Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1989-7-13
pubmed:abstractText
The Semliki Forest virus capsid (C) protein was introduced into various target cells by electroporation-, liposome-, and erythrocyte-ghost-mediated delivery. Data are presented which show that the incorporated C protein is biologically active and, at low concentrations (10(3) to 10(4) molecules per cell), markedly induces host cellular protein synthesis (average value, up to 90%). On the other hand, high concentrations (10(5) to 10(6) molecules per cell) led to a significant inhibition (average value, up to 60%). The cellular response to C protein was found to be identical in P3X63Ag8 suspension cells, CV-1 cells, and GpBind4 cells. Following electroporation-mediated delivery of C-protein molecules, both induction and repression of cellular protein synthesis were immediate, whereas with liposome-mediated delivery these events were delayed by about 1 h. Maximum stimulation and repression occurred between 0 and 1 h after delivery of C protein and decreased thereafter to reach control values at about 4 h. The analysis of the proteins synthesized suggests that low amounts of microinjected C protein are responsible for the induction of classes with specific Mrs, whereas high amounts lead to an inhibition of overall protein synthesis.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/2724418-1170772, http://linkedlifedata.com/resource/pubmed/commentcorrection/2724418-14907713, http://linkedlifedata.com/resource/pubmed/commentcorrection/2724418-216013, http://linkedlifedata.com/resource/pubmed/commentcorrection/2724418-2450774, http://linkedlifedata.com/resource/pubmed/commentcorrection/2724418-2578112, http://linkedlifedata.com/resource/pubmed/commentcorrection/2724418-2990897, http://linkedlifedata.com/resource/pubmed/commentcorrection/2724418-3028771, http://linkedlifedata.com/resource/pubmed/commentcorrection/2724418-3034197, http://linkedlifedata.com/resource/pubmed/commentcorrection/2724418-3161750, http://linkedlifedata.com/resource/pubmed/commentcorrection/2724418-3553612, http://linkedlifedata.com/resource/pubmed/commentcorrection/2724418-3829124, http://linkedlifedata.com/resource/pubmed/commentcorrection/2724418-3895223, http://linkedlifedata.com/resource/pubmed/commentcorrection/2724418-4077952, http://linkedlifedata.com/resource/pubmed/commentcorrection/2724418-4364899, http://linkedlifedata.com/resource/pubmed/commentcorrection/2724418-516447, http://linkedlifedata.com/resource/pubmed/commentcorrection/2724418-5388361, http://linkedlifedata.com/resource/pubmed/commentcorrection/2724418-543547, http://linkedlifedata.com/resource/pubmed/commentcorrection/2724418-5754569, http://linkedlifedata.com/resource/pubmed/commentcorrection/2724418-6293187, http://linkedlifedata.com/resource/pubmed/commentcorrection/2724418-6298601, http://linkedlifedata.com/resource/pubmed/commentcorrection/2724418-6312678, http://linkedlifedata.com/resource/pubmed/commentcorrection/2724418-632811, http://linkedlifedata.com/resource/pubmed/commentcorrection/2724418-6404557, http://linkedlifedata.com/resource/pubmed/commentcorrection/2724418-6692830, http://linkedlifedata.com/resource/pubmed/commentcorrection/2724418-6852050, http://linkedlifedata.com/resource/pubmed/commentcorrection/2724418-689099, http://linkedlifedata.com/resource/pubmed/commentcorrection/2724418-7143579, http://linkedlifedata.com/resource/pubmed/commentcorrection/2724418-7151177, http://linkedlifedata.com/resource/pubmed/commentcorrection/2724418-726255, http://linkedlifedata.com/resource/pubmed/commentcorrection/2724418-824460
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0022-538X
pubmed:author
pubmed:issnType
Print
pubmed:volume
63
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2921-8
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Semliki Forest virus capsid protein acts as a pleiotropic regulator of host cellular protein synthesis.
pubmed:affiliation
Institute of Hygiene and Medical Microbiology, University of Berne, Switzerland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't