{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T19:46:59Z","timestamp":1792784819981,"version":"4.5.0"},"reference-count":52,"publisher":"American Chemical Society (ACS)","issue":"37","license":[{"start":{"date-parts":[[2026,9,8]],"date-time":"2026-09-08T00:00:00Z","timestamp":1788825600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100004271","name":"Sapienza Universit? di Roma","doi-asserted-by":"publisher","award":["RM123188F763A9D5"],"award-info":[{"award-number":["RM123188F763A9D5"]}],"id":[{"id":"10.13039\/501100004271","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100021856","name":"Ministero dell'Universit? e della Ricerca","doi-asserted-by":"publisher","award":["IR0000009"],"award-info":[{"award-number":["IR0000009"]}],"id":[{"id":"10.13039\/501100021856","id-type":"DOI","asserted-by":"publisher"}]},{"name":"CNCCS (Collezione di Composti Chimici ed attivit? di screening) CNR\/FOE","award":["DSB.AD011.013.001"],"award-info":[{"award-number":["DSB.AD011.013.001"]}]},{"name":"Instruct-ERIC","award":["32193"],"award-info":[{"award-number":["32193"]}],"id":[{"id":"https:\/\/ror.org\/05528ey35","id-type":"ROR","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,9,22]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Leishmaniasis is a neglected disease that affects around two million people every year. Current treatments are often highly toxic or prone to resistance, underscoring the urgent need for new therapeutic strategies. PROTACs may offer a promising alternative, as they can potentially mitigate both toxicity and resistance. However, very little is known about the ubiquitin\u2013proteasome system (UPS) in Leishmania. Notably, only two E3 ligases containing a CULT domain have been identified so far, and none carrying a von Hippel\u2013Lindau (VHL) domain\u2500the classical E3 ligase used by clinically advanced PROTACs. In this work, we take an important step toward understanding the UPS in Leishmania, and we propose that in this organism the UbC4 E2 enzyme, rather than an E3, may be directly exploited to develop a PROTAC able to engage a protein of interest. Here, we report the biochemical and structural characterization of the Leishmania major ubiquitin-conjugating enzyme 4 (UbC4). Through a fragment screening campaign, we identified 10 fragments binding to distinct cavities on UbC4. Among these, five interact with the same noncatalytic pocket that is poorly conserved in humans, while one fragment binds near the catalytic cysteine. Using DeepFrag predictions and molecular docking, we explored fragment elongation strategies to enhance affinity for their respective binding sites, with the goal of guiding the development of E2-recruiting PROTACs or UPS inhibitors for the treatment of leishmaniasis.<\/jats:p>","DOI":"10.1021\/acsomega.6c05158","type":"journal-article","created":{"date-parts":[[2026,9,8]],"date-time":"2026-09-08T16:02:45Z","timestamp":1788883365000},"page":"55759-55771","source":"Crossref","is-referenced-by-count":0,"title":["UbC4 from Leishmania\nis a Druggable E2 Ubiquitin Conjugating\nEnzyme: Structural Basis and Fragment Hits for Future E2-Recruiting\nPROTAC Development"],"prefix":"10.1021","volume":"11","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-7457-6895","authenticated-orcid":true,"given":"Ce\u0301cile","family":"Exertier","sequence":"first","affiliation":[{"name":"Sapienza University of Rome , , Ed. CU027, P.le A. Moro 5 , ,","place":["Rome, Italy, 00185"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lorenzo","family":"Antonelli","sequence":"additional","affiliation":[{"name":"Sapienza University of Rome , , Ed. CU027, P.le A. Moro 5 , ,","place":["Rome, Italy, 00185"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anastasia","family":"Liuzzi","sequence":"additional","affiliation":[{"name":"Sapienza University of Rome , , Ed. CU027, P.le A. Moro 5 , ,","place":["Rome, Italy, 00185"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marcus","family":"Ruffa","sequence":"additional","affiliation":[{"name":"Sapienza University of Rome , , Ed. CU027, P.le A. Moro 5 , ,","place":["Rome, Italy, 00185"]},{"name":"Sapienza University of Rome , , Ed. CU027, P.le A. Moro 5 , ,","place":["Rome, Italy, 00185"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vittorio","family":"Brufani","sequence":"additional","affiliation":[{"name":"Sapienza University of Rome , , Ed. CU027, P.le A. Moro 5 , ,","place":["Rome, Italy, 00185"]},{"name":"Sapienza University of Rome , , Ed. CU027, P.le A. Moro 5 , ,","place":["Rome, Italy, 00185"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9913-0635","authenticated-orcid":true,"given":"Gianni","family":"Colotti","sequence":"additional","affiliation":[{"name":"Sapienza University of Rome , , Ed. CU027, P.le A. Moro 5 , ,","place":["Rome, Italy, 00185"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Annarita","family":"Fiorillo","sequence":"additional","affiliation":[{"name":"Sapienza University of Rome , , Ed. CU027, P.le A. Moro 5 , ,","place":["Rome, Italy, 00185"]},{"name":"Sapienza University of Rome , , Ed. CU027, P.le A. Moro 5 , ,","place":["Rome, Italy, 00185"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7754-399X","authenticated-orcid":true,"given":"Andrea","family":"Ilari","sequence":"additional","affiliation":[{"name":"Sapienza University of Rome , , Ed. CU027, P.le A. Moro 5 , ,","place":["Rome, Italy, 00185"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,9,8]]},"reference":[{"key":"2026092210583836500_cit1","first-page":"776","volume-title":"Leishmaniasis: General\nPrinciples","author":"Aronson","year":"2020"},{"issue":"5","key":"2026092210583836500_cit2","doi-asserted-by":"publisher","first-page":"1541","DOI":"10.1007\/s00436-021-07139-2","article-title":"Leishmaniasis: where are we and where\nare we heading?","volume":"120","author":"Sasidharan","year":"2021","journal-title":"Parasitol. Res."},{"key":"2026092210583836500_cit3","unstructured":"Leishmaniasis\n(WHO), 2022. https:\/\/www.who.int\/news-room\/fact-sheets\/detail\/leishmaniasis."},{"issue":"10151","key":"2026092210583836500_cit4","doi-asserted-by":"publisher","first-page":"951","DOI":"10.1016\/S0140-6736(18)31204-2","article-title":"Leishmaniasis","volume":"392","author":"Burza","year":"2018","journal-title":"Lancet"},{"issue":"8","key":"2026092210583836500_cit5","doi-asserted-by":"publisher","DOI":"10.3390\/molecules25081924","article-title":"Targeting Trypanothione\nReductase, a Key Enzyme in the Redox Trypanosomatid Metabolism, to\nDevelop New Drugs against Leishmaniasis and Trypanosomiases","volume":"25","author":"Battista","year":"2020","journal-title":"Molecules"},{"issue":"3","key":"2026092210583836500_cit6","doi-asserted-by":"publisher","first-page":"516","DOI":"10.1111\/ced.14919","article-title":"Treatment\noptions for leishmaniasis","volume":"47","author":"Pradhan","year":"2022","journal-title":"Clin. Exp. Dermatol."},{"issue":"8","key":"2026092210583836500_cit7","doi-asserted-by":"publisher","first-page":"2603","DOI":"10.1021\/jm900185q","article-title":"Molecular Basis of\nAntimony Treatment in Leishmaniasis","volume":"52","author":"Baiocco","year":"2009","journal-title":"J. Med.\nChem."},{"issue":"5","key":"2026092210583836500_cit8","doi-asserted-by":"publisher","DOI":"10.3390\/pathogens12050706","article-title":"Recent Advances\nin Chemotherapeutics for Leishmaniasis: Importance of the Cellular\nBiochemistry of the Parasite and Its Molecular Interaction with the\nHost","volume":"12","author":"Singh","year":"2023","journal-title":"Pathogens"},{"issue":"4","key":"2026092210583836500_cit9","doi-asserted-by":"publisher","first-page":"1425","DOI":"10.1128\/AAC.01123-06","article-title":"Miltefosine Affects Lipid Metabolism\nin Leishmania donovani Promastigotes","volume":"51","author":"Rakotomanga","year":"2007","journal-title":"Antimicrob.\nAgents Chemother."},{"key":"2026092210583836500_cit10","doi-asserted-by":"publisher","DOI":"10.3389\/fchem.2021.622286","article-title":"An Overview on the Therapeutics of\nNeglected Infectious Diseases\u2500Leishmaniasis and Chagas Diseases","volume":"9","author":"Brindha","year":"2021","journal-title":"Front. Chem."},{"issue":"10","key":"2026092210583836500_cit11","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0026660","article-title":"Paromomycin\nAffects Translation and Vesicle-Mediated Trafficking as Revealed by\nProteomics of Paromomycin \u2013 Susceptible \u2013 Resistant\nLeishmania donovani","volume":"6","author":"Chawla","year":"2011","journal-title":"PLoS One"},{"issue":"6","key":"2026092210583836500_cit12","doi-asserted-by":"publisher","first-page":"1871","DOI":"10.1021\/acsinfecdis.4c00010","article-title":"Revolutionizing\nLeishmaniasis Treatment with Cutting\nEdge Drug Delivery Systems and Nanovaccines: An Updated Review","volume":"10","author":"Tambe","year":"2024","journal-title":"ACS Infect. Dis."},{"issue":"1","key":"2026092210583836500_cit13","doi-asserted-by":"publisher","first-page":"32","DOI":"10.1021\/acsbiomedchemau.2c00063","article-title":"Targeted Protein Degradation for\nInfectious Diseases: from Basic Biology to Drug Discovery","volume":"3","author":"Espinoza-Cha\u0301vez","year":"2023","journal-title":"ACS Bio Med Chem Au"},{"issue":"1","key":"2026092210583836500_cit14","doi-asserted-by":"publisher","DOI":"10.1038\/s41598-018-26532-z","article-title":"Ubiquitin\nProteasome pathway proteins as potential drug targets in parasite\nTrypanosoma cruzi","volume":"8","author":"Gupta","year":"2018","journal-title":"Sci. Rep."},{"key":"2026092210583836500_cit15","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1155\/2015\/141526","article-title":"Role of the\nUbiquitin-Proteasome Systems in the Biology and Virulence of Protozoan\nParasites","volume":"2015","author":"Mun\u0303oz","year":"2015","journal-title":"Biomed. Res. Int."},{"issue":"2","key":"2026092210583836500_cit16","doi-asserted-by":"publisher","first-page":"323","DOI":"10.1016\/j.molcel.2024.12.015","article-title":"Ubiquitin\u2500A\nstructural perspective","volume":"85","author":"Agrata","year":"2025","journal-title":"Mol. Cell"},{"issue":"10","key":"2026092210583836500_cit17","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1008784","article-title":"Leishmania\ndifferentiation requires ubiquitin conjugation mediated by a UBC2-UEV1\nE2 complex","volume":"16","author":"Burge","year":"2020","journal-title":"PLoS Pathog."},{"issue":"3","key":"2026092210583836500_cit18","doi-asserted-by":"publisher","first-page":"531","DOI":"10.1242\/jcs.091777","article-title":"HECT and\nRING finger families of\nE3 ubiquitin ligases at a glance","volume":"125","author":"Metzger","year":"2012","journal-title":"J. Cell Sci."},{"issue":"21","key":"2026092210583836500_cit19","doi-asserted-by":"publisher","first-page":"6682","DOI":"10.3390\/molecules26216682","article-title":"Structural\nDiversity of Ubiquitin E3 Ligase","volume":"26","author":"Toma-Fukai","year":"2021","journal-title":"Molecules"},{"issue":"7619","key":"2026092210583836500_cit20","doi-asserted-by":"publisher","first-page":"229","DOI":"10.1038\/nature19339","article-title":"Proteasome\ninhibition for treatment of leishmaniasis,\nChagas disease and sleeping sickness","volume":"537","author":"Khare","year":"2016","journal-title":"Nature"},{"issue":"19","key":"2026092210583836500_cit21","doi-asserted-by":"publisher","first-page":"10773","DOI":"10.1021\/acs.jmedchem.0c00499","article-title":"Discovery and Characterization of Clinical Candidate\nLXE408 as a Kinetoplastid-Selective Proteasome Inhibitor for the Treatment\nof Leishmaniases","volume":"63","author":"Nagle","year":"2020","journal-title":"J. Med. Chem."},{"key":"2026092210583836500_cit22","doi-asserted-by":"publisher","DOI":"10.1016\/j.molbiopara.2024.111619","article-title":"Formation of functional E3 ligase complexes with UBC2\nand UEV1 of Leishmania mexicana","volume":"258","author":"Burge","year":"2024","journal-title":"Mol. Biochem.\nParasitol."},{"issue":"1","key":"2026092210583836500_cit23","doi-asserted-by":"publisher","DOI":"10.1038\/s41392-024-02004-x","article-title":"Targeted protein degradation:\nadvances in drug discovery and clinical practice","volume":"9","author":"Zhong","year":"2024","journal-title":"Signal Transduction Targeted Ther."},{"issue":"1","key":"2026092210583836500_cit24","doi-asserted-by":"publisher","DOI":"10.1038\/s42003-024-06803-4","article-title":"Targeted protein degradation using chimeric human E2\nubiquitin-conjugating enzymes","volume":"7","author":"Taylor","year":"2024","journal-title":"Commun. Biol."},{"issue":"4","key":"2026092210583836500_cit25","doi-asserted-by":"publisher","first-page":"897","DOI":"10.1021\/acschembio.3c00040","article-title":"Targeted\nProtein Degradation through\nE2 Recruitment","volume":"18","author":"Forte","year":"2023","journal-title":"ACS Chem. Biol."},{"key":"2026092210583836500_cit26","doi-asserted-by":"publisher","DOI":"10.3389\/fchbi.2025.1605579","article-title":"Expanding\nthe molecular landscape of fragments binding\nto trypanothione reductase, a legitimate target for drug design against\nhuman African trypanosomiasis","volume":"4","author":"Exertier","year":"2025","journal-title":"Front. Chem.\nBiol."},{"key":"2026092210583836500_cit27","doi-asserted-by":"publisher","DOI":"10.3389\/fmolb.2022.900882","article-title":"Innovative\nApproach for a Classic Target: Fragment\nScreening on Trypanothione Reductase Reveals New Opportunities for\nDrug Design","volume":"9","author":"Fiorillo","year":"2022","journal-title":"Front. Mol. Biosci."},{"issue":"1","key":"2026092210583836500_cit28","doi-asserted-by":"publisher","first-page":"402","DOI":"10.1021\/acs.jmedchem.3c01439","article-title":"Fragment\nMerging, Growing, and Linking Identify\nNew Trypanothione Reductase Inhibitors for Leishmaniasis","volume":"67","author":"Exertier","year":"2024","journal-title":"J. Med. Chem."},{"key":"2026092210583836500_cit29","doi-asserted-by":"publisher","first-page":"497","DOI":"10.1007\/978-1-60327-058-8_33","article-title":"Structural\nGenomics of Pathogenic Protozoa:\nan Overview","volume":"426","author":"Fan","year":"2008","journal-title":"Methods Mol. Biol."},{"issue":"3","key":"2026092210583836500_cit30","doi-asserted-by":"publisher","first-page":"246","DOI":"10.1107\/S205979831700331X","article-title":"Gentle, fast and effective\ncrystal soaking by acoustic dispensing","volume":"73","author":"Collins","year":"2017","journal-title":"Acta\nCrystallogr., Sect. D: Struct. Biol."},{"issue":"1","key":"2026092210583836500_cit31","doi-asserted-by":"publisher","first-page":"62","DOI":"10.1107\/S2059798320014114","article-title":"The low-cost\nShifter microscope stage transforms the\nspeed and robustness of protein crystal harvesting","volume":"77","author":"Wright","year":"2021","journal-title":"Acta Crystallogr., Sect. D: Struct. Biol."},{"issue":"171","key":"2026092210583836500_cit32","doi-asserted-by":"publisher","DOI":"10.3791\/62414","article-title":"Achieving\nEfficient Fragment Screening at XChem Facility\nat Diamond Light Source","author":"Douangamath","year":"2021","journal-title":"J. Visualized Exp."},{"issue":"3","key":"2026092210583836500_cit33","doi-asserted-by":"publisher","first-page":"267","DOI":"10.1107\/S2059798316020234","article-title":"The XChemExplorer graphical\nworkflow tool for routine or large-scale protein\u2013ligand structure\ndetermination","volume":"73","author":"Krojer","year":"2017","journal-title":"Acta Crystallogr., Sect. D: Struct.\nBiol."},{"issue":"3","key":"2026092210583836500_cit34","doi-asserted-by":"publisher","DOI":"10.1063\/1.4974176","article-title":"Partial-occupancy binders identified\nby the Pan-Dataset\nDensity Analysis method offer new chemical opportunities and reveal\ncryptic binding sites","volume":"4","author":"Pearce","year":"2017","journal-title":"Struct. Dyn."},{"issue":"4","key":"2026092210583836500_cit35","doi-asserted-by":"publisher","first-page":"368","DOI":"10.1107\/S0907444911056058","article-title":"Exploiting\nstructure similarity in refinement: automated\nNCS and target-structure restraints in BUSTER","volume":"68","author":"Smart","year":"2012","journal-title":"Acta Crystallogr., Sect. D: Biol. Crystallogr."},{"issue":"6","key":"2026092210583836500_cit36","doi-asserted-by":"publisher","first-page":"2523","DOI":"10.1021\/acs.jcim.1c00103","article-title":"DeepFrag: An Open-Source\nBrowser App for Deep-Learning\nLead Optimization","volume":"61","author":"Green","year":"2021","journal-title":"J. Chem. Inf. Model."},{"issue":"2","key":"2026092210583836500_cit37","doi-asserted-by":"publisher","first-page":"455","DOI":"10.1002\/jcc.21334","article-title":"AutoDock Vina: Improving the speed and accuracy of\ndocking with a new scoring function, efficient optimization, and multithreading","volume":"31","author":"Trott","year":"2010","journal-title":"J. Comput. Chem."},{"issue":"8","key":"2026092210583836500_cit38","doi-asserted-by":"publisher","first-page":"3891","DOI":"10.1021\/acs.jcim.1c00203","article-title":"AutoDock Vina 1.2.0:\nNew Docking Methods, Expanded Force Field, and Python Bindings","volume":"61","author":"Eberhardt","year":"2021","journal-title":"J. Chem. Inf. Model."},{"key":"2026092210583836500_cit39","doi-asserted-by":"publisher","first-page":"1605","DOI":"10.1002\/jcc.20084","article-title":"UCSF Chimera\u2500A\nVisualization\nSystem for Exploratory Research and Analysis","volume":"25","author":"Pettersen","year":"2004","journal-title":"J. Comput. Chem."},{"issue":"D1","key":"2026092210583836500_cit40","doi-asserted-by":"publisher","first-page":"D368","DOI":"10.1093\/nar\/gkad1011","article-title":"AlphaFold Protein Structure Database in 2024:\nproviding structure coverage for over 214 million protein sequences","volume":"52","author":"Varadi","year":"2024","journal-title":"Nucleic Acids Res."},{"issue":"4","key":"2026092210583836500_cit41","doi-asserted-by":"publisher","first-page":"423","DOI":"10.1038\/cr.2016.35","article-title":"E2 enzymes: more\nthan just middle men","volume":"26","author":"Stewart","year":"2016","journal-title":"Cell Res."},{"issue":"7","key":"2026092210583836500_cit42","doi-asserted-by":"publisher","first-page":"1679","DOI":"10.1016\/j.bpj.2020.02.012","article-title":"Recruitment of Ubiquitin within an\nE2 Chain Elongation Complex","volume":"118","author":"Cook","year":"2020","journal-title":"Biophys. J."},{"issue":"3","key":"2026092210583836500_cit43","doi-asserted-by":"publisher","first-page":"889","DOI":"10.1021\/acs.chemrev.6b00737","article-title":"Ubiquitin-like Protein Conjugation: Structures, Chemistry,\nand Mechanism","volume":"118","author":"Cappadocia","year":"2018","journal-title":"Chem. Rev."},{"issue":"1","key":"2026092210583836500_cit44","doi-asserted-by":"publisher","first-page":"31","DOI":"10.1042\/BJ20100985","article-title":"E2s: structurally\neconomical and\nfunctionally replete","volume":"433","author":"Wenzel","year":"2011","journal-title":"Biochem. J."},{"issue":"4","key":"2026092210583836500_cit45","doi-asserted-by":"publisher","first-page":"981","DOI":"10.1096\/fj.09-136259","article-title":"The family of ubiquitin-conjugating\nenzymes (E2s): deciding between life and death of proteins","volume":"24","author":"van Wijk","year":"2010","journal-title":"FASEB J."},{"issue":"W1","key":"2026092210583836500_cit46","doi-asserted-by":"publisher","first-page":"W194","DOI":"10.1093\/nar\/gkae415","article-title":"CASTpFold: Computed\nAtlas of Surface Topography of the universe of protein Folds","volume":"52","author":"Ye","year":"2024","journal-title":"Nucleic Acids Res."},{"issue":"1","key":"2026092210583836500_cit47","doi-asserted-by":"publisher","DOI":"10.1038\/srep16793","article-title":"The molecular basis\nof lysine 48 ubiquitin chain synthesis\nby Ube2K","volume":"5","author":"Middleton","year":"2015","journal-title":"Sci. Rep."},{"issue":"8","key":"2026092210583836500_cit48","doi-asserted-by":"publisher","first-page":"329","DOI":"10.1074\/mcp.O111.013706","article-title":"A Human Ubiquitin Conjugating Enzyme (E2)-HECT\nE3 Ligase Structure-function Screen","volume":"11","author":"Sheng","year":"2012","journal-title":"Mol. Cell.\nProteomics"},{"issue":"19","key":"2026092210583836500_cit49","doi-asserted-by":"publisher","first-page":"5241","DOI":"10.1093\/emboj\/cdg501","article-title":"A conserved catalytic\nresidue in the ubiquitin-conjugating enzyme family","volume":"22","author":"Wu","year":"2003","journal-title":"EMBO J."},{"issue":"7","key":"2026092210583836500_cit50","doi-asserted-by":"publisher","first-page":"1075","DOI":"10.1016\/j.cell.2011.05.039","article-title":"An Allosteric Inhibitor of the Human Cdc34\nUbiquitin-Conjugating Enzyme","volume":"145","author":"Ceccarelli","year":"2011","journal-title":"Cell"},{"issue":"1","key":"2026092210583836500_cit51","doi-asserted-by":"publisher","DOI":"10.1186\/s12943-022-01538-4","article-title":"Targeting E2 ubiquitin-conjugating enzyme UbcH5c by\nsmall molecule inhibitor suppresses pancreatic cancer growth and metastasis","volume":"21","author":"Qi","year":"2022","journal-title":"Mol. Cancer"},{"issue":"W1","key":"2026092210583836500_cit52","doi-asserted-by":"publisher","first-page":"W463","DOI":"10.1093\/nar\/gkaf361","article-title":"PLIP 2025:\nintroducing protein\u2013protein interactions to the protein\u2013ligand\ninteraction profiler","volume":"53","author":"Schake","year":"2025","journal-title":"Nucleic Acids Res."}],"container-title":["ACS Omega"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/acsomega.6c05158","content-type":"application\/pdf","content-version":"vor","intended-application":"unspecified"},{"URL":"https:\/\/pubs.acs.org\/acsodf\/article-pdf\/11\/37\/55759\/68451214\/acsomega.6c05158.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pubs.acs.org\/acsodf\/article-pdf\/11\/37\/55759\/68451214\/acsomega.6c05158.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,9,22]],"date-time":"2026-09-22T15:51:00Z","timestamp":1790092260000},"score":1,"resource":{"primary":{"URL":"https:\/\/pubs.acs.org\/acsodf\/article\/11\/37\/55759\/5426522\/UbC4-from-Leishmania-is-a-Druggable-E2-Ubiquitin"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,9,8]]},"references-count":52,"journal-issue":{"issue":"37","published-online":{"date-parts":[[2026,9,8]]},"published-print":{"date-parts":[[2026,9,22]]}},"URL":"https:\/\/doi.org\/10.1021\/acsomega.6c05158","relation":{},"ISSN":["2470-1343"],"issn-type":[{"value":"2470-1343","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,9,8]]}}}