Linked Life Data

21088491

Source:http://linkedlifedata.com/resource/pubmed/id/21088491

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
22
pubmed:dateCreated
2010-12-8
pubmed:abstractText
Atomistic simulations of a set of stapled peptides derived from the transactivation domain of p53 (designed by Verdine & colleagues, JACS 2007 129:2456) and complexed to MDM2 reveal that the good binders are uniquely characterized by higher helicity and by extensive interactions between the hydrocarbon staples and the MDM2 surface; in contrast the poor binders have reduced helicity and their staples are mostly solvent exposed. Our studies also find that the best binders can also potentially inhibit MDMX with similar affinities, suggesting that such stapled peptides can be evolved for dual inhibition with therapeutic potential.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1551-4005
pubmed:author
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4560-8
pubmed:dateRevised
2011-3-30
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Stapled peptides in the p53 pathway: computer simulations reveal novel interactions of the staples with the target protein.
pubmed:affiliation
Bioinformatics Institute, Matrix, Singapore.
pubmed:publicationType
Journal Article