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dc.creatorPatarroyo, Manuel E. 
dc.creatorCifuentes, Gladys 
dc.creatorPiraján, Camilo 
dc.creatorMoreno-Vranich, Armando 
dc.creatorVanegas, Magnolia 
dc.date.accessioned2020-05-26T00:02:37Z
dc.date.available2020-05-26T00:02:37Z
dc.date.created2010
dc.identifier.issn0006291X
dc.identifier.issn10902104
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/23507
dc.description.abstract"Based on the 3D X-ray crystallographic structures of relevant proteins of the malaria parasite involved in invasion to host cells and 3D NMR structures of High Activity Binding Peptides (HABPs) and their respective analogues, it was found that HABPs are rendered into highly immunogenic and sterile immunity inducers in the Aotus experimental model by modifying those amino acids that establish H-bonds with other HABPs or binding to host's cells. This finding adds striking and novel physicochemical principles, at the atomic level, for a logical and rational vaccine development methodology against infectious disease, among them malaria. © 2010 Elsevier Inc. All rights reserved."
dc.format.mimetypeapplication/pdf
dc.language.isoeng
dc.relation.ispartofBiochemical and Biophysical Research Communications, ISSN:0006291X, 10902104, Vol.394, No.3 (2010); pp. 529-535
dc.relation.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-77950517324&doi=10.1016%2fj.bbrc.2010.03.004&partnerID=40&md5=81f947136ff0a7d59323b1ed3dcd4001
dc.sourceinstname:Universidad del Rosario
dc.sourcereponame:Repositorio Institucional EdocUR
dc.titleAtomic evidence that modification of H-bonds established with amino acids critical for host-cell binding induces sterile immunity against malaria
dc.typearticle
dc.subject.keywordMalaria vaccine
dc.subject.keywordParasite antigen
dc.subject.keywordprotozoan
dc.subject.keywordprotozoan
dc.subject.keywordx-ray
dc.subject.keywordbiomolecular
dc.subject.keywordAmino acid composition
dc.subject.keywordAnimal experiment
dc.subject.keywordAnimal model
dc.subject.keywordAotus
dc.subject.keywordArticle
dc.subject.keywordControlled study
dc.subject.keywordHost resistance
dc.subject.keywordHydrogen bond
dc.subject.keywordImmunogenicity
dc.subject.keywordMalaria falciparum
dc.subject.keywordNonhuman
dc.subject.keywordPhysical chemistry
dc.subject.keywordPlasmodium falciparum
dc.subject.keywordPriority journal
dc.subject.keywordVaccine production
dc.subject.keywordAmino acid sequence
dc.subject.keywordAnimals
dc.subject.keywordAntibodies
dc.subject.keywordAntigens
dc.subject.keywordAotus trivirgatus
dc.subject.keywordCrystallography
dc.subject.keywordHost-parasite interactions
dc.subject.keywordHydrogen bonding
dc.subject.keywordMalaria
dc.subject.keywordMalaria vaccines
dc.subject.keywordMolecular sequence data
dc.subject.keywordNuclear magnetic resonance
dc.subject.keywordPeptides
dc.subject.keywordProtein conformation
dc.subject.keywordPlasmodium falciparum
dc.subject.keywordH-bonds
dc.subject.keywordMalaria
dc.subject.keywordPlasmodium falciparum
dc.subject.keywordSterile immunity
dc.rights.accesRightsinfo:eu-repo/semantics/openAccess
dc.type.spaArtículo
dc.rights.accesoAbierto (Texto Completo)
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.identifier.doihttps://doi.org/10.1016/j.bbrc.2010.03.004
dc.relation.citationEndPage535
dc.relation.citationIssueNo. 3
dc.relation.citationStartPage529
dc.relation.citationTitleBiochemical and Biophysical Research Communications
dc.relation.citationVolumeVol. 394


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