Full metadata record
DC Field | Value | Language |
---|---|---|
dc.creator | Vacas, A. (Andrés) | - |
dc.creator | Fernández-Rubio, C. (Celia) | - |
dc.creator | Algarabel, M. (Miriam) | - |
dc.creator | Peña-Guerrero, J. (José) | - |
dc.creator | Larrea, E. (Esther) | - |
dc.creator | Formiga, F.R. (Fabio R.) | - |
dc.creator | García-Sosa, A.T. (Alfonso T.) | - |
dc.creator | Nguewa, P.A. (Paul Alain) | - |
dc.date.accessioned | 2022-02-23T08:28:55Z | - |
dc.date.available | 2022-02-23T08:28:55Z | - |
dc.date.issued | 2019 | - |
dc.identifier.citation | Vacas, A. (Andrés); Fernández-Rubio, C. (Celia); Algarabel, M. (Miriam); et al. "The novel serine/threonine protein kinase LmjF.22.0810 from leishmania major may be involved in the resistance to drugs such as paromomycin". Biomolecules. 9 (11), 2019, 723 | es_ES |
dc.identifier.issn | 2218-273X | - |
dc.identifier.uri | https://hdl.handle.net/10171/62954 | - |
dc.description.abstract | The identification and clarification of the mechanisms of action of drugs used against leishmaniasis may improve their administration regimens and prevent the development of resistant strains. Herein, for the first time, we describe the structure of the putatively essential Ser/Thr kinase LmjF.22.0810 from Leishmania major. Molecular dynamics simulations were performed to assess the stability of the kinase model. The analysis of its sequence and structure revealed two druggable sites on the protein. Furthermore, in silico docking of small molecules showed that aminoglycosides preferentially bind to the phosphorylation site of the protein. Given that transgenic LmjF.22.0810-overexpressing parasites displayed less sensitivity to aminoglycosides such as paromomycin, our predicted models support the idea that the mechanism of drug resistance observed in those transgenic parasites is the tight binding of such compounds to LmjF.22.0810 associated with its overexpression. These results may be helpful to understand the complex machinery of drug response in Leishmania. | es_ES |
dc.description.sponsorship | This research was funded by Obra Social la Caixa and Fundación Caja Navarra, Gobierno de Navarra Salud (12/2017), Fundación Roviralta, Ubesol, Inversiones Garcilaso de la Vega S. L., by Government of Navarre and Laser Ebro. J.P.-G. was supported by a Ministerio de Educacion Cultura y Deporte fellowship (FPU17/03304). A.T.G.-S. thanks Haridus- ja teadusministeerium for grant IUT34-14. | es_ES |
dc.language.iso | eng | es_ES |
dc.publisher | MDPI AG | es_ES |
dc.rights | info:eu-repo/semantics/openAccess | es_ES |
dc.subject | Leishmania | es_ES |
dc.subject | NTD | es_ES |
dc.subject | Docking | es_ES |
dc.subject | Molecular dynamics | es_ES |
dc.subject | Drug resistance | es_ES |
dc.subject | Paromomycin | es_ES |
dc.subject | Kinase | es_ES |
dc.subject | Treatment | es_ES |
dc.subject | LmjF.22.0810 | es_ES |
dc.subject | LmJean3 | es_ES |
dc.title | The novel serine/threonine protein kinase LmjF.22.0810 from leishmania major may be involved in the resistance to drugs such as paromomycin | es_ES |
dc.type | info:eu-repo/semantics/article | es_ES |
dc.description.note | Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/) | es_ES |
dc.identifier.doi | 10.3390/biom9110723 | - |
dadun.citation.number | 11 | es_ES |
dadun.citation.publicationName | Biomolecules | es_ES |
dadun.citation.startingPage | 723 | es_ES |
dadun.citation.volume | 9 | es_ES |
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