Dimerization of arginyl-tRNA synthetase by free heme drives its inactivation in plasmodium falciparum
Excess cellular heme is toxic, and malaria parasites regulate its levels during hemoglobin digestion. Aminoacyl-tRNA synthetases are ubiquitous enzymes, and of these, arginyl-tRNA synthetase (RRS) is unique as its enzymatic product of charged tRNA is required for protein synthesis and degradation. W...
Príomhchruthaitheoirí: | Jain, V, Yogavel, M, Sharma, A |
---|---|
Formáid: | Journal article |
Foilsithe / Cruthaithe: |
Cell Press
2016
|
Míreanna comhchosúla
Míreanna comhchosúla
-
Reaction hijacking inhibition of Plasmodium falciparum asparagine tRNA synthetase
de réir: Stanley C. Xie, et al.
Foilsithe / Cruthaithe: (2024-01-01) -
Drug targeting of one or more aminoacyl-tRNA synthetase in the malaria parasite Plasmodium falciparum
de réir: Manickam, Y, et al.
Foilsithe / Cruthaithe: (2018) -
A genomic glimpse of aminoacyl-tRNA synthetases in malaria parasite <it>Plasmodium falciparum</it>
de réir: Santoni Daniele, et al.
Foilsithe / Cruthaithe: (2009-12-01) -
The structural basis of tRNA recognition by arginyl-tRNA-protein transferase
de réir: Thilini Abeywansha, et al.
Foilsithe / Cruthaithe: (2023-04-01) -
Structure of prolyl-tRNA synthetase-halofuginone complex provides basis for development of drugs against malaria and toxoplasmosis
de réir: Jain, V, et al.
Foilsithe / Cruthaithe: (2015)