Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1983-10-8
pubmed:databankReference
pubmed:abstractText
The proteins from cells infected with influenza A virus field isolates were labeled with [35S]methionine and analyzed by SDS-polyacrylamide gel electrophoresis. By screening more than 100 field isolates, it was found that the NS1 proteins had the greatest mobility differences, far exceeding those observed among other corresponding viral polypeptides. Partial sequence determination of RNA segment eight from 12 viruses revealed the existence of nonsense mutations at six different positions in their NS1 coding regions. The termination codons consisted of opal, ochre, and amber mutations. The sizes predicted from these sequences of 202, 217, 219, 220, 230, and 237 amino acids were in agreement with the observed mobilities of the viral polypeptides on SDS-polyacrylamide gels. The observation of large deletions in the carboxy termini of the NS1 proteins of field virus isolates would suggest that a high degree of variation can be tolerated in this polypeptide without affecting its functional capability.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0042-6822
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
128
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
512-7
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Nonsense mutations affecting the lengths of the NS1 nonstructural proteins of influenza A virus isolates.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't