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Cloning and characterization of Plasmodium vivax serine hydroxymethyltransferase.
Parasitol Int. 2008 Jun; 57(2):223-8.PI

Abstract

Serine 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.

Authors+Show Affiliations

National Center for Genetic Engineering and Biotechnology, 113 Paholyothin Road, Klong 1, Klong Luang, Pathumthani 12120, Thailand. ubolsree@biotec.or.thNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

18096429

Citation

Leartsakulpanich, Ubolsree, et al. "Cloning and Characterization of Plasmodium Vivax Serine Hydroxymethyltransferase." Parasitology International, vol. 57, no. 2, 2008, pp. 223-8.
Leartsakulpanich U, Kongkasuriyachai D, Imwong M, et al. Cloning and characterization of Plasmodium vivax serine hydroxymethyltransferase. Parasitol Int. 2008;57(2):223-8.
Leartsakulpanich, U., Kongkasuriyachai, D., Imwong, M., Chotivanich, K., & Yuthavong, Y. (2008). Cloning and characterization of Plasmodium vivax serine hydroxymethyltransferase. Parasitology International, 57(2), 223-8.
Leartsakulpanich U, et al. Cloning and Characterization of Plasmodium Vivax Serine Hydroxymethyltransferase. Parasitol Int. 2008;57(2):223-8. PubMed PMID: 18096429.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Cloning and characterization of Plasmodium vivax serine hydroxymethyltransferase. AU - Leartsakulpanich,Ubolsree, AU - Kongkasuriyachai,Darin, AU - Imwong,Mallika, AU - Chotivanich,Kesinee, AU - Yuthavong,Yongyuth, Y1 - 2007/11/12/ PY - 2007/08/31/received PY - 2007/11/02/revised PY - 2007/11/05/accepted PY - 2007/12/22/pubmed PY - 2008/6/19/medline PY - 2007/12/22/entrez SP - 223 EP - 8 JF - Parasitology international JO - Parasitol. Int. VL - 57 IS - 2 N2 - Serine 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. SN - 1383-5769 UR - https://www.unboundmedicine.com/medline/citation/18096429/Cloning_and_characterization_of_Plasmodium_vivax_serine_hydroxymethyltransferase_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S1383-5769(07)00135-3 DB - PRIME DP - Unbound Medicine ER -