Linked Life Data

8126452

Source:http://linkedlifedata.com/resource/pubmed/id/8126452

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1994-4-11
pubmed:abstractText
P protein, the structural phosphoprotein of the Long strain of respiratory syncytial (RS) virus, is phosphorylated at serine residues. Some of these residues are candidates for modification by casein kinase II, as they are contained in consensus sequences. A cellular protein kinase, able to phosphorylate the P protein in vitro and apparently associated with purified RS virions, has been partially purified from HEp-2 cells. It shows several characteristics similar to those of casein kinase II. The P protein is modified in vitro by this activity mainly at serine residues located near the C terminus, which are also modified during virus infection. Thus, the P protein is phosphorylated in vivo in two regions, a central region as previously described, and another located in the C-terminal part of the molecule. The protein kinase involved in the phosphorylation of the C-terminal domain is similar to a cellular casein kinase II.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0022-1317
pubmed:author
pubmed:issnType
Print
pubmed:volume
75 ( Pt 3)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
555-65
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Identification of a protein kinase involved in the phosphorylation of the C-terminal region of human respiratory syncytial virus P protein.
pubmed:affiliation
Servicio de Virología, Centro Nacional de Microbiología, Virología e Inmunología Sanitarias, Instituto de Salud Carlos III, Madrid, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't