{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,31]],"date-time":"2026-07-31T10:56:04Z","timestamp":1785495364055,"version":"3.56.0"},"reference-count":27,"publisher":"Elsevier BV","issue":"3","license":[{"start":{"date-parts":[[2024,3,1]],"date-time":"2024-03-01T00:00:00Z","timestamp":1709251200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2024,3,1]],"date-time":"2024-03-01T00:00:00Z","timestamp":1709251200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2024,2,10]],"date-time":"2024-02-10T00:00:00Z","timestamp":1707523200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"NIH","doi-asserted-by":"publisher","award":["CA251425"],"award-info":[{"award-number":["CA251425"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2024,3]]},"DOI":"10.1016\/j.jbc.2024.105752","type":"journal-article","created":{"date-parts":[[2024,2,13]],"date-time":"2024-02-13T00:03:42Z","timestamp":1707782622000},"page":"105752","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":8,"title":["Modulation of Cullin-RING E3 ubiquitin ligase-dependent ubiquitination by small molecule compounds"],"prefix":"10.1016","volume":"300","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-3513-5143","authenticated-orcid":false,"given":"Kenneth","family":"Wu","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robert J.","family":"DeVita","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhen-Qiang","family":"Pan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jbc.2024.105752_bib1","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1038\/nrm1547","article-title":"Function and regulation of cullin-RING ubiquitin ligases","volume":"6","author":"Petroski","year":"2005","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.jbc.2024.105752_bib2","doi-asserted-by":"crossref","first-page":"220","DOI":"10.1186\/gb-2011-12-4-220","article-title":"The cullin protein family","volume":"12","author":"Sarikas","year":"2011","journal-title":"Genome Biol."},{"key":"10.1016\/j.jbc.2024.105752_bib3","doi-asserted-by":"crossref","first-page":"1985","DOI":"10.1038\/sj.onc.1207414","article-title":"Nedd8 on cullin: building an expressway to protein destruction","volume":"23","author":"Pan","year":"2004","journal-title":"Oncogene"},{"key":"10.1016\/j.jbc.2024.105752_bib4","doi-asserted-by":"crossref","first-page":"1198","DOI":"10.1016\/j.cell.2016.07.027","article-title":"Two distinct types of E3 ligases work in unison to regulate substrate ubiquitylation","volume":"166","author":"Scott","year":"2016","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2024.105752_bib5","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1038\/s41586-020-2000-y","article-title":"NEDD8 nucleates a multivalent cullin-RING-UBE2D ubiquitin ligation assembly","volume":"578","author":"Baek","year":"2020","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2024.105752_bib6","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1038\/s41586-021-03197-9","article-title":"Ubiquitin ligation to F-box protein targets by SCF-RBR E3-E3 super-assembly","volume":"590","author":"Horn-Ghetko","year":"2021","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2024.105752_bib7","doi-asserted-by":"crossref","first-page":"957","DOI":"10.1016\/j.cell.2009.10.030","article-title":"Rapid E2-E3 assembly and disassembly enable processive ubiquitylation of cullin-RING ubiquitin ligase substrates","volume":"139","author":"Kleiger","year":"2009","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2024.105752_bib8","doi-asserted-by":"crossref","first-page":"1106","DOI":"10.1074\/jbc.M114.615559","article-title":"Ubiquitin-conjugating enzyme Cdc34 and ubiquitin ligase Skp1-cullin-F-box ligase (SCF) interact through multiple conformations","volume":"290","author":"Sandoval","year":"2015","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2024.105752_bib9","doi-asserted-by":"crossref","first-page":"784","DOI":"10.1016\/j.molcel.2010.02.025","article-title":"Priming and extending: an UbcH5\/Cdc34 E2 handoff mechanism for polyubiquitination on a SCF substrate","volume":"37","author":"Wu","year":"2010","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jbc.2024.105752_bib10","doi-asserted-by":"crossref","first-page":"7068","DOI":"10.1074\/jbc.M113.530576","article-title":"A\u00a0snapshot at ubiquitin chain elongation: lysine 48-tetra-ubiquitin slows down ubiquitination","volume":"289","author":"Kovacev","year":"2014","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2024.105752_bib11","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.40958","article-title":"UBE2G1 governs the destruction of cereblon neomorphic substrates","volume":"7","author":"Lu","year":"2018","journal-title":"Elife"},{"key":"10.1016\/j.jbc.2024.105752_bib12","doi-asserted-by":"crossref","first-page":"1293","DOI":"10.1182\/blood-2018-01-821769","article-title":"Genome-wide screen identifies cullin-RING ligase machinery required for lenalidomide-dependent CRL4CRBN activity","volume":"132","author":"Sievers","year":"2018","journal-title":"Blood"},{"key":"10.1016\/j.jbc.2024.105752_bib13","doi-asserted-by":"crossref","first-page":"995","DOI":"10.1016\/j.cell.2008.07.022","article-title":"Structural insights into NEDD8 activation of cullin-RING ligases: conformational control of conjugation","volume":"134","author":"Duda","year":"2008","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2024.105752_bib14","doi-asserted-by":"crossref","first-page":"12230","DOI":"10.1073\/pnas.0806155105","article-title":"Autoinhibitory regulation of SCF-mediated ubiquitination by human cullin 1's C-terminal tail","volume":"105","author":"Yamoah","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2024.105752_bib15","doi-asserted-by":"crossref","first-page":"1075","DOI":"10.1038\/s41589-021-00858-8","article-title":"CUL5-ARIH2 E3-E3 ubiquitin ligase structure reveals cullin-specific NEDD8 activation","volume":"17","author":"Kostrhon","year":"2021","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.jbc.2024.105752_bib16","article-title":"Inhibitors of cullin-RING E3 ubiquitin ligase 4 with antitumor potential","volume":"118","author":"Wu","year":"2021","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2024.105752_bib17","doi-asserted-by":"crossref","first-page":"E2011","DOI":"10.1073\/pnas.1601089113","article-title":"Suramin inhibits cullin-RING E3 ubiquitin ligases","volume":"113","author":"Wu","year":"2016","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2024.105752_bib18","doi-asserted-by":"crossref","first-page":"1445","DOI":"10.1016\/S1097-2765(03)00234-X","article-title":"Structure of a beta-TrCP1-Skp1-beta-catenin complex: destruction motif binding and lysine specificity of the SCF(beta-TrCP1) ubiquitin ligase","volume":"11","author":"Wu","year":"2003","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jbc.2024.105752_bib19","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1042\/bj20030755","article-title":"Saccharomyces cerevisiae ubiquitin-like protein Rub1 conjugates to cullin proteins Rtt101 and Cul3 in\u00a0vivo","volume":"377","author":"Laplaza","year":"2004","journal-title":"Biochem. J."},{"key":"10.1016\/j.jbc.2024.105752_bib20","doi-asserted-by":"crossref","first-page":"590","DOI":"10.1038\/nature05175","article-title":"Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase machinery","volume":"443","author":"Angers","year":"2006","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2024.105752_bib21","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1038\/416703a","article-title":"Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex","volume":"416","author":"Zheng","year":"2002","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2024.105752_bib22","doi-asserted-by":"crossref","first-page":"901","DOI":"10.1016\/j.str.2017.04.009","article-title":"Crystal structure of the Cul2-Rbx1-EloBC- VHL ubiquitin ligase complex","volume":"25","author":"Cardote","year":"2017","journal-title":"Structure"},{"key":"10.1016\/j.jbc.2024.105752_bib23","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1038\/s41580-022-00543-1","article-title":"An expanded lexicon for the ubiquitin code","volume":"24","author":"Dikic","year":"2023","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.jbc.2024.105752_bib24","article-title":"A\u00a0new Forster resonance energy transfer-based platform to track substrate ubiquitination by fluorescence","volume":"296","author":"Wu","year":"2020","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2024.105752_bib25","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1038\/nature14610","article-title":"Lenalidomide induces ubiquitination\u00a0and degradation of CK1\u03b1 indel(5q) MDS","volume":"523","author":"Kr\u00f6nke","year":"2015","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2024.105752_bib26","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1038\/nature16979","article-title":"Structural basis of lenalidomide-induced CK1\u03b1 degradation by the CRL4(CRBN) ubiquitin ligase","volume":"532","author":"Petzold","year":"2016","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2024.105752_bib27","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1002\/jcb.22019","article-title":"Autophosphorylation of carboxy-terminal residues inhibits the activity of protein kinase CK1alpha","volume":"106","author":"Budini","year":"2009","journal-title":"J.\u00a0Cell Biochem."}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925824001285?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925824001285?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,19]],"date-time":"2025-09-19T01:02:29Z","timestamp":1758243749000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925824001285"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,3]]},"references-count":27,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2024,3]]}},"alternative-id":["S0021925824001285"],"URL":"https:\/\/doi.org\/10.1016\/j.jbc.2024.105752","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2024,3]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Modulation of Cullin-RING E3 ubiquitin ligase-dependent ubiquitination by small molecule compounds","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jbc.2024.105752","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"https:\/\/doi.org\/10.1016\/j.jbc.2024.105753","name":"associatedlink","label":"CrossRef DOI link to the associated document"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2024 The Authors. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}],"article-number":"105752"}}