ArticlemicroPublication biology2026
Workflow for Accurate Measurement of PDI Reductase Kinetics Using a Fluorescent Disulfide Substrate.
Article in microPublication biology, 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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Authors and funding
2 authors.
Funding
Abstract
Protein disulfide isomerase (PDI) is essential for oxidative protein folding, proteostasis, and redox regulation and has become a promising target for thromboinflammation, cancer, and neurodegenerative disorders. Fluorogenic disulfide substrates like Bodipy FL L-cystine (BDSS) are essential for mechanistic studies but have low affinity for PDI, necessitating high micromolar concentrations to measure Michaelis-Menten kinetics. These conditions can lead to optical artifacts, requiring development of correction methods to enable rigorous characterization of PDI inhibitors and allosteric modulators. Here, we present a simple workflow for correcting fluorescence quenching during BDSS reduction assays and provide an example of its utility with two allosteric modulators.
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Registered trials
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