A5083431783- Heme Oxygenase-1 and Carbon Monoxide
- Autophagy in Disease and Therapy
- Mosquito-borne diseases and control
- Malaria Research and Control
- Hemoglobin structure and function
- ATP Synthase and ATPases Research
- CRISPR and Genetic Engineering
- thermodynamics and calorimetric analyses
- RNA and protein synthesis mechanisms
- Photosynthetic Processes and Mechanisms
- Metabolomics and Mass Spectrometry Studies
University of Utah
2023-2024
malaria parasites retain an essential mitochondrional electron transport chain (ETC) that is critical for growth within humans and mosquitoes a key antimalarial drug target. ETC function requires cytochromes
The mitochondrial electron transport chain (ETC) of Plasmodium malaria parasites is a major antimalarial drug target, but critical cytochrome (cyt) functions remain unstudied and enigmatic. Parasites express two distinct cyt c homologs (c c-2) with unusually sparse sequence identity uncertain fitness contributions. P. falciparum c-2 the most divergent eukaryotic homolog currently known has features predicted to be incompatible canonical ETC function. We tagged both related c1 for inducible...
malaria parasites retain an essential mitochondrional electron transport chain (ETC) that is critical for growth within humans and mosquitoes a key antimalarial drug target. ETC function requires cytochromes
Malaria parasites have evolved unusual metabolic adaptations that specialize them for growth within heme-rich human erythrocytes. During blood-stage infection,
Malaria parasites have evolved unusual metabolic adaptations that specialize them for growth within heme-rich human erythrocytes. During blood-stage infection, Plasmodium falciparum internalize and digest abundant host hemoglobin the digestive vacuole. This massive catabolic process generates copious free heme, most of which is biomineralized into inert hemozoin. Parasites also express a divergent heme oxygenase (HO)-like protein (PfHO) lacks key active-site residues has lost canonical HO...
Malaria parasites have evolved unusual metabolic adaptations that specialize them for growth within heme-rich human erythrocytes. During blood-stage infection, Plasmodium falciparum internalize and digest abundant host hemoglobin the digestive vacuole. This massive catabolic process generates copious free heme, most of which is biomineralized into inert hemozoin. Parasites also express a divergent heme oxygenase (HO)-like protein (PfHO) lacks key active-site residues has lost canonical HO...
Malaria parasites have evolved unusual metabolic adaptations that specialize them for growth within heme-rich human erythrocytes. During blood-stage infection, Plasmodium falciparum internalize and digest abundant host hemoglobin the digestive vacuole. This massive catabolic process generates copious free heme, most of which is biomineralized into inert hemozoin. Parasites also express a divergent heme oxygenase (HO)-like protein (PfHO) lacks key active-site residues has lost canonical HO...
Malaria parasites have evolved unusual metabolic adaptations that specialize them for growth within heme-rich human erythrocytes. During blood-stage infection, Plasmodium falciparum internalize and digest abundant host hemoglobin the digestive vacuole. This massive catabolic process generates copious free heme, most of which is biomineralized into inert hemozoin. Parasites also express a divergent heme oxygenase (HO)-like protein (PfHO) lacks key active-site residues has lost canonical HO...
The mitochondrial electron transport chain (ETC) of