{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,13]],"date-time":"2026-05-13T00:07:01Z","timestamp":1778630821513,"version":"3.51.4"},"reference-count":0,"publisher":"American Society for Cell Biology (ASCB)","issue":"12","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["MBoC"],"published-print":{"date-parts":[[1996,12]]},"abstract":"<jats:p> A search was carried out for homologues of possible fusogenic proteins to study their function in a genetically tractable animal. The isolation, molecular, and cellular characterization of the Caenorhabditis elegans adm-1 gene (a disintegrin and metalloprotease domain) are described. A glycoprotein analogous to viral fusion proteins has been identified on the surface of guinea pig sperm (PH-30\/fertilin) and is implicated in sperm-egg fusion. adm-1 is the first reported invertebrate gene related to PH-30 and a family of proteins containing snake venom disintegrin- and metalloprotease-like domains. ADM-1 shows a domain organization identical to PH-30. It contains prepro, metalloprotease, disintegrin, cysteine rich with putative fusion peptide, epidermal growth factor-like repeat, transmembrane, and cytoplasmic domains. Antibodies which recognize ADM-1 protein in immunoblots were generated. Using immunofluorescence and in situ hybridization, the products of adm-1 have been detected in specific cells during different stages of development. The localization of ADM-1 to the plasma membrane of embryonic cells and to the sheath cells of sensory organs suggests a function in cell adhesion. ADM-1 expression in the hypodermis, pharynx, vulva, and mature sperm is consistent with a putative role in somatic and gamete cell fusions. <\/jats:p>","DOI":"10.1091\/mbc.7.12.1877","type":"journal-article","created":{"date-parts":[[2013,8,16]],"date-time":"2013-08-16T23:13:18Z","timestamp":1376694798000},"page":"1877-1893","source":"Crossref","is-referenced-by-count":35,"title":["ADM-1, a protein with metalloprotease- and disintegrin-like domains, is expressed in syncytial organs, sperm, and sheath cells of sensory organs in Caenorhabditis elegans."],"prefix":"10.1091","volume":"7","author":[{"given":"B","family":"Podbilewicz","sequence":"first","affiliation":[{"name":"Department of Biology, Technion-Israel Institute of Technology, Haifa, Israel."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1076","container-title":["Molecular Biology of the Cell"],"original-title":[],"language":"en","deposited":{"date-parts":[[2019,7,14]],"date-time":"2019-07-14T16:25:11Z","timestamp":1563121511000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.molbiolcell.org\/doi\/10.1091\/mbc.7.12.1877"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1996,12]]},"references-count":0,"journal-issue":{"issue":"12","published-print":{"date-parts":[[1996,12]]}},"alternative-id":["10.1091\/mbc.7.12.1877"],"URL":"https:\/\/doi.org\/10.1091\/mbc.7.12.1877","relation":{},"ISSN":["1059-1524","1939-4586"],"issn-type":[{"value":"1059-1524","type":"print"},{"value":"1939-4586","type":"electronic"}],"subject":[],"published":{"date-parts":[[1996,12]]}}}