Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1991-7-5
pubmed:abstractText
A cDNA encoding non-selective type (ETB) of endothelin receptor was isolated from a human liver cDNA library. The cDNA had an open reading frame encoding a protein of 442 amino acid residues with a relative Mr of 49,643. The deduced amino acid sequence of human ETB receptor was 88% and 64% identical to those of rat lung ETB receptor and bovine lung ET-1-specific (ETA) receptor, respectively, and contained a relatively long and proline-rich extracellular N-terminal region in addition to a significant similarity with the G protein-coupled receptor super-family with seven transmembrane segments.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
177
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
34-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:1710450-Adult, pubmed-meshheading:1710450-Amino Acid Sequence, pubmed-meshheading:1710450-Animals, pubmed-meshheading:1710450-Base Sequence, pubmed-meshheading:1710450-Blotting, Northern, pubmed-meshheading:1710450-Cloning, Molecular, pubmed-meshheading:1710450-DNA, pubmed-meshheading:1710450-Endothelins, pubmed-meshheading:1710450-Humans, pubmed-meshheading:1710450-Liver, pubmed-meshheading:1710450-Molecular Sequence Data, pubmed-meshheading:1710450-Oligonucleotide Probes, pubmed-meshheading:1710450-Peptide Fragments, pubmed-meshheading:1710450-Poly A, pubmed-meshheading:1710450-RNA, pubmed-meshheading:1710450-RNA, Messenger, pubmed-meshheading:1710450-Rats, pubmed-meshheading:1710450-Receptors, Cell Surface, pubmed-meshheading:1710450-Receptors, Endothelin, pubmed-meshheading:1710450-Sequence Homology, Nucleic Acid
pubmed:year
1991
pubmed:articleTitle
Cloning and sequence analysis of a cDNA encoding human non-selective type of endothelin receptor.
pubmed:affiliation
Third Department of Internal Medicine, Faculty of Medicine, Kyushu University, Japan.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't