Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1995-6-21
pubmed:abstractText
The human 5-HT1A receptor was screened for naturally occurring mutations. The PCR product of the 5-HT1A receptor gene was digested with several restriction enzymes and evaluated by single-strand conformational polymorphism (SSCP) analysis. Comparison of the SSCP electrophoretic pattern with a restriction map of the 5-HT1A receptor allowed localization of the polymorphic sites facilitating their identification by sequence analysis. Two polymorphisms were identified in the human 5-HT1A receptor gene that altered amino acid composition. The polymorphisms encode amino acid substitutions in the 5-HT1A receptor of a glycine to serine at amino acid 22 and an isoleucine to valine at amino acid 28, respectively. Both polymorphisms alter the extracellular amino terminal domain of the 5-HT1A receptor. The polymorphic 5-HT1A alleles have been found in American and Finnish Caucasians and in native American Indians. This is the first report of a polymorphism in the human 5-HT1A receptor gene that alters the structure of the 5-HT1A receptor protein composition.
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
16
pubmed:volume
210
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
530-6
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Two naturally occurring amino acid substitutions in the human 5-HT1A receptor: glycine 22 to serine 22 and isoleucine 28 to valine 28.
pubmed:affiliation
Section of Molecular Genetics, NIAAA, National Institutes of Health, Rockville, MD 20852, USA.
pubmed:publicationType
Journal Article