The anti-platelet approach targeting the fibrinogen ligand of the GPIIb/IIIa receptor
dc.contributor.author | Tsikaris, V. | en |
dc.date.accessioned | 2015-11-24T16:50:10Z | |
dc.date.available | 2015-11-24T16:50:10Z | |
dc.identifier.issn | 1075-2617 | - |
dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/9576 | |
dc.rights | Default Licence | - |
dc.subject | alpha(iib)beta(3) receptor | en |
dc.subject | fibrinogen blockers | en |
dc.subject | gpilb/lila binding domains | en |
dc.subject | integrin inhibitors | en |
dc.subject | platelet aggregation inhibitors | en |
dc.subject | glycoprotein-iib-iiia | en |
dc.subject | platelet integrin gpiib/iiia | en |
dc.subject | monoclonal-antibody epitopes | en |
dc.subject | rgd-containing peptides | en |
dc.subject | amino-acid-sequence | en |
dc.subject | asp-binding domain | en |
dc.subject | a-alpha-chain | en |
dc.subject | glanzmann thrombasthenia | en |
dc.subject | iib/iiia antagonists | en |
dc.subject | beta(3) subunit | en |
dc.title | The anti-platelet approach targeting the fibrinogen ligand of the GPIIb/IIIa receptor | en |
heal.abstract | Activation of the platelet surface receptor GPIib/IIIa is the final pathway of platelet aggregation, regardless of the initiating stimulus. RGD analogues, peptidomimetics and monoclonal antibodies to GPIib/IIIa have been developed targeting the blockage of the receptor and inhibition of the fibrinogen binding. However, the intrinsic activating effect of GPIIb/IIIa blockers is widely discussed as one potential contributing factor for the disappointing outcome of trials with GPIIb/IIIa inhibitors. An alternative method for thrombus prevention could be the use of specific fibrinogen blockers since they will act at the final step of the platelet aggregation and are expected to leave the receptor unaffected. To achieve this target the design of the fibrinogen ligands could be based on (i) sequences derived from GPIIb/IIIa ligand binding sites, and (ii) sequences complementary to RGD and/or to fibrinogen gamma-chain. The available information, which could be used as a starting point for developing potent fibrinogen ligands, is reviewed. Copyright (C) 2004 European Peptide Society and John Wiley Sons, Ltd. | en |
heal.access | campus | - |
heal.fullTextAvailability | TRUE | - |
heal.identifier.secondary | <Go to ISI>://000224655900001 | - |
heal.identifier.secondary | http://onlinelibrary.wiley.com/store/10.1002/psc.603/asset/603_ftp.pdf?v=1&t=h0f8tzzb&s=a299bba9b484c14fd3f7df6d6376dc97049bc835 | - |
heal.journalName | Journal of Peptide Science | en |
heal.journalType | peer reviewed | - |
heal.language | en | - |
heal.publicationDate | 2004 | - |
heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
heal.type | journalArticle | - |
heal.type.el | Άρθρο Περιοδικού | el |
heal.type.en | Journal article | en |
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