Linked Life Data

16338391

Source:http://linkedlifedata.com/resource/pubmed/id/16338391

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2005-12-12
pubmed:abstractText
The cyclin-dependent kinase inhibitor p27(Kip1) is a critical cell cycle regulator frequently altered in human cancer. The cellular level of p27 is controlled by ubiquitin-dependent degradation mediated by the E3 ligase SCF(Skp1). Decreased p27 level in cancer cells has been associated with enhanced ubiquitin-dependent degradation and linked to poor prognosis. Therefore, restoration of p27 by inhibiting SCF(Skp2) activity has been proposed as a novel therapeutic strategy. Recently, the small regulatory protein Cks1 has been found to bind Skp2 and dramatically increases the affinity of Skp2 to p27, thus facilitating its ubiquitylation and degradation. Here, we describe a high-throughput screening assay for inhibitors of the Cks1-Skp2 interaction. The assay measures the binding of recombinant human GST-Cks1 and His6-Skp2-Skp1 using a homogeneous time-resolved fluorescence format and permits a throughput in excess of 100,000 data points per day when implemented on the Zeiss uHTS system.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0076-6879
pubmed:author
pubmed:issnType
Print
pubmed:volume
399
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
717-28
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
High-throughput screening for inhibitors of the Cks1-Skp2 interaction.
pubmed:affiliation
Discovery Technologies, Hoffmann-La Roche, Inc., Nutley, New Jersey, USA.
pubmed:publicationType
Journal Article