{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,19]],"date-time":"2026-08-19T08:27:29Z","timestamp":1787128049210,"version":"build-2736575974"},"reference-count":5,"publisher":"Portland Press Ltd.","issue":"9","funder":[{"DOI":"10.13039\/100024032","name":"HHS | NIH | NIGMS | Native American Research Centers for Health","doi-asserted-by":"publisher","award":["GM157928"],"award-info":[{"award-number":["GM157928"]}],"id":[{"id":"10.13039\/100024032","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2026,9,2]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>E3 ligases catalyze the final step in transferring ubiquitin to protein substrates, but resulting intermediates are characterized by conformational flexibility. Recent work by Chandler and colleagues ( Biochem J. (2026) 483, 1115\u20131130) demonstrates that photocross-linking activity-based probes can trap transient conformations of the intermediates, providing a valuable tool to map interfaces during the ubiquitin transfer process.<\/jats:p>","DOI":"10.1042\/bcj20260338","type":"journal-article","created":{"date-parts":[[2026,8,19]],"date-time":"2026-08-19T08:07:48Z","timestamp":1787126868000},"page":"1709-1711","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Photoreactive crosslinkers capture the ubiquitin\u2013E2\u2013E3 ligases intermediates"],"prefix":"10.1042","volume":"483","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-4101-9691","authenticated-orcid":false,"given":"Tingting","family":"Yao","sequence":"first","affiliation":[{"name":"1Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7375-6990","authenticated-orcid":false,"given":"Tatiana\u00a0G.","family":"Kutateladze","sequence":"additional","affiliation":[{"name":"2Department of Pharmacology, University of Colorado School of Medicine, Aurora, CO 80045, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2026,8,19]]},"reference":[{"key":"2026081904074255300_B1","doi-asserted-by":"publisher","first-page":"626","DOI":"10.1038\/nrm.2016.91","article-title":"Structural insights into the catalysis and regulation of E3 ubiquitin ligases","volume":"17","author":"Buetow","year":"2016","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"2026081904074255300_B2","doi-asserted-by":"publisher","first-page":"1624","DOI":"10.1021\/bi101913m","article-title":"Ubiquitin in motion: structural studies of the ubiquitin-conjugating enzyme approximately ubiquitin conjugate","volume":"50","author":"Pruneda","year":"2011","journal-title":"Biochemistry"},{"key":"2026081904074255300_B3","doi-asserted-by":"publisher","first-page":"115","DOI":"10.1038\/nature11376","article-title":"Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis","volume":"489","author":"Plechanovova","year":"2012","journal-title":"Nature"},{"key":"2026081904074255300_B4","doi-asserted-by":"publisher","first-page":"933","DOI":"10.1016\/j.molcel.2012.07.001","article-title":"Structure of an E3:E2\u223cUb complex reveals an allosteric mechanism shared among RING\/U-box ligases","volume":"47","author":"Pruneda","year":"2012","journal-title":"Mol. Cell."},{"key":"2026081904074255300_B5","doi-asserted-by":"publisher","first-page":"1115","DOI":"10.1042\/BCJ20260213","article-title":"Photocross-linking activity-based probes to capture the dynamics of ubiquitin RING E3 ligase interactions","volume":"483","author":"Chandler","year":"2026","journal-title":"Biochem. J."}],"container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/483\/9\/1709\/991031\/bcj-2026-0338c.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/483\/9\/1709\/991031\/bcj-2026-0338c.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,8,19]],"date-time":"2026-08-19T08:07:49Z","timestamp":1787126869000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/483\/9\/1709\/237934\/Photoreactive-crosslinkers-capture-the-ubiquitin"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,8,19]]},"references-count":5,"journal-issue":{"issue":"9","published-print":{"date-parts":[[2026,9,2]]}},"URL":"https:\/\/doi.org\/10.1042\/bcj20260338","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published-other":{"date-parts":[[2026,9]]},"published":{"date-parts":[[2026,8,19]]}}}