Linked Life Data

1716026

Source:http://linkedlifedata.com/resource/pubmed/id/1716026

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1991-10-9
pubmed:abstractText
Recently it has been reported that a membrane fraction can be isolated from West Nile virus-infected BHK cells which contains the viral nonstructural (NS) proteins as major constituents (Wengler et al., 1990). In this report we show that treatment of these membranes with subtilisin releases the carboxy-terminal segment of the NS 3 protein as a soluble protein of about 50 kDa apparent molecular weight. This molecule, which is called the p50-S protein, can be purified by standard chromatographic procedures. The p50-S protein binds to poly(A) and apparently represents a nucleoside triphosphatase which is stimulated in the presence of ssRNA molecules. The data represent experimental support for the predicted role of this segment of the NS 3 protein as an RNA helicase. Some properties of the p50-S protein are described and a possible function of this protein segment during RNA synthesis is discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0042-6822
pubmed:author
pubmed:issnType
Print
pubmed:volume
184
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
707-15
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
The carboxy-terminal part of the NS 3 protein of the West Nile flavivirus can be isolated as a soluble protein after proteolytic cleavage and represents an RNA-stimulated NTPase.
pubmed:affiliation
Institut für Virologie, Justus-Liebig-Universität Giessen, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't