ReviewJournal of biochemistry2026
Zinc-mediated structural and functional regulation of ERp44 and ERGIC-53 in protein quality control.
Review in Journal of biochemistry, 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
Zinc ions (Zn2+) are essential trace metal ions in the human body. Intracellular Zn2+ levels are tightly regulated by two metal transporter families: ZIPs, which mediate Zn2+ influx into the cytosol, and ZnTs, which export Zn2+ from the cytosol to the extracellular space or sequester it into the cellular organelles. Within cells, Zn2+ plays multiple roles, acting as a catalytic cofactor for numerous enzymes, stabilizing protein structures, and functioning as a second messenger in signal transduction. In addition, Zn2+ is involved in the transient regulation of enzymatic activities. Here, we review recent findings that reveal novel roles of Zn2+ in the structural and functional regulations of the molecular chaperone ERp44 and the cargo receptor ERGIC-53, both of which operate for protein quality control in the early secretory pathway.
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