Publication:
Cloning and characterization of Plasmodium vivax serine hydroxymethyltransferase

dc.contributor.authorUbolsree Leartsakulpanichen_US
dc.contributor.authorDarin Kongkasuriyachaien_US
dc.contributor.authorMallika Imwongen_US
dc.contributor.authorKesinee Chotivanichen_US
dc.contributor.authorYongyuth Yuthavongen_US
dc.contributor.otherThailand National Center for Genetic Engineering and Biotechnologyen_US
dc.contributor.otherMahidol Universityen_US
dc.date.accessioned2018-07-12T02:30:27Z
dc.date.available2018-07-12T02:30:27Z
dc.date.issued2008-06-01en_US
dc.description.abstractSerine hydroxymethyltransferase (SHMT), which catalyzes the reversible reaction of serine and tetrahydrofolate to glycine and methylenetetrahydrofolate, is one of the three enzymes in dTMP synthesis pathway that is highly active during cell division and has been proposed as a potential chemotherapeutic target in infectious diseases and cancer. This is the first study to describe nucleotide and amino acid sequences of SHMT from the malaria parasite Plasmodium vivax. Sequencing of 12 P. vivax isolates revealed limited polymorphisms in 3 noncoding regions. Its biological function is also reported. © 2007 Elsevier Ireland Ltd. All rights reserved.en_US
dc.identifier.citationParasitology International. Vol.57, No.2 (2008), 223-228en_US
dc.identifier.doi10.1016/j.parint.2007.11.001en_US
dc.identifier.issn13835769en_US
dc.identifier.other2-s2.0-40849089375en_US
dc.identifier.urihttps://repository.li.mahidol.ac.th/handle/20.500.14594/19323
dc.rightsMahidol Universityen_US
dc.rights.holderSCOPUSen_US
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=40849089375&origin=inwarden_US
dc.subjectImmunology and Microbiologyen_US
dc.subjectMedicineen_US
dc.titleCloning and characterization of Plasmodium vivax serine hydroxymethyltransferaseen_US
dc.typeArticleen_US
dspace.entity.typePublication
mu.datasource.scopushttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=40849089375&origin=inwarden_US

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