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The malaria parasite’s Achilles’ heel: Functionallyrelevant invasion structures

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dc.creatorPatarroyo M.E.spa
dc.creatorAlba M.P.spa
dc.creatorReyes C.spa
dc.creatorRojas-Luna R.spa
dc.creatorPatarroyo M.A.spa
dc.date.accessioned2020-05-26T00:05:38Z
dc.date.available2020-05-26T00:05:38Z
dc.date.created2016spa
dc.description.abstractMalaria parasites have their Achilles’ heel; they are vulnerable in small parts of their relevant molecules where they can be wounded and killed. These are sporozoite and merozoite protein conserved high activity binding peptides (cHABPs), playing a critical role in binding to and invasion of host cells (hepatocytes and erythrocytes, respectively). cHABPs can be modified by specific amino acid replacement, according to previously published physicochemical rules, to produce analogues (mHABPs) having left-handed polyproline II (PPIIL)-like structures which can modulate an immune response due to fitting perfectly into the HLA-DR?1* peptide binding region (PBR) and having an appropriate presentation to the T-cell receptor (TCR). © 2015, Caister Academic Press. All rights reserved.eng
dc.format.mimetypeapplication/pdf
dc.identifier.issn14673037
dc.identifier.issn14673045
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/23811
dc.language.isoengspa
dc.publisherCaister Academic Pressspa
dc.relation.citationEndPage20
dc.relation.citationIssueNo. 1
dc.relation.citationStartPage11
dc.relation.citationTitleCurrent Issues in Molecular Biology
dc.relation.citationVolumeVol. 18
dc.relation.ispartofCurrent Issues in Molecular Biology, ISSN:14673037, 14673045, Vol.18, No.1 (2016); pp. 11-20spa
dc.relation.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-84937906953&partnerID=40&md5=dd72bf8f9a437ff3a7ffc89db746d376spa
dc.rights.accesRightsinfo:eu-repo/semantics/openAccess
dc.rights.accesoAbierto (Texto Completo)spa
dc.source.instnameinstname:Universidad del Rosariospa
dc.source.reponamereponame:Repositorio Institucional EdocURspa
dc.subject.keywordHLA DR antigenspa
dc.subject.keywordFalciparumeng
dc.subject.keywordMembrane proteinspa
dc.subject.keywordProlinespa
dc.subject.keywordProtein chabpspa
dc.subject.keywordT lymphocyte receptorspa
dc.subject.keywordUnclassified drugspa
dc.subject.keywordAntimalarial agentspa
dc.subject.keywordProtozoal proteinspa
dc.subject.keywordAmino acid sequencespa
dc.subject.keywordAmino acid substitutionspa
dc.subject.keywordArticlespa
dc.subject.keywordBinding affinityspa
dc.subject.keywordBinding sitespa
dc.subject.keywordHost parasite interactionspa
dc.subject.keywordImmune responsespa
dc.subject.keywordImmunomodulationspa
dc.subject.keywordNonhumanspa
dc.subject.keywordParasite transmissionspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordProtein bindingspa
dc.subject.keywordProtein conformationspa
dc.subject.keywordProtein functionspa
dc.subject.keywordProtein protein interactionspa
dc.subject.keywordProtein structurespa
dc.subject.keywordStructure activity relationspa
dc.subject.keywordStructure analysisspa
dc.subject.keywordAnimalspa
dc.subject.keywordChemistryspa
dc.subject.keywordHost parasite interactionspa
dc.subject.keywordHumanspa
dc.subject.keywordMalariaeng
dc.subject.keywordParasitologyspa
dc.subject.keywordPhysiologyspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordAmino Acid Sequencespa
dc.subject.keywordAnimalsspa
dc.subject.keywordAntimalarialsspa
dc.subject.keywordHost-Parasite Interactionsspa
dc.subject.keywordHumansspa
dc.subject.keywordMalariaeng
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordProtozoan Proteinsspa
dc.titleThe malaria parasite’s Achilles’ heel: Functionallyrelevant invasion structuresspa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
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