Biochemical characterization of cytidine triphosphate synthase (CTPase) from Toxoplasma gondii
Toxoplasma gondii is a ubiquitous intracellular parasite with worldwide distribution. New antiparasitic drugs with greater effectiveness in controlling T. gondii are necessary. The enzymes of de novo pyrimidine biosynthetic pathway are considered potential drug targets, because they are required for...
- Autores:
-
López Moreno, Andrea Johana
- Tipo de recurso:
- Fecha de publicación:
- 2015
- Institución:
- Universidad de los Andes
- Repositorio:
- Séneca: repositorio Uniandes
- Idioma:
- eng
- OAI Identifier:
- oai:repositorio.uniandes.edu.co:1992/13345
- Acceso en línea:
- http://hdl.handle.net/1992/13345
- Palabra clave:
- Toxoplasma gondii - Investigaciones
Interacciones proteína-proteína - Investigaciones
Biología
- Rights
- openAccess
- License
- http://creativecommons.org/licenses/by-nc-sa/4.0/
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Al consultar y hacer uso de este recurso, está aceptando las condiciones de uso establecidas por los autores.http://creativecommons.org/licenses/by-nc-sa/4.0/info:eu-repo/semantics/openAccesshttp://purl.org/coar/access_right/c_abf2Zimmermann, Barbara Hanna81271423-588b-479b-a844-0d7443608a49500Morizono, Hirokifd90ab6c-aa4b-48fd-8117-20c6f7b733a7500Garavito Aguilar, Zayra Vivianavirtual::1875-1López Moreno, Andrea Johanae502b006-2e0c-4cc5-a543-60d87108dc4d5002018-09-28T10:34:15Z2018-09-28T10:34:15Z2015http://hdl.handle.net/1992/13345u722094.pdfinstname:Universidad de los Andesreponame:Repositorio Institucional Sénecarepourl:https://repositorio.uniandes.edu.co/Toxoplasma gondii is a ubiquitous intracellular parasite with worldwide distribution. New antiparasitic drugs with greater effectiveness in controlling T. gondii are necessary. The enzymes of de novo pyrimidine biosynthetic pathway are considered potential drug targets, because they are required for the parasite' s virulence and survival. Cytidine triphosphate synthase (CTPase) catalyzes the conversion of UTP to CTP, the final step in the production of cytidine nucleotides, and the first step in the formation of phospholipid intermediates. In many organisms, CTPase also plays a structural role in vivo, forming filaments together with other proteins. The function of these filaments is unknown, and identification of their protein components could aid in elucidating function. Our goal was the biochemical characterization of cytidine triphosphate synthase of T. gondii (TgCTPase), and generated tools to study protein-protein interactions, in order to begin to determine its importance as a potential antiparasitic targetMagíster en BiologíaMaestría61 hojasapplication/pdfengUniandesMaestría en Ciencias BiológicasFacultad de CienciasDepartamento de Biologíainstname:Universidad de los Andesreponame:Repositorio Institucional SénecaBiochemical characterization of cytidine triphosphate synthase (CTPase) from Toxoplasma gondiiTrabajo de grado - Maestríainfo:eu-repo/semantics/masterThesishttp://purl.org/coar/version/c_970fb48d4fbd8a85Texthttp://purl.org/redcol/resource_type/TMToxoplasma gondii - InvestigacionesInteracciones proteína-proteína - InvestigacionesBiologíaPublicationhttps://scholar.google.es/citations?user=J1xQFB4AAAAJvirtual::1875-10000-0001-5671-7017virtual::1875-1https://scienti.minciencias.gov.co/cvlac/visualizador/generarCurriculoCv.do?cod_rh=0001443145virtual::1875-14033451d-4829-428f-99e0-968786798fcbvirtual::1875-14033451d-4829-428f-99e0-968786798fcbvirtual::1875-1ORIGINALu722094.pdfapplication/pdf9249498https://repositorio.uniandes.edu.co/bitstreams/dc4bd469-2466-4536-8977-8d7326c106f3/download94e0a2f54171385f7c33b4a28a5833b0MD51THUMBNAILu722094.pdf.jpgu722094.pdf.jpgIM Thumbnailimage/jpeg5157https://repositorio.uniandes.edu.co/bitstreams/2e73b75a-dd5a-42cb-b671-a995f3b451b7/download013102953e8b26429a15d41be173b915MD55TEXTu722094.pdf.txtu722094.pdf.txtExtracted texttext/plain110868https://repositorio.uniandes.edu.co/bitstreams/26dee614-c957-4aa3-a225-c85188b9c233/download015cca355b924eac14c7099883da39adMD541992/13345oai:repositorio.uniandes.edu.co:1992/133452024-03-13 12:04:12.294http://creativecommons.org/licenses/by-nc-sa/4.0/open.accesshttps://repositorio.uniandes.edu.coRepositorio institucional Sénecaadminrepositorio@uniandes.edu.co |
dc.title.es_CO.fl_str_mv |
Biochemical characterization of cytidine triphosphate synthase (CTPase) from Toxoplasma gondii |
title |
Biochemical characterization of cytidine triphosphate synthase (CTPase) from Toxoplasma gondii |
spellingShingle |
Biochemical characterization of cytidine triphosphate synthase (CTPase) from Toxoplasma gondii Toxoplasma gondii - Investigaciones Interacciones proteína-proteína - Investigaciones Biología |
title_short |
Biochemical characterization of cytidine triphosphate synthase (CTPase) from Toxoplasma gondii |
title_full |
Biochemical characterization of cytidine triphosphate synthase (CTPase) from Toxoplasma gondii |
title_fullStr |
Biochemical characterization of cytidine triphosphate synthase (CTPase) from Toxoplasma gondii |
title_full_unstemmed |
Biochemical characterization of cytidine triphosphate synthase (CTPase) from Toxoplasma gondii |
title_sort |
Biochemical characterization of cytidine triphosphate synthase (CTPase) from Toxoplasma gondii |
dc.creator.fl_str_mv |
López Moreno, Andrea Johana |
dc.contributor.advisor.none.fl_str_mv |
Zimmermann, Barbara Hanna Morizono, Hiroki Garavito Aguilar, Zayra Viviana |
dc.contributor.author.none.fl_str_mv |
López Moreno, Andrea Johana |
dc.subject.keyword.es_CO.fl_str_mv |
Toxoplasma gondii - Investigaciones Interacciones proteína-proteína - Investigaciones |
topic |
Toxoplasma gondii - Investigaciones Interacciones proteína-proteína - Investigaciones Biología |
dc.subject.themes.none.fl_str_mv |
Biología |
description |
Toxoplasma gondii is a ubiquitous intracellular parasite with worldwide distribution. New antiparasitic drugs with greater effectiveness in controlling T. gondii are necessary. The enzymes of de novo pyrimidine biosynthetic pathway are considered potential drug targets, because they are required for the parasite' s virulence and survival. Cytidine triphosphate synthase (CTPase) catalyzes the conversion of UTP to CTP, the final step in the production of cytidine nucleotides, and the first step in the formation of phospholipid intermediates. In many organisms, CTPase also plays a structural role in vivo, forming filaments together with other proteins. The function of these filaments is unknown, and identification of their protein components could aid in elucidating function. Our goal was the biochemical characterization of cytidine triphosphate synthase of T. gondii (TgCTPase), and generated tools to study protein-protein interactions, in order to begin to determine its importance as a potential antiparasitic target |
publishDate |
2015 |
dc.date.issued.none.fl_str_mv |
2015 |
dc.date.accessioned.none.fl_str_mv |
2018-09-28T10:34:15Z |
dc.date.available.none.fl_str_mv |
2018-09-28T10:34:15Z |
dc.type.spa.fl_str_mv |
Trabajo de grado - Maestría |
dc.type.coarversion.fl_str_mv |
http://purl.org/coar/version/c_970fb48d4fbd8a85 |
dc.type.driver.spa.fl_str_mv |
info:eu-repo/semantics/masterThesis |
dc.type.content.spa.fl_str_mv |
Text |
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http://purl.org/redcol/resource_type/TM |
dc.identifier.uri.none.fl_str_mv |
http://hdl.handle.net/1992/13345 |
dc.identifier.pdf.none.fl_str_mv |
u722094.pdf |
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instname:Universidad de los Andes |
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reponame:Repositorio Institucional Séneca |
dc.identifier.repourl.spa.fl_str_mv |
repourl:https://repositorio.uniandes.edu.co/ |
url |
http://hdl.handle.net/1992/13345 |
identifier_str_mv |
u722094.pdf instname:Universidad de los Andes reponame:Repositorio Institucional Séneca repourl:https://repositorio.uniandes.edu.co/ |
dc.language.iso.es_CO.fl_str_mv |
eng |
language |
eng |
dc.rights.uri.*.fl_str_mv |
http://creativecommons.org/licenses/by-nc-sa/4.0/ |
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info:eu-repo/semantics/openAccess |
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openAccess |
dc.format.extent.es_CO.fl_str_mv |
61 hojas |
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application/pdf |
dc.publisher.es_CO.fl_str_mv |
Uniandes |
dc.publisher.program.es_CO.fl_str_mv |
Maestría en Ciencias Biológicas |
dc.publisher.faculty.es_CO.fl_str_mv |
Facultad de Ciencias |
dc.publisher.department.es_CO.fl_str_mv |
Departamento de Biología |
dc.source.es_CO.fl_str_mv |
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Universidad de los Andes |
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