Outputs (4)

An essential role in molting and morphogenesis of Caenorhabditis elegans for ACN-1, a novel member of the angiotensis-converting enzyme family that lacks a metallopeptidase active site (2003)
Journal Article
Brooks, D., Appleford, P., Murray, L., & Isaac, R. (2003). An essential role in molting and morphogenesis of Caenorhabditis elegans for ACN-1, a novel member of the angiotensis-converting enzyme family that lacks a metallopeptidase active site. Journal of Biological Chemistry, 278(52), 52340-52346. https://doi.org/10.1074/jbc.M308858200

Genome sequence analyses predict many proteins that are structurally related to proteases but lack catalytic residues, thus making functional assignment difficult. We show that one of these proteins (ACN-1), a unique multi-domain angiotensin-converti... Read More about An essential role in molting and morphogenesis of Caenorhabditis elegans for ACN-1, a novel member of the angiotensis-converting enzyme family that lacks a metallopeptidase active site.

An essential role in molting and morphogenesis of Caenorhabditis elegans for ACN-1, a novel member of the angiotensis-converting enzyme family that lacks a metallopeptidase active site (2003)
Journal Article
Brooks, D., Appleford, P., Murray, L., & Isaac, R. (2003). An essential role in molting and morphogenesis of Caenorhabditis elegans for ACN-1, a novel member of the angiotensis-converting enzyme family that lacks a metallopeptidase active site. Journal of Biological Chemistry, 278(52), 52340-52346. https://doi.org/10.1074/jbc.M308858200

Genome sequence analyses predict many proteins that are structurally related to proteases but lack catalytic residues, thus making functional assignment difficult. We show that one of these proteins (ACN-1), a unique multi-domain angiotensin-converti... Read More about An essential role in molting and morphogenesis of Caenorhabditis elegans for ACN-1, a novel member of the angiotensis-converting enzyme family that lacks a metallopeptidase active site.

The Caenorhabditis elegans orthologue of mammalian puromycinsensitive aminepeptidas has roles in embryogenesis and reproduction (2003)
Journal Article
Brooks, D., Hooper, N., & Isaac, R. (2003). The Caenorhabditis elegans orthologue of mammalian puromycinsensitive aminepeptidas has roles in embryogenesis and reproduction. Journal of Biological Chemistry, 278(44), 42795-42801. https://doi.org/10.1074/jbc.M306216200

Mammals possess membrane-associated and cytosolic forms of the puromycin-sensitive aminopeptidase (PSA; EC 3.4.11.14). Increasing evidence suggests the membrane PSA is involved in neuromodulation within the central nervous system and in reproductive... Read More about The Caenorhabditis elegans orthologue of mammalian puromycinsensitive aminepeptidas has roles in embryogenesis and reproduction.

The Caenorhabditis elegans orthologue of mammalian puromycinsensitive aminepeptidas has roles in embryogenesis and reproduction (2003)
Journal Article
Brooks, D., Hooper, N., & Isaac, R. (2003). The Caenorhabditis elegans orthologue of mammalian puromycinsensitive aminepeptidas has roles in embryogenesis and reproduction. Journal of Biological Chemistry, 278(44), 42795-42801. https://doi.org/10.1074/jbc.M306216200

Mammals possess membrane-associated and cytosolic forms of the puromycin-sensitive aminopeptidase (PSA; EC 3.4.11.14). Increasing evidence suggests the membrane PSA is involved in neuromodulation within the central nervous system and in reproductive... Read More about The Caenorhabditis elegans orthologue of mammalian puromycinsensitive aminepeptidas has roles in embryogenesis and reproduction.