{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T02:15:09Z","timestamp":1790734509722,"version":"4.1.0"},"reference-count":64,"publisher":"Elsevier BV","issue":"6","license":[{"start":{"date-parts":[[2016,12,1]],"date-time":"2016-12-01T00:00:00Z","timestamp":1480550400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2017,12,1]],"date-time":"2017-12-01T00:00:00Z","timestamp":1512086400000},"content-version":"vor","delay-in-days":365,"URL":"https:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"content-domain":{"domain":["cell.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Cell"],"published-print":{"date-parts":[[2016,12]]},"DOI":"10.1016\/j.cell.2016.11.019","type":"journal-article","created":{"date-parts":[[2016,12,1]],"date-time":"2016-12-01T15:20:06Z","timestamp":1480605606000},"page":"1636-1649.e13","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":321,"title":["Phosphoribosylation of Ubiquitin Promotes Serine Ubiquitination and Impairs Conventional Ubiquitination"],"prefix":"10.1016","volume":"167","author":[{"given":"Sagar","family":"Bhogaraju","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sissy","family":"Kalayil","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yaobin","family":"Liu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Florian","family":"Bonn","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thomas","family":"Colby","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ivan","family":"Matic","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ivan","family":"Dikic","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.cell.2016.11.019_bib1","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1107\/S0907444909052925","article-title":"PHENIX: a comprehensive Python-based system for macromolecular structure solution","volume":"66","author":"Adams","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"issue":"W1","key":"10.1016\/j.cell.2016.11.019_bib2","doi-asserted-by":"crossref","first-page":"W410","DOI":"10.1093\/nar\/gkw348","article-title":"The MPI bioinformatics Toolkit as an integrative platform for advanced protein sequence and structure analysis","volume":"44","author":"Alva","year":"2016","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.cell.2016.11.019_bib3","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1111\/j.1365-2958.2005.04539.x","article-title":"IcmS-dependent translocation of SdeA into macrophages by the Legionella pneumophila type IV secretion system","volume":"56","author":"Bardill","year":"2005","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.cell.2016.11.019_bib4","doi-asserted-by":"crossref","first-page":"7300","DOI":"10.1021\/bi00189a035","article-title":"Site-directed mutagenesis of ubiquitin. Differential roles for arginine in the interaction with ubiquitin-activating enzyme","volume":"33","author":"Burch","year":"1994","journal-title":"Biochemistry"},{"key":"10.1016\/j.cell.2016.11.019_bib5","doi-asserted-by":"crossref","first-page":"1100","DOI":"10.1016\/0006-291X(78)91249-4","article-title":"A heat-stable polypeptide component of an ATP-dependent proteolytic system from reticulocytes","volume":"81","author":"Ciehanover","year":"1978","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.cell.2016.11.019_bib6","doi-asserted-by":"crossref","first-page":"1367","DOI":"10.1038\/nbt.1511","article-title":"MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification","volume":"26","author":"Cox","year":"2008","journal-title":"Nat. Biotechnol."},{"key":"10.1016\/j.cell.2016.11.019_bib7","doi-asserted-by":"crossref","first-page":"1215","DOI":"10.1126\/science.1193844","article-title":"Glutamine deamidation and dysfunction of ubiquitin\/NEDD8 induced by a bacterial effector family","volume":"329","author":"Cui","year":"2010","journal-title":"Science"},{"key":"10.1016\/j.cell.2016.11.019_bib8","doi-asserted-by":"crossref","first-page":"3510","DOI":"10.1021\/pr401032q","article-title":"Phosphoproteomic approach to characterize protein mono- and poly(ADP-ribosyl)ation sites from cells","volume":"13","author":"Daniels","year":"2014","journal-title":"J.\u00a0Proteome Res."},{"key":"10.1016\/j.cell.2016.11.019_bib9","doi-asserted-by":"crossref","first-page":"911","DOI":"10.1016\/j.molcel.2015.06.012","article-title":"The promise of proteomics for the study of ADP-ribosylation","volume":"58","author":"Daniels","year":"2015","journal-title":"Mol. Cell"},{"key":"10.1016\/j.cell.2016.11.019_bib10","doi-asserted-by":"crossref","first-page":"18271","DOI":"10.1038\/srep18271","article-title":"Nudix hydrolases degrade protein-conjugated ADP-ribose","volume":"5","author":"Daniels","year":"2015","journal-title":"Sci. Rep."},{"key":"10.1016\/j.cell.2016.11.019_bib11","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1083\/jcb.200510071","article-title":"A\u00a0dynamic ubiquitin equilibrium couples proteasomal activity to chromatin remodeling","volume":"173","author":"Dantuma","year":"2006","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1016\/j.cell.2016.11.019_bib12","doi-asserted-by":"crossref","DOI":"10.1101\/cshperspect.a016865","article-title":"Endocytosis, signaling, and beyond","volume":"6","author":"Di Fiore","year":"2014","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"10.1016\/j.cell.2016.11.019_bib13","doi-asserted-by":"crossref","first-page":"6980","DOI":"10.1021\/bi00396a019","article-title":"Structure and function of ubiquitin: evidence for differential interactions of arginine-74 with the activating enzyme and the proteases of ATP-dependent proteolysis","volume":"26","author":"Duerksen-Hughes","year":"1987","journal-title":"Biochemistry"},{"key":"10.1016\/j.cell.2016.11.019_bib14","doi-asserted-by":"crossref","first-page":"2126","DOI":"10.1107\/S0907444904019158","article-title":"Coot: model-building tools for molecular graphics","volume":"60","author":"Emsley","year":"2004","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.cell.2016.11.019_bib15","doi-asserted-by":"crossref","first-page":"3905","DOI":"10.1128\/IAI.00344-10","article-title":"E3 ubiquitin ligase activity and targeting of BAT3 by multiple Legionella pneumophila translocated substrates","volume":"78","author":"Ensminger","year":"2010","journal-title":"Infect. Immun."},{"key":"10.1016\/j.cell.2016.11.019_bib16","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1146\/annurev.biochem.78.081507.101607","article-title":"Recognition and processing of ubiquitin-protein conjugates by the proteasome","volume":"78","author":"Finley","year":"2009","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.cell.2016.11.019_bib17","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1038\/ncb2012","article-title":"PINK1\/Parkin-mediated mitophagy is dependent on VDAC1 and p62\/SQSTM1","volume":"12","author":"Geisler","year":"2010","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.cell.2016.11.019_bib18","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1007\/s13361-011-0261-2","article-title":"StavroX--a software for analyzing crosslinked products in protein interaction studies","volume":"23","author":"G\u00f6tze","year":"2012","journal-title":"J.\u00a0Am. Soc. Mass Spectrom."},{"key":"10.1016\/j.cell.2016.11.019_bib19","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1038\/nrm3099","article-title":"The spatial and temporal organization of ubiquitin networks","volume":"12","author":"Grabbe","year":"2011","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.cell.2016.11.019_bib20","doi-asserted-by":"crossref","first-page":"3506","DOI":"10.1128\/IAI.00497-15","article-title":"Toxicity and SidJ-mediated suppression of\u00a0toxicity require distinct regions in the SidE family of Legionella pneumophila effectors","volume":"83","author":"Havey","year":"2015","journal-title":"Infect. Immun."},{"key":"10.1016\/j.cell.2016.11.019_bib21","doi-asserted-by":"crossref","first-page":"1071","DOI":"10.15252\/embr.201540891","article-title":"Expanding the ubiquitin code through post-translational modification","volume":"16","author":"Herhaus","year":"2015","journal-title":"EMBO Rep."},{"key":"10.1016\/j.cell.2016.11.019_bib22","doi-asserted-by":"crossref","first-page":"1073","DOI":"10.1038\/80384","article-title":"The ubiquitin system","volume":"6","author":"Hershko","year":"2000","journal-title":"Nat. Med."},{"key":"10.1016\/j.cell.2016.11.019_bib23","doi-asserted-by":"crossref","first-page":"316","DOI":"10.1038\/nrmicro3009","article-title":"Exploitation of eukaryotic subcellular targeting mechanisms by bacterial effectors","volume":"11","author":"Hicks","year":"2013","journal-title":"Nat. Rev. Microbiol."},{"key":"10.1016\/j.cell.2016.11.019_bib24","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1038\/nsmb.2547","article-title":"Assembly, analysis and architecture of atypical ubiquitin chains","volume":"20","author":"Hospenthal","year":"2013","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.cell.2016.11.019_bib25","doi-asserted-by":"crossref","first-page":"10538","DOI":"10.1073\/pnas.1402605111","article-title":"The Legionella effector SidC defines a unique family of ubiquitin ligases important for bacterial phagosomal remodeling","volume":"111","author":"Hsu","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.cell.2016.11.019_bib26","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1146\/annurev-cellbio-100109-104034","article-title":"Modulation of host cell function by Legionella pneumophila type IV effectors","volume":"26","author":"Hubber","year":"2010","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"10.1016\/j.cell.2016.11.019_bib27","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1146\/annurev-biochem-051810-094654","article-title":"Ubiquitin-binding proteins: decoders of ubiquitin-mediated cellular functions","volume":"81","author":"Husnjak","year":"2012","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.cell.2016.11.019_bib28","doi-asserted-by":"crossref","first-page":"e1004695","DOI":"10.1371\/journal.ppat.1004695","article-title":"Spatiotemporal regulation of a Legionella pneumophila T4SS substrate by the metaeffector SidJ","volume":"11","author":"Jeong","year":"2015","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.cell.2016.11.019_bib29","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1107\/S0907444909047337","article-title":"XDS","volume":"66","author":"Kabsch","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.cell.2016.11.019_bib30","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1042\/BJ20140334","article-title":"Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser65","volume":"460","author":"Kazlauskaite","year":"2014","journal-title":"Biochem. J."},{"key":"10.1016\/j.cell.2016.11.019_bib31","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/S0959-437X(02)00010-2","article-title":"The von Hippel-Lindau tumor suppressor protein: new insights into oxygen sensing and cancer","volume":"13","author":"Kim","year":"2003","journal-title":"Curr. Opin. Genet. Dev."},{"key":"10.1016\/j.cell.2016.11.019_bib32","doi-asserted-by":"crossref","first-page":"1307","DOI":"10.1111\/j.1365-2958.2008.06124.x","article-title":"Legionella translocates an E3 ubiquitin ligase that has multiple U-boxes with distinct functions","volume":"67","author":"Kubori","year":"2008","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.cell.2016.11.019_bib33","doi-asserted-by":"crossref","first-page":"268","DOI":"10.1016\/j.cell.2008.05.046","article-title":"Structural insights into E1-catalyzed ubiquitin activation and transfer to conjugating enzymes","volume":"134","author":"Lee","year":"2008","journal-title":"Cell"},{"key":"10.1016\/j.cell.2016.11.019_bib34","doi-asserted-by":"crossref","DOI":"10.1038\/nchembio.2180","article-title":"Serine is a new target residue for endogenous ADP-ribosylation on histones","author":"Leidecker","year":"2016","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.cell.2016.11.019_bib35","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1111\/j.1365-2958.2009.06751.x","article-title":"Bacterial type IV secretion systems in human disease","volume":"73","author":"Llosa","year":"2009","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.cell.2016.11.019_bib36","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1038\/cr.2016.30","article-title":"Bacteria-host relationship: ubiquitin ligases as weapons of invasion","volume":"26","author":"Maculins","year":"2016","journal-title":"Cell Res."},{"key":"10.1016\/j.cell.2016.11.019_bib37","doi-asserted-by":"crossref","first-page":"771","DOI":"10.1038\/nmeth.2106","article-title":"Reanalysis of phosphoproteomics data uncovers ADP-ribosylation sites","volume":"9","author":"Matic","year":"2012","journal-title":"Nat. Methods"},{"key":"10.1016\/j.cell.2016.11.019_bib38","doi-asserted-by":"crossref","first-page":"795","DOI":"10.1083\/jcb.200809125","article-title":"Parkin is recruited selectively to impaired mitochondria and promotes their autophagy","volume":"183","author":"Narendra","year":"2008","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1016\/j.cell.2016.11.019_bib39","doi-asserted-by":"crossref","DOI":"10.1101\/cshperspect.a006049","article-title":"Signaling in innate immunity and inflammation","volume":"4","author":"Newton","year":"2012","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"10.1016\/j.cell.2016.11.019_bib40","doi-asserted-by":"crossref","first-page":"360","DOI":"10.1016\/j.molcel.2014.09.007","article-title":"Quantitative proteomics reveal a feedforward mechanism for mitochondrial PARKIN translocation and ubiquitin chain synthesis","volume":"56","author":"Ordureau","year":"2014","journal-title":"Mol. Cell"},{"key":"10.1016\/j.cell.2016.11.019_bib41","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1042\/BJ20141554","article-title":"Processing of protein ADP-ribosylation by Nudix hydrolases","volume":"468","author":"Palazzo","year":"2015","journal-title":"Biochem. J."},{"key":"10.1016\/j.cell.2016.11.019_bib42","doi-asserted-by":"crossref","first-page":"3371","DOI":"10.1111\/febs.13811","article-title":"ENPP1 processes protein ADP-ribosylation in\u00a0vitro","volume":"283","author":"Palazzo","year":"2016","journal-title":"FEBS J."},{"key":"10.1016\/j.cell.2016.11.019_bib43","doi-asserted-by":"crossref","first-page":"1553","DOI":"10.1126\/science.1212868","article-title":"Host proteasomal degradation generates amino acids essential for intracellular bacterial growth","volume":"334","author":"Price","year":"2011","journal-title":"Science"},{"key":"10.1016\/j.cell.2016.11.019_bib44","doi-asserted-by":"crossref","first-page":"284","DOI":"10.1016\/j.molcel.2016.03.035","article-title":"Enhanced efflux activity facilitates drug tolerance in dormant bacterial cells","volume":"62","author":"Pu","year":"2016","journal-title":"Mol. Cell"},{"key":"10.1016\/j.cell.2016.11.019_bib45","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1038\/nature17657","article-title":"Ubiquitination independent of E1 and E2 enzymes by bacterial effectors","volume":"533","author":"Qiu","year":"2016","journal-title":"Nature"},{"key":"10.1016\/j.cell.2016.11.019_bib46","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1016\/j.micinf.2015.01.004","article-title":"How bacterial pathogens colonize their hosts and invade deeper tissues","volume":"17","author":"Ribet","year":"2015","journal-title":"Microbes Infect."},{"key":"10.1016\/j.cell.2016.11.019_bib47","doi-asserted-by":"crossref","first-page":"4039","DOI":"10.1073\/pnas.1523926113","article-title":"Phosphorylation of OPTN by TBK1 enhances its binding to Ub chains and promotes selective autophagy of damaged mitochondria","volume":"113","author":"Richter","year":"2016","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.cell.2016.11.019_bib48","doi-asserted-by":"crossref","first-page":"1525","DOI":"10.1128\/JB.02606-14","article-title":"Structural basis of functional diversification of the HD-GYP domain revealed by the Pseudomonas aeruginosa PA4781 protein, which displays an unselective bimetallic binding site","volume":"197","author":"Rinaldo","year":"2015","journal-title":"J.\u00a0Bacteriol."},{"key":"10.1016\/j.cell.2016.11.019_bib49","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1016\/j.molcel.2013.12.014","article-title":"Interactions between autophagy receptors and ubiquitin-like proteins form the molecular basis for selective autophagy","volume":"53","author":"Rogov","year":"2014","journal-title":"Mol. Cell"},{"key":"10.1016\/j.cell.2016.11.019_bib50","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/j.molcel.2011.03.016","article-title":"Essential role for ubiquitin-ubiquitin-conjugating enzyme interaction in ubiquitin discharge from Cdc34 to substrate","volume":"42","author":"Saha","year":"2011","journal-title":"Mol. Cell"},{"key":"10.1016\/j.cell.2016.11.019_bib51","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1196\/annals.1326.025","article-title":"The bacterial weaponry: lessons from Shigella","volume":"1072","author":"Sansonetti","year":"2006","journal-title":"Ann. N Y Acad. Sci."},{"key":"10.1016\/j.cell.2016.11.019_bib52","doi-asserted-by":"crossref","first-page":"15090","DOI":"10.1073\/pnas.1514568112","article-title":"Structural basis of substrate recognition by a bacterial deubiquitinase important for\u00a0dynamics of phagosome ubiquitination","volume":"112","author":"Sheedlo","year":"2015","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.cell.2016.11.019_bib53","doi-asserted-by":"crossref","first-page":"W244","DOI":"10.1093\/nar\/gki408","article-title":"The HHpred interactive server for protein homology detection and structure prediction","volume":"33","author":"S\u00f6ding","year":"2005","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.cell.2016.11.019_bib54","doi-asserted-by":"crossref","first-page":"432","DOI":"10.1107\/S0907444903028956","article-title":"Likelihood-enhanced fast rotation functions","volume":"60","author":"Storoni","year":"2004","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.cell.2016.11.019_bib55","doi-asserted-by":"crossref","first-page":"479","DOI":"10.1038\/nrm2921","article-title":"Ubiquitin signalling in DNA replication and repair","volume":"11","author":"Ulrich","year":"2010","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.cell.2016.11.019_bib56","doi-asserted-by":"crossref","first-page":"21244","DOI":"10.1074\/jbc.R115.675165","article-title":"Regulating the regulators: recent revelations in the control of E3 ubiquitin ligases","volume":"290","author":"Vittal","year":"2015","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.cell.2016.11.019_bib57","doi-asserted-by":"crossref","DOI":"10.1093\/nar\/gkw880","article-title":"2016 update of the PRIDE database and its related tools","author":"Vizca\u00edno","year":"2016","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.cell.2016.11.019_bib58","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1111\/j.1600-0854.2011.01269.x","article-title":"Ubiquitination of substrates by esterification","volume":"13","author":"Wang","year":"2012","journal-title":"Traffic"},{"key":"10.1016\/j.cell.2016.11.019_bib59","doi-asserted-by":"crossref","first-page":"1377","DOI":"10.1021\/pr301024c","article-title":"A proteomics search algorithm specifically designed for high-resolution tandem mass spectra","volume":"12","author":"Wenger","year":"2013","journal-title":"J.\u00a0Proteome Res."},{"key":"10.1016\/j.cell.2016.11.019_bib60","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1107\/S0907444910045749","article-title":"Overview of the CCP4 suite and current developments","volume":"67","author":"Winn","year":"2011","journal-title":"Acta Crystallogr. Sect. D Biol. Crystallogr."},{"key":"10.1016\/j.cell.2016.11.019_bib61","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1038\/nmeth.1322","article-title":"Universal sample preparation method for proteome analysis","volume":"6","author":"Wi\u015bniewski","year":"2009","journal-title":"Nat. Methods"},{"key":"10.1016\/j.cell.2016.11.019_bib62","doi-asserted-by":"crossref","first-page":"24727","DOI":"10.1074\/jbc.M115.671263","article-title":"Structure of the Legionella effector, lpg1496, suggests a role in nucleotide metabolism","volume":"290","author":"Wong","year":"2015","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.cell.2016.11.019_bib63","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1016\/j.micinf.2012.11.001","article-title":"Cell biology of infection by Legionella pneumophila","volume":"15","author":"Xu","year":"2013","journal-title":"Microbes Infect."},{"key":"10.1016\/j.cell.2016.11.019_bib64","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1038\/ncb3358","article-title":"The increasing complexity of the ubiquitin code","volume":"18","author":"Yau","year":"2016","journal-title":"Nat. Cell Biol."}],"container-title":["Cell"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0092867416315914?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0092867416315914?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2018,9,6]],"date-time":"2018-09-06T03:51:57Z","timestamp":1536205917000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0092867416315914"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,12]]},"references-count":64,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2016,12]]}},"alternative-id":["S0092867416315914"],"URL":"https:\/\/doi.org\/10.1016\/j.cell.2016.11.019","relation":{"has-review":[{"id-type":"doi","id":"10.3410\/f.727060495.793537411","asserted-by":"object"}]},"ISSN":["0092-8674"],"issn-type":[{"value":"0092-8674","type":"print"}],"subject":[],"published":{"date-parts":[[2016,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Phosphoribosylation of Ubiquitin Promotes Serine Ubiquitination and Impairs Conventional Ubiquitination","name":"articletitle","label":"Article Title"},{"value":"Cell","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.cell.2016.11.019","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2016 Elsevier Inc.","name":"copyright","label":"Copyright"}]}}