{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,22]],"date-time":"2026-10-22T13:05:27Z","timestamp":1792674327649,"version":"4.5.0"},"reference-count":0,"publisher":"Canadian Science Publishing","issue":"2-3","license":[{"start":{"date-parts":[[1998,5,1]],"date-time":"1998-05-01T00:00:00Z","timestamp":893980800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.nrcresearchpress.com\/page\/about\/CorporateTextAndDataMining"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biochem. Cell Biol."],"published-print":{"date-parts":[[1998,5,1]]},"abstract":"<jats:p> The cysteine-rich zinc-binding motifs known as the RING and B-box are found in several unrelated proteins. Structural, biochemical, and biological studies of these motifs reveal that they mediate protein-protein interactions. Several RING-containing proteins are oncoproteins and recent data indicate that proapoptotic activities can be mediated through the RING. <jats:sup>1<\/jats:sup>H NMR methods were used to determine the structures of RINGs and a B-box domain and to monitor the conformational changes these motifs undergo upon zinc ligation. This review discusses in detail the structural features of the RING and B-box domains. Further, possible structure function relationships for these motifs particularly in their role as protein interaction domains are discussed.Key words: RING, B-box, PML, NMR. <\/jats:p>","DOI":"10.1139\/o98-021","type":"journal-article","created":{"date-parts":[[2011,4,23]],"date-time":"2011-04-23T02:18:16Z","timestamp":1303525096000},"page":"351-358","source":"Crossref","is-referenced-by-count":228,"title":["RING fingers and B-boxes: zinc-binding protein-protein interaction domains"],"prefix":"10.1139","volume":"76","author":[{"given":"Katherine LB","family":"Borden","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"155","container-title":["Biochemistry and Cell Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/cdnsciencepub.com\/doi\/pdf\/10.1139\/o98-021","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,7,2]],"date-time":"2025-07-02T18:35:52Z","timestamp":1751481352000},"score":1,"resource":{"primary":{"URL":"https:\/\/cdnsciencepub.com\/doi\/10.1139\/o98-021"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1998,5,1]]},"references-count":0,"aliases":["10.1139\/bcb-76-2-3-351"],"journal-issue":{"issue":"2-3","published-print":{"date-parts":[[1998,5,1]]}},"alternative-id":["10.1139\/o98-021"],"URL":"https:\/\/doi.org\/10.1139\/o98-021","relation":{},"ISSN":["0829-8211","1208-6002"],"issn-type":[{"value":"0829-8211","type":"print"},{"value":"1208-6002","type":"electronic"}],"subject":[],"published":{"date-parts":[[1998,5,1]]}}}