Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5099
pubmed:dateCreated
1993-4-8
pubmed:databankReference
pubmed:abstractText
The glycosylphosphatidylinositol (GPI) anchor is a membrane attachment structure of many proteins and occurs in a wide variety of eukaryotes from yeasts to mammals. The structure of the core of the GPI anchor is conserved in protozoa and mammals and so is its biosynthetic pathway. A complementary DNA encoding a human protein termed PIG-A (phosphatidylinositol glycan-class A) was cloned. PIG-A was necessary for synthesis of N-acetylglucosaminyl-phosphatidylinositol, the very early intermediate in GPI-anchor biosynthesis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0036-8075
pubmed:author
pubmed:issnType
Print
pubmed:day
26
pubmed:volume
259
pubmed:geneSymbol
PIG-A
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1318-20
pubmed:dateRevised
2007-3-19
pubmed:meshHeading
pubmed-meshheading:7680492-Amino Acid Sequence, pubmed-meshheading:7680492-Animals, pubmed-meshheading:7680492-Antigens, CD, pubmed-meshheading:7680492-Antigens, CD55, pubmed-meshheading:7680492-Antigens, CD59, pubmed-meshheading:7680492-Antigens, Surface, pubmed-meshheading:7680492-Antigens, Thy-1, pubmed-meshheading:7680492-Cloning, Molecular, pubmed-meshheading:7680492-DNA, pubmed-meshheading:7680492-Genetic Complementation Test, pubmed-meshheading:7680492-Glycosylphosphatidylinositols, pubmed-meshheading:7680492-HeLa Cells, pubmed-meshheading:7680492-Humans, pubmed-meshheading:7680492-Membrane Glycoproteins, pubmed-meshheading:7680492-Membrane Proteins, pubmed-meshheading:7680492-Mice, pubmed-meshheading:7680492-Molecular Sequence Data, pubmed-meshheading:7680492-Solubility, pubmed-meshheading:7680492-Species Specificity
pubmed:year
1993
pubmed:articleTitle
The cloning of PIG-A, a component in the early step of GPI-anchor biosynthesis.
pubmed:affiliation
Department of Immunoregulation, Osaka University, Japan.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't