Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
238
pubmed:dateCreated
2004-6-23
pubmed:abstractText
The development of green fluorescent protein (GFP) technology combined with live cell microscopy techniques have revealed the dynamic properties of GFP-tagged proteins in the nucleus. The mobility of a GFP-tagged protein can be assessed using a quantitative photobleaching technique, fluorescence recovery after photobleaching (FRAP) analysis. FRAP experiments demonstrate that many nuclear proteins are highly mobile within the nucleus. However, the factors within the nucleus that regulate this mobility are not known. This is partly due to an absence of protocols that can be used to identify such nuclear mobility factors. We developed a novel in situ assay that combines a biochemical permeabilization and extraction procedure with a quantitative FRAP technique, a method we used to uncover a new functional role for molecular chaperones in the nuclear mobility of steroid receptors. This assay can readily be adapted to identify and characterize other nuclear mobility factors.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1525-8882
pubmed:author
pubmed:issnType
Electronic
pubmed:day
22
pubmed:volume
2004
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
pl10
pubmed:dateRevised
2004-12-15
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
A novel in situ assay for the identification and characterization of soluble nuclear mobility factors.
pubmed:affiliation
Laboratory of Receptor Biology and Gene Expression, Building 41, Room B602, National Cancer Institute, Bethesda, MD 20892-5055, USA.
pubmed:publicationType
Journal Article