Sulfa-drug resistance in Plasmodium falciparum.

No abstract is available for this paper.

• Publication year

  2001

• Venue

  Trends in Parasitology

• Publication date

  2001-06-01

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1016/S1471-4922(01)01949-3PMID 11426433
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Crystal structure of Mycobacterium tuberculosis 7,8-dihydropteroate synthase in complex with pterin monophosphate: new insight into the enzymatic mechanism and sulfa-drug action.

  2000cited by this paper
• Allelic exchange at the endogenous genomic locus in Plasmodium falciparum proves the role of dihydropteroate synthase in sulfadoxine‐resistant malaria

  1998cited by this paper
• P. falciparum dihydrofolate reductase and dihydropteroate synthase mutations: epidemiology and role in clinical resistance to antifolates.

  1998cited by this paper
• Sulfadoxine resistance in the human malaria parasite Plasmodium falciparum is determined by mutations in dihydropteroate synthetase and an additional factor associated with folate utilization

  1997cited by this paper
• Mutations in dihydropteroate synthase are responsible for sulfone and sulfonamide resistance in Plasmodium falciparum.

  1997cited by this paper
• Resistance to antifolates in Plasmodium falciparum monitored by sequence analysis of dihydropteroate synthetase and dihydrofolate reductase alleles in a large number of field samples of diverse origins.

  1997cited by this paper
• Crystal structure of the anti-bacterial sulfonamide drug target dihydropteroate synthase

  1997cited by this paper
• Structure and function of the dihydropteroate synthase from Staphylococcus aureus.

  1997cited by this paper
• Primary structure and expression of the dihydropteroate synthetase gene of Plasmodium falciparum.

  1994cited by this paper
• Sequence variation of the hydroxymethyldihydropterin pyrophosphokinase: dihydropteroate synthase gene in lines of the human malaria parasite, Plasmodium falciparum, with differing resistance to sulfadoxine.

  1994cited by this paper

• Molecular and biological aspects of antimalarial resistance in Plasmodium falciparum and Plasmodium vivax.

  2009cites this paper
• Malaria combination therapies: advantages and shortcomings.

  2008cites this paper
• Targeting purine and pyrimidine metabolism in human apicomplexan parasites.

  2007cites this paper
• Malaria Chemotherapeutics Part I: History of Antimalarial Drug Development, Currently Used Therapeutics, and Drugs in Clinical Development

  2007cites this paper
• Antifolates can have a role in the treatment of Plasmodium vivax.

  2007cites this paper
• Microbial Responses to Antibiotics – Stability of Resistance and Extended Potential of Targeting the Folate Synthesis

  2005cites this paper
• Mechanisms of Resistance of Malaria Parasites to Antifolates

  2005cites this paper
• The Uniqueness of Tetrahydrofolate Synthesis and One-Carbon Metabolism in Plants

  2004cites this paper
• Mechanisms of resistance of Plasmodium falciparum to antimalarial drugs.

  2002cites this paper