VOLUME 280 (2005) PAGES 30367–30375
This article has been withdrawn by the authors upon request from the Journal. The Journal raised questions regarding Figs. 4 and 5A. In Fig. 4, the labeling of the lanes corresponding to adult small intestine and ovary were swapped. The actin panels were reused from previous publications of the group using these commercial membranes, and incorrectly oriented. The first two lanes of the Coomassie panel in Fig. 5A appeared to be inappropriately manipulated. The original data were located for some, but not all, gels used to prepare this panel. The authors assert that all of the results reported in this article are valid.
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Published online: January 25, 2019
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- Identification and Characterization of Human Archaemetzincin-1 and -2, Two Novel Members of a Family of Metalloproteases Widely Distributed in ArchaeaJournal of Biological ChemistryVol. 280Issue 34
- PreviewSystematic analysis of degradomes, the complete protease repertoires of organisms, has demonstrated the large and growing complexity of proteolytic systems operating in all cells and tissues. We report here the identification of two new human metalloproteases that have been called archaemetzincin-1 (AMZ1) and archaemetzincin-2 (AMZ2) to emphasize their close relationship to putative proteases predicted by bioinformatic analysis of archaeal genomes. Both human proteins contain a catalytic domain with a core motif (HEXXHXXGX3CX4CXMX17CXXC) that includes an archetypal zinc-binding site, the methionine residue characteristic of metzincins, and four conserved cysteine residues that are not present at the equivalent positions of other human metalloproteases.
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