{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,16]],"date-time":"2026-01-16T19:33:57Z","timestamp":1768592037242,"version":"3.49.0"},"reference-count":70,"publisher":"Public Library of Science (PLoS)","issue":"3","license":[{"start":{"date-parts":[[2018,3,15]],"date-time":"2018-03-15T00:00:00Z","timestamp":1521072000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"EU FP7 HEALTH-2013-INNOVATION","award":["602773 (KINDRED)"],"award-info":[{"award-number":["602773 (KINDRED)"]}]}],"content-domain":{"domain":["www.plosone.org"],"crossmark-restriction":false},"short-container-title":["PLoS ONE"],"DOI":"10.1371\/journal.pone.0193602","type":"journal-article","created":{"date-parts":[[2018,3,15]],"date-time":"2018-03-15T17:33:11Z","timestamp":1521135191000},"page":"e0193602","update-policy":"https:\/\/doi.org\/10.1371\/journal.pone.corrections_policy","source":"Crossref","is-referenced-by-count":19,"title":["The crystal structure of the Leishmania infantum Silent Information Regulator 2 related protein 1: Implications to protein function and drug design"],"prefix":"10.1371","volume":"13","author":[{"given":"C\u00e9line","family":"Ronin","sequence":"first","affiliation":[]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0213-5673","authenticated-orcid":true,"given":"David Mendes","family":"Costa","sequence":"additional","affiliation":[]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0391-2622","authenticated-orcid":true,"given":"Joana","family":"Tavares","sequence":"additional","affiliation":[]},{"given":"Joana","family":"Faria","sequence":"additional","affiliation":[]},{"given":"Fabrice","family":"Ciesielski","sequence":"additional","affiliation":[]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3906-7547","authenticated-orcid":true,"given":"Paola","family":"Ciapetti","sequence":"additional","affiliation":[]},{"given":"Terry K.","family":"Smith","sequence":"additional","affiliation":[]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4715-8222","authenticated-orcid":true,"given":"Jane","family":"MacDougall","sequence":"additional","affiliation":[]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2392-6087","authenticated-orcid":true,"given":"Anabela","family":"Cordeiro-da-Silva","sequence":"additional","affiliation":[]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7304-9767","authenticated-orcid":true,"given":"Iain K.","family":"Pemberton","sequence":"additional","affiliation":[]}],"member":"340","published-online":{"date-parts":[[2018,3,15]]},"reference":[{"key":"ref1","first-page":"33","article-title":"Investing to overcome the global impact of neglected tropical diseases","volume":"90","year":"2015","journal-title":"Third WHO report on neglected tropical diseases"},{"issue":"10","key":"ref2","doi-asserted-by":"crossref","first-page":"1372","DOI":"10.1016\/j.bbapap.2016.06.007","article-title":"The world of protein acetylation","volume":"1864","author":"A Drazic","year":"2016","journal-title":"Biochim Biophys Acta"},{"issue":"4","key":"ref3","doi-asserted-by":"crossref","first-page":"a018713","DOI":"10.1101\/cshperspect.a018713","article-title":"Erasers of histone acetylation: the histone deacetylase enzymes","volume":"6","author":"E Seto","year":"2014","journal-title":"Cold Spring Harb Perspect Biol"},{"issue":"4","key":"ref4","doi-asserted-by":"crossref","first-page":"258","DOI":"10.1038\/nrm3931","article-title":"50 years of protein acetylation: from gene regulation to epigenetics, metabolism and beyond","volume":"16","author":"E Verdin","year":"2015","journal-title":"Nat Rev Mol Cell Biol"},{"issue":"6771","key":"ref5","doi-asserted-by":"crossref","first-page":"795","DOI":"10.1038\/35001622","article-title":"Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase","volume":"403","author":"S Imai","year":"2000","journal-title":"Nature"},{"issue":"2","key":"ref6","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1016\/S1097-2765(03)00038-8","article-title":"The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase","volume":"11","author":"BJ North","year":"2003","journal-title":"Mol Cell"},{"issue":"5602","key":"ref7","doi-asserted-by":"crossref","first-page":"2390","DOI":"10.1126\/science.1077650","article-title":"Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine","volume":"298","author":"VJ Starai","year":"2002","journal-title":"Science"},{"issue":"8","key":"ref8","doi-asserted-by":"crossref","first-page":"1604","DOI":"10.1016\/j.bbapap.2009.09.009","article-title":"Structural basis for sirtuin function: what we know and what we don\u2019t","volume":"1804","author":"BD Sanders","year":"2010","journal-title":"Biochim Biophys Acta"},{"key":"ref9","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1186\/1471-2148-13-60","article-title":"Genealogy of an ancient protein family: the Sirtuins, a family of disordered members","volume":"13","author":"S Costantini","year":"2013","journal-title":"BMC Evol Biol"},{"issue":"43","key":"ref10","doi-asserted-by":"crossref","first-page":"36073","DOI":"10.1074\/jbc.M508247200","article-title":"Unstructured conformations are a substrate requirement for the Sir2 family of NAD-dependent protein deacetylases","volume":"280","author":"AN Khan","year":"2005","journal-title":"J Biol Chem"},{"issue":"8","key":"ref11","doi-asserted-by":"crossref","first-page":"1231","DOI":"10.1016\/j.str.2006.06.006","article-title":"Insights into the sirtuin mechanism from ternary complexes containing NAD+ and acetylated peptide","volume":"14","author":"KG Hoff","year":"2006","journal-title":"Structure"},{"issue":"24","key":"ref12","doi-asserted-by":"crossref","first-page":"7511","DOI":"10.1021\/bi0526332","article-title":"The structural basis of sirtuin substrate affinity","volume":"45","author":"MS Cosgrove","year":"2006","journal-title":"Biochemistry"},{"issue":"3","key":"ref13","doi-asserted-by":"crossref","first-page":"526","DOI":"10.1016\/j.jmb.2013.10.009","article-title":"Structural and functional analysis of human SIRT1","volume":"426","author":"AM Davenport","year":"2014","journal-title":"J Mol Biol"},{"issue":"1","key":"ref14","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1006\/bbrc.1999.0897","article-title":"Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity","volume":"260","author":"RA Frye","year":"1999","journal-title":"Biochem Biophys Res Commun"},{"key":"ref15","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1016\/j.ejmech.2012.11.014","article-title":"Sirtuins as emerging anti-parasitic targets","volume":"59","author":"W Zheng","year":"2013","journal-title":"Eur J Med Chem"},{"issue":"7","key":"ref16","doi-asserted-by":"crossref","first-page":"735","DOI":"10.1016\/S0092-8674(00)81671-2","article-title":"An enzymatic activity in the yeast Sir2 protein that is essential for gene silencing","volume":"99","author":"JC Tanny","year":"1999","journal-title":"Cell"},{"issue":"21","key":"ref17","doi-asserted-by":"crossref","first-page":"5851","DOI":"10.1093\/emboj\/cdg553","article-title":"A chromosomal SIR2 homologue with both histone NAD-dependent ADP-ribosyltransferase and deacetylase activities is involved in DNA repair in Trypanosoma brucei","volume":"22","author":"JA Garcia-Salcedo","year":"2003","journal-title":"EMBO J"},{"issue":"5","key":"ref18","doi-asserted-by":"crossref","first-page":"e1631","DOI":"10.1371\/journal.pntd.0001631","article-title":"Cultivation-independent methods reveal differences among bacterial gut microbiota in triatomine vectors of Chagas disease","volume":"6","author":"FF da Mota","year":"2012","journal-title":"PLoS Negl Trop Dis"},{"issue":"2","key":"ref19","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1016\/j.actatropica.2007.05.017","article-title":"Characterization of the anti-Leishmania effect induced by cisplatin, an anticancer drug","volume":"103","author":"J Tavares","year":"2007","journal-title":"Acta Trop"},{"issue":"2","key":"ref20","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1016\/j.molbiopara.2012.08.003","article-title":"Sirtuins of parasitic protozoa: in search of function(s)","volume":"185","author":"AA Religa","year":"2012","journal-title":"Mol Biochem Parasitol"},{"issue":"3","key":"ref21","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1042\/BJ20080666","article-title":"The Leishmania infantum cytosolic SIR2-related protein 1 (LiSIR2RP1) is an NAD+ -dependent deacetylase and ADP-ribosyltransferase","volume":"415","author":"J Tavares","year":"2008","journal-title":"Biochem J"},{"key":"ref22","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1016\/j.gene.2005.06.047","article-title":"Targeted disruption of cytosolic SIR2 deacetylase discloses its essential role in Leishmania survival and proliferation","volume":"363","author":"B Vergnes","year":"2005","journal-title":"Gene"},{"issue":"1","key":"ref23","doi-asserted-by":"crossref","first-page":"e1469","DOI":"10.1371\/journal.pntd.0001469","article-title":"Impact of continuous axenic cultivation in Leishmania infantum virulence","volume":"6","author":"D Moreira","year":"2012","journal-title":"PLoS Negl Trop Dis"},{"issue":"13","key":"ref24","doi-asserted-by":"crossref","first-page":"3701","DOI":"10.1093\/nar\/gkg519","article-title":"GlobPlot: Exploring protein sequences for globularity and disorder","volume":"31","author":"R Linding","year":"2003","journal-title":"Nucleic Acids Res"},{"issue":"16","key":"ref25","doi-asserted-by":"crossref","first-page":"3433","DOI":"10.1093\/bioinformatics\/bti541","article-title":"IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content","volume":"21","author":"Z Dosztanyi","year":"2005","journal-title":"Bioinformatics"},{"issue":"3","key":"ref26","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1016\/S0968-0004(99)01540-6","article-title":"NPS@: network protein sequence analysis","volume":"25","author":"C Combet","year":"2000","journal-title":"Trends Biochem Sci"},{"issue":"4","key":"ref27","doi-asserted-by":"crossref","first-page":"404","DOI":"10.1093\/bioinformatics\/16.4.404","article-title":"The PSIPRED protein structure prediction server","volume":"16","author":"LJ McGuffin","year":"2000","journal-title":"Bioinformatics"},{"issue":"21","key":"ref28","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":"MA Larkin","year":"2007","journal-title":"Bioinformatics"},{"issue":"2","key":"ref29","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1093\/bioinformatics\/bti770","article-title":"The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling","volume":"22","author":"K Arnold","year":"2006","journal-title":"Bioinformatics"},{"issue":"Pt 2","key":"ref30","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1107\/S0907444909047337","article-title":"Xds","volume":"66","author":"W Kabsch","year":"2010","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"issue":"Pt 4","key":"ref31","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1107\/S0907444910045749","article-title":"Overview of the CCP4 suite and current developments","volume":"67","author":"MD Winn","year":"2011","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"issue":"Pt 4","key":"ref32","doi-asserted-by":"crossref","first-page":"447","DOI":"10.1107\/S0907444907002661","article-title":"Automated search-model discovery and preparation for structure solution by molecular replacement","volume":"63","author":"RM Keegan","year":"2007","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"issue":"6","key":"ref33","doi-asserted-by":"crossref","first-page":"1022","DOI":"10.1107\/S0021889897006766","article-title":"MOLREP: an automated program for molecular replacement","volume":"30","author":"TA Vagin A","year":"1997","journal-title":"J Appl Crystallogr"},{"key":"ref34","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1107\/S0021889808006985","article-title":"CHAINSAW: a program for mutating pdb files used as templates in molecular replacement","volume":"41","author":"N Stein","year":"2008","journal-title":"J Appl Crystallogr"},{"issue":"Pt 4","key":"ref35","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1107\/S0907444910007493","article-title":"Features and development of Coot","volume":"66","author":"P Emsley","year":"2010","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"issue":"Pt 4","key":"ref36","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1107\/S0907444911001314","article-title":"REFMAC5 for the refinement of macromolecular crystal structures","volume":"67","author":"GN Murshudov","year":"2011","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"ref37","article-title":"The PyMOL Molecular Graphics System","author":"W DeLano","year":"2002"},{"issue":"13","key":"ref38","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1002\/jcc.20084","article-title":"UCSF Chimera\u2014a visualization system for exploratory research and analysis","volume":"25","author":"EF Pettersen","year":"2004","journal-title":"J Comput Chem"},{"issue":"11","key":"ref39","doi-asserted-by":"crossref","first-page":"1453","DOI":"10.1016\/j.str.2003.10.002","article-title":"Protein disorder prediction: implications for structural proteomics","volume":"11","author":"R Linding","year":"2003","journal-title":"Structure"},{"issue":"1\u20132","key":"ref40","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1016\/S0378-1119(02)00842-9","article-title":"Cytoplasmic SIR2 homologue overexpression promotes survival of Leishmania parasites by preventing programmed cell death","volume":"296","author":"B Vergnes","year":"2002","journal-title":"Gene"},{"key":"ref41","doi-asserted-by":"crossref","first-page":"26937","DOI":"10.1038\/srep26937","article-title":"Disclosing the essentiality of ribose-5-phosphate isomerase B in Trypanosomatids","volume":"6","author":"J Faria","year":"2016","journal-title":"Sci Rep"},{"issue":"9","key":"ref42","doi-asserted-by":"crossref","first-page":"e45","DOI":"10.1093\/nar\/29.9.e45","article-title":"A new mathematical model for relative quantification in real-time RT-PCR","volume":"29","author":"MW Pfaffl","year":"2001","journal-title":"Nucleic Acids Res"},{"issue":"1","key":"ref43","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1016\/j.jsb.2012.05.013","article-title":"High-throughput characterization of intrinsic disorder in proteins from the Protein Structure Initiative","volume":"180","author":"DE Johnson","year":"2012","journal-title":"J Struct Biol"},{"issue":"5","key":"ref44","doi-asserted-by":"crossref","first-page":"757","DOI":"10.1002\/pro.5560030505","article-title":"Modeling studies of the change in conformation required for cleavage of limited proteolytic sites","volume":"3","author":"SJ Hubbard","year":"1994","journal-title":"Protein Sci"},{"issue":"5","key":"ref45","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1093\/protein\/11.5.349","article-title":"Assessment of conformational parameters as predictors of limited proteolytic sites in native protein structures","volume":"11","author":"SJ Hubbard","year":"1998","journal-title":"Protein Eng"},{"issue":"3","key":"ref46","doi-asserted-by":"crossref","first-page":"534","DOI":"10.1016\/j.jsb.2016.10.008","article-title":"Human sirtuins: Structures and flexibility","volume":"196","author":"L Sacconnay","year":"2016","journal-title":"J Struct Biol"},{"issue":"2","key":"ref47","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1016\/j.jsb.2013.02.012","article-title":"Crystal structure analysis of human Sirt2 and its ADP-ribose complex","volume":"182","author":"S Moniot","year":"2013","journal-title":"J Struct Biol"},{"issue":"7","key":"ref48","doi-asserted-by":"crossref","first-page":"621","DOI":"10.1038\/89668","article-title":"Structure of the histone deacetylase SIRT2","volume":"8","author":"MS Finnin","year":"2001","journal-title":"Nat Struct Biol"},{"issue":"10","key":"ref49","doi-asserted-by":"crossref","first-page":"864","DOI":"10.1038\/nsb978","article-title":"Structure and autoregulation of the yeast Hst2 homolog of Sir2","volume":"10","author":"K Zhao","year":"2003","journal-title":"Nat Struct Biol"},{"issue":"11","key":"ref50","doi-asserted-by":"crossref","first-page":"1403","DOI":"10.1016\/j.str.2003.09.016","article-title":"Structure of the yeast Hst2 protein deacetylase in ternary complex with 2'-O-acetyl ADP ribose and histone peptide","volume":"11","author":"K Zhao","year":"2003","journal-title":"Structure"},{"issue":"23","key":"ref51","doi-asserted-by":"crossref","first-page":"8563","DOI":"10.1073\/pnas.0401057101","article-title":"Structural basis for nicotinamide cleavage and ADP-ribose transfer by NAD(+)-dependent Sir2 histone\/protein deacetylases","volume":"101","author":"K Zhao","year":"2004","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"2","key":"ref52","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1016\/j.str.2013.12.001","article-title":"Structural basis for potent inhibition of SIRT2 deacetylase by a macrocyclic peptide inducing dynamic structural change","volume":"22","author":"K Yamagata","year":"2014","journal-title":"Structure"},{"issue":"Pt 1","key":"ref53","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1107\/S0907444907050172","article-title":"BALBES: a molecular-replacement pipeline","volume":"64","author":"F Long","year":"2008","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"issue":"36","key":"ref54","doi-asserted-by":"crossref","first-page":"24394","DOI":"10.1074\/jbc.M109.014928","article-title":"Crystal structures of human SIRT3 displaying substrate-induced conformational changes","volume":"284","author":"L Jin","year":"2009","journal-title":"J Biol Chem"},{"key":"ref55","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1146\/annurev-biochem-060815-014537","article-title":"The Substrate Specificity of Sirtuins","volume":"85","author":"P Bheda","year":"2016","journal-title":"Annu Rev Biochem"},{"issue":"8","key":"ref56","doi-asserted-by":"crossref","first-page":"2263","DOI":"10.1039\/C5MB00205B","article-title":"Selectivity hot-spots of sirtuin catalytic cores","volume":"11","author":"MD Parenti","year":"2015","journal-title":"Mol Biosyst"},{"key":"ref57","doi-asserted-by":"crossref","first-page":"6263","DOI":"10.1038\/ncomms7263","article-title":"Selective Sirt2 inhibition by ligand-induced rearrangement of the active site","volume":"6","author":"T Rumpf","year":"2015","journal-title":"Nat Commun"},{"issue":"Pt 12","key":"ref58","doi-asserted-by":"crossref","first-page":"1498","DOI":"10.1107\/S2053230X15019986","article-title":"Seeding for sirtuins: microseed matrix seeding to obtain crystals of human Sirt3 and Sirt2 suitable for soaking","volume":"71","author":"T Rumpf","year":"2015","journal-title":"Acta Crystallogr F Struct Biol Commun"},{"issue":"5","key":"ref59","doi-asserted-by":"crossref","first-page":"1928","DOI":"10.1021\/acs.jmedchem.6b01690","article-title":"Thienopyrimidinone Based Sirtuin-2 (SIRT2)-Selective Inhibitors Bind in the Ligand Induced Selectivity Pocket","volume":"60","author":"S Sundriyal","year":"2017","journal-title":"J Med Chem"},{"key":"ref60","doi-asserted-by":"crossref","first-page":"1100","DOI":"10.1186\/1471-2164-15-1100","article-title":"Intrinsically disordered proteins (IDPs) in trypanosomatids","volume":"15","author":"P de Cassia Ruy","year":"2014","journal-title":"BMC Genomics"},{"issue":"3","key":"ref61","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1038\/nrm1589","article-title":"Intrinsically unstructured proteins and their functions","volume":"6","author":"HJ Dyson","year":"2005","journal-title":"Nat Rev Mol Cell Biol"},{"issue":"7","key":"ref62","doi-asserted-by":"crossref","first-page":"1886","DOI":"10.1039\/c2mb25102g","article-title":"More than just tails: intrinsic disorder in histone proteins","volume":"8","author":"Z Peng","year":"2012","journal-title":"Mol Biosyst"},{"key":"ref63","first-page":"94","article-title":"Correlation between posttranslational modification and intrinsic disorder in protein","author":"J Gao","year":"2012","journal-title":"Pac Symp Biocomput"},{"issue":"3","key":"ref64","doi-asserted-by":"crossref","first-page":"1037","DOI":"10.1093\/nar\/gkh253","article-title":"The importance of intrinsic disorder for protein phosphorylation","volume":"32","author":"LM Iakoucheva","year":"2004","journal-title":"Nucleic Acids Res"},{"issue":"Web Server issue","key":"ref65","doi-asserted-by":"crossref","first-page":"W588","DOI":"10.1093\/nar\/gkm322","article-title":"KinasePhos 2.0: a web server for identifying protein kinase-specific phosphorylation sites based on sequences and coupling patterns","volume":"35","author":"YH Wong","year":"2007","journal-title":"Nucleic Acids Res"},{"key":"ref66","doi-asserted-by":"crossref","first-page":"29","DOI":"10.3389\/fphar.2012.00029","article-title":"Regulation of sirtuin function by posttranslational modifications","volume":"3","author":"F Flick","year":"2012","journal-title":"Front Pharmacol"},{"issue":"10","key":"ref67","doi-asserted-by":"crossref","first-page":"4623","DOI":"10.1091\/mbc.E05-01-0033","article-title":"Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins","volume":"16","author":"E Michishita","year":"2005","journal-title":"Mol Biol Cell"},{"issue":"4","key":"ref68","doi-asserted-by":"crossref","first-page":"2468","DOI":"10.1074\/jbc.M111.285031","article-title":"SIRT1 contains N- and C-terminal regions that potentiate deacetylase activity","volume":"287","author":"M Pan","year":"2012","journal-title":"J Biol Chem"},{"issue":"10","key":"ref69","doi-asserted-by":"crossref","first-page":"1245","DOI":"10.1017\/S0031182011001077","article-title":"Sir2-Related Protein 1 from Leishmania amazonensis is a glycosylated NAD+-dependent deacetylase","volume":"138","author":"MR Fessel","year":"2011","journal-title":"Parasitology"},{"issue":"20","key":"ref70","doi-asserted-by":"crossref","first-page":"8340","DOI":"10.1021\/jm500777s","article-title":"Discovery of potent and selective sirtuin 2 (SIRT2) inhibitors using a fragment-based approach","volume":"57","author":"H Cui","year":"2014","journal-title":"J Med Chem"}],"container-title":["PLOS ONE"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.pone.0193602","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2020,5,9]],"date-time":"2020-05-09T04:28:28Z","timestamp":1588998508000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pone.0193602"}},"subtitle":[],"editor":[{"given":"Michael","family":"Massiah","sequence":"first","affiliation":[]}],"short-title":[],"issued":{"date-parts":[[2018,3,15]]},"references-count":70,"journal-issue":{"issue":"3","published-online":{"date-parts":[[2018,3,15]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pone.0193602","relation":{},"ISSN":["1932-6203"],"issn-type":[{"value":"1932-6203","type":"electronic"}],"subject":[],"published":{"date-parts":[[2018,3,15]]}}}