Linked Life Data

17570365

Source:http://linkedlifedata.com/resource/pubmed/id/17570365

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
17
pubmed:dateCreated
2007-7-2
pubmed:abstractText
ATP synthase, or F-ATPase, purified from bovine heart mitochondria in the absence of phospholipids is an assembly of 16 different subunits. In the presence of exogenous phospholipids, two additional hydrophobic proteins, a 6.8kDa proteolipid and diabetes associated protein in insulin sensitive tissue (DAPIT), were associated with the purified complex, with DAPIT at sub-stoichiometric levels. Both proteins are conserved in vertebrates and invertebrates, but not in fungi, and prokaryotic F-ATPases do not contain orthologues of either of them. Therefore, their roles are likely to be peripheral to the synthesis of ATP.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
581
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3145-8
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Association of two proteolipids of unknown function with ATP synthase from bovine heart mitochondria.
pubmed:affiliation
Medical Research Council Dunn Human Nutrition Unit, Hills Road, Cambridge, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't