Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2008-3-27
pubmed:abstractText
Saccharomyces cerevisiae squalene epoxidase contains two highly conserved motifs, 1 and 2, of unknown function. Amino acid substitutions in both regions reduce enzyme activity and/or alter allylamine sensitivity. In the homology model, these motifs flank the flavin adenine dinucleotide cofactor and form part of the interface between cofactor and substrate binding domains.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/18212112-12963042, http://linkedlifedata.com/resource/pubmed/commentcorrection/18212112-14638499, http://linkedlifedata.com/resource/pubmed/commentcorrection/18212112-15013417, http://linkedlifedata.com/resource/pubmed/commentcorrection/18212112-16120615, http://linkedlifedata.com/resource/pubmed/commentcorrection/18212112-16246080, http://linkedlifedata.com/resource/pubmed/commentcorrection/18212112-17043127, http://linkedlifedata.com/resource/pubmed/commentcorrection/18212112-2553983, http://linkedlifedata.com/resource/pubmed/commentcorrection/18212112-3877503, http://linkedlifedata.com/resource/pubmed/commentcorrection/18212112-3959077, http://linkedlifedata.com/resource/pubmed/commentcorrection/18212112-8003958, http://linkedlifedata.com/resource/pubmed/commentcorrection/18212112-8771716, http://linkedlifedata.com/resource/pubmed/commentcorrection/18212112-9385648
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0066-4804
pubmed:author
pubmed:issnType
Print
pubmed:volume
52
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1496-9
pubmed:dateRevised
2011-4-6
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Structure-function correlations of two highly conserved motifs in Saccharomyces cerevisiae squalene epoxidase.
pubmed:affiliation
Institute of Molecular Biosciences, Karl-Franzens-Universität Graz, Humboldtstrasse 50, A-8010 Graz, Austria.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't