DISENTANGLING SUB-GEV DARK MATTER FROM THE DIFFUSE SUPERNOVA NEUTRINO BACKGROUND USING HYPER-KAMIOKANDE


Substrate-induced unfolding of protein disulfide isomerase displaces the cholera toxin A1 subunit from its holotoxin.

To generate a cytopathic effect, the catalytic A1 subunit of cholera toxin (CT) must be separated from the rest of the toxin.Protein disulfide isomerase (PDI) is thought to mediate CT disassembly by Accessories acting as a redox-driven chaperone that actively unfolds the CTA1 subunit.Here, we show that PDI itself unfolds upon contact with CTA1.The

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