Linked Life Data

6160037

Source:http://linkedlifedata.com/resource/pubmed/id/6160037

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1981-2-24
pubmed:abstractText
In the presence of fluoroglucose, an inhibitor of formation of mannosylphosphoryl and glucosylphosphoryl-dolichol, lipid-dependent glycosylation of influenza virus glycoproteins is strongly, but not completely inhibited. The oligosaccharides that were transferred to protein in the presence of fluoroglucose came directly dolichol-linked intermediates. However, they were smaller than the normal high-mannose oligosaccharides and, furthermore, resistant towards digestion with endo-beta-N-acetylglucosaminidase H. By excluding mannosylphosphoryl-dolichol, similar dolichyl-pyrophosphate-liked intermediates were synthesized in vitro by membranes from fluoroglucose-treated cells and they were shown to glycosylate protein.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:volume
110
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
355-61
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Glycosylation of influenza virus proteins in the presence of fluoroglucose occurs via a different pathway.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't