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| http://dx.doi.org/10.1038/s41421-023-00637-w | DOI Listing |
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Reduced nicotinamide adenine dinucleotide phosphate (NADPH) is a crucial reducing cofactor for reductive biosynthesis and protection from oxidative stress. To fulfill their heightened anabolic and reductive power demands, cancer cells must boost their NADPH production. Progrowth and mitogenic protein kinases promote the activity of cytosolic NAD kinase (NADK), which produces NADP, a limiting NADPH precursor.
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Apicomplexans, a large phylum of protozoan intracellular parasites, well known for their ability to invade and proliferate within host cells, cause diseases with major health and economic impacts worldwide. These parasites are responsible for conditions such as malaria, cryptosporidiosis, and toxoplasmosis, which affect humans and other animals. Apicomplexans exhibit complex life cycles, marked by diverse modes of cell division, which are closely associated with their pathogenesis.
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The respiratory syncytial virus (RSV) is a major cause of lower respiratory tract infections in children and adults. With nearly everyone infected by the age of five, there is an opportunity to develop booster vaccines that enhance B-cell immunity, promoting potent and broadly neutralizing antibodies. One potential approach involves using anti-idiotypic antibodies (anti-IDs) to mimic specific antigenic sites and enhance preexisting immunity in an epitope-specific manner.
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The C3 protein is the central molecule within the complement system and undergoes proteolytic activation to C3b in the presence of pathogens. Pattern-independent activation of C3 also occurs via hydrolysis, resulting in C3(HO), but the structural details of C3 hydrolysis remain elusive. Here we show that the conformation of the C3(HO) analog, C3MA, is indistinguishable from C3b.
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