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Terminally misfolded proteins, recognized by chaperones on the endoplasmic reticulum (ER), are transported to depots for ubiquitination and proteasomal degradation by the ER-associated protein degradation (ERAD) pathway. Eeyarestatin 1 is an inhibitor of the ERAD pathway, blocking the degradation of misfolded proteins at a dose of 8 µM.[1] It associates with the p97-associated deubiquitinating complex in cells, preventing deubiquitination of substrates by ataxin-3.[2],[3] Eeyarestatin 1, at 4 µM, interferes with both retrograde and anterograde trafficking of proteins, including certain toxins, and potentially, viruses.[4]

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