional interactions with Na,K-ATPase.Semantic proximity Read ↗

Conformational alterations resulting from mutations in cytoplasmic domains of the alpha subunit of the Na,K-ATPase.Semantic proximity Read ↗

The structure of the Na+,K+-ATPase and mapping of isoform differences and disease-related mutations.Semantic proximity Read ↗

Structure-function relationships in transmembrane segments 4, 5, and 6 of the yeast plasma-membrane H(+)-ATPase.Semantic proximity Read ↗

Electrophysiological analysis of the mutated Na,K-ATPase cation binding pocket.Semantic proximity Read ↗

Intracellular localization of Na,K-ATPase alpha2 subunit mutants.Semantic proximity Read ↗

Mutations Phe785Leu and Thr618Met in Na+,K+-ATPase, associated with familial rapid-onset dystonia parkinsonism, interfere with Na+ interaction by distinct mechanisms.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.