Withdrawal: Human calpain-3 and its structural plasticity: Dissociation of a homohexamer into dimers on binding titin
The authors have withdrawn this article. The authors determined that the multimer that was purified and partially characterized by cryo-electron microscopy was not recombinant human calpain-3, but instead an E. coli protein contaminant, the bifunctional polymyxin resistance protein ArnA. This enzyme has internal histidine residues that likely enabled it to accumulate during Ni-Agarose affinity chromatography. To confirm this result, mass spectrometry sequencing was applied to the cryo-EM sample in question, which was found to be almost entirely ArnA.
Authors
- Peter L. Davies (ORCID: https://orcid.org/0000-0002-8026-7818)
- Qilu Ye (ORCID: https://orcid.org/0009-0008-9995-4440)
- Borries Demeler (ORCID: https://orcid.org/0000-0002-2414-9518)
- Amy Henrickson (ORCID: https://orcid.org/0000-0003-3266-5202)
- Vitor Hugo Balasco Serrão
Publication Details
- Journal
- Journal of Biological Chemistry
- Published
- 2026-07-27
- DOI
- https://doi.org/10.1016/j.jbc.2026.113313
- Primary Topic
- Calpain Protease Function and Regulation
- Type
- article
- Field-Weighted Citation Impact
- 0.00