Linked Life Data

8999886

Source:http://linkedlifedata.com/resource/pubmed/id/8999886

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1997-2-13
pubmed:abstractText
Computer-assisted alignment of known palmitylproteins was used to identify a potential peptide motif, TMDX1-12AAC(C)A (TMD, transmembrane domain; X, any amino acid; C, cysteine acceptor residues; A, aliphatic residue) responsible for directing internal palmitylation of the vaccinia virus 37-kDa major envelope antigen, p37. Site-directed mutagenesis was used to confirm this motif as the site of modification and to produce a nonpalmitylated version of the p37 protein. Comparative phenotypic analysis of the wild-type and mutant p37 alleles confirmed that the p37 protein is involved in viral envelopment and egress, and suggested that attachment of the palmitate moiety was essential for correct intracellular targeting and protein function.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
272
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1956-64
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Palmitylation of the vaccinia virus 37-kDa major envelope antigen. Identification of a conserved acceptor motif and biological relevance.
pubmed:affiliation
Center for Gene Research and Biotechnology, Department of Microbiology, Oregon State University, Corvallis, Oregon 97331-3804, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.