Linked Life Data

8825028

Source:http://linkedlifedata.com/resource/pubmed/id/8825028

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1996-11-21
pubmed:abstractText
The results of site-directed mutagenesis studies of the sarcoplasmic reticulum Ca(2+)-ATPase are reviewed. More than 250 different point mutants have been expressed in cell culture and analysed by a panel of functional assays. Thereby, 40-50 important amino acid residues have been pinpointed, and the mutants have been assigned to functional classes: the Ca(2+)-affinity mutants, the phosphorylation-negative mutants, the ATP-affinity mutants, the E1P mutants, the E2P mutants, and the uncoupled mutants. Moreover, regions important to the specific inhibition by thapsigargin have been identified by analysis of Ca(2+)-ATPase/Na+,K(+)-ATPase chimeric constructs.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0144-8463
pubmed:author
pubmed:issnType
Print
pubmed:volume
15
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
243-61
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Dissection of the functional domains of the sarcoplasmic reticulum Ca(2+)-ATPase by site-directed mutagenesis.
pubmed:affiliation
Department of Physiology, University of Aarhus, Denmark.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't