Linked Life Data

3967299

Source:http://linkedlifedata.com/resource/pubmed/id/3967299

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1985-3-21
pubmed:abstractText
The influenza virus hemagglutinin (HA) mediates viral entry into cells by a low pH induced membrane-fusion event in endosomal vesicles. Mutant viruses with altered pH dependence for both hemolysis and the HA conformational change required for fusion were selected for their ability to grow in cells treated with amantadine hydrochloride, which raises the endosomal pH. The amino acid sequence and three-dimensional location of 19 substitutions on the HA are reported. The mutations fall into two groups, one that results in the destabilization of the pH 7.0 location of the hydrophobic N-terminal HA2 peptide, and a second that results in the alteration of intersubunit contacts, suggesting a large distortion or disruption of these contacts in the "fusion-active" conformation.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0092-8674
pubmed:author
pubmed:issnType
Print
pubmed:volume
40
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
431-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Fusion mutants of the influenza virus hemagglutinin glycoprotein.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.