Linked Life Data

3788061

Source:http://linkedlifedata.com/resource/pubmed/id/3788061

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1987-1-20
pubmed:abstractText
Incubation of X-31 influenza virus at 62 degrees results in changes in hemagglutinin structure which cause the virus to fuse with liposomes at neutral pH. Mutants of X-31 which contain different hemagglutinins and as a consequence fuse with liposomes at higher pH than wild-type virus also fuse at a lower temperature. The heat-induced changes in hemagglutinin structure were monitored by CD, fluorescence spectroscopy, electron microscopy, and proteolytic digestion and compared with the characteristic changes which occur at low pH required for hemagglutinin-mediated membrane fusion at physiological temperature. The results indicate that the heat-induced changes in hemagglutinin which allow fusion activity result in partial denaturation of the molecule. By comparison the changes in structure required for fusion at low pH and normal temperature are specifically restricted.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0042-6822
pubmed:author
pubmed:issnType
Print
pubmed:volume
155
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
484-97
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Conformational changes in the hemagglutinin of influenza virus which accompany heat-induced fusion of virus with liposomes.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.