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The authors have withdrawn this article.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

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
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article

Withdrawal: Human calpain-3 and its structural plasticity: Dissociation of a homohexamer into dimers on binding titin

Peter L. Davies, Qilu Ye, Borries Demeler, Amy Henrickson et al.
Journal of Biological Chemistry
Calpain Protease Function and Regulation
article

Withdrawal: Human calpain-3 and its structural plasticity: Dissociation of a homohexamer into dimers on binding titin

Peter L. Davies, Qilu Ye, Borries Demeler, Amy Henrickson, Vitor Hugo Balasco Serrão
article en

Abstract

The authors have withdrawn this article.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.

Journal of Biological ChemistryVol. 302(8)
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Calpain Protease Function and Regulation
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