{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,9]],"date-time":"2026-10-09T06:44:22Z","timestamp":1791528262457,"version":"4.3.4"},"reference-count":70,"publisher":"Public Library of Science (PLoS)","issue":"6","license":[{"start":{"date-parts":[[2015,6,12]],"date-time":"2015-06-12T00:00:00Z","timestamp":1434067200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["www.plospathogens.org"],"crossmark-restriction":false},"short-container-title":["PLoS Pathog"],"DOI":"10.1371\/journal.ppat.1004965","type":"journal-article","created":{"date-parts":[[2015,6,12]],"date-time":"2015-06-12T22:33:50Z","timestamp":1434148430000},"page":"e1004965","update-policy":"https:\/\/doi.org\/10.1371\/journal.ppat.corrections_policy","source":"Crossref","is-referenced-by-count":98,"title":["Structure of the Legionella Virulence Factor, SidC Reveals a Unique PI(4)P-Specific Binding Domain Essential for Its Targeting to the Bacterial Phagosome"],"prefix":"10.1371","volume":"11","author":[{"given":"Xi","family":"Luo","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David J.","family":"Wasilko","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yao","family":"Liu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jiayi","family":"Sun","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiaochun","family":"Wu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhao-Qing","family":"Luo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yuxin","family":"Mao","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2015,6,12]]},"reference":[{"key":"ref1","doi-asserted-by":"crossref","first-page":"506","DOI":"10.1128\/CMR.15.3.506-526.2002","article-title":"Legionella and Legionnaires' disease: 25 years of investigation","volume":"15","author":"BS Fields","year":"2002","journal-title":"Clin Microbiol Rev"},{"key":"ref2","doi-asserted-by":"crossref","first-page":"771","DOI":"10.1172\/JCI111493","article-title":"Interaction between the legionnaires' disease bacterium (Legionella pneumophila) and human alveolar macrophages. Influence of antibody, lymphokines, and hydrocortisone","volume":"74","author":"TW Nash","year":"1984","journal-title":"J Clin Invest"},{"key":"ref3","doi-asserted-by":"crossref","first-page":"e17638","DOI":"10.1371\/journal.pone.0017638","article-title":"Comprehensive identification of protein substrates of the Dot\/Icm type IV transporter of Legionella pneumophila","volume":"6","author":"W Zhu","year":"2011","journal-title":"PLoS One"},{"key":"ref4","doi-asserted-by":"crossref","first-page":"1669","DOI":"10.1073\/pnas.95.4.1669","article-title":"Host cell killing and bacterial conjugation require overlapping sets of genes within a 22-kb region of the Legionella pneumophila genome","volume":"95","author":"G Segal","year":"1998","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref5","doi-asserted-by":"crossref","first-page":"873","DOI":"10.1126\/science.279.5352.873","article-title":"Conjugative transfer by the virulence system of Legionella pneumophila","volume":"279","author":"JP Vogel","year":"1998","journal-title":"Science"},{"key":"ref6","doi-asserted-by":"crossref","unstructured":"Asrat S, de Jesus DA, Hempstead AD, Ramabhadran V, Isberg RR (2014) Bacterial Pathogen Manipulation of Host Membrane Trafficking. Annu Rev Cell Dev Biol.","DOI":"10.1146\/annurev-cellbio-100913-013439"},{"key":"ref7","doi-asserted-by":"crossref","first-page":"4637","DOI":"10.1242\/jcs.114.24.4637","article-title":"How the parasitic bacterium Legionella pneumophila modifies its phagosome and transforms it into rough ER: implications for conversion of plasma membrane to the ER membrane","volume":"114","author":"LG Tilney","year":"2001","journal-title":"J Cell Sci"},{"key":"ref8","doi-asserted-by":"crossref","first-page":"3609","DOI":"10.1128\/IAI.63.9.3609-3620.1995","article-title":"Association of Legionella pneumophila with the macrophage endoplasmic reticulum","volume":"63","author":"MS Swanson","year":"1995","journal-title":"Infect Immun"},{"key":"ref9","doi-asserted-by":"crossref","first-page":"945","DOI":"10.1038\/ncb883","article-title":"Legionella phagosomes intercept vesicular traffic from endoplasmic reticulum exit sites","volume":"4","author":"JC Kagan","year":"2002","journal-title":"Nat Cell Biol"},{"key":"ref10","doi-asserted-by":"crossref","first-page":"1319","DOI":"10.1084\/jem.158.4.1319","article-title":"Formation of a novel phagosome by the Legionnaires' disease bacterium (Legionella pneumophila) in human monocytes","volume":"158","author":"MA Horwitz","year":"1983","journal-title":"J Exp Med"},{"key":"ref11","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1038\/nrmicro1967","article-title":"The Legionella pneumophila replication vacuole: making a cosy niche inside host cells","volume":"7","author":"RR Isberg","year":"2009","journal-title":"Nat Rev Microbiol"},{"key":"ref12","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1038\/nrm2728","article-title":"Rab GTPases as coordinators of vesicle traffic","volume":"10","author":"H Stenmark","year":"2009","journal-title":"Nat Rev Mol Cell Biol"},{"key":"ref13","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":"MP Machner","year":"2006","journal-title":"Dev Cell"},{"key":"ref14","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":"T Murata","year":"2006","journal-title":"Nat Cell Biol"},{"key":"ref15","doi-asserted-by":"crossref","first-page":"946","DOI":"10.1126\/science.1192276","article-title":"The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b","volume":"329","author":"MP Muller","year":"2010","journal-title":"Science"},{"key":"ref16","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1038\/nature10335","article-title":"Modulation of Rab GTPase function by a protein phosphocholine transferase","volume":"477","author":"S Mukherjee","year":"2011","journal-title":"Nature"},{"key":"ref17","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":"MR Neunuebel","year":"2011","journal-title":"Science"},{"key":"ref18","doi-asserted-by":"crossref","first-page":"506","DOI":"10.1038\/nature10307","article-title":"Legionella pneumophila SidD is a deAMPylase that modifies Rab1","volume":"475","author":"Y Tan","year":"2011","journal-title":"Nature"},{"key":"ref19","doi-asserted-by":"crossref","first-page":"21212","DOI":"10.1073\/pnas.1114023109","article-title":"Legionella pneumophila regulates the small GTPase Rab1 activity by reversible phosphorylcholination","volume":"108","author":"Y Tan","year":"2011","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref20","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1038\/nature06336","article-title":"Legionella pneumophila proteins that regulate Rab1 membrane cycling","volume":"450","author":"A Ingmundson","year":"2007","journal-title":"Nature"},{"key":"ref21","doi-asserted-by":"crossref","first-page":"256","DOI":"10.1016\/j.chom.2013.08.010","article-title":"A Rab-centric perspective of bacterial pathogen-occupied vacuoles","volume":"14","author":"RK Sherwood","year":"2013","journal-title":"Cell Host Microbe"},{"key":"ref22","doi-asserted-by":"crossref","first-page":"e00839","DOI":"10.1128\/mBio.00839-13","article-title":"Live-cell imaging of phosphoinositide dynamics and membrane architecture during Legionella infection","volume":"5","author":"S Weber","year":"2014","journal-title":"MBio"},{"key":"ref23","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1038\/nature05185","article-title":"Phosphoinositides in cell regulation and membrane dynamics","volume":"443","author":"G Di Paolo","year":"2006","journal-title":"Nature"},{"key":"ref24","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":"SS Weber","year":"2006","journal-title":"PLoS Pathog"},{"key":"ref25","doi-asserted-by":"crossref","first-page":"13567","DOI":"10.1073\/pnas.1207903109","article-title":"Structural basis for substrate recognition by a unique Legionella phosphoinositide phosphatase","volume":"109","author":"F Hsu","year":"2012","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref26","doi-asserted-by":"crossref","first-page":"24518","DOI":"10.1074\/jbc.M113.474239","article-title":"Identification and structural characterization of a Legionella phosphoinositide phosphatase","volume":"288","author":"L Toulabi","year":"2013","journal-title":"J Biol Chem"},{"key":"ref27","doi-asserted-by":"crossref","first-page":"442","DOI":"10.1111\/j.1462-5822.2008.01266.x","article-title":"The inositol polyphosphate 5-phosphatase OCRL1 restricts intracellular growth of Legionella, localizes to the replicative vacuole and binds to the bacterial effector LpnE","volume":"11","author":"SS Weber","year":"2009","journal-title":"Cell Microbiol"},{"key":"ref28","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":"E Brombacher","year":"2009","journal-title":"J Biol Chem"},{"key":"ref29","doi-asserted-by":"crossref","first-page":"e1004222","DOI":"10.1371\/journal.ppat.1004222","article-title":"The machinery at endoplasmic reticulum-plasma membrane contact sites contributes to spatial regulation of multiple Legionella effector proteins","volume":"10","author":"A Hubber","year":"2014","journal-title":"PLoS Pathog"},{"key":"ref30","doi-asserted-by":"crossref","first-page":"598","DOI":"10.1038\/embor.2010.97","article-title":"High-affinity binding of phosphatidylinositol 4-phosphate by Legionella pneumophila DrrA","volume":"11","author":"S Schoebel","year":"2010","journal-title":"EMBO Rep"},{"key":"ref31","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1016\/j.str.2013.12.018","article-title":"Structural basis for PI(4)P-specific membrane recruitment of the Legionella pneumophila effector DrrA\/SidM","volume":"22","author":"CM Del Campo","year":"2014","journal-title":"Structure"},{"key":"ref32","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":"C Ragaz","year":"2008","journal-title":"Cell Microbiol"},{"key":"ref33","doi-asserted-by":"crossref","unstructured":"Horenkamp FA, Mukherjee S, Alix E, Schauder CM, Hubber AM, et al. (2014) Legionella pneumophila Subversion of Host Vesicular Transport by SidC Effector Proteins. Traffic.","DOI":"10.1111\/tra.12158"},{"key":"ref34","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":"F Hsu","year":"2014","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref35","doi-asserted-by":"crossref","unstructured":"Gazdag EM, Schobel S, Shkumatov AV, Goody RS, Itzen A (2014) The structure of the N-terminal domain of the Legionella protein SidC. J Struct Biol.","DOI":"10.2210\/pdb4ooj\/pdb"},{"key":"ref36","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":"ZQ Luo","year":"2004","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref37","doi-asserted-by":"crossref","first-page":"1925","DOI":"10.1073\/pnas.1115025109","article-title":"Crystal structures of two bacterial HECT-like E3 ligases in complex with a human E2 reveal atomic details of pathogen-host interactions","volume":"109","author":"DY Lin","year":"2012","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref38","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1016\/S1097-2765(02)00774-8","article-title":"Conformational flexibility underlies ubiquitin ligation mediated by the WWP1 HECT domain E3 ligase","volume":"11","author":"MA Verdecia","year":"2003","journal-title":"Mol Cell"},{"key":"ref39","doi-asserted-by":"crossref","first-page":"488","DOI":"10.1111\/tra.12158","article-title":"Legionella pneumophila subversion of host vesicular transport by SidC effector proteins","volume":"15","author":"FA Horenkamp","year":"2014","journal-title":"Traffic"},{"key":"ref40","doi-asserted-by":"crossref","first-page":"1095","DOI":"10.1016\/j.molcel.2009.11.010","article-title":"Insights into ubiquitin transfer cascades from a structure of a UbcH5B approximately ubiquitin-HECT(NEDD4L) complex","volume":"36","author":"HB Kamadurai","year":"2009","journal-title":"Mol Cell"},{"key":"ref41","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1006\/meth.2000.0955","article-title":"The use of liposomes to study COPII- and COPI-coated vesicle formation and membrane protein sorting","volume":"20","author":"K Matsuoka","year":"2000","journal-title":"Methods"},{"key":"ref42","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1146\/annurev.biophys.33.110502.133337","article-title":"Membrane-protein interactions in cell signaling and membrane trafficking","volume":"34","author":"W Cho","year":"2005","journal-title":"Annu Rev Biophys Biomol Struct"},{"key":"ref43","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/j.str.2011.11.012","article-title":"Conditional peripheral membrane proteins: facing up to limited specificity","volume":"20","author":"K Moravcevic","year":"2012","journal-title":"Structure"},{"key":"ref44","doi-asserted-by":"crossref","first-page":"1282","DOI":"10.1091\/mbc.E04-07-0578","article-title":"A plasma membrane pool of phosphatidylinositol 4-phosphate is generated by phosphatidylinositol 4-kinase type-III alpha: studies with the PH domains of the oxysterol binding protein and FAPP1","volume":"16","author":"A Balla","year":"2005","journal-title":"Mol Biol Cell"},{"key":"ref45","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1042\/bj3510019","article-title":"Identification of pleckstrin-homology-domain-containing proteins with novel phosphoinositide-binding specificities","volume":"351","author":"S Dowler","year":"2000","journal-title":"Biochem J"},{"key":"ref46","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":"GR Hammond","year":"2014","journal-title":"J Cell Biol"},{"key":"ref47","doi-asserted-by":"crossref","first-page":"20179","DOI":"10.1016\/S0021-9258(17)32143-9","article-title":"Expression and characterization of an inositol 1,4,5-trisphosphate binding domain of phosphatidylinositol-specific phospholipase C-delta 1","volume":"269","author":"H Yagisawa","year":"1994","journal-title":"J Biol Chem"},{"key":"ref48","first-page":"451","article-title":"Immunocytochemical localization of the Golgi apparatus using protein-specific antibodies to galactosyltransferase","volume":"56","author":"G Watzele","year":"1991","journal-title":"Eur J Cell Biol"},{"key":"ref49","doi-asserted-by":"crossref","first-page":"3597","DOI":"10.1128\/IAI.02060-05","article-title":"Members of a Legionella pneumophila family of proteins with ExoU (phospholipase A) active sites are translocated to target cells","volume":"74","author":"SM VanRheenen","year":"2006","journal-title":"Infect Immun"},{"key":"ref50","doi-asserted-by":"crossref","first-page":"e34","DOI":"10.1371\/journal.ppat.0020034","article-title":"RNA interference analysis of Legionella in Drosophila cells: exploitation of early secretory apparatus dynamics","volume":"2","author":"MS Dorer","year":"2006","journal-title":"PLoS Pathog"},{"key":"ref51","doi-asserted-by":"crossref","first-page":"592","DOI":"10.1128\/IAI.01278-06","article-title":"The Legionella pneumophila effector SidJ is required for efficient recruitment of endoplasmic reticulum proteins to the bacterial phagosome","volume":"75","author":"Y Liu","year":"2007","journal-title":"Infect Immun"},{"key":"ref52","doi-asserted-by":"crossref","first-page":"1293","DOI":"10.1038\/nsmb.1511","article-title":"Structure of the Shigella T3SS effector IpaH defines a new class of E3 ubiquitin ligases","volume":"15","author":"AU Singer","year":"2008","journal-title":"Nat Struct Mol Biol"},{"key":"ref53","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1016\/j.tcb.2010.10.002","article-title":"Coordination of Golgi functions by phosphatidylinositol 4-kinases","volume":"21","author":"TR Graham","year":"2011","journal-title":"Trends Cell Biol"},{"key":"ref54","doi-asserted-by":"crossref","first-page":"1955","DOI":"10.1242\/jcs.023630","article-title":"The multiple roles of PtdIns(4)P\u2014not just the precursor of PtdIns(4,5)P2","volume":"121","author":"G D'Angelo","year":"2008","journal-title":"J Cell Sci"},{"key":"ref55","doi-asserted-by":"crossref","first-page":"44683","DOI":"10.1074\/jbc.M401583200","article-title":"Multiple pools of phosphatidylinositol 4-phosphate detected using the pleckstrin homology domain of Osh2p","volume":"279","author":"A Roy","year":"2004","journal-title":"J Biol Chem"},{"key":"ref56","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1038\/ncb1119","article-title":"FAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and PtdIns(4)P","volume":"6","author":"A Godi","year":"2004","journal-title":"Nat Cell Biol"},{"key":"ref57","doi-asserted-by":"crossref","first-page":"18650","DOI":"10.1074\/jbc.M111.233015","article-title":"Molecular basis of phosphatidylinositol 4-phosphate and ARF1 GTPase recognition by the FAPP1 pleckstrin homology (PH) domain","volume":"286","author":"J He","year":"2011","journal-title":"J Biol Chem"},{"key":"ref58","doi-asserted-by":"crossref","first-page":"695","DOI":"10.1016\/S0960-9822(02)00779-0","article-title":"Targeting of Golgi-specific pleckstrin homology domains involves both PtdIns 4-kinase-dependent and-independent components","volume":"12","author":"TP Levine","year":"2002","journal-title":"Curr Biol"},{"key":"ref59","doi-asserted-by":"crossref","first-page":"22059","DOI":"10.1074\/jbc.272.35.22059","article-title":"A comparative analysis of the phosphoinositide binding specificity of pleckstrin homology domains","volume":"272","author":"LE Rameh","year":"1997","journal-title":"J Biol Chem"},{"key":"ref60","doi-asserted-by":"crossref","first-page":"4699","DOI":"10.1073\/pnas.0914231107","article-title":"Structural mechanism of host Rab1 activation by the bifunctional Legionella type IV effector SidM\/DrrA","volume":"107","author":"Y Zhu","year":"2010","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref61","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1016\/S0076-6879(97)76066-X","article-title":"Processing of X-ray diffraction data collected in oscillation mode","volume":"276","author":"Z Otwinowski","year":"1997","journal-title":"Methods Enzymol"},{"key":"ref62","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1016\/0022-2836(68)90205-2","article-title":"Solvent content of protein crystals","volume":"33","author":"BW Matthews","year":"1968","journal-title":"J Mol Biol"},{"key":"ref63","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1107\/S0907444907044460","article-title":"AMoRe: classical and modern","volume":"64","author":"S Trapani","year":"2008","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"ref64","doi-asserted-by":"crossref","unstructured":"Collaborative Computational Project N (1994) The CCP4 suite: programs for protein crystallography. Acta Cryst D: 760\u2013763.","DOI":"10.1107\/S0907444994003112"},{"key":"ref65","doi-asserted-by":"crossref","first-page":"2126","DOI":"10.1107\/S0907444904019158","article-title":"Coot: model-building tools for molecular graphics","volume":"60","author":"P Emsley","year":"2004","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"ref66","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1107\/S0907444996012255","article-title":"Refinement of macromolecular structures by the maximum-likelihood method","volume":"53","author":"GN Murshudov","year":"1997","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"ref67","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1107\/S0021889892009944","article-title":"PROCHECK: a program to check the stereochemical quality of protein structures","volume":"26","author":"RA Laskowski","year":"1993","journal-title":"J Appl Cryst"},{"key":"ref68","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":"KH Berger","year":"1993","journal-title":"Mol Microbiol"},{"key":"ref69","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":"GM Conover","year":"2003","journal-title":"Mol Microbiol"},{"key":"ref70","doi-asserted-by":"crossref","first-page":"e1000822","DOI":"10.1371\/journal.ppat.1000822","article-title":"Inhibition of host vacuolar H+-ATPase activity by a Legionella pneumophila effector","volume":"6","author":"L Xu","year":"2010","journal-title":"PLoS Pathog"}],"container-title":["PLOS Pathogens"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.ppat.1004965","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,5,12]],"date-time":"2022-05-12T23:37:32Z","timestamp":1652398652000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.ppat.1004965"}},"subtitle":[],"editor":[{"given":"Craig R.","family":"Roy","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]}],"short-title":[],"issued":{"date-parts":[[2015,6,12]]},"references-count":70,"journal-issue":{"issue":"6","published-online":{"date-parts":[[2015,6,12]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.ppat.1004965","relation":{},"ISSN":["1553-7374"],"issn-type":[{"value":"1553-7374","type":"electronic"}],"subject":[],"published":{"date-parts":[[2015,6,12]]}}}