Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1994-6-6
pubmed:abstractText
Using the vaccinia virus/T7-RNA polymerase transient protein expression system, the AAV Rep78 protein was expressed in mammalian cells. Rep78 protein was found localized primarily to the nucleus of cells. Maximal steady-state protein levels were reached as early as 12 hr postinfection, with no discernable increase at later time points. The Rep78 protein has been partially purified from nuclear extracts of the expression system. We have successfully used the cloned, purified Rep78 protein to complement an uninfected HeLa cell extract in an in vitro AAV DNA replication assay. Rep78-containing fractions are sufficient to make an uninfected HeLa cell extract competent for AAV DNA replication.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0042-6822
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
200
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
566-73
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Cloning, expression, and partial purification of Rep78: an adeno-associated virus replication protein.
pubmed:affiliation
Hearst Microbiology Research Center, Department of Microbiology, Cornell University Medical College, New York, New York 10021.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.