{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,29]],"date-time":"2026-10-29T18:21:49Z","timestamp":1793298109564,"version":"4.5.0"},"reference-count":62,"publisher":"Elsevier BV","issue":"42","license":[{"start":{"date-parts":[[2015,10,1]],"date-time":"2015-10-01T00:00:00Z","timestamp":1443657600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,9,6]],"date-time":"2020-09-06T00:00:00Z","timestamp":1599350400000},"content-version":"vor","delay-in-days":1802,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2015,10]]},"DOI":"10.1074\/jbc.m115.637397","type":"journal-article","created":{"date-parts":[[2015,9,2]],"date-time":"2015-09-02T23:58:04Z","timestamp":1441238284000},"page":"25766-25781","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":66,"title":["Host Cell-catalyzed S-Palmitoylation Mediates Golgi Targeting of the Legionella Ubiquitin Ligase GobX"],"prefix":"10.1016","volume":"290","author":[{"given":"Yi-Han","family":"Lin","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alexandra G.","family":"Doms","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eric","family":"Cheng","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Byoungkwan","family":"Kim","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Timothy R.","family":"Evans","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Matthias P.","family":"Machner","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.M115.637397_bib1","doi-asserted-by":"crossref","first-page":"241","DOI":"10.2217\/fmb.11.150","article-title":"Bacterial Type IV secretion systems: versatile virulence machines","volume":"7","author":"Voth","year":"2012","journal-title":"Future Microbiol"},{"key":"10.1074\/jbc.M115.637397_bib2","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":"10.1074\/jbc.M115.637397_bib3","doi-asserted-by":"crossref","first-page":"1870","DOI":"10.1111\/j.1462-5822.2011.01710.x","article-title":"Manipulation of host vesicular trafficking and innate immune defence by Legionella Dot\/Icm effectors","volume":"13","author":"Ge","year":"2011","journal-title":"Cell. Microbiol"},{"key":"10.1074\/jbc.M115.637397_bib4","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1016\/j.mib.2008.12.004","article-title":"Legionella pneumophila Dot\/Icm translocated substrates: a sum of parts","volume":"12","author":"Ensminger","year":"2009","journal-title":"Curr. Opin. Microbiol"},{"key":"10.1074\/jbc.M115.637397_bib5","doi-asserted-by":"crossref","first-page":"14733","DOI":"10.1073\/pnas.1111678108","article-title":"Minimization of the Legionella pneumophila genome reveals chromosomal regions involved in host range expansion","volume":"108","author":"O'Connor","year":"2011","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M115.637397_bib6","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1111\/j.1365-2958.1993.tb01092.x","article-title":"Two distinct defects in intracellular growth complemented by a single genetic locus in Legionella pneumophila","volume":"7","author":"Berger","year":"1993","journal-title":"Mol. Microbiol"},{"key":"10.1074\/jbc.M115.637397_bib7","doi-asserted-by":"crossref","first-page":"1165","DOI":"10.1038\/ng1447","article-title":"Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity","volume":"36","author":"Cazalet","year":"2004","journal-title":"Nat. Genet"},{"key":"10.1074\/jbc.M115.637397_bib8","doi-asserted-by":"crossref","first-page":"7716","DOI":"10.1128\/JB.187.22.7716-7726.2005","article-title":"Evidence for acquisition of Legionella type IV secretion substrates via interdomain horizontal gene transfer","volume":"187","author":"de Felipe","year":"2005","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.M115.637397_bib9","doi-asserted-by":"crossref","first-page":"33111","DOI":"10.1074\/jbc.M102755200","article-title":"U box proteins as a new family of ubiquitin-protein ligases","volume":"276","author":"Hatakeyama","year":"2001","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M115.637397_bib10","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":"10.1074\/jbc.M115.637397_bib11","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":"10.1074\/jbc.M115.637397_bib12","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":"10.1074\/jbc.M115.637397_bib13","doi-asserted-by":"crossref","first-page":"145","DOI":"10.3389\/fmicb.2011.00145","article-title":"Bacterial effector-involved temporal and spatial regulation by hijack of the host ubiquitin pathway","volume":"2","author":"Kubori","year":"2011","journal-title":"Front. Microbiol"},{"key":"10.1074\/jbc.M115.637397_bib14","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. U.S.A"},{"key":"10.1074\/jbc.M115.637397_bib15","doi-asserted-by":"crossref","first-page":"4846","DOI":"10.1074\/jbc.M807505200","article-title":"Rab1 guanine nucleotide exchange factor SidM is a major phosphatidylinositol 4-phosphate-binding effector protein of Legionella pneumophila","volume":"284","author":"Brombacher","year":"2009","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M115.637397_bib16","doi-asserted-by":"crossref","first-page":"2416","DOI":"10.1111\/j.1462-5822.2008.01219.x","article-title":"The Legionella pneumophila phosphatidylinositol-4 phosphate-binding type IV substrate SidC recruits endoplasmic reticulum vesicles to a replication-permissive vacuole","volume":"10","author":"Ragaz","year":"2008","journal-title":"Cell. Microbiol"},{"key":"10.1074\/jbc.M115.637397_bib17","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1083\/jcb.201312072","article-title":"A novel probe for phosphatidylinositol 4-phosphate reveals multiple pools beyond the Golgi","volume":"205","author":"Hammond","year":"2014","journal-title":"J. Cell Biol"},{"key":"10.1074\/jbc.M115.637397_bib18","doi-asserted-by":"crossref","first-page":"1389","DOI":"10.1128\/JB.06306-11","article-title":"Legionella pneumophila LidA affects nucleotide binding and activity of the host GTPase Rab1","volume":"194","author":"Neunuebel","year":"2012","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.M115.637397_bib19","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1003082","article-title":"VipD of Legionella pneumophila targets activated Rab5 and Rab22 to interfere with endosomal trafficking in macrophages","volume":"8","author":"Ku","year":"2012","journal-title":"PLoS Pathog"},{"key":"10.1074\/jbc.M115.637397_bib20","doi-asserted-by":"crossref","first-page":"4560","DOI":"10.1073\/pnas.1316376111","article-title":"VipD is a Rab5-activated phospholipase A1 that protects Legionella pneumophila from endosomal fusion","volume":"111","author":"Gaspar","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M115.637397_bib21","doi-asserted-by":"crossref","first-page":"E3514","DOI":"10.1073\/pnas.1405391111","article-title":"Structural basis for the recruitment and activation of the Legionella phospholipase VipD by the host GTPase Rab5","volume":"111","author":"Lucas","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M115.637397_bib22","doi-asserted-by":"crossref","first-page":"34686","DOI":"10.1074\/jbc.M110.170746","article-title":"Lipidation by the host prenyltransferase machinery facilitates membrane localization of Legionella pneumophila effector proteins","volume":"285","author":"Ivanov","year":"2010","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M115.637397_bib23","doi-asserted-by":"crossref","first-page":"131","DOI":"10.3389\/fmicb.2010.00131","article-title":"Host-mediated post-translational prenylation of novel Dot\/Icm-translocated effectors of Legionella pneumophila","volume":"1","author":"Price","year":"2010","journal-title":"Front. Microbiol"},{"key":"10.1074\/jbc.M115.637397_bib24","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1016\/j.tibs.2011.01.003","article-title":"DHHC palmitoyltransferases: substrate interactions and (patho)physiology","volume":"36","author":"Greaves","year":"2011","journal-title":"Trends Biochem. Sci"},{"key":"10.1074\/jbc.M115.637397_bib25","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1128\/jcm.10.4.437-441.1979","article-title":"Charcoal-yeast extract agar: primary isolation medium for Legionella pneumophila","volume":"10","author":"Feeley","year":"1979","journal-title":"J. Clin. Microbiol"},{"key":"10.1074\/jbc.M115.637397_bib26","doi-asserted-by":"crossref","first-page":"2947","DOI":"10.1093\/bioinformatics\/btm404","article-title":"Clustal W and Clustal X version 2.0","volume":"23","author":"Larkin","year":"2007","journal-title":"Bioinformatics"},{"key":"10.1074\/jbc.M115.637397_bib27","doi-asserted-by":"crossref","first-page":"841","DOI":"10.1073\/pnas.0304916101","article-title":"Multiple substrates of the Legionella pneumophila Dot\/Icm system identified by interbacterial protein transfer","volume":"101","author":"Luo","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M115.637397_bib28","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1126\/science.1207193","article-title":"De-AMPylation of the small GTPase Rab1 by the pathogen Legionella pneumophila","volume":"333","author":"Neunuebel","year":"2011","journal-title":"Science"},{"key":"10.1074\/jbc.M115.637397_bib29","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1000117","article-title":"Legionella eukaryotic-like type IV substrates interfere with organelle trafficking","volume":"4","author":"de Felipe","year":"2008","journal-title":"PLoS Pathog"},{"key":"10.1074\/jbc.M115.637397_bib30","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1046\/j.1365-2958.2003.03400.x","article-title":"The Legionella pneumophila LidA protein: a translocated substrate of the Dot\/Icm system associated with maintenance of bacterial integrity","volume":"48","author":"Conover","year":"2003","journal-title":"Mol. Microbiol"},{"key":"10.1074\/jbc.M115.637397_bib31","doi-asserted-by":"crossref","DOI":"10.1002\/0471143030.cb0309s10","article-title":"Isolation of Golgi membranes from tissues and cells by differential and density gradient centrifugation","author":"Graham","year":"2001","journal-title":"Curr. Protoc. Cell Biol"},{"key":"10.1074\/jbc.M115.637397_bib32","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/j.devcel.2006.05.013","article-title":"Targeting of host Rab GTPase function by the intravacuolar pathogen Legionella pneumophila","volume":"11","author":"Machner","year":"2006","journal-title":"Dev. Cell"},{"key":"10.1074\/jbc.M115.637397_bib33","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1111\/j.1462-5822.2010.01531.x","article-title":"The E Block motif is associated with Legionella pneumophila translocated substrates","volume":"13","author":"Huang","year":"2011","journal-title":"Cell. Microbiol"},{"key":"10.1074\/jbc.M115.637397_bib34","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":"10.1074\/jbc.M115.637397_bib35","doi-asserted-by":"crossref","first-page":"1912","DOI":"10.1021\/cb400380s","article-title":"Profiling targets of the irreversible palmitoylation inhibitor 2-bromopalmitate","volume":"8","author":"Davda","year":"2013","journal-title":"ACS Chem. Biol"},{"key":"10.1074\/jbc.M115.637397_bib36","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1074\/jbc.275.1.261","article-title":"Inhibition of protein palmitoylation, raft localization, and T cell signaling by 2-bromopalmitate and polyunsaturated fatty acids","volume":"275","author":"Webb","year":"2000","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M115.637397_bib37","doi-asserted-by":"crossref","first-page":"987","DOI":"10.1016\/j.neuron.2004.12.005","article-title":"Identification of PSD-95 palmitoylating enzymes","volume":"44","author":"Fukata","year":"2004","journal-title":"Neuron"},{"key":"10.1074\/jbc.M115.637397_bib38","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/j.cbpa.2012.11.008","article-title":"Emerging roles for protein S-palmitoylation in immunity from chemical proteomics","volume":"17","author":"Yount","year":"2013","journal-title":"Curr. Opin. Chem. Biol"},{"key":"10.1074\/jbc.M115.637397_bib39","doi-asserted-by":"crossref","first-page":"382","DOI":"10.1016\/j.cbpa.2009.07.010","article-title":"Chemical tools for understanding protein lipidation in eukaryotes","volume":"13","author":"Charron","year":"2009","journal-title":"Curr. Opin. Chem. Biol"},{"key":"10.1074\/jbc.M115.637397_bib40","doi-asserted-by":"crossref","first-page":"4967","DOI":"10.1021\/ja810122f","article-title":"Robust fluorescent detection of protein fatty-acylation with chemical reporters","volume":"131","author":"Charron","year":"2009","journal-title":"J. Am. Chem. Soc"},{"key":"10.1074\/jbc.M115.637397_bib41","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1016\/j.cbpa.2012.11.023","article-title":"Profiling and inhibiting reversible palmitoylation","volume":"17","author":"Hernandez","year":"2013","journal-title":"Curr. Opin. Chem. Biol"},{"key":"10.1074\/jbc.M115.637397_bib42","doi-asserted-by":"crossref","first-page":"4007","DOI":"10.1242\/jcs.059287","article-title":"Palmitoylation and depalmitoylation dynamics at a glance","volume":"123","author":"Conibear","year":"2010","journal-title":"J. Cell Sci"},{"key":"10.1074\/jbc.M115.637397_bib43","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1038\/nchembio.362","article-title":"Small-molecule inhibition of APT1 affects Ras localization and signaling","volume":"6","author":"Dekker","year":"2010","journal-title":"Nat. Chem. Biol"},{"key":"10.1074\/jbc.M115.637397_bib44","doi-asserted-by":"crossref","first-page":"4543","DOI":"10.1091\/mbc.e12-05-0336","article-title":"Analysis of substrate specificity of human DHHC protein acyltransferases using a yeast expression system","volume":"23","author":"Ohno","year":"2012","journal-title":"Mol. Biol. Cell"},{"key":"10.1074\/jbc.M115.637397_bib45","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1083\/jcb.200206120","article-title":"The yeast DHHC cysteine-rich domain protein Akr1p is a palmitoyltransferase","volume":"159","author":"Roth","year":"2002","journal-title":"J. Cell Biol"},{"key":"10.1074\/jbc.M115.637397_bib46","doi-asserted-by":"crossref","first-page":"474","DOI":"10.1016\/j.bbalip.2006.03.010","article-title":"Intracellular localization and tissue-specific distribution of human and yeast DHHC cysteine-rich domain-containing proteins","volume":"1761","author":"Ohno","year":"2006","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1074\/jbc.M115.637397_bib47","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1016\/j.chom.2011.06.003","article-title":"Subcellular targeting of Salmonella virulence proteins by host-mediated S-palmitoylation","volume":"10","author":"Hicks","year":"2011","journal-title":"Cell Host Microbe"},{"key":"10.1074\/jbc.M115.637397_bib48","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1038\/nmeth.1293","article-title":"Large-scale profiling of protein palmitoylation in mammalian cells","volume":"6","author":"Martin","year":"2009","journal-title":"Nat. Methods"},{"key":"10.1074\/jbc.M115.637397_bib49","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1038\/nmeth.1769","article-title":"Global profiling of dynamic protein palmitoylation","volume":"9","author":"Martin","year":"2012","journal-title":"Nat. Methods"},{"key":"10.1074\/jbc.M115.637397_bib50","doi-asserted-by":"crossref","first-page":"14620","DOI":"10.1074\/jbc.M500076200","article-title":"A Salmonella typhimurium effector protein SifA is modified by host cell prenylation and S-acylation machinery","volume":"280","author":"Reinicke","year":"2005","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M115.637397_bib51","doi-asserted-by":"crossref","first-page":"15867","DOI":"10.1074\/jbc.M900519200","article-title":"A family of bacterial cysteine protease type III effectors utilizes acylation-dependent and -independent strategies to localize to plasma membranes","volume":"284","author":"Dowen","year":"2009","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M115.637397_bib52","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1016\/S0092-8674(00)80846-6","article-title":"Eukaryotic fatty acylation drives plasma membrane targeting and enhances function of several type III effector proteins from Pseudomonas syringae","volume":"101","author":"Nimchuk","year":"2000","journal-title":"Cell"},{"key":"10.1074\/jbc.M115.637397_bib53","doi-asserted-by":"crossref","DOI":"10.1128\/IAI.00785-15","article-title":"The Legionella pneumophila effector LpdA is a palmitoylated phospholipase D virulence factor","author":"Schroeder","year":"2015","journal-title":"Infect. Immun"},{"key":"10.1074\/jbc.M115.637397_bib54","doi-asserted-by":"crossref","first-page":"584","DOI":"10.1038\/nchembio834","article-title":"Trafficking and signaling by fatty-acylated and prenylated proteins","volume":"2","author":"Resh","year":"2006","journal-title":"Nat. Chem. Biol"},{"key":"10.1074\/jbc.M115.637397_bib55","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0095021","article-title":"Palmitoylation of the immunity related GTPase, Irgm1: impact on membrane localization and ability to promote mitochondrial fission","volume":"9","author":"Henry","year":"2014","journal-title":"PLoS ONE"},{"key":"10.1074\/jbc.M115.637397_bib56","doi-asserted-by":"crossref","DOI":"10.1038\/ncomms4552","article-title":"Molecular insights into the membrane-associated phosphatidylinositol 4-kinase II\u03b1","volume":"5","author":"Zhou","year":"2014","journal-title":"Nat. Commun"},{"key":"10.1074\/jbc.M115.637397_bib57","doi-asserted-by":"crossref","first-page":"971","DOI":"10.1038\/ncb1463","article-title":"The Legionella pneumophila effector protein DrrA is a Rab1 guanine nucleotide-exchange factor","volume":"8","author":"Murata","year":"2006","journal-title":"Nat. Cell Biol"},{"key":"10.1074\/jbc.M115.637397_bib58","doi-asserted-by":"crossref","first-page":"3048","DOI":"10.1128\/IAI.72.5.3048-3053.2004","article-title":"Legionella pneumophila replication vacuole formation involves rapid recruitment of proteins of the early secretory system","volume":"72","author":"Derr\u00e9","year":"2004","journal-title":"Infect. Immun"},{"key":"10.1074\/jbc.M115.637397_bib59","doi-asserted-by":"crossref","first-page":"1201","DOI":"10.1084\/jem.20031706","article-title":"Legionella subvert the functions of Rab1 and Sec22b to create a replicative organelle","volume":"199","author":"Kagan","year":"2004","journal-title":"J. Exp. Med"},{"key":"10.1074\/jbc.M115.637397_bib60","doi-asserted-by":"crossref","first-page":"e46","DOI":"10.1371\/journal.ppat.0020046","article-title":"Legionella pneumophila exploits PI(4)P to anchor secreted effector proteins to the replicative vacuole","volume":"2","author":"Weber","year":"2006","journal-title":"PLoS Pathog"},{"key":"10.1074\/jbc.M115.637397_bib61","doi-asserted-by":"crossref","first-page":"489","DOI":"10.1016\/j.ijmm.2009.03.006","article-title":"Proteomic analysis of Legionella-containing phagosomes isolated from Dictyostelium","volume":"299","author":"Shevchuk","year":"2009","journal-title":"Int. J. Med. Microbiol"},{"key":"10.1074\/jbc.M115.637397_bib62","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1111\/j.1600-0854.2008.00851.x","article-title":"Proteome analysis of Legionella vacuoles purified by magnetic immunoseparation reveals secretory and endosomal GTPases","volume":"10","author":"Urwyler","year":"2009","journal-title":"Traffic"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820445892?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820445892?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.M115.637397","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,12,17]],"date-time":"2021-12-17T01:38:58Z","timestamp":1639705138000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925820445892"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2015,10]]},"references-count":62,"journal-issue":{"issue":"42","published-print":{"date-parts":[[2015,10]]}},"alternative-id":["S0021925820445892"],"URL":"https:\/\/doi.org\/10.1074\/jbc.m115.637397","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2015,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Host Cell-catalyzed S-Palmitoylation Mediates Golgi Targeting of the Legionella Ubiquitin Ligase GobX","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1074\/jbc.M115.637397","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2015 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}]}}