ReviewCellular and molecular life sciences : CMLS2026
Oxidative protein folding and Ca
Review in Cellular and molecular life sciences : CMLS, 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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3 authors.
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Abstract
Secretory and membrane proteins undergo oxidative folding, the process of forming disulfide bonds between cysteine side chains to construct a stable higher-order structure, primarily in the endoplasmic reticulum (ER) followed by further post-translational modification in the Golgi apparatus, after which proteins proceed to pathways for secretion and membrane localization. Proteins involved in transferring oxidizing power to target proteins possess a pair of highly reactive forms of cysteine residue that mediate reduction-oxidation (redox) reactions. Oxidizing power, which is generally provided in the form of reactive oxygen/reactive nitrogen oxide species. Endoplasmic reticulum oxidoreductin 1 (ERO1) is the ancient ER oxidase that utilizes molecular oxygen to produce hydrogen peroxide, which is then utilized for thiol oxidation to form a disulfide bridge in target proteins. Excessive elevation of these species could promote aberrant oxidation of susceptible molecules, which could lead to an accumulation of misfolded proteins and consequent ER stress. The ER is also involved in cellular Ca
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