|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
1
|
|
pubmed:dateCreated |
1991-6-4
|
|
pubmed:abstractText |
The oligosaccharide side chains of the glycoprotein of Marburg virus (MW 170,000) have been analyzed by determining their sensitivity to enzymatic degradation and their reactivity with lectins. It was found that they consist of N- and O-glycans. Studies employing chemical cross-linking showed that the glycoprotein is present as a homotrimer in the viral envelope.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
May
|
|
pubmed:issn |
0042-6822
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
182
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
353-6
|
|
pubmed:dateRevised |
2006-11-15
|
|
pubmed:meshHeading |
|
|
pubmed:year |
1991
|
|
pubmed:articleTitle |
Glycosylation and oligomerization of the spike protein of Marburg virus.
|
|
pubmed:affiliation |
Institut für Virologie, Philipps-Universität, Germany.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
