Linked Life Data

17092916

Source:http://linkedlifedata.com/resource/pubmed/id/17092916

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2006-12-14
pubmed:abstractText
Rapid identification of small molecules that interact with protein targets using a generic screening method greatly facilitates the development of therapeutic agents. The authors describe a novel method for performing homogeneous biophysical assays in a high-throughput format. The use of light scattering as a method to evaluate protein stability during thermal denaturation in a 384-well format yields a robust assay with a low frequency of false positives. This novel method leads to the identification of interacting small molecules without the addition of extraneous fluorescent probes. The analysis and interpretation of data is rapid, with sensitivity for protein stability comparable to differential scanning calorimetry. The authors propose potential uses in drug discovery, structural genomics, and functional genomics as a method to evaluate small-molecule interactions, identify natural cofactors that stabilize target proteins, and identify natural substrates and products for previously uncharacterized protein targets.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1087-0571
pubmed:author
pubmed:issnType
Print
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
940-8
pubmed:dateRevised
2011-5-23
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Screening for ligands using a generic and high-throughput light-scattering-based assay.
pubmed:affiliation
Structural Genomics Consortium, University of Toronto, Toronto, Ontario, Canada. senisterra@utoronto.ca
pubmed:publicationType
Journal Article, Evaluation Studies