{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T23:22:59Z","timestamp":1791328979101,"version":"4.3.1"},"reference-count":157,"publisher":"The Company of Biologists","issue":"21","license":[{"start":{"date-parts":[[1999,11,1]],"date-time":"1999-11-01T00:00:00Z","timestamp":941414400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/www.biologists.com\/user-licence-1-1\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[1999,11,1]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n               <jats:p>Metalloprotease-disintegrins (ADAMs) have captured our attention as key players in fertilization and in the processing of the ectodomains of proteins such as tumor necrosis factor \u03b1 (TNF\u03b1), and because of their roles in Notch-mediated signaling, neurogenesis and muscle fusion. ADAMs are integral membrane glycoproteins that contain a disintegrin domain, which is related to snake-venom integrin ligands, and a metalloprotease domain (which can contain or lack a catalytic site). Here, we review and critically discuss current topics in the ADAMs field, including the central role of fertilin in fertilization, the role of the TNF\u03b1 convertase in protein ectodomain processing, the role of Kuzbanian in Notch signaling, and links between ADAMs and processing of the amyloid-precursor protein.<\/jats:p>","DOI":"10.1242\/jcs.112.21.3603","type":"journal-article","created":{"date-parts":[[2021,4,25]],"date-time":"2021-04-25T17:23:40Z","timestamp":1619371420000},"page":"3603-3617","source":"Crossref","is-referenced-by-count":438,"title":["Metalloprotease-disintegrins: modular proteins capable of promoting cell-cell interactions and triggering signals by protein-ectodomain shedding"],"prefix":"10.1242","volume":"112","author":[{"given":"Johannes","family":"Schl\u00f6ndorff","sequence":"first","affiliation":[{"name":"Cellular Biochemistry and Biophysics Program, Memorial Sloan Kettering Cancer Center, Box 368, 1275 York Avenue, Tri-Institutional (Cornell\/ Rockefeller University\/Sloan-Kettering Institute) MD\/PhD Program, New York, NY 10021, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carl P.","family":"Blobel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"237","published-online":{"date-parts":[[1999,11,1]]},"reference":[{"key":"2024062700314654200_JOCES_112_21_3603C1","doi-asserted-by":"publisher","first-page":"681","DOI":"10.1083\/jcb.138.3.681","article-title":"Cellular redistribution of protein tyrosine phosphatases LAR and PTPsigma by inducible proteolytic processing","volume":"138","author":"Aicher","year":"1997","journal-title":"J. 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