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Cited by 1,181

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Biochemistry of Na,K-ATPase

Kaplan, Jack H.·2002·Annual Review of Biochemistry

Abstract

▪ Abstract The Na,K-ATPase or sodium pump carries out the coupled extrusion and uptake of Na and K ions across the plasma membranes of cells of most higher eukaryotes. It is a member of the P-type ATPase superfamily. This heterodimeric integral membrane protein is composed of a 100-kDa α-subunit with ten transmembrane segments and a heavily glycosylated β subunit of about 55 kDa, which is a type II membrane protein. Current ideas on how the protein achieves active transport are based on a fusion of results of transport physiology, protein chemistry, and heterologous expression of mutant proteins. Recently acquired high resolution structural information provides an important new avenue for a more complete understanding of this protein. In this review, the current status of knowledge of Na,K-ATPase is discussed, and areas where there is still considerable uncertainty are highlighted.

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Metadata

Authors
Kaplan, J. H.
Venue
Annual Review of Biochemistry
Published
2002-06
Volume
71
Issue
1
Pages
511-535
ISSN
  • 0066-4154 (ISSN-L)
  • 1545-4509
OpenAlex
W2142048790
Cited by
1,181
References
1
FWCI
1.59
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Biochemistry of Na,K-ATPase. https://app.cochat.ai/papers/10.1146/annurev.biochem.71.102201.141218
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Kaplan, J. H. (2002). Biochemistry of Na,K-ATPase. Annual Review of Biochemistry. https://doi.org/10.1146/annurev.biochem.71.102201.141218

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.