Please use this identifier to cite or link to this item: https://hdl.handle.net/11147/11869
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dc.contributor.authorDinç, Melikeen_US
dc.contributor.authorYalçın, Talaten_US
dc.contributor.authorÇavuş, İbrahimen_US
dc.contributor.authorÖzbilgin, Ahmeten_US
dc.date.accessioned2021-12-17T13:16:14Z-
dc.date.available2021-12-17T13:16:14Z-
dc.date.issued2021-11-
dc.identifier.urihttps://doi.org/10.1017/S0031182021001967-
dc.identifier.urihttps://hdl.handle.net/11147/11869-
dc.descriptionNational Mass Spectrometry Application and Research Center (NMSC) in Izmir Institute of Technology (IzTech)en_US
dc.description.abstractLeishmaniasis is an infectious disease in which different clinical manifestations are classified into three main forms as visceral, cutaneous, and mucocutaneous. These disease forms are associated with parasite species of protozoan genus, Leishmania. For instance, Leishmania infantum and Leishmania tropica are typically linked with visceral (VL) and cutaneous (CL) leishmaniasis respectively, however these two species can also cause other form to a lesser extent. What is more alarming is this characteristic, which threatens classic diagnoses and therapies, is started to be acquired by other species. To address this issue, gel-based and gel-free proteomic analyses were carried out on the species, Leishmania infantum to determine the proteins differentiating between the parasites caused visceral and cutaneous leishmaniasis. In addition, Leishmania tropica parasites representing the typical cases for cutaneous leishmaniasis were included. Electrophoresis gels of parasites caused to visceral leishmaniasis were distinguishable from the others in terms of repetitive down-regulation on some specific locations. In addition, a distinct spot of an antioxidant enzyme, superoxide dismutase was shown up only on the gels of cutaneous leishmaniasis samples regardless of the species. In the gel-free approach, 37 proteins which were verified with a second database search using a different search engine, were distinguished from the comparison between VL and CL samples. Among them, 31 proteins for the CL group and 6 proteins for the VL group were determined differentially abundant. Two proteins from the gel-based analysis namely pyruvate kinase and succinly-coA:3-ketoacid-coenzyme A transferase analysis were encountered in the protein list of the CL group.en_US
dc.language.isoenen_US
dc.publisherCambridge University Pressen_US
dc.relation.ispartofParasitologyen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subject2D-PAGEen_US
dc.subjectCutaneousen_US
dc.subjectLeishmaniasisen_US
dc.subjectShotgunen_US
dc.subjectParasiteen_US
dc.titleComparative proteomic analysis of Leishmania parasites isolated from visceral and cutaneous leishmaniasis patientsen_US
dc.typeArticleen_US
dc.authorid0000-0003-0466-1781en_US
dc.authorid0000-0003-3780-702Xen_US
dc.institutionauthorDinç, Melikeen_US
dc.institutionauthorYalçın, Talaten_US
dc.departmentİzmir Institute of Technology. Chemistryen_US
dc.identifier.wosWOS:000727518000001en_US
dc.identifier.scopus2-s2.0-85119509448en_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.identifier.doi10.1017/S0031182021001967-
dc.identifier.pmid34758895en_US
dc.contributor.affiliationIzmir Institute of Technologyen_US
dc.contributor.affiliationIzmir Institute of Technologyen_US
dc.contributor.affiliationManisa Celâl Bayar Üniversitesien_US
dc.contributor.affiliationManisa Celâl Bayar Üniversitesien_US
dc.relation.issn0031-1820en_US
dc.identifier.wosqualityQ2-
item.fulltextWith Fulltext-
item.openairetypeArticle-
item.cerifentitytypePublications-
item.grantfulltextopen-
item.languageiso639-1en-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
crisitem.author.dept04.01. Department of Chemistry-
Appears in Collections:Chemistry / Kimya
PubMed İndeksli Yayınlar Koleksiyonu / PubMed Indexed Publications Collection
Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection
WoS İndeksli Yayınlar Koleksiyonu / WoS Indexed Publications Collection
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