Cardiovascular Research 2004 63(4):756; doi:10.1016/j.cardiores.2004.06.015
© 2004 by European Society of Cardiology
Copyright © 2004, European Society of Cardiology
Corrigendum to: "The ubiquitin–proteasome system in cardiovascular diseases—a hypothesis extended" [Cardiovasc. Res. 61 (2004) 11–21]
aDivision of Cardiovascular Diseases, Mayo Clinic, Rochester, MN, USA
bRappaport Institute for Research in Medical Sciences, Technion-Israel Institute of Technology, Haifa, Israel
cDivision of Hypertension, Mayo Clinic, Rochester, MN, USA
* Corresponding author. Department of Internal Medicine, Mayo Clinic Rochester, 200 First Street SW, Rochester, MN 55905, USA. Tel.: +1-507-255-5890; fax: +1-507-255-1824. Email address: herrmann.joerg{at}mayo.edu
As an addendum to our recent review, entitled "The ubiquitin–proteasome system in cardiovascular diseases—a hypothesis extended" [Cardiovasc. Res. 61 (2004) 11–21], it should be noted that boronate-type proteasome inhibitors are eventually reversible in their effect, although boronate-proteasome adducts have a very slow dissociation rate, constituting a mode of inhibition that is practically irreversible over hours. Furthermore, the majority of reports attribute not only reversibility, but also selectivity to boronate-type proteasome inhibitors, and appropriate revisions were made to Table 2 to remain most accurate in these aspects [1]. In addition, it should be mentioned that the enzymatic β1 sites, which were traditionally considered to harbor "peptidyl glutamyl peptide hydrolase" activity, cleave faster after aspartic acid than after glutamate residues, hence favoring the label "caspase-like activity". Also, to be more informative, a grading of the effect of the various inhibitors on the different enzymatic activities of the 20S proteasome was provided in the revised version of Table 2.
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- Kisselev A.F., Goldberg A.L. Proteasome inhibitors: from research tools to drug candidates. Chem. Biol. (2001) 8:739–758.[CrossRef][Web of Science][Medline]
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