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Background: (Iron-Sulfur Cluster Assembly 1) is involved in the assembly of iron-sulfur (Fe-S) clusters, which are vital for electron transport and enzyme activity. Some studies suggest the potential involvement of in tumor progression through interactions with ferroptosis-related genes (FRGs) and the tumor immune microenvironment (TME). However, there has been no systematic analysis of its role in FRGs and the TME or its predictive value for prognosis and immunotherapy response across different cancer types.

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Glutathione S-transferases (GSTs) are evolutionarily conserved enzymes crucial for cell detoxication. They are viewed as having evolved in cyanobacteria, the ancient photosynthetic prokaryotes that colonize our planet and play a crucial role for its biosphere. Xi-class GSTs, characterized by their specific glutathionyl-hydroquinone reductase activity, have been observed in prokaryotes, fungi and plants, but have not yet been studied in cyanobacteria.

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The outer mitochondrial membrane protein known as mitoNEET was discovered when it was labeled by a photoaffinity derivative of the anti-diabetes medication, pioglitazone. The biological role for mitoNEET and its specific mechanism for achieving this remains an active subject for research. There is accumulating evidence suggesting that mitoNEET could be a component of mitochondrial FeS cofactor biogenesis.

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Ferredoxin 2 Is Critical for Tumor Suppression and Lipid Homeostasis but Dispensable for Embryonic Development.

Am J Pathol

December 2024

Comparative Oncology Laboratory, Schools of Veterinary Medicine and Medicine, University of California at Davis, Davis, California. Electronic address:

Ferredoxin 1 and 2 (FDX1/2) constitute an evolutionarily conserved FDX family of iron-sulfur cluster-containing proteins. FDX1/2 are cognate substrates of ferredoxin reductase and serve as conduits for electron transfer from NADPH to a set of proteins involved in biogenesis of corticosteroids, hemes, iron-sulfur cluster, and lipoylated proteins. Recently, we showed that Fdx1 is essential for embryonic development and lipid homeostasis.

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In-situ synthesis of FeS nanoparticles enhances Sulfamethoxazole degradation via accelerated electron transfer in anaerobic bacterial communities.

Water Res

December 2024

College of Water Sciences, Beijing Normal University, Beijing 100875, China; Beijing ENFI Environmental Protection Co., Ltd., Beijing, 100038, China.

The impact of nanominerals on microbial electron transfer and energy metabolism strategies during pollutant degradation remains uncertain. This study used in situ synthesized FeS nanoparticles (FeS NPs) to increase the degradation efficiency of SMX by anaerobic bacterial communities from 25.80 % to 47.

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