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

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

Acta physiologica Scandinavica. Supplementum - 1 Aug 1998

Blostein R, Daly S E, Boxenbaum N, Lane L K, Arguello J M, Lingrel J B, Karlish S J, Caplan M J, Dunbar L

Abstract excerpt

This paper summarizes experiments concerned with the functional consequences of mutations in cytoplasmic regions of the alpha 1 subunit of the Na,K-ATPase, in particular the amino terminus, the first cytoplasmic loop between transmembrane segments M2 and M3, and the major cytoplasmic loop between M4 and M5. In the first mutation (alpha 1M32), 32 residues were removed from the N-terminus. The second mutation...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Substitution
Share to Cytoplasm

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

Share to Isoenzymes

Share to Mutation

Share to Protein Conformation

Share to Sodium-Potassium-Exchanging ATPase

Source

Identifiers

PMID: 9789570

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

Conformational alterations resulting from mutations in cytoplasmic domains of the alpha subunit of the Na,K-ATPase.PMID 9789570Read ↗

Changes in steady-state conformational equilibrium resulting from cytoplasmic mutations of the Na,K-ATPase alpha-subunit.Semantic proximity Read ↗

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

Functional consequences of alterations to Ile279, Ile283, Glu284, His285, Phe286, and His288 in the NH2-terminal part of transmembrane helix M3 of the Na+,K(+)-ATPase.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 ↗

Structural basis for alpha1 versus alpha2 isoform-distinct behavior of the Na,K-ATPase.Semantic proximity Read ↗

A Highly Conserved Glycine in a Hotspot for Neurological Disease Mutations in Na+,K+-ATPase Is Critical to Na+ and K+ Occlusion.Semantic proximity Read ↗

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

Interaction between the catalytic site and the A-M3 linker stabilizes E2/E2P conformational states of Na+,K+-ATPase.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 ↗

Rescue of Na+ affinity in aspartate 928 mutants of Na+,K+-ATPase by secondary mutation of glutamate 314.Semantic proximity Read ↗

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

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