Linked Life Data

9405808

Source:http://linkedlifedata.com/resource/pubmed/id/9405808

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1998-1-13
pubmed:abstractText
From the structural data obtained by systematically altering residues of the Na,K-ATPase, we are beginning to understand portions of how this active cation transporter couples hydrolysis of ATP with the vectorial movement of cations against their ionic gradients. In addition, the inhibitory action of cardiac glycosides and their interaction sites on the protein has focused our attentions on a catalytic core of the protein involving the H5-H6 transmembrane segment. In future investigations, both the ATP and the Na+ sites of the Na,K-ATPase must be uncovered to refine the structural picture of this complex transporter.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0077-8923
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
834
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
194-206
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Cation and cardiac glycoside binding sites of the Na,K-ATPase.
pubmed:affiliation
Department of Molecular Genetics, Biochemistry and Microbiology, University of Cincinnati College of Medicine, Ohio 45267-0524, USA. Lingrejb@uc.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review