Linked Life Data

10028059

Source:http://linkedlifedata.com/resource/pubmed/id/10028059

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2000-10-13
pubmed:abstractText
Amiloride and its derivatives are important tools for studying NHE-1, the ubiquitous isoform of the sodium/hydrogen exchanger protein family. Three residues in putative transmembrane domains IV and IX have been implicated in amiloride binding and several models of the proposed amiloride-binding site have been reported. Though it has been shown that sodium ions and amiloride molecules interact at unique regions of the NHE-1 protein, physiological experiments reveal a competitive relationship between the two under some circumstances. The two binding sites are thus on closely related but distinct regions on the protein.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1107-3756
pubmed:author
pubmed:issnType
Print
pubmed:volume
3
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
315-21
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Amiloride and the Na(+)/H(+) exchanger protein: mechanism and significance of inhibition of the Na(+)/H(+) exchanger (review).
pubmed:affiliation
Department of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2H7, Canada.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't