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...

Full description

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/
id UNIANDES2_19fb0321d7982ad78b29308c88bf4073
oai_identifier_str oai:repositorio.uniandes.edu.co:1992/13345
network_acronym_str UNIANDES2
network_name_str Séneca: repositorio Uniandes
repository_id_str
spelling 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
dc.type.redcol.spa.fl_str_mv 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
dc.identifier.instname.spa.fl_str_mv instname:Universidad de los Andes
dc.identifier.reponame.spa.fl_str_mv 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/
dc.rights.accessrights.spa.fl_str_mv info:eu-repo/semantics/openAccess
dc.rights.coar.spa.fl_str_mv http://purl.org/coar/access_right/c_abf2
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
http://purl.org/coar/access_right/c_abf2
eu_rights_str_mv openAccess
dc.format.extent.es_CO.fl_str_mv 61 hojas
dc.format.mimetype.es_CO.fl_str_mv 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 instname:Universidad de los Andes
reponame:Repositorio Institucional Séneca
instname_str Universidad de los Andes
institution Universidad de los Andes
reponame_str Repositorio Institucional Séneca
collection Repositorio Institucional Séneca
bitstream.url.fl_str_mv https://repositorio.uniandes.edu.co/bitstreams/dc4bd469-2466-4536-8977-8d7326c106f3/download
https://repositorio.uniandes.edu.co/bitstreams/2e73b75a-dd5a-42cb-b671-a995f3b451b7/download
https://repositorio.uniandes.edu.co/bitstreams/26dee614-c957-4aa3-a225-c85188b9c233/download
bitstream.checksum.fl_str_mv 94e0a2f54171385f7c33b4a28a5833b0
013102953e8b26429a15d41be173b915
015cca355b924eac14c7099883da39ad
bitstream.checksumAlgorithm.fl_str_mv MD5
MD5
MD5
repository.name.fl_str_mv Repositorio institucional Séneca
repository.mail.fl_str_mv adminrepositorio@uniandes.edu.co
_version_ 1812133822391648256