Title |
Insights into the role of the junctional region of Plasmodium falciparum dihydrofolate reductase-thymidylate synthase
|
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Published in |
Malaria Journal, March 2013
|
DOI | 10.1186/1475-2875-12-91 |
Pubmed ID | |
Authors |
Natpasit Chaianantakul, Rachada Sirawaraporn, Worachart Sirawaraporn |
Abstract |
Plasmodium falciparum dihydrofolate reductase-thymidylate synthase (pfDHFR-TS) is a well-defined target of anti-malarial drug, such as pyrimethamine and cycloguanil. Emergence of malaria parasites resistant to these drugs has been shown to be associated with point mutations of the gene coding for the target enzymes. Although the 3D-structure of P. falciparum bifunctional pfDHFR-TS has been reported previously, relatively little is known about the interactions between the pfDHFR and pfTS domains and the roles of the junctional region that links the two domains together. Therefore, a thorough understanding of the interaction of the two domains and the role of the junctional region of this target is important as the knowledge could assist the development of new effective anti-malarial drugs aimed at overcoming drug-resistant malaria. |
X Demographics
Geographical breakdown
Country | Count | As % |
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United Kingdom | 2 | 100% |
Demographic breakdown
Type | Count | As % |
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Members of the public | 1 | 50% |
Unknown | 1 | 50% |
Mendeley readers
Geographical breakdown
Country | Count | As % |
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United Kingdom | 1 | 3% |
Unknown | 38 | 97% |
Demographic breakdown
Readers by professional status | Count | As % |
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Student > Ph. D. Student | 9 | 23% |
Student > Master | 7 | 18% |
Student > Bachelor | 5 | 13% |
Researcher | 3 | 8% |
Lecturer | 2 | 5% |
Other | 7 | 18% |
Unknown | 6 | 15% |
Readers by discipline | Count | As % |
---|---|---|
Chemistry | 8 | 21% |
Agricultural and Biological Sciences | 6 | 15% |
Biochemistry, Genetics and Molecular Biology | 5 | 13% |
Medicine and Dentistry | 4 | 10% |
Pharmacology, Toxicology and Pharmaceutical Science | 2 | 5% |
Other | 6 | 15% |
Unknown | 8 | 21% |