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Journal Article
Journal Article
Structure, ISSN 0969-2126, 09/2016, Volume 24, Issue 9, pp. 1476 - 1487
Excess cellular heme is toxic, and malaria parasites regulate its levels during hemoglobin digestion. Aminoacyl-tRNA synthetases are ubiquitous enzymes, and of... 
DRUG | BIOCHEMISTRY & MOLECULAR BIOLOGY | HALOFUGINONE | CHLOROQUINE | HEMOGLOBIN DEGRADATION | PROTEIN-SYNTHESIS | ANTIMALARIAL | CELL BIOLOGY | INHIBITION | BIOPHYSICS | METABOLISM | MALARIA | END RULE PATHWAY | Plasmodium falciparum - enzymology | Species Specificity | Humans | Protein Multimerization | Substrate Specificity | Crystallography, X-Ray | Plasmodium falciparum - drug effects | Protozoan Proteins - genetics | Chloroquine - pharmacology | Heme - pharmacology | Arginine-tRNA Ligase - genetics | Protozoan Proteins - metabolism | Heme - chemistry | Plasmodium falciparum - genetics | RNA, Transfer, Arg - metabolism | Arginine-tRNA Ligase - chemistry | Protozoan Proteins - chemistry | Protein Interaction Domains and Motifs | Hemin - pharmacology | Binding Sites | Recombinant Proteins - metabolism | Amino Acid Sequence | Gene Expression | Protein Structure, Secondary | Arginine-tRNA Ligase - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Antimalarials - pharmacology | Arginine - chemistry | Sequence Homology, Amino Acid | Sequence Alignment | RNA, Transfer, Arg - chemistry | Antimalarials - chemistry | Chloroquine - chemistry | Hemin - chemistry | Protein Binding | Protein Biosynthesis - drug effects | Plasmodium falciparum - growth & development | Arginine - metabolism | Malaria | Crystals | Genetically modified organisms | Heme | Hemoglobin | Antimalarials | Protein biosynthesis | Genetic engineering | Structure | Aminoacyl-tRNA synthetases | Transfer RNA
Journal Article
Journal Article