rdf:type |
|
lifeskim:mentions |
umls-concept:C0033684,
umls-concept:C0178539,
umls-concept:C0205160,
umls-concept:C0851285,
umls-concept:C1167622,
umls-concept:C1335858,
umls-concept:C1514562,
umls-concept:C1707520,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
|
pubmed:issue |
32
|
pubmed:dateCreated |
1994-9-6
|
pubmed:abstractText |
Sp1 is a well characterized and ubiquitously expressed transcription factor that regulates the constitutive and induced expression of a variety of mammalian genes. It is unclear whether Sp1 activity is regulated in vivo; the mechanism by which Sp1 interacts with the basal transcription complex has not been firmly established. We report the identification of a ubiquitously expressed and evolutionarily conserved nuclear protein, p74, that specifically binds Sp1 in vivo and in vitro. p74 interacts with several portions of the Sp1 trans-activation domain in vitro, and we correlate the binding of p74 to the amino-terminal serine/threonine-rich subdomain of Sp1 with the inhibition of Sp1-mediated transcription in vivo.
|
pubmed:grant |
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Aug
|
pubmed:issn |
0021-9258
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
12
|
pubmed:volume |
269
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
20674-81
|
pubmed:dateRevised |
2009-11-19
|
pubmed:meshHeading |
pubmed-meshheading:8051168-Binding Sites,
pubmed-meshheading:8051168-Cells, Cultured,
pubmed-meshheading:8051168-DNA-Binding Proteins,
pubmed-meshheading:8051168-Fungal Proteins,
pubmed-meshheading:8051168-Nuclear Proteins,
pubmed-meshheading:8051168-Recombinant Fusion Proteins,
pubmed-meshheading:8051168-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:8051168-Sp1 Transcription Factor,
pubmed-meshheading:8051168-Transcription, Genetic,
pubmed-meshheading:8051168-Transcription Factors,
pubmed-meshheading:8051168-Transcriptional Activation
|
pubmed:year |
1994
|
pubmed:articleTitle |
Negative regulation of Sp1 trans-activation is correlated with the binding of cellular proteins to the amino terminus of the Sp1 trans-activation domain.
|
pubmed:affiliation |
Department of Molecular Cancer Biology, Duke University Medical Center, Durham, North Carolina 27710.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|