{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,16]],"date-time":"2026-09-16T08:08:34Z","timestamp":1789546114677,"version":"build-2803163510"},"reference-count":87,"publisher":"Portland Press Ltd.","issue":"9","license":[{"start":{"date-parts":[[2026,9,16]],"date-time":"2026-09-16T00:00:00Z","timestamp":1789516800000},"content-version":"vor","delay-in-days":15,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Cancer Research UK","award":["CC2075"],"award-info":[{"award-number":["CC2075"]}]},{"name":"UKRI | Medical Research Council","award":["CC2075"],"award-info":[{"award-number":["CC2075"]}]},{"name":"Wellcome Trust","award":["CC2075"],"award-info":[{"award-number":["CC2075"]}]}],"content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2026,9,23]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>TRIpartite Motif (TRIM) family proteins are required for healthy development and homeostasis, while their dysregulation is observed in a wide range of diseases. Although diverse cellular roles are emerging for TRIMs, the majority function as ubiquitin E3 ligases by means of their RING (really interesting new gene) domain. Here, we delve into what is known about TRIM ubiquitin E3 ligase mechanisms, their ubiquitin chain specificities, and how they can be regulated through homo- and hetero-multimerisation and post-translational modifications.<\/jats:p>","DOI":"10.1042\/bst20260079","type":"journal-article","created":{"date-parts":[[2026,9,16]],"date-time":"2026-09-16T07:55:52Z","timestamp":1789545352000},"page":"1251-1260","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Ubiquitin E3 ligase activity in TRIpartite Motif (TRIM) family proteins"],"prefix":"10.1042","volume":"54","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-1571-3524","authenticated-orcid":false,"given":"Jane","family":"Dudley-Fraser","sequence":"first","affiliation":[{"name":"Molecular Structure of Cell Signalling Laboratory, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7698-4435","authenticated-orcid":false,"given":"Katrin","family":"Rittinger","sequence":"additional","affiliation":[{"name":"Molecular Structure of Cell Signalling Laboratory, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2026,9,16]]},"reference":[{"key":"2026091603554772300_B1","doi-asserted-by":"publisher","first-page":"1287257","DOI":"10.3389\/fnmol.2023.1287257","article-title":"It's a TRIM-endous view from the top: the varied roles of TRIpartite Motif proteins in brain development and disease","volume":"16","author":"Dudley-Fraser","year":"2023","journal-title":"Front. 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