VOLUME 279 (2004) PAGES 26627–26634
This article has been withdrawn by the authors upon request from the Journal. The Journal raised questions regarding Fig. 4. The authors were able to locate original autoradiographs and state that during assembly of this panel, an actin lane was duplicated. The authors assert that all of the results reported in this article are valid, some of which have been independently validated in the literature (Burkart et al. (2012) J. Cell Biol. 197, 37).
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Published online: January 25, 2019
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- Identification and Characterization of Human and Mouse Ovastacin: A NOVEL METALLOPROTEINASE SIMILAR TO HATCHING ENZYMES FROM ARTHROPODS, BIRDS, AMPHIBIANS, AND FISHJournal of Biological ChemistryVol. 279Issue 25
- PreviewWe have cloned and characterized human and mouse ovary cDNAs encoding a new protein of the astacin family of metalloproteinases, called ovastacin because of its predominant expression in ovarian tissues. Human and mouse ovastacins exhibit the same domain organization as other astacins, including signal sequence, propeptide, and metalloproteinase domain. However, ovastacins show an additional C-terminal domain of about 150 amino acids with no similarity to other ancillary domains present in the equivalent region of most astacins.
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