Linked Life Data

15755645

Source:http://linkedlifedata.com/resource/pubmed/id/15755645

Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:15755645rdf:typepubmed:Citationlld:pubmed
pubmed-article:15755645lifeskim:mentionsumls-concept:C0002159lld:lifeskim
pubmed-article:15755645lifeskim:mentionsumls-concept:C0030956lld:lifeskim
pubmed-article:15755645lifeskim:mentionsumls-concept:C1333707lld:lifeskim
pubmed-article:15755645lifeskim:mentionsumls-concept:C0220825lld:lifeskim
pubmed-article:15755645lifeskim:mentionsumls-concept:C1521827lld:lifeskim
pubmed-article:15755645lifeskim:mentionsumls-concept:C0920591lld:lifeskim
pubmed-article:15755645lifeskim:mentionsumls-concept:C1707271lld:lifeskim
pubmed-article:15755645pubmed:issue7lld:pubmed
pubmed-article:15755645pubmed:dateCreated2005-3-9lld:pubmed
pubmed-article:15755645pubmed:abstractTextPreferential binding of ligands to Grb2 SH2 domains in beta-bend conformations has made peptide cyclization a logical means of effecting affinity enhancement. This is based on the concept that constraint of open-chain sequences to bend geometries may reduce entropy penalties of binding. The current study extends this approach by undertaking ring-closing metathesis (RCM) macrocyclization between i and i+3 residues through a process involving allylglycines and beta-vinyl-functionalized residues. Ring closure in this fashion results in minimal macrocyclic tetrapeptide mimetics. The predominant effects of such macrocyclization on Grb2 SH2 domain binding affinity were increases in rates of association (from 7- to 16-fold) relative to an open-chain congener, while decreases in dissociation rates were less pronounced (approximately 2-fold). The significant increases in association rates were consistent with pre-ordering of solution conformations to near those required for binding. Data from NMR experiments and molecular modeling simulations were used to interpret the binding results. An understanding of the conformational consequences of such i to i+3 ring closure may facilitate its application to other systems where bend geometries are desired.lld:pubmed
pubmed-article:15755645pubmed:languageenglld:pubmed
pubmed-article:15755645pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15755645pubmed:citationSubsetIMlld:pubmed
pubmed-article:15755645pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15755645pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15755645pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15755645pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15755645pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15755645pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15755645pubmed:statusMEDLINElld:pubmed
pubmed-article:15755645pubmed:monthAprlld:pubmed
pubmed-article:15755645pubmed:issn0968-0896lld:pubmed
pubmed-article:15755645pubmed:authorpubmed-author:BurkeTerrence...lld:pubmed
pubmed-article:15755645pubmed:authorpubmed-author:FisherRobert...lld:pubmed
pubmed-article:15755645pubmed:authorpubmed-author:OishiShinyaSlld:pubmed
pubmed-article:15755645pubmed:authorpubmed-author:NicklausMarc...lld:pubmed
pubmed-article:15755645pubmed:authorpubmed-author:BarchiJoseph...lld:pubmed
pubmed-article:15755645pubmed:authorpubmed-author:ShiZhen-DanZDlld:pubmed
pubmed-article:15755645pubmed:authorpubmed-author:GilletteWilli...lld:pubmed
pubmed-article:15755645pubmed:authorpubmed-author:HartleyJamesJlld:pubmed
pubmed-article:15755645pubmed:authorpubmed-author:FrankPeterPlld:pubmed
pubmed-article:15755645pubmed:authorpubmed-author:WorthyKaren...lld:pubmed
pubmed-article:15755645pubmed:authorpubmed-author:ChertovOlegOlld:pubmed
pubmed-article:15755645pubmed:authorpubmed-author:MaderiaMeliss...lld:pubmed
pubmed-article:15755645pubmed:authorpubmed-author:KarkiRajeshri...lld:pubmed
pubmed-article:15755645pubmed:authorpubmed-author:EspositoDomin...lld:pubmed
pubmed-article:15755645pubmed:authorpubmed-author:BinduLakshman...lld:pubmed
pubmed-article:15755645pubmed:issnTypePrintlld:pubmed
pubmed-article:15755645pubmed:day1lld:pubmed
pubmed-article:15755645pubmed:volume13lld:pubmed
pubmed-article:15755645pubmed:ownerNLMlld:pubmed
pubmed-article:15755645pubmed:authorsCompleteYlld:pubmed
pubmed-article:15755645pubmed:pagination2431-8lld:pubmed
pubmed-article:15755645pubmed:dateRevised2005-11-17lld:pubmed
pubmed-article:15755645pubmed:meshHeadingpubmed-meshheading:15755645...lld:pubmed
pubmed-article:15755645pubmed:meshHeadingpubmed-meshheading:15755645...lld:pubmed
pubmed-article:15755645pubmed:meshHeadingpubmed-meshheading:15755645...lld:pubmed
pubmed-article:15755645pubmed:meshHeadingpubmed-meshheading:15755645...lld:pubmed
pubmed-article:15755645pubmed:meshHeadingpubmed-meshheading:15755645...lld:pubmed
pubmed-article:15755645pubmed:meshHeadingpubmed-meshheading:15755645...lld:pubmed
pubmed-article:15755645pubmed:meshHeadingpubmed-meshheading:15755645...lld:pubmed
pubmed-article:15755645pubmed:meshHeadingpubmed-meshheading:15755645...lld:pubmed
pubmed-article:15755645pubmed:meshHeadingpubmed-meshheading:15755645...lld:pubmed
pubmed-article:15755645pubmed:meshHeadingpubmed-meshheading:15755645...lld:pubmed
pubmed-article:15755645pubmed:meshHeadingpubmed-meshheading:15755645...lld:pubmed
pubmed-article:15755645pubmed:meshHeadingpubmed-meshheading:15755645...lld:pubmed
pubmed-article:15755645pubmed:meshHeadingpubmed-meshheading:15755645...lld:pubmed
pubmed-article:15755645pubmed:meshHeadingpubmed-meshheading:15755645...lld:pubmed
pubmed-article:15755645pubmed:meshHeadingpubmed-meshheading:15755645...lld:pubmed
pubmed-article:15755645pubmed:year2005lld:pubmed
pubmed-article:15755645pubmed:articleTitleEvaluation of macrocyclic Grb2 SH2 domain-binding peptide mimetics prepared by ring-closing metathesis of C-terminal allylglycines with an N-terminal beta-vinyl-substituted phosphotyrosyl mimetic.lld:pubmed
pubmed-article:15755645pubmed:affiliationLaboratory of Medicinal Chemistry, Center for Cancer Research, National Cancer Institute, National Institutes of Health, PO Box B, Bldg. 376 Boyles St. Frederick, MD 21702-1201, USA.lld:pubmed
pubmed-article:15755645pubmed:publicationTypeJournal Articlelld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:15755645lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:15755645lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:15755645lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:15755645lld:pubmed