{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T08:31:15Z","timestamp":1791275475854,"version":"4.1.0"},"reference-count":54,"publisher":"eLife Sciences Publications, Ltd","license":[{"start":{"date-parts":[[2024,9,2]],"date-time":"2024-09-02T00:00:00Z","timestamp":1725235200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2024,9,2]],"date-time":"2024-09-02T00:00:00Z","timestamp":1725235200000},"content-version":"am","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2024,9,2]],"date-time":"2024-09-02T00:00:00Z","timestamp":1725235200000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"PMRF","award":["0403018"],"award-info":[{"award-number":["0403018"]}]},{"DOI":"10.13039\/100010269","name":"Wellcome Trust Senior Research Fellowship in Clinical Science","doi-asserted-by":"publisher","award":["10.35802\/210753"],"award-info":[{"award-number":["10.35802\/210753"],"id":[{"id":"10.35802\/210753","id-type":"DOI","asserted-by":"publisher"}]}],"id":[{"id":"10.13039\/100010269","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000864","name":"Michael J Fox Foundation","doi-asserted-by":"publisher","award":["M.M.K.M."],"award-info":[{"award-number":["M.M.K.M."]}],"id":[{"id":"10.13039\/100000864","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Innovative Young Biotechnologist Award","award":["DBT\/12\/IYBAl2019\/03"],"award-info":[{"award-number":["DBT\/12\/IYBAl2019\/03"]}]},{"name":"Ramalingaswami Re-entry Fellowship","award":["DBT\/RLF\/Re-entry\/42\/2019"],"award-info":[{"award-number":["DBT\/RLF\/Re-entry\/42\/2019"]}]},{"DOI":"10.13039\/501100001843","name":"SERB","doi-asserted-by":"crossref","award":["SERB\/F\/6520\/2019-2020"],"award-info":[{"award-number":["SERB\/F\/6520\/2019-2020"]}],"id":[{"id":"10.13039\/501100001843","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100010713","name":"IISER Bhopal","doi-asserted-by":"publisher","award":["AK"],"award-info":[{"award-number":["AK"]}],"id":[{"id":"10.13039\/501100010713","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elifesciences.org"],"crossmark-restriction":false},"short-container-title":[],"abstract":"<jats:p>\n                    Loss-of-function Parkin mutations lead to early-onset of Parkinson\u2019s disease. Parkin is an auto-inhibited ubiquitin E3 ligase activated by dual phosphorylation of its ubiquitin-like (Ubl) domain and ubiquitin by the PINK1 kinase. Herein, we demonstrate a competitive binding of the phospho-Ubl and RING2 domains towards the RING0 domain, which regulates Parkin activity. We show that phosphorylated Parkin can complex with native Parkin, leading to the activation of autoinhibited native Parkin in\n                    <jats:italic>trans<\/jats:italic>\n                    . Furthermore, we show that the activator element (ACT) of Parkin is required to maintain the enzyme kinetics, and the removal of ACT slows the enzyme catalysis. We also demonstrate that ACT can activate Parkin in\n                    <jats:italic>trans<\/jats:italic>\n                    but less efficiently than when present in the\n                    <jats:italic>cis<\/jats:italic>\n                    molecule. Furthermore, the crystal structure reveals a donor ubiquitin binding pocket in the linker connecting REP and RING2, which plays a crucial role in Parkin activity.\n                  <\/jats:p>","DOI":"10.7554\/elife.96699","type":"journal-article","created":{"date-parts":[[2024,5,1]],"date-time":"2024-05-01T09:27:16Z","timestamp":1714555636000},"update-policy":"https:\/\/doi.org\/10.7554\/elife.96699","source":"Crossref","is-referenced-by-count":2,"title":["Additional feedforward mechanism of Parkin activation via binding of phospho-UBL and RING0 in trans"],"prefix":"10.7554","volume":"13","author":[{"ORCID":"https:\/\/orcid.org\/0009-0009-8890-8331","authenticated-orcid":true,"given":"Dipti Ranjan","family":"Lenka","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/02rb21j89","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Biological Sciences, Indian Institute of Science Education and Research (IISER) Bhopal","place":["Bhopal, India"]}],"role":[{"role":"author","vocabulary":"crossref"},{"role":"conceptualization","vocabulary":"credit"},{"role":"data-curation","vocabulary":"credit"},{"role":"formal-analysis","vocabulary":"credit"},{"role":"investigation","vocabulary":"credit"},{"role":"methodology","vocabulary":"credit"},{"role":"resources","vocabulary":"credit"},{"role":"validation","vocabulary":"credit"},{"role":"visualization","vocabulary":"credit"},{"role":"writing-review-editing","vocabulary":"credit"}]},{"ORCID":"https:\/\/orcid.org\/0009-0009-8909-240X","authenticated-orcid":true,"given":"Shakti Virendra","family":"Dahe","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/02rb21j89","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Biological Sciences, Indian Institute of Science Education and Research (IISER) Bhopal","place":["Bhopal, India"]}],"role":[{"role":"author","vocabulary":"crossref"},{"role":"investigation","vocabulary":"credit"},{"role":"methodology","vocabulary":"credit"}]},{"given":"Odetta","family":"Antico","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/03h2bxq36","id-type":"ROR","asserted-by":"publisher"}],"name":"MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee","place":["Dundee, United Kingdom"]}],"role":[{"role":"author","vocabulary":"crossref"},{"role":"formal-analysis","vocabulary":"credit"},{"role":"investigation","vocabulary":"credit"},{"role":"methodology","vocabulary":"credit"},{"role":"visualization","vocabulary":"credit"},{"role":"writing-review-editing","vocabulary":"credit"}]},{"given":"Pritiranjan","family":"Sahoo","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/02rb21j89","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Biological Sciences, Indian Institute of Science Education and Research (IISER) Bhopal","place":["Bhopal, India"]}],"role":[{"role":"author","vocabulary":"crossref"},{"role":"methodology","vocabulary":"credit"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0747-7317","authenticated-orcid":true,"given":"Alan R","family":"Prescott","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/03h2bxq36","id-type":"ROR","asserted-by":"publisher"}],"name":"Division of Cell Signalling and Immunology, Dundee Imaging Facility, School of Life Sciences, University of Dundee","place":["Dundee, United Kingdom"]}],"role":[{"role":"author","vocabulary":"crossref"},{"role":"methodology","vocabulary":"credit"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9733-2404","authenticated-orcid":true,"given":"Miratul MK","family":"Muqit","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/03h2bxq36","id-type":"ROR","asserted-by":"publisher"}],"name":"MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee","place":["Dundee, United Kingdom"]}],"role":[{"role":"author","vocabulary":"crossref"},{"role":"formal-analysis","vocabulary":"credit"},{"role":"funding-acquisition","vocabulary":"credit"},{"role":"project-administration","vocabulary":"credit"},{"role":"supervision","vocabulary":"credit"},{"role":"writing-review-editing","vocabulary":"credit"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4675-6623","authenticated-orcid":true,"given":"Atul","family":"Kumar","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/02rb21j89","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Biological Sciences, Indian Institute of Science Education and Research (IISER) Bhopal","place":["Bhopal, India"]}],"role":[{"role":"author","vocabulary":"crossref"},{"role":"corresponding-author","vocabulary":"crossref"},{"role":"conceptualization","vocabulary":"credit"},{"role":"data-curation","vocabulary":"credit"},{"role":"formal-analysis","vocabulary":"credit"},{"role":"funding-acquisition","vocabulary":"credit"},{"role":"investigation","vocabulary":"credit"},{"role":"methodology","vocabulary":"credit"},{"role":"project-administration","vocabulary":"credit"},{"role":"resources","vocabulary":"credit"},{"role":"supervision","vocabulary":"credit"},{"role":"validation","vocabulary":"credit"},{"role":"visualization","vocabulary":"credit"},{"role":"writing-original-draft","vocabulary":"credit"},{"role":"writing-review-editing","vocabulary":"credit"}]}],"member":"4374","published-online":{"date-parts":[[2024,9,2]]},"reference":[{"key":"bib1","doi-asserted-by":"publisher","first-page":"102","DOI":"10.1016\/j.ab.2011.06.034","type":"journal-article","article-title":"A spectrophotometric assay for conjugation of ubiquitin and ubiquitin-like proteins","volume":"418","author":"Berndsen","year":"2011","journal-title":"Analytical Biochemistry"},{"key":"bib2","doi-asserted-by":"publisher","first-page":"S59","DOI":"10.1007\/s100720200069","type":"journal-article","article-title":"Autosomal recessive early onset parkinsonism is linked to three loci: PARK2, PARK6, and PARK7","volume":"23 Suppl 2","author":"Bonifati","year":"2002","journal-title":"Neurological Sciences"},{"key":"bib3","doi-asserted-by":"publisher","first-page":"1149","DOI":"10.1016\/s1074-5521(02)00248-x","type":"journal-article","article-title":"Chemistry-based functional proteomics reveals novel members of the deubiquitinating enzyme family","volume":"9","author":"Borodovsky","year":"2002","journal-title":"Chemistry & Biology"},{"key":"bib4","doi-asserted-by":"publisher","first-page":"1726","DOI":"10.1093\/hmg\/ddr048","type":"journal-article","article-title":"Broad activation of the ubiquitin-proteasome system by parkin is critical for mitophagy","volume":"20","author":"Chan","year":"2011","journal-title":"Human Molecular Genetics"},{"key":"bib5","doi-asserted-by":"publisher","first-page":"2853","DOI":"10.1038\/emboj.2011.204","type":"journal-article","article-title":"Autoregulation of parkin activity through its ubiquitin-like domain","volume":"30","author":"Chaugule","year":"2011","journal-title":"The EMBO Journal"},{"key":"bib6","doi-asserted-by":"publisher","first-page":"664","DOI":"10.1016\/j.stemcr.2016.08.012","type":"journal-article","article-title":"Parkin and pink1 patient ipsc-derived midbrain dopamine neurons exhibit mitochondrial dysfunction and \u03b1-synuclein accumulation","volume":"7","author":"Chung","year":"2016","journal-title":"Stem Cell Reports"},{"key":"bib7","doi-asserted-by":"publisher","first-page":"760","DOI":"10.1107\/S0907444994003112","type":"journal-article","article-title":"The CCP4 suite: programs for protein crystallography","volume":"50","author":"Collaborative Computational Project, Number 4","year":"1994","journal-title":"Acta Crystallographica Section D Biological Crystallography"},{"key":"bib8","doi-asserted-by":"publisher","DOI":"10.15252\/embj.2018100014","type":"journal-article","article-title":"Synergistic recruitment of UbcH7~Ub and phosphorylated Ubl domain triggers parkin activation","volume":"37","author":"Condos","year":"2018","journal-title":"The EMBO Journal"},{"key":"bib9","doi-asserted-by":"publisher","first-page":"2126","DOI":"10.1107\/S0907444904019158","type":"journal-article","article-title":"Coot: model-building tools for molecular graphics","volume":"60","author":"Emsley","year":"2004","journal-title":"Acta Crystallographica. Section D, Biological Crystallography"},{"key":"bib10","doi-asserted-by":"publisher","first-page":"3038","DOI":"10.1038\/emboj.2012.170","type":"journal-article","article-title":"Mitochondrial dysfunction in parkinson\u2019s disease: molecular mechanisms and pathophysiological consequences","volume":"31","author":"Exner","year":"2012","journal-title":"The EMBO Journal"},{"key":"bib11","doi-asserted-by":"publisher","first-page":"410","DOI":"10.1038\/s41586-018-0224-x","type":"journal-article","article-title":"Mechanism of parkin activation by PINK1","volume":"559","author":"Gladkova","year":"2018","journal-title":"Nature"},{"key":"bib12","doi-asserted-by":"publisher","first-page":"671","DOI":"10.1038\/s41586-021-03197-9","type":"journal-article","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":"bib13","doi-asserted-by":"publisher","DOI":"10.1107\/S0907444909047337","type":"journal-article","article-title":"Acta Crystallogr","volume":"66","author":"Kabsch","year":"2010","journal-title":"Sect. D Biol. Crystallogr"},{"key":"bib14","doi-asserted-by":"publisher","first-page":"143","DOI":"10.1083\/jcb.201402104","type":"journal-article","article-title":"PINK1 phosphorylates ubiquitin to activate parkin E3 ubiquitin ligase activity","volume":"205","author":"Kane","year":"2014","journal-title":"The Journal of Cell Biology"},{"key":"bib15","doi-asserted-by":"publisher","first-page":"127","DOI":"10.1042\/BJ20140334","type":"journal-article","article-title":"Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser65","volume":"460","author":"Kazlauskaite","year":"2014","journal-title":"The Biochemical Journal"},{"key":"bib16","doi-asserted-by":"publisher","first-page":"939","DOI":"10.15252\/embr.201540352","type":"journal-article","article-title":"Binding to serine 65-phosphorylated ubiquitin primes parkin for optimal PINK1-dependent phosphorylation and activation","volume":"16","author":"Kazlauskaite","year":"2015","journal-title":"EMBO Reports"},{"key":"bib17","doi-asserted-by":"publisher","first-page":"605","DOI":"10.1038\/33416","type":"journal-article","article-title":"Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism","volume":"392","author":"Kitada","year":"1998","journal-title":"Nature"},{"key":"bib18","doi-asserted-by":"publisher","DOI":"10.1098\/rsob.120080","type":"journal-article","article-title":"PINK1 is activated by mitochondrial membrane potential depolarization and stimulates parkin E3 ligase activity by phosphorylating Serine 65","volume":"2","author":"Kondapalli","year":"2012","journal-title":"Open Biology"},{"key":"bib19","doi-asserted-by":"publisher","first-page":"162","DOI":"10.1038\/nature13392","type":"journal-article","article-title":"Ubiquitin is phosphorylated by PINK1 to activate parkin","volume":"510","author":"Koyano","year":"2014","journal-title":"Nature"},{"key":"bib20","doi-asserted-by":"publisher","first-page":"2506","DOI":"10.15252\/embj.201592337","type":"journal-article","article-title":"Disruption of the autoinhibited state primes the E3 ligase parkin for activation and catalysis","volume":"34","author":"Kumar","year":"2015","journal-title":"The EMBO Journal"},{"key":"bib21","doi-asserted-by":"publisher","first-page":"475","DOI":"10.1038\/nsmb.3400","type":"journal-article","article-title":"Parkin-phosphoubiquitin complex reveals cryptic ubiquitin-binding site required for RBR ligase activity","volume":"24","author":"Kumar","year":"2017","journal-title":"Nature Structural & Molecular Biology"},{"key":"bib22","doi-asserted-by":"publisher","first-page":"1062","DOI":"10.1002\/jcb.26274","type":"journal-article","article-title":"Differential expression of PARK2 splice isoforms in an in vitro model of dopaminergic-like neurons exposed to toxic insults mimicking parkinson\u2019s disease","volume":"119","author":"La Cognata","year":"2018","journal-title":"Journal of Cellular Biochemistry"},{"key":"bib23","doi-asserted-by":"publisher","first-page":"163","DOI":"10.1083\/jcb.201210111","type":"journal-article","article-title":"PINK1 drives parkin self-association and HECT-like E3 activity upstream of mitochondrial binding","volume":"200","author":"Lazarou","year":"2013","journal-title":"The Journal of Cell Biology"},{"key":"bib24","doi-asserted-by":"publisher","first-page":"546","DOI":"10.1038\/nature16511","type":"journal-article","article-title":"Structure of a HOIP\/E2~ubiquitin complex reveals RBR E3 ligase mechanism and regulation","volume":"529","author":"Lechtenberg","year":"2016","journal-title":"Nature"},{"key":"bib25","doi-asserted-by":"publisher","DOI":"10.1101\/2023.11.21.568018","type":"journal-article","article-title":"Intricate mechanism (s) of substrate specificity and loss of function on disease mutation (k211n) of parkin","volume":"01","author":"Lenka","year":"2023","journal-title":"Biochemistry"},{"key":"bib26","doi-asserted-by":"publisher","first-page":"301","DOI":"10.1146\/annurev-genom-082410-101440","type":"journal-article","article-title":"Recent advances in the genetics of parkinson\u2019s disease","volume":"12","author":"Martin","year":"2011","journal-title":"Annual Review of Genomics and Human Genetics"},{"key":"bib27","doi-asserted-by":"publisher","DOI":"10.1098\/rsob.180108","type":"journal-article","article-title":"Phosphorylation of parkin at serine 65 is essential for its activation in vivo","volume":"8","author":"McWilliams","year":"2018","journal-title":"Open Biology"},{"key":"bib28","doi-asserted-by":"publisher","first-page":"679","DOI":"10.1038\/s41592-022-01488-1","type":"journal-article","article-title":"ColabFold: making protein folding accessible to all","volume":"19","author":"Mirdita","year":"2022","journal-title":"Nature Methods"},{"key":"bib29","doi-asserted-by":"publisher","first-page":"355","DOI":"10.1107\/S0907444911001314","type":"journal-article","article-title":"REFMAC5 for the refinement of macromolecular crystal structures","volume":"67","author":"Murshudov","year":"2011","journal-title":"Acta Crystallographica. Section D, Biological Crystallography"},{"key":"bib30","doi-asserted-by":"publisher","DOI":"10.1101\/cshperspect.a011338","type":"journal-article","article-title":"Mitochondrial quality control mediated by PINK1 and parkin: links to parkinsonism","volume":"4","author":"Narendra","year":"2012","journal-title":"Cold Spring Harbor Perspectives in Biology"},{"key":"bib31","doi-asserted-by":"publisher","first-page":"360","DOI":"10.1016\/j.molcel.2014.09.007","type":"journal-article","article-title":"Quantitative proteomics reveal a feedforward mechanism for mitochondrial PARKIN translocation and ubiquitin chain synthesis","volume":"56","author":"Ordureau","year":"2014","journal-title":"Molecular Cell"},{"key":"bib32","doi-asserted-by":"publisher","DOI":"10.1038\/ncomms2982","type":"journal-article","article-title":"Structure and function of Parkin E3 ubiquitin ligase reveals aspects of RING and HECT ligases","volume":"4","author":"Riley","year":"2013","journal-title":"Nature Communications"},{"key":"bib33","doi-asserted-by":"publisher","first-page":"2492","DOI":"10.15252\/embj.201592237","type":"journal-article","article-title":"A Ubl\/ubiquitin switch in the activation of Parkin","volume":"34","author":"Sauv\u00e9","year":"2015","journal-title":"The EMBO Journal"},{"key":"bib34","doi-asserted-by":"publisher","first-page":"623","DOI":"10.1038\/s41594-018-0088-7","type":"journal-article","article-title":"Mechanism of parkin activation by phosphorylation","volume":"25","author":"Sauv\u00e9","year":"2018","journal-title":"Nature Structural & Molecular Biology"},{"key":"bib35","doi-asserted-by":"publisher","first-page":"51","DOI":"10.1038\/nature24645","type":"journal-article","article-title":"Structure of PINK1 in complex with its substrate ubiquitin","volume":"552","author":"Schubert","year":"2017","journal-title":"Nature"},{"key":"bib36","doi-asserted-by":"publisher","DOI":"10.1155\/2014\/690796","type":"journal-article","article-title":"Alternative splicing generates different parkin protein isoforms: evidences in human, rat, and mouse brain","volume":"2014","author":"Scuderi","year":"2014","journal-title":"BioMed Research International"},{"key":"bib37","doi-asserted-by":"publisher","DOI":"10.1038\/srep01002","type":"journal-article","article-title":"PINK1-mediated phosphorylation of the parkin ubiquitin-like domain primes mitochondrial translocation of parkin and regulates mitophagy","volume":"2","author":"Shiba-Fukushima","year":"2012","journal-title":"Scientific Reports"},{"key":"bib38","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pgen.1004861","type":"journal-article","article-title":"Phosphorylation of mitochondrial polyubiquitin by PINK1 promotes parkin mitochondrial tethering","volume":"10","author":"Shiba-Fukushima","year":"2014","journal-title":"PLOS Genetics"},{"key":"bib39","doi-asserted-by":"publisher","first-page":"421","DOI":"10.1042\/BJ20140006","type":"journal-article","article-title":"RBR E3 ubiquitin ligases: new structures, new insights, new questions","volume":"458","author":"Spratt","year":"2014","journal-title":"The Biochemical Journal"},{"key":"bib40","doi-asserted-by":"publisher","first-page":"1367","DOI":"10.1083\/jcb.201007013","type":"journal-article","article-title":"Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by parkin","volume":"191","author":"Tanaka","year":"2010","journal-title":"The Journal of Cell Biology"},{"key":"bib41","doi-asserted-by":"publisher","DOI":"10.1038\/ncomms14697","type":"journal-article","article-title":"Structure-guided mutagenesis reveals a hierarchical mechanism of parkin activation","volume":"8","author":"Tang","year":"2017","journal-title":"Nature Communications"},{"key":"bib42","doi-asserted-by":"publisher","first-page":"1451","DOI":"10.1126\/science.1237908","type":"journal-article","article-title":"Structure of parkin reveals mechanisms for ubiquitin ligase activation","volume":"340","author":"Trempe","year":"2013","journal-title":"Science"},{"key":"bib43","doi-asserted-by":"publisher","first-page":"1158","DOI":"10.1126\/science.1096284","type":"journal-article","article-title":"Hereditary early-onset parkinson\u2019s disease caused by mutations in PINK1","volume":"304","author":"Valente","year":"2004","journal-title":"Science"},{"key":"bib44","doi-asserted-by":"publisher","first-page":"440","DOI":"10.1038\/s41594-018-0063-3","type":"journal-article","article-title":"RBR ligase-mediated ubiquitin transfer: a tale with many twists and turns","volume":"25","author":"Walden","year":"2018","journal-title":"Nature Structural & Molecular Biology"},{"key":"bib45","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-023-35871-z","type":"journal-article","article-title":"The unifying catalytic mechanism of the RING-between-RING E3 ubiquitin ligase family","volume":"14","author":"Wang","year":"2023","journal-title":"Nature Communications"},{"key":"bib46","doi-asserted-by":"publisher","first-page":"2099","DOI":"10.1038\/emboj.2013.125","type":"journal-article","article-title":"Structure of the human Parkin ligase domain in an autoinhibited state","volume":"32","author":"Wauer","year":"2013","journal-title":"The EMBO Journal"},{"key":"bib47","doi-asserted-by":"publisher","first-page":"370","DOI":"10.1038\/nature14879","type":"journal-article","article-title":"Mechanism of phospho-ubiquitin-induced PARKIN activation","volume":"524","author":"Wauer","year":"2015","journal-title":"Nature"},{"key":"bib48","doi-asserted-by":"publisher","first-page":"105","DOI":"10.1038\/nature09966","type":"journal-article","article-title":"UBCH7 reactivity profile reveals parkin and HHARI to be RING\/HECT hybrids","volume":"474","author":"Wenzel","year":"2011","journal-title":"Nature"},{"key":"bib49","doi-asserted-by":"publisher","DOI":"10.1038\/cddis.2016.396","type":"journal-article","article-title":"PINK1-dependent phosphorylation of PINK1 and parkin is essential for mitochondrial quality control","volume":"7","author":"Zhuang","year":"2016","journal-title":"Cell Death & Disease"},{"key":"dataset1","type":"dataset","article-title":"Crystal Structure","volume-title":"RCSB Protein Data Bank","author":"Lenka et al.","year":"2024","unstructured":"Lenka et al. 2024. Crystal Structure. RCSB Protein Data Bank. https:\/\/www.rcsb.org\/search?request=8IKM. 8IKM."},{"key":"dataset2","type":"dataset","article-title":"Crystal Structure","volume-title":"RCSB Protein Data Bank","author":"Lenka","year":"2024","unstructured":"Lenka DR, Kumar A. 2024. Crystal Structure. RCSB Protein Data Bank. https:\/\/www.rcsb.org\/search?request=8IK6. 8IK6."},{"key":"dataset3","type":"dataset","article-title":"Crystal Structure","volume-title":"RCSB Protein Data Bank","author":"Lenka","year":"2024","unstructured":"Lenka DR, Kumar A. 2024. Crystal Structure. RCSB Protein Data Bank. https:\/\/www.rcsb.org\/search?request=8JWV. 8JWV."},{"key":"dataset4","type":"dataset","article-title":"Crystal Structure","volume-title":"RCSB Protein Data Bank","author":"Lenka","year":"2024","unstructured":"Lenka DR, Kumar A. 2024. Crystal Structure. RCSB Protein Data Bank. https:\/\/www.rcsb.org\/search?request=8IKT. 8IKT."},{"key":"dataset5","type":"dataset","article-title":"Crystal Structure","volume-title":"RCSB Protein Data Bank","author":"Lenka","year":"2024","unstructured":"Lenka DR, Kumar A. 2024. Crystal Structure. RCSB Protein Data Bank. https:\/\/www.rcsb.org\/search?request=8IKV. 8IKV."}],"container-title":["eLife"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/cdn.elifesciences.org\/articles\/96699\/elife-96699-v1.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/cdn.elifesciences.org\/articles\/96699\/elife-96699-v1.xml","content-type":"application\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/elifesciences.org\/articles\/96699","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,8,24]],"date-time":"2026-08-24T10:14:50Z","timestamp":1787566490000},"score":1,"resource":{"primary":{"URL":"https:\/\/elifesciences.org\/articles\/96699"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,9,2]]},"references-count":54,"alternative-id":["10.7554\/eLife.96699"],"URL":"https:\/\/doi.org\/10.7554\/elife.96699","archive":["CLOCKSS"],"relation":{"has-preprint":[{"id-type":"doi","id":"10.21203\/rs.3.rs-2859540\/v4","asserted-by":"subject"}],"is-same-as":[{"id-type":"doi","id":"10.7554\/eLife.96699.3","asserted-by":"subject"}],"is-version-of":[{"id-type":"doi","id":"10.7554\/eLife.96699.1","asserted-by":"subject"},{"id-type":"doi","id":"10.7554\/eLife.96699.2","asserted-by":"subject"}],"is-financed-by":[{"id-type":"doi","id":"10.35802\/210753","asserted-by":"subject"},{"id-type":"doi","id":"10.35802\/210753","asserted-by":"object"}],"is-supplemented-by":[{"id-type":"accession","id":"8IKM","asserted-by":"subject"},{"id-type":"accession","id":"8IK6","asserted-by":"subject"},{"id-type":"accession","id":"8JWV","asserted-by":"subject"},{"id-type":"accession","id":"8IKT","asserted-by":"subject"},{"id-type":"accession","id":"8IKV","asserted-by":"subject"}]},"ISSN":["2050-084X"],"issn-type":[{"value":"2050-084X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,9,2]]},"assertion":[{"value":"single anonymised","name":"peer_review_transparency","label":"Peer review transparency","group":{"name":"peer_review_taxonomy"}},{"value":"other reviewer(s), editor","name":"peer_review_interaction","label":"Peer review interaction","group":{"name":"peer_review_taxonomy"}},{"value":"review summaries, review reports, author\/editor communication, reviewer identities reviewer opt in, editor identities","name":"peer_review_published","label":"Peer review published","group":{"name":"peer_review_taxonomy"}},{"value":"open (sign in with ORCID iD required)","name":"post_publication_commenting","label":"Post publication commenting","group":{"name":"post_publication_commenting"}}],"article-number":"RP96699"}}