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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1-2
|
| pubmed:dateCreated |
1997-12-4
|
| pubmed:abstractText |
Phosphatidic acid phosphatase (PAP) has long been known as a key enzyme involved in both glycerolipid biosynthesis and cellular signal transduction. The cDNA cloning of a plasma membrane-bound type 2 PAP has revealed the existence of a novel glycoprotein with six transmembrane domains. The type 2 PAP now represents an enzyme family consisting of Drosophila Wunen and rat Dri 42, which participate in germ cell migration and epithelial differentiation, respectively. Such novel functions of the type 2 PAP suggest the unexpected importance of lipids and/or their metabolic enzymes.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Sep
|
| pubmed:issn |
0006-3002
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
4
|
| pubmed:volume |
1348
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
56-62
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:9370316-Amino Acid Sequence,
pubmed-meshheading:9370316-Animals,
pubmed-meshheading:9370316-DNA, Complementary,
pubmed-meshheading:9370316-Glycoproteins,
pubmed-meshheading:9370316-Humans,
pubmed-meshheading:9370316-Molecular Sequence Data,
pubmed-meshheading:9370316-Phosphatidate Phosphatase,
pubmed-meshheading:9370316-Sequence Homology, Amino Acid,
pubmed-meshheading:9370316-Substrate Specificity
|
| pubmed:year |
1997
|
| pubmed:articleTitle |
Phosphatidic acid phosphatase from mammalian tissues: discovery of channel-like proteins with unexpected functions.
|
| pubmed:affiliation |
Department of Biochemistry, Sapporo Medical University, School of Medicine, Japan. kanoh@sapmed.ac.jp
|
| pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
|