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Protein-Driven Copper Redox Regulation: Uncovering the Role of Disulphide Bonds and Allosteric Modulation

2025-08-24

Abstract excerpt

<h4>ABSTRACT</h4> Copper plays essential roles in enzymatic activity, redox reactions, and cellular signalling, but becomes toxic when redox homeostasis is disrupted. While Cu(II) reduction is commonly attributed to unfolded or amyloid proteins, here we show that the well-folded plasma protein human serum albumin (HSA) intrinsically reduces Cu(II) to Cu(I) in the absence of external reductants. Using X-ray absorp...

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Literature Corpus work
2558ecfc-7573-53fe-970c-dc31b0d6db10
DOI
10.1101/2025.08.20.671251
Open publication

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Protein-Driven Copper Redox Regulation: Uncovering the Role of Disulphide Bonds and Allosteric ModulationDOI 10.1101/2025.08.20.671251
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