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- W2035673321 abstract "The terminal end of the short arm of human chromosome 1, 1p36.3, is frequently deleted in a number of tumors and is believed to be the location of multiple tumor suppressor genes. Thus far, abona fidetumor suppressor gene from this region has not been identified. The isolation and characterization of new 1p36 genes is, therefore, of some interest. Two novel matrix metalloproteinase genes,MMP21andMMP22, have been identified in theCdc2L1–2locus, which spans approximately 120 kb on 1p36.3. These genes encode novel metalloproteinases that contain prepro, catalytic, cysteine-rich, interleukin-1 receptor-related, and proline-rich domains. Their catalytic domains are most closely related to stromelysin-3 and contain the consensus HEXXH zinc-binding region required for enzyme activation, while their cysteine-rich domains appear to be related to a number of human, mouse, andCaenorhabditis elegansmetalloproteinase sequences.Of some possible interest is the absence of a highly conserved cysteine residue in the proenzyme domain, the so-called “cysteine switch,” which has been shown to be involved in the autocatalytic activation of many metalloproteinases. TheMMPgenes are located less than 1 kb from the 3′ regions ofCdc2L1andCdc2L2,suggesting that theMMPandCdc2Lgenes are part of a larger region that has been duplicated. Finally, theMMP21/22genes express multiple mRNAs, some of which are derived by alternative splicing, in a tissue-specific manner." @default.
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- W2035673321 date "1998-08-01" @default.
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- W2035673321 title "Isolation and Characterization of Two Novel Metalloproteinase Genes Linked to theCdc2LLocus on Human Chromosome 1p36.3" @default.
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- W2035673321 doi "https://doi.org/10.1006/geno.1998.5401" @default.
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