Linked Life Data

9599005

Source:http://linkedlifedata.com/resource/pubmed/id/9599005

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1998-6-2
pubmed:abstractText
This paper describes the process of dimer assembly of mitochondrial very-long-chain acyl-CoA dehydrogenase (VLCAD) subunit. Mature VLCAD is a homodimer of a 70-kDa protein associated with the mitochondrial membrane. Newly synthesized VLCAD was present as a monomer and the major fraction was associated with the mitochondrial inner membrane. The association of VLCAD subunit with the mitochondrial membrane was observed early during dimer formation. In contrast, a VLCAD monomeric mutant S583W, a novel mutation identified from a patient with VLCAD deficiency, did not associate with the mitochondrial membrane after import and the major fraction remained in the mitochondrial matrix. These results suggest that association of VLCAD protein with mitochondrial inner membrane is necessary for dimer assembly and formation of mature VLCAD.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
426
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
187-90
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Very-long-chain acyl-CoA dehydrogenase subunit assembles to the dimer form on mitochondrial inner membrane.
pubmed:affiliation
Department of Biochemistry, Shinshu University School of Medicine, Matsumoto, Nagano, Japan. msouri@med.id.yamagata-u.ac.jp
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't