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Heme sensing and trafficking in fungi
Fungal Biology Reviews, 2023Fungal pathogens cause life-threatening diseases in humans, and the increasing prevalence of these diseases emphasizes the need for new targets for therapeutic intervention. Nutrient acquisition during infection is a promising target, and recent studies highlight the contributions of endomembrane trafficking, mitochondria, and vacuoles in the sensing ...
Peng Xue +5 more
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Heme biosynthesis and trafficking
Free Radical Biology and Medicine, 2018Heme is an essential cofactor involved in a plethora of vital functions. Heme is required to be in most subcellular compartments, but the way, in which it is transported from the mitochondria - its site of synthesis - to those compartments is poorly understood.
Jonathan Dietz +5 more
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Heme requirement and intracellular trafficking in Trypanosoma cruzi epimastigotes
Biochemical and Biophysical Research Communications, 2007Epimastigotes multiplies in the insect midgut by taking up nutrients present in the blood meal including heme bound to hemoglobin of red blood cell. During blood meal digestion by vector proteases in the posterior midgut, hemoglobin is clipped off into amino acids, peptides, and free heme.
F A, Lara +10 more
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JBIC Journal of Biological Inorganic Chemistry, 2015
C. elegans is a heme auxotroph that requires environmental heme for sustenance. As such, worms utilize HRG-3, a small heme-trafficking protein, to traffic heme from the intestine to extra-intestinal tissues and embryos. However, how HRG-3 binds and delivers heme remains unknown.
Ortal, Marciano +3 more
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C. elegans is a heme auxotroph that requires environmental heme for sustenance. As such, worms utilize HRG-3, a small heme-trafficking protein, to traffic heme from the intestine to extra-intestinal tissues and embryos. However, how HRG-3 binds and delivers heme remains unknown.
Ortal, Marciano +3 more
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Heme Trafficking and the Importance of Handling Nature’s Most Versatile Cofactor
Chemical ReviewsHeme is one of the most versatile cofactors in nature from its role in oxygen transport and sensing, bioenergetics, and enzyme catalysis and is therefore an ideal regulatory molecule in responding to the redox status of the cell. However, due to both its redox reactivity and hydrophobicity, heme requires tight regulation at the level of its synthesis ...
Angela Wilks, Riki Egoshi
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Biochemistry, 2007
PhuS is a cytoplasmic, 39 kDa heme-binding protein from Pseudomonas aeruginosa. It has previously been shown to transfer heme to its cognate heme oxygenase. It is expressed from the phu operon, which encodes a group of proteins known to actively internalize and transport heme from host organisms. This study combines the spectral resolution of resonance
Darci R, Block +5 more
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PhuS is a cytoplasmic, 39 kDa heme-binding protein from Pseudomonas aeruginosa. It has previously been shown to transfer heme to its cognate heme oxygenase. It is expressed from the phu operon, which encodes a group of proteins known to actively internalize and transport heme from host organisms. This study combines the spectral resolution of resonance
Darci R, Block +5 more
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Heme, an iron-containing organic ring, is a vital cofactor responsible for diverse biologicalfunctions and is the major source of bioavailable iron in the human diet. As a hydrophobic and cytotoxic cofactor, heme must be transported in a highly controlled manner through membranes via specific intra- and inter-cellular pathways.
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Porphyrin and Heme Trafficking in Metazoans
2013Iqbal Hamza, Harry A. Dailey
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Biophysical Perspectives on the Acquisition, Transport, and Trafficking of Heme in Bacteria
2013Kenton R. Rodgers +1 more
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