Linked Life Data

3685975

Source:http://linkedlifedata.com/resource/pubmed/id/3685975

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4831
pubmed:dateCreated
1987-12-28
pubmed:abstractText
Drosophila heat shock activator protein, a rare transacting factor which is induced upon heat shock to bind specifically to the heat shock regulatory sequence in vivo, has been purified from shocked cells to more than 95 percent homogeneity by sequence-specific duplex oligonucleotide affinity chromatography. The purified protein has a relative molecular mass of 110 kilodaltons, binds to the regulatory sequence with great affinity and specificity, and strongly stimulates transcription of the Drosophila hsp70 gene. Studies with this regulatory protein should lead to an understanding of the biochemical pathway underlying the heat shock phenomenon.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0036-8075
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
238
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1247-53
pubmed:dateRevised
2007-3-19
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Purification and properties of Drosophila heat shock activator protein.
pubmed:affiliation
Laboratory of Biochemistry, National Cancer Institute, Bethesda, MD 20892.
pubmed:publicationType
Journal Article