ArticlemBio2026
A protein disulfide isomerase coordinates redox homeostasis and ER calcium regulation for optimal lytic cycle progression in
Article in mBio, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Abstract
The endoplasmic reticulum (ER) maintains an oxidative environment that facilitates the formation of disulfide bonds, a critical process for proper protein folding. Protein disulfide isomerases (PDIs) are ER-resident enzymes that facilitate the formation, breakage, and rearrangement of disulfide bonds between cysteine residues, thereby stabilizing protein structures. Although PDIs are functionally diverse, they all contain at least 1 thioredoxin-like domain and most mediate disulfide exchange through their conserved CXXC motifs. The apicomplexan parasite,
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