Linked Life Data

10675554

Source:http://linkedlifedata.com/resource/pubmed/id/10675554

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2-3
pubmed:dateCreated
2000-3-31
pubmed:abstractText
Purified human respiratory syncytial virus (HRSV) P phosphoprotein from transfected HEp-2 cells is able to oligomerize forming tetramers. The bulk of constitutive P protein phosphorylation (99. 8%) (serine residues 116, 117, 119, 232 and 237) can be removed without affecting protein oligomerization. However, dephosphorylated P protein, produced in bacteria, is unable to oligomerize. This difference can be explained by a transient P protein phosphorylation, detected in HEp-2 cells, that could be essential for P protein oligomerization.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
467
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
279-84
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Regulated but not constitutive human respiratory syncytial virus (HRSV) P protein phosphorylation is essential for oligomerization.
pubmed:affiliation
Centro Nacional de Microbiologia (C.N.M), Instituto de Salud Carlos III (ISCIII), Carretera Majadahonda-Pozuelo Km 2, Majadahonda, Madrid, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't