Estudio de la Miosina C de Plasmodium falciparum (PfMYO-C)

dc.contributor.advisorChaparro Olaya, Jacqueline
dc.contributor.authorAponte Briceño, Samanda Lizbeth
dc.date.accessioned2023-03-02T15:06:20Z
dc.date.available2023-03-02T15:06:20Z
dc.date.issued2011
dc.description.abstractDe las cinco especies de Plasmodium que causan la malaria, P. falciparum es la que produce la mayor mortalidad en el mundo, a pesar de los esfuerzos de los países endémicos por implementar diferentes estrategias para su control y potencial erradicación. El conocimiento de los procesos biológicos de P. falciparum es una herramienta clave para la postulación de blancos terapéuticos o blancos para vacunas. Las miosinas son proteínas motoras que participan en muchos de estos procesos en las células eucariotas y hasta el momento en P. falciparum se han identificado seis secuencias que codifican para miosinas y se han caracterizado cinco durante el ciclo intraeritrocitario. Por su transcripción, localización y función, dos de estas miosinas se han visto potencialmente involucradas en el proceso de invasión (Pfmyo-A y Pfmyo-B) mientras que las otras tres (Pfmyo-D, Pfmyo-E y Pfmyo-F) al parecer se encuentran actuando en procesos diferentes aún desconocidos. Pfmyo-C es la única miosina de P. falciparum que aún no se ha caracterizado; sinembargo de esta proteína se conoce su patrón de transcripción y varias características particulares en su secuencia, en especial la presencia de repeticiones de tipo WD40 que sugieren que esta miosina puede estar involucrada en procesos diferentes al de la invasión. El objetivo de este trabajo fue realizar un acercamiento a la caracterización de Pfmyo-C durante el ciclo intraeritrocitario en cuanto a su transcripción, expresión y localización, así como analizar su secuencia empleando herramientas bioinformáticas con el fin de inferir la posible función de esta proteína en P. falciparum. Los resultados obtenidos mediante RT-PCR muestran que la expresión de mARN de Pfmyo-C se da principalmente en el estadío de trofozoitos maduros y esquizontes tempranos, y este patrón correlaciona directamente con la expresión de Pfmyo-C en el estadío de esquizonte temprano determinada por western-blot empleando sueros policlonales obtenidos a partir de ratones inoculados con una proteína recombinante para Pfmyo-C. No obstante, el tamaño detectado de la proteína no correlaciona con el tamaño esperado (250KDa), lo que nos hace sugerir la presencia de un intrón no predicho en las bases de datos, o la existencia de una modificación o procesamiento de la proteína. Con base en los análisis de dominios de Pfmyo-C, podemos sugerir de manera muy preliminar que esta proteína puede estar involucrada en procesos de transducción de señales durante las últimas etapas de desarrollo del parásito dentro del glóbulo rojo.spa
dc.description.abstractenglishIn spite of the efforts made in order to implement strategies for its control and potential eradication, Malaria remains the most important vector-borne infectious disease. Currently, it is worldwide accepted that knowledge of the biological processes of Plasmodium falciparum is a key tool for the postulation of therapeutic targets and vaccines candidates. Myosins are molecular motors involved in many processes for a range of functions like muscle contraction, vision, hearing, and host cell invasion of Apicomplexa, phylum which comprises unicellular eukaryotes that live as obligate intracellular parasites and includes important pathogens such as Plasmodium. Sequence encoding six „true‟ myosin genes is present in the genome of P. falciparum and until today, five of these myosins have been characterized during the red blood cell cycle of the parasite. Due to their pattern of transcription, location and expression, two of these myosins are apparently involved in the invasion process (Pfmyo-A and Pfmyo-B) whereas the other three (Pfmyo-D, Pfmyo-E and Pfmyo-F) do not. Since Pfmyo-C is the only one myosin not characterized in P. falciparum, the aim of this project was to define the transcription and expression patterns as well as the cellular localization of Pfmyo-C along the intra red blood cell cycle of the parasite. We also analyzed Pfmyo-C sequence using bioinformatics with the purpose of inferring possible functions of the protein. The results show that the transcription of the pfmyo-c gene occurs mainly in the stage of mature trophozoites and early schizonts, and this pattern correlates directly with the specific expression of Pfmyo-C in the early schizont stage. However, the size of the protein detected is smaller than the expected one (250KDa) and that suggests the presence of a non-predicted intron or a potential modification of the protein. Finally, the bioinformatics analysis let us to suggest that Pfmyo-C can be involved in signal transduction processes during the last stages of the asexual cycle of the parasite.eng
dc.description.degreelevelMaestríaspa
dc.description.degreenameMagíster en Ciencias Básicas Biomédicasspa
dc.format.mimetypeapplication/pdf
dc.identifier.instnameinstname:Universidad El Bosquespa
dc.identifier.reponamereponame:Repositorio Institucional Universidad El Bosquespa
dc.identifier.repourlrepourl:https://repositorio.unbosque.edu.co
dc.identifier.urihttps://hdl.handle.net/20.500.12495/10091
dc.language.isospa
dc.publisher.facultyFacultad de Medicinaspa
dc.publisher.grantorUniversidad El Bosquespa
dc.publisher.programMaestría en Ciencias Básicas Biomédicasspa
dc.relation.referencesAbrahamsen, M. S., T. J. Templeton, et al. (2004). "Complete genome sequence of the Apicomplexan, Cryptosporidium parvum." Science 304(5669): 441-445.spa
dc.relation.referencesAmino, R., S. Thiberge, et al. (2006). "Quantitative imaging of Plasmodiumsporozoites in the mammalian host." C R Biol 329(11): 858-862.spa
dc.relation.referencesBannister, L. H., J. M. Hopkins, et al. (2000). "A brief illustrated guide to the ultrastructure of Plasmodium falciparum asexual blood stages." Parasitology Today 16(10): 427-433.spa
dc.relation.referencesBaum, J., A. T. Papenfuss, et al. (2006). "Regulation of Apicomplexan actin-based motility." Nat Rev Microbiol 4(8): 621-628.spa
dc.relation.referencesBen Mamoun, C., I. Y. Gluzman, et al. (2001). "Co-ordinated programme of gene expression during asexual intraerythrocytic development of the human malaria parasite Plasmodiumfalciparum revealed by microarray analysis." Mol Microbiol 39(1): 26-36.spa
dc.relation.referencesBergman, L. W., K. Kaiser, et al. (2003). "Myosin A tail domain interacting protein (MTIP) localizes to the inner membrane complex of Plasmodium sporozoites." J Cell Sci 116(Pt 1): 39-49.spa
dc.relation.referencesBotero, D. and M. Restrepo (2005). Parasitosis Humanas. Medellin, Antioquia.spa
dc.relation.referencesBozdech, Z., M. Llinas, et al. (2003). "The transcriptome of the intraerythrocytic developmental cycle of Plasmodiumfalciparum." PLoS Biol 1(1): E5.spa
dc.relation.referencesBradford, M. M. (1976). "A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding." Anal Biochem 72: 248-254.spa
dc.relation.referencesBuguliskis, J. S., F. Brossier, et al. (2010). "Rhomboid 4 (ROM4) affects the processing of surface adhesins and facilitates host cell invasion by Toxoplasma gondii." PLoS Pathog 6(4): e1000858.spa
dc.relation.referencesBuscaglia, C. A., I. Coppens, et al. (2003). "Sites of interaction between aldolase and thrombospondin-related anonymous protein in Plasmodium." Mol Biol Cell 14(12): 4947-4957.spa
dc.relation.referencesColigan, J., B. Dunn, et al., Eds. (2003). Short Protocols in Protein Science: a compendium of methods from current protocols in protein science. USA, Wiley.spa
dc.relation.referencesColuccio, L. M. (2008). Myosins: A superfamily of molecular motors. Watertown, MA USA, Springer.spa
dc.relation.referencesCooper, G. M. (2000). The Cell, A Molecular Approach. Boston University.spa
dc.relation.referencesChaparro-Olaya, J., A. R. Dluzewski, et al. (2003). "The multiple myosins of malaria: The smallest malaria myosin, Plasmodium falciparum myosin-B (Pfmyo-B) is expressed in mature schizonts and merozoites." Europ. J. Protistol 39: 423–427.spa
dc.relation.referencesChaparro-Olaya, J., G. Margos, et al. (2005). "Plasmodiumfalciparum myosins: transcription and translation during asexual parasite development." Cell Motil Cytoskeleton 60(4): 200-213.spa
dc.relation.referencesChavatte, J. M., F. Chiron, et al. (2007). "[Probable speciations by "host-vector 'fidelity'": 14 species of Plasmodium from magpies]." Parasite 14(1): 21-37.spa
dc.relation.referencesDame, J. B., D. E. Arnot, et al. (1996). "Current status of the Plasmodium falciparum genome project." Mol Biochem Parasitol 79(1): 1-12.spa
dc.relation.referencesDelbac, F., A. Sanger, et al. (2001). "Toxoplasma gondii myosins B/C: one gene, two tails, two localizations, and a role in parasite division." J Cell Biol 155(4): 613-623.spa
dc.relation.referencesDesnos, C., S. Huet, et al. (2007). "'Should I stay or should I go?': myosin V function in organelle trafficking." Biol Cell 99(8): 411-423.spa
dc.relation.referencesDobrowolski, J. M., V. B. Carruthers, et al. (1997). "Participation of myosin in gliding motility and host cell invasion by Toxoplasma gondii." Mol Microbiol 26(1): 163-173.spa
dc.relation.referencesDubrovskaya, V., A. C. Lavigne, et al. (1996). "Distinct domains of hTAFII100 are required for functional interaction with transcription factor TFIIF beta (RAP30) and incorporation into the TFIID complex." Embo J 15(14): 3702-3712.spa
dc.relation.referencesDunn, T. A., S. Chen, et al. (2006). "A novel role of myosin VI in human prostate cancer." Am J Pathol 169(5): 1843-1854.spa
dc.relation.referencesFerreira, M. a. P., H (2008). Control of Gene Expression in Plasmodium. Bioinformatics in Tropical Disease Research: A Practical and Case-Study Approach. e. B. (MD):, National Library of Medicine (US) NCBI.spa
dc.relation.referencesFoth, B. J., M. C. Goedecke, et al. (2006). "New insights into myosin evolution and classification." Proc Natl Acad Sci U S A 103(10): 3681-3686.spa
dc.relation.referencesFrackman, S. (1999). "Rapid Ligation for the pGEM®-T and pGEM®-T Easy Vector Systems." Promega Notes 71: 08.spa
dc.relation.referencesFrankel, S., R. Sohn, et al. (1991). "The use of sarkosyl in generating soluble protein after bacterial expression." Proc Natl Acad Sci U S A 88(4): 1192-1196.spa
dc.relation.referencesGanter, M., H. Schuler, et al. (2009). "Vital role for the Plasmodiumactin capping protein (CP) beta-subunit in motility of malaria sporozoites." Mol Microbiol 74(6): 1356-1367.spa
dc.relation.referencesGardner, M. J., N. Hall, et al. (2002). "Genome sequence of the human malaria parasite Plasmodium falciparum." Nature 419(6906): 498-511.spa
dc.relation.referencesGeisbrecht, E. R. and D. J. Montell (2002). "Myosin VI is required for E-cadherin-mediated border cell migration." Nat Cell Biol 4(8): 616-620.spa
dc.relation.referencesGerich, B., L. Orci, et al. (1995). "Non-clathrin-coat protein alpha is a conserved subunit of coatomer and in Saccharomyces cerevisiae is essential for growth." Proc Natl Acad Sci U S A 92(8): 3229-3233.spa
dc.relation.referencesGonsalvez, G. B., C. R. Urbinati, et al. (2005). "RNA localization in yeast: moving towards a mechanism." Biol Cell 97(1): 75-86.spa
dc.relation.referencesHakansson, S., H. Morisaki, et al. (1999). "Time-lapse video microscopy of gliding motility in Toxoplasma gondii reveals a novel, biphasic mechanism of cell locomotion." Mol Biol Cell 10(11): 3539-3547.spa
dc.relation.referencesHarlow, Ed. (1988). Antibodies a laboratory Manual. United States of America, Cold Spring Harbor Laboratory.spa
dc.relation.referencesHeintzelman, M. B. (2006). "Cellular and molecular mechanics of gliding locomotion in eukaryotes." Int Rev Cytol 251: 79-129.spa
dc.relation.referencesHeintzelman, M. B. and M. J. Mateer (2008). "GpMyoF, a WD40 repeat-containing myosin associated with the myonemes of Gregarina polymorpha." J Parasitol 94(1): 158-168.spa
dc.relation.referencesHeintzelman, M. B. and J. D. Schwartzman (1997). "A novel class of unconventional myosins from Toxoplasma gondii." J Mol Biol 271(1): 139-146.spa
dc.relation.referencesHerm-Gotz, A., S. Weiss, et al. (2002). "Toxoplasma gondii myosin A and its light chain: a fast, singleheaded, plus-end-directed motor." Embo J 21(9): 2149-2158.spa
dc.relation.referencesHettmann, C., A. Herm, et al. (2000). "A dibasic motif in the tail of a class XIV Apicomplexan myosin is an essential determinant of plasma membrane localization." Mol Biol Cell 11(4): 1385-1400.spa
dc.relation.referencesHofmann, W. A., T. Johnson, et al. (2006). "From transcription to transport: emerging roles for nuclear myosin I." Biochem Cell Biol 84(4): 418-426.spa
dc.relation.referencesHudson, A. M. and L. Cooley (2008). "Phylogenetic, structural and functional relationships between WD- and Kelch-repeat proteins." Subcell Biochem 48: 6-19.spa
dc.relation.referencesKim, S. V., W. Z. Mehal, et al. (2006). "Modulation of cell adhesion and motility in the immune system by Myo1f." Science 314(5796): 136-139.spa
dc.relation.referencesKirsten Moll, I. L., Hedvig Perlmann, Artur Scherf, Mats Wahlgren (2008). METHODS IN MALARIA RESEARCH MR4. Manassas Virginia: 351.spa
dc.relation.referencesKokubo, T., D. W. Gong, et al. (1993). "Molecular cloning, expression, and characterization of the Drosophila 85-kilodalton TFIID subunit." Mol Cell Biol 13(12): 7859-7863.spa
dc.relation.referencesKros, C. J., W. Marcotti, et al. (2002). "Reduced climbing and increased slipping adaptation in cochlear hair cells of mice with Myo7a mutations." Nat Neurosci 5(1): 41-47.spa
dc.relation.referencesLANCHEROS, E. R. (2007). Estudio de las miosinas Pfmyo-E y Pfmyo-F de Plasmodiumfalciparum. Maestria en Ciencias-Bioquimica. Bogotá- Colombia, Universidad Nacional de Colombia.spa
dc.relation.referencesLi, D. and R. Roberts (2001). "WD-repeat proteins: structure characteristics, biological function, and their involvement in human diseases." Cell Mol Life Sci 58(14): 2085-2097.spa
dc.relation.referencesLu, F., H. Jiang, et al. (2007). "cDNA sequences reveal considerable gene prediction inaccuracy in the Plasmodiumfalciparum genome." BMC Genomics 8: 255.spa
dc.relation.referencesLu, Q., D. C. Pallas, et al. (2004). "Striatin assembles a membrane signaling complex necessary for rapid, nongenomic activation of endothelial NO synthase by estrogen receptor alpha." Proc Natl Acad Sci U S A 101(49): 17126-17131.spa
dc.relation.referencesMargos, G., I. Siden-Kiamos, et al. (2000). "Myosin A expressions in sporogonic stages of Plasmodium." Mol Biochem Parasitol 111(2): 465-469.spa
dc.relation.referencesMatuschewski, K., M. M. Mota, et al. (2001). "Identification of the class XIV myosins Pb-MyoA and PyMyoA and expression in Plasmodium sporozoites." Mol Biochem Parasitol 112(1): 157-161.spa
dc.relation.referencesMatuschewski, K. and H. Schuler (2008). "Actin/myosin-based gliding motility in Apicomplexan parasites." Subcell Biochem 47: 110-120.spa
dc.relation.referencesMeissner, M., M. Reiss, et al. (2002). "A family of transmembrane microneme proteins of Toxoplasma gondii contain EGF-like domains and function as escorters." J Cell Sci 115(Pt 3): 563-574.spa
dc.relation.referencesMeissner, M., D. Schluter, et al. (2002). "Role of Toxoplasma gondii myosin A in powering parasite gliding and host cell invasion." Science 298(5594): 837-840.spa
dc.relation.referencesMenard, R. (2001). "Gliding motility and cell invasion by Apicomplexa: insights from the Plasmodium sporozoite." Cell Microbiol 3(2): 63-73.spa
dc.relation.referencesMorrissette, N. S. and L. D. Sibley (2002). "Cytoskeleton of Apicomplexan parasites." Microbiol Mol Biol Rev 66(1): 21-38; table of contents.spa
dc.relation.referencesNOVAGEN (2006). pET System Manual 11a Edition: 1-80. Osterweil, E., D. G. Wells, et al. (2005). "A role for myosin VI in postsynaptic structure and glutamate receptor endocytosis." J Cell Biol 168(2): 329-338.spa
dc.relation.referencesPain, A., H. Renauld, et al. (2005). "Genome of the host-cell transforming parasite Theileria annulate compared with T. parva." Science 309(5731): 131-133.spa
dc.relation.referencesPinder, J., R. Fowler, et al. (2000). "Motile systems in malaria merozoites: how is the red blood cell invaded?" Parasitol Today 16(6): 240-245.spa
dc.relation.referencesPinder, J. C., R. E. Fowler, et al. (1998). "Actomyosin motor in the merozoite of the malaria parasite, Plasmodiumfalciparum: implications for red cell invasion." J Cell Sci 111 ( Pt 13): 1831-1839.spa
dc.relation.referencesPorter, J. A., B. Minke, et al. (1995). "Calmodulin binding to Drosophila NinaC required for termination of phototransduction." Embo J 14(18): 4450-4459.spa
dc.relation.referencesPoupel, O. and I. Tardieux (1999). "Toxoplasma gondii motility and host cell invasiveness are drastically impaired by jasplakinolide, a cyclic peptide stabilizing F-actin." Microbes Infect 1(9): 653-662.spa
dc.relation.referencesReck-Peterson, S. L., D. W. Provance, Jr., et al. (2000). "Class V myosins." Biochim Biophys Acta 1496(1): 36-51.spa
dc.relation.referencesRichards, T. A. and T. Cavalier-Smith (2005). "Myosin domain evolution and the primary divergence of eukaryotes." Nature 436(7054): 1113-1118.spa
dc.relation.referencesSahoo, N., W. Beatty, et al. (2006). "Unusual kinetic and structural properties control rapid assembly and turnover of actin in the parasite Toxoplasma gondii." Mol Biol Cell 17(2): 895-906.spa
dc.relation.referencesScheer, J. M. and C. A. Ryan (2001). "A method for the quantitative recovery of proteins from polyacrylamide gels." Anal Biochem 298(1): 130-132.spa
dc.relation.referencesSchmitz, S., M. Grainger, et al. (2005). "Malaria parasite actin filaments are very short." J Mol Biol 349(1): 113-125.spa
dc.relation.referencesSchmitz, S., I. A. Schaap, et al. (2010). "Malaria parasite actin polymerisation and filament structure." J Biol Chem.spa
dc.relation.referencesSchuler, H. and K. Matuschewski (2006). "Regulation of Apicomplexan microfilament dynamics by a minimal set of actin-binding proteins." Traffic 7(11): 1433-1439.spa
dc.relation.referencesSchuler, H., A. K. Mueller, et al. (2005). "A Plasmodium actin-depolymerizing factor that binds exclusively to actin monomers." Mol Biol Cell 16(9): 4013-4023.spa
dc.relation.referencesSchuler, H., A. K. Mueller, et al. (2005). "Unusual properties of Plasmodiumfalciparum actin: new insights into microfilament dynamics of Apicomplexan parasites." FEBS Lett 579(3): 655-660.spa
dc.relation.referencesSiden-Kiamos, I., J. C. Pinder, et al. (2006). "Involvement of actin and myosins in Plasmodiumberghei ookinete motility." Mol Biochem Parasitol 150(2): 308-317.spa
dc.relation.referencesSIVIGILA, I. N. d. S. d. C. (2009). Comportamiento de la malaria en Colombia según los casos notificados al sivigila en 2009. Bogotá- Colombia, Instituto Nacional de Salud.spa
dc.relation.referencesSmith, T. F., C. Gaitatzes, et al. (1999). "The WD repeat: a common architecture for diverse functions." Trends Biochem Sci 24(5): 181-185.spa
dc.relation.referencesSong, J. J. and R. E. Kingston (2008). "WDR5 interacts with mixed lineage leukemia (MLL) protein via the histone H3-binding pocket." J Biol Chem 283(50): 35258-35264.spa
dc.relation.referencesStow, J. L., K. R. Fath, et al. (1998). "Budding roles for myosin II on the Golgi." Trends Cell Biol 8(4): 138141.spa
dc.relation.referencesThompson RF, Langford GM. 2002; Myosin superfamily evolutionary history. Anat Rec. 268(3):276-89.spa
dc.relation.referencesVale, R. D. (2003). "The molecular motor toolbox for intracellular transport." Cell 112(4): 467-480.spa
dc.relation.referencesVBI, V. B. i. (2010). "Plasmo DB;PlasmodiumGenomics Resource." Version 7.0. Retrieved 22 Sep 2010.spa
dc.relation.referencesVlachou, D., T. Zimmermann, et al. (2004). "Real-time, in vivo analysis of malaria ookinete locomotion and mosquito midgut invasion." Cell Microbiol 6(7): 671-685.spa
dc.relation.referencesWagner, M. C., B. L. Blazer-Yost, et al. (2005). "Expression of the unconventional myosin Myo1c alters sodium transport in M1 collecting duct cells." Am J Physiol Cell Physiol 289(1): C120-129.spa
dc.relation.referencesWakaguri, H., Y. Suzuki, et al. (2009). "Inconsistencies of genome annotations in Apicomplexan parasites revealed by 5'-end-one-pass and full-length sequences of oligo-capped cDNAs." BMC Genomics 10: 312.spa
dc.relation.referencesWesseling, J. G., P. J. Snijders, et al. (1989). "Stage-specific expression and genomic organization of the actin genes of the malaria parasite Plasmodiumfalciparum." Mol Biochem Parasitol 35(2): 167176.spa
dc.relation.referencesWetzel, D. M., S. Hakansson, et al. (2003). "Actin filament polymerization regulates gliding motility by Apicomplexan parasites." Mol Biol Cell 14(2): 396-406.spa
dc.relation.referencesWhite, N. J. (2008). "Plasmodiumknowlesi: the fifth human malaria parasite." Clin Infect Dis 46(2): 172-173.spa
dc.relation.referencesWHO, W. H. O., UNICEF (2008). Word Malaria Report 2008. Geneva.spa
dc.relation.referencesWHO, W. H. O., UNICEF (2009). Word Malaria Report 2009. Geneva.spa
dc.relation.referencesWilkerson, C. G., S. M. King, et al. (1995). "The 78,000 M(r) intermediate chain of Chlamydomonas outer arm dynein isa WD-repeat protein required for arm assembly." J Cell Biol 129(1): 169-178.spa
dc.relation.referencesWiser, M. F., L. V. Faur, et al. (1993). "Accessibility and distribution of intraerythrocytic antigens of Plasmodium-infected erythrocytes following mild glutaraldehyde fixation and detergent extraction." Parasitol Res 79(7): 579-586.spa
dc.relation.referencesXu, C., C. Bian, et al. (2010). "Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2)." Proc Natl Acad Sci U S A 107(45): 1926619271.spa
dc.relation.referencesYoshida, H., W. Cheng, et al. (2004). "Lessons from border cell migration in the Drosophila ovary: A role for myosin VI in dissemination of human ovarian cancer." Proc Natl Acad Sci U S A 101(21): 8144-8149.spa
dc.rights.accessrightsinfo:eu-repo/semantics/closedAccess
dc.rights.accessrightshttps://purl.org/coar/access_right/c_14cb
dc.subjectMiosina Cspa
dc.subjectPlasmodium falciparumspa
dc.subjectBlancos terapéuticosspa
dc.subjectBlancos para vacunasspa
dc.subject.keywordsMyosin Cspa
dc.subject.keywordsPlasmodium falciparumspa
dc.subject.keywordsTherapeutic Targetsspa
dc.subject.keywordsVaccine Targetsspa
dc.subject.nlmW 50
dc.titleEstudio de la Miosina C de Plasmodium falciparum (PfMYO-C)spa
dc.title.translatedPlasmodium falciparum myosin C (PfMYO-C) studyspa
dc.type.coarhttps://purl.org/coar/resource_type/c_bdcc
dc.type.coarversionhttps://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.driverinfo:eu-repo/semantics/masterThesis
dc.type.hasversioninfo:eu-repo/semantics/acceptedVersion
dc.type.localTesis/Trabajo de grado - Monografía - Maestríaspa

Archivos

Bloque original
Mostrando 1 - 1 de 1
No hay miniatura disponible
Nombre:
Estudio de la Miosina C de Plasmodium falciparum (PfMYO-C)
Tamaño:
2.6 MB
Formato:
Adobe Portable Document Format
Descripción:
Estudio de la Miosina C de Plasmodium falciparum (PfMYO-C)
Bloque de licencias
Mostrando 1 - 1 de 1
No hay miniatura disponible
Nombre:
license.txt
Tamaño:
1.71 KB
Formato:
Item-specific license agreed upon to submission
Descripción: