Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
1999-1-13
|
pubmed:abstractText |
The surface protein S of transmissible gastroenteritis virus (TGEV) has a sialic acid binding activity that enables the virus to agglutinate erythrocytes. A protocol is described that has been successfully applied to the isolation of hemgglutination-defective mutants. The potential of these mutants for the characterization of the sialic acid-binding site and the function of the binding activity is discussed.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:issn |
0065-2598
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
440
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
563-8
|
pubmed:dateRevised |
2003-11-14
|
pubmed:meshHeading |
pubmed-meshheading:9782330-Animals,
pubmed-meshheading:9782330-Defective Viruses,
pubmed-meshheading:9782330-Hemagglutination, Viral,
pubmed-meshheading:9782330-Mutation,
pubmed-meshheading:9782330-N-Acetylneuraminic Acid,
pubmed-meshheading:9782330-Swine,
pubmed-meshheading:9782330-Transmissible gastroenteritis virus
|
pubmed:year |
1998
|
pubmed:articleTitle |
Isolation of hemagglutination-defective mutants for the analysis of the sialic acid binding activity of transmissible gastroenteritis virus.
|
pubmed:affiliation |
Institut für Virologie Philipps-Universität Marburg, Germany.
|
pubmed:publicationType |
Journal Article
|