Linked Life Data

8053156

Source:http://linkedlifedata.com/resource/pubmed/id/8053156

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1994-9-8
pubmed:databankReference
pubmed:abstractText
Chlorella virus PBCV-1 particles contain three glycoproteins, the major capsid protein Vp54 and two minor proteins Vp280 and Vp260. The major capsid protein is myristylated as well as glycosylated. Both modifications are in the carboxyl-terminal portion of the protein. A gene which is modified in a PBCV-1 antiserum-resistant mutant was cloned and sequenced. This gene has an open reading frame of 3099 bases and encodes one of the two large virion glycoproteins (Vp260). Vp260 contains 13 tandem repeats of 61 to 65 amino acids. The mutation deletes the equivalent of four of the amino acid repeat sequences and duplicates one of these sequences.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0042-6822
pubmed:author
pubmed:issnType
Print
pubmed:volume
203
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
320-7
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Protein glycosylation and myristylation in Chlorella virus PBCV-1 and its antigenic variants.
pubmed:affiliation
Department of Plant Pathology, University of Nebraska, Lincoln 68583-0722.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't