{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,28]],"date-time":"2026-02-28T20:03:33Z","timestamp":1772309013615,"version":"3.50.1"},"update-to":[{"DOI":"10.1371\/journal.ppat.1009355","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2021,3,9]],"date-time":"2021-03-09T00:00:00Z","timestamp":1615248000000}}],"reference-count":58,"publisher":"Public Library of Science (PLoS)","issue":"2","license":[{"start":{"date-parts":[[2021,2,25]],"date-time":"2021-02-25T00:00:00Z","timestamp":1614211200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100009053","name":"The Wellcome Trust DBT India Alliance","doi-asserted-by":"publisher","award":["IA\/S\/15\/1\/501831"],"award-info":[{"award-number":["IA\/S\/15\/1\/501831"]}],"id":[{"id":"10.13039\/501100009053","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Department of Biotechnology","award":["BT\/HRD\/NBA\/37\/01\/2014"],"award-info":[{"award-number":["BT\/HRD\/NBA\/37\/01\/2014"]}]},{"name":"Science and Engineering Research Board, Department of Science and Technology","award":["EMR\/2016\/005375"],"award-info":[{"award-number":["EMR\/2016\/005375"]}]}],"content-domain":{"domain":["www.plospathogens.org"],"crossmark-restriction":false},"short-container-title":["PLoS Pathog"],"abstract":"<jats:p>A family of eleven glycosylphosphatidylinositol-anchored aspartyl proteases, commonly referred to as CgYapsins, regulate a myriad of cellular processes in the pathogenic yeast <jats:italic>Candida glabrata<\/jats:italic>, but their protein targets are largely unknown. Here, using the immunoprecipitation-mass spectrometry approach, we identify the flavodoxin-like protein (Fld-LP), CgPst2, to be an interactor of one of the aspartyl protease CgYps1. We also report the presence of four Fld-LPs in <jats:italic>C<\/jats:italic>. <jats:italic>glabrata<\/jats:italic>, which are required for survival in kidneys in the murine model of systemic candidiasis. We further demonstrated that of four Fld-LPs, CgPst2 was solely required for menadione detoxification. CgPst2 was found to form homo-oligomers, and contribute to cellular NADH:quinone oxidoreductase activity. CgYps1 cleaved CgPst2 at the C-terminus, and this cleavage was pivotal to oligomerization, activity and function of CgPst2. The arginine-174 residue in CgPst2 was essential for CgYps1-mediated cleavage, with alanine substitution of the arginine-174 residue also leading to elevated activity and oligomerization of CgPst2. Finally, we demonstrate that menadione treatment led to increased CgPst2 and CgYps1 protein levels, diminished CgYps1-CgPst2 interaction, and enhanced CgPst2 cleavage and activity, thereby implicating CgYps1 in activating CgPst2. Altogether, our findings of proteolytic cleavage as a key regulatory determinant of CgPst2, which belongs to the family of highly conserved, electron-carrier flavodoxin-fold-containing proteins, constituting cellular oxidative stress defense system in diverse organisms, unveil a hidden regulatory layer of environmental stress response mechanisms.<\/jats:p>","DOI":"10.1371\/journal.ppat.1009355","type":"journal-article","created":{"date-parts":[[2021,2,25]],"date-time":"2021-02-25T19:03:11Z","timestamp":1614279791000},"page":"e1009355","update-policy":"https:\/\/doi.org\/10.1371\/journal.ppat.corrections_policy","source":"Crossref","is-referenced-by-count":6,"title":["An aspartyl protease-mediated cleavage regulates structure and function of a flavodoxin-like protein and aids oxidative stress survival"],"prefix":"10.1371","volume":"17","author":[{"given":"Anamika","family":"Battu","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rajaram","family":"Purushotham","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Partha","family":"Dey","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"S. Surya","family":"Vamshi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3287-1700","authenticated-orcid":true,"given":"Rupinder","family":"Kaur","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"340","published-online":{"date-parts":[[2021,2,25]]},"reference":[{"key":"ppat.1009355.ref001","doi-asserted-by":"crossref","first-page":"165rv13","DOI":"10.1126\/scitranslmed.3004404","article-title":"Hidden killers: human fungal infections","volume":"4","author":"GD Brown","year":"2012","journal-title":"Sci Transl Med"},{"key":"ppat.1009355.ref002","doi-asserted-by":"crossref","first-page":"4167","DOI":"10.1128\/JCM.01998-13","article-title":"Epidemiology, Species Distribution, Antifungal Susceptibility, and outcome of Candidemia across five sites in Italy and Spain","volume":"51","author":"M Bassetti","year":"2013","journal-title":"J Clin Microbiol"},{"key":"ppat.1009355.ref003","doi-asserted-by":"crossref","first-page":"i4","DOI":"10.1093\/jac\/dkx444","article-title":"Changes in the epidemiological landscape of invasive candidiasis","volume":"73","author":"F Lamoth","year":"2018","journal-title":"J Antimicrob Chemother"},{"key":"ppat.1009355.ref004","first-page":"1","article-title":"Invasive candidiasis","volume":"4","author":"PG Pappas","year":"2018","journal-title":"Nat Rev Dis Prim"},{"key":"ppat.1009355.ref005","doi-asserted-by":"crossref","first-page":"S79","DOI":"10.1093\/ofid\/ofy358","article-title":"Twenty years of the SENTRY antifungal surveillance program: Results for Candida species from 1997\u20132016","volume":"6","author":"MA Pfaller","year":"2019","journal-title":"Open forum Infect Dis"},{"key":"ppat.1009355.ref006","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1007\/s00134-014-3603-2","article-title":"Incidence, characteristics and outcome of ICU-acquired candidemia in India","volume":"41","author":"A Chakrabarti","year":"2015","journal-title":"Intensive Care Med"},{"key":"ppat.1009355.ref007","first-page":"1","article-title":"Update from a 12-year nationwide fungemia surveillance: Increasing intrinsic and acquired resistance causes concern","volume":"56","author":"KMT Astvad","year":"2018","journal-title":"J Clin Microbiol"},{"key":"ppat.1009355.ref008","first-page":"1","article-title":"Surveillance study of the prevalence, species distribution, antifungal susceptibility, risk factors and mortality of invasive candidiasis in a tertiary teaching hospital in Southwest China","volume":"19","author":"ZR Zeng","year":"2019","journal-title":"BMC Infect Dis"},{"key":"ppat.1009355.ref009","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1038\/nature02579","article-title":"Genome evolution in yeasts","volume":"430","author":"B Dujon","year":"2004","journal-title":"Nature"},{"key":"ppat.1009355.ref010","doi-asserted-by":"crossref","first-page":"2345","DOI":"10.3390\/ijms20092345","article-title":"Divergent Approaches to virulence in C. albicans and C. glabrata: Two sides of the same coin.","volume":"20","author":"M Galocha","year":"2019","journal-title":"Int J Mol Sci"},{"key":"ppat.1009355.ref011","doi-asserted-by":"crossref","first-page":"39","DOI":"10.3390\/microorganisms7020039","article-title":"Candida glabrata: A lot more than meets the eye","volume":"7","author":"K Kumar","year":"2019","journal-title":"Microorganisms"},{"key":"ppat.1009355.ref012","doi-asserted-by":"crossref","first-page":"7628","DOI":"10.1073\/pnas.0611195104","article-title":"A family of glycosylphosphatidylinositol-linked aspartyl proteases is required for virulence of Candida glabrata","volume":"104","author":"R Kaur","year":"2007","journal-title":"Proc Natl Acad Sci"},{"key":"ppat.1009355.ref013","doi-asserted-by":"crossref","first-page":"900","DOI":"10.1111\/j.1365-2958.2010.07496.x","article-title":"A novel role for a glycosylphosphatidylinositol-anchored aspartyl protease, CgYps1, in the regulation of pH homeostasis in Candida glabrata","volume":"79","author":"G Bairwa","year":"2011","journal-title":"Mol Microbiol"},{"key":"ppat.1009355.ref014","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1042\/BJ20130757","article-title":"GPI (glycosylphosphatidylinositol)-linked aspartyl proteases regulate vacuole homoeostasis in Candida glabrata","volume":"458","author":"Bairwa","year":"2014","journal-title":"Biochem J"},{"key":"ppat.1009355.ref015","doi-asserted-by":"crossref","first-page":"6410","DOI":"10.1074\/jbc.M117.813741","article-title":"Aspartyl proteases in Candida glabrata are required for suppression of the host innate immune response","volume":"293","author":"M Rasheed","year":"2018","journal-title":"J Biol Chem"},{"key":"ppat.1009355.ref016","doi-asserted-by":"crossref","first-page":"814","DOI":"10.1128\/EC.00011-08","article-title":"High resistance to oxidative stress in the fungal pathogen Candida glabrata is mediated by a single catalase, Cta1p, and is controlled by the transcription factors Yap1p, Skn7p, Msn2p, and Msn4p","volume":"7","author":"M Cu\u00e9llar-Cruz","year":"2008","journal-title":"Eukaryot Cell"},{"key":"ppat.1009355.ref017","doi-asserted-by":"crossref","first-page":"855","DOI":"10.1007\/s00018-005-5514-4","article-title":"Flavodoxins: Sequence, folding, binding, function and beyond","volume":"63","author":"J. Sancho","year":"2006","journal-title":"Cell Mol Life Sci"},{"key":"ppat.1009355.ref018","doi-asserted-by":"crossref","first-page":"2917","DOI":"10.1016\/j.febslet.2012.07.026","article-title":"The importance of flavodoxin for environmental stress tolerance in photosynthetic microorganisms and transgenic plants. Mechanism, evolution and biotechnological potential","volume":"586","author":"AF Lodeyro","year":"2012","journal-title":"FEBS Lett"},{"key":"ppat.1009355.ref019","doi-asserted-by":"crossref","first-page":"2301","DOI":"10.1110\/ps.073018907","article-title":"WrbA bridges bacterial flavodoxins and eukaryotic NAD(P)H:quinone oxidoreductases","volume":"16","author":"J Carey","year":"2007","journal-title":"Protein Sci"},{"key":"ppat.1009355.ref020","doi-asserted-by":"crossref","first-page":"710","DOI":"10.1038\/nchembio.1579","article-title":"Evolutionary relationship of two ancient protein superfolds","volume":"10","author":"JA Far\u00edas-Rico","year":"2014","journal-title":"Nat Chem Biol"},{"key":"ppat.1009355.ref021","doi-asserted-by":"crossref","first-page":"8411","DOI":"10.1073\/pnas.94.16.8411","article-title":"Three-dimensional structure of NADPH-cytochrome P450 reductase: Prototype for FMN- and FAD-containing enzymes","volume":"94","author":"M Wang","year":"1997","journal-title":"Proc Natl Acad Sci"},{"key":"ppat.1009355.ref022","doi-asserted-by":"crossref","first-page":"2185","DOI":"10.1002\/pro.5560031204","article-title":"Six new candidate members of the \u03b1\/\u03b2 twisted open-sheet family detected by sequence similarity to flavodoxin","volume":"3","author":"R Grandori","year":"1994","journal-title":"Protein Sci"},{"key":"ppat.1009355.ref023","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1007\/s00203-011-0696-7","article-title":"The Saccharomyces cerevisiae flavodoxin-like proteins Ycp4 and Rfs1 play a role in stress response and in the regulation of genes related to metabolism","volume":"193","author":"F Cardona","year":"2011","journal-title":"Arch Microbiol"},{"key":"ppat.1009355.ref024","doi-asserted-by":"crossref","first-page":"e24205","DOI":"10.1371\/journal.pone.0024205","article-title":"Genome-wide functional profiling reveals genes required for tolerance to Benzene metabolites in Yeast","volume":"6","author":"M North","year":"2011","journal-title":"PLoS One"},{"key":"ppat.1009355.ref025","doi-asserted-by":"crossref","first-page":"e1005147","DOI":"10.1371\/journal.ppat.1005147","article-title":"Flavodoxin-Like proteins protect Candida albicans from oxidative stress and promote virulence","volume":"11","author":"L Li","year":"2015","journal-title":"PLOS Pathog"},{"key":"ppat.1009355.ref026","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1016\/0003-9861(79)90289-3","article-title":"Intracellular production of superoxide radical and of hydrogen peroxide by redox active compounds","volume":"196","author":"HM Hassan","year":"1979","journal-title":"Arch Biochem Biophys"},{"key":"ppat.1009355.ref027","doi-asserted-by":"crossref","first-page":"20960","DOI":"10.1074\/jbc.273.33.20960","article-title":"Biochemical characterization of WrbA, founding member of a new family of multimeric flavodoxin-like proteins","volume":"273","author":"R Grandori","year":"1998","journal-title":"J Biol Chem"},{"key":"ppat.1009355.ref028","doi-asserted-by":"crossref","first-page":"3498","DOI":"10.1128\/JB.188.10.3498-3506.2006","article-title":"WrbA from Escherichia coli and Archaeoglobus fulgidus is an NAD(P)H:Quinone oxidoreductase","volume":"188","author":"V Patridge E","year":"2006","journal-title":"J Bacteriol"},{"key":"ppat.1009355.ref029","doi-asserted-by":"crossref","first-page":"9101","DOI":"10.1128\/JB.01336-07","article-title":"Ferry JG, Einsle O. Crystal structure of the NADH:quinone oxidoreductase WrbA from Escherichia coli","volume":"189","author":"SLA Andrade","year":"2007","journal-title":"J Bacteriol"},{"key":"ppat.1009355.ref030","doi-asserted-by":"crossref","first-page":"1046","DOI":"10.1016\/j.bbapap.2017.05.005","article-title":"Structure, biochemical and kinetic properties of recombinant Pst2p from Saccharomyces cerevisiae, a FMN-dependent NAD(P)H:quinone oxidoreductase","volume":"1865","author":"K Koch","year":"2017","journal-title":"Biochim Biophys Acta\u2014Proteins Proteomics"},{"key":"ppat.1009355.ref031","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1021\/acs.jproteome.9b00299","article-title":"Global secretome characterization of the pathogenic yeast Candida glabrata","volume":"19","author":"M Rasheed","year":"2020","journal-title":"J Proteome Res"},{"key":"ppat.1009355.ref032","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/1471-2105-9-40","article-title":"I-TASSER server for protein 3D structure prediction","volume":"9","author":"Y. Zhang","year":"2008","journal-title":"BMC Bioinformatics"},{"key":"ppat.1009355.ref033","doi-asserted-by":"crossref","first-page":"1771","DOI":"10.1093\/bioinformatics\/btu097","article-title":"ZDOCK server: Interactive docking prediction of protein-protein complexes and symmetric multimers","volume":"30","author":"BG Pierce","year":"2014","journal-title":"Bioinformatics"},{"key":"ppat.1009355.ref034","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1002\/j.1460-2075.1993.tb05655.x","article-title":"Isolation and characterization of S. cerevisiae mutants defective in somatostatin expression: cloning and functional role of a yeast gene encoding an aspartyl protease in precursor processing at monobasic cleavage sites","volume":"12","author":"Y Bourbonnais","year":"1993","journal-title":"EMBO J"},{"key":"ppat.1009355.ref035","doi-asserted-by":"crossref","first-page":"966","DOI":"10.1111\/j.1567-1364.2006.00129.x","article-title":"Fungal yapsins and cell wall: A unique family of aspartic peptidases for a distinctive cellular function","volume":"6","author":"I Gagnon-Arsenault","year":"2006","journal-title":"FEMS Yeast Res"},{"key":"ppat.1009355.ref036","doi-asserted-by":"crossref","first-page":"1003","DOI":"10.1016\/j.cell.2006.03.042","article-title":"Global analysis of protein palmitoylation in yeast","volume":"125","author":"AF Roth","year":"2006","journal-title":"Cell"},{"key":"ppat.1009355.ref037","doi-asserted-by":"crossref","first-page":"1574","DOI":"10.1111\/j.1365-2958.2011.07542.x","article-title":"Molecular and proteomic analyses highlight the importance of ubiquitination for the stress resistance, metabolic adaptation, morphogenetic regulation and virulence of Candida albicans","volume":"79","author":"MD Leach","year":"2011","journal-title":"Mol Microbiol"},{"key":"ppat.1009355.ref038","doi-asserted-by":"crossref","first-page":"543","DOI":"10.1021\/bi061769c","article-title":"Role of flavin mononucleotide in the thermostability and oligomerization of Escherichia coli stress-defense protein WrbA","volume":"46","author":"A Natalello","year":"2007","journal-title":"Biochemistry"},{"key":"ppat.1009355.ref039","doi-asserted-by":"crossref","first-page":"688","DOI":"10.1074\/jbc.M509297200","article-title":"Glycosylphosphatidylinositol-anchored proteases of Candida albicans target proteins necessary for both cellular processes and host-pathogen interactions","volume":"281","author":"A Albrecht","year":"2006","journal-title":"J Biol Chem"},{"key":"ppat.1009355.ref040","doi-asserted-by":"crossref","first-page":"571","DOI":"10.1107\/S1744309107026103","article-title":"Crystallization and preliminary diffraction analysis of Escherichia coli WrbA in complex with its cofactor flavin mononucleotide","volume":"63","author":"J Wolfov\u00e1","year":"2007","journal-title":"Acta Crystallogr Sect F Struct Biol Cryst Commun"},{"key":"ppat.1009355.ref041","doi-asserted-by":"crossref","first-page":"8846","DOI":"10.1073\/pnas.92.19.8846","article-title":"The three-dimensional structure of NAD(P)H:quinone reductase a flavoprotein involved in cancer chemoprotection and chemotherapy: Mechanism of the two-electron reduction","volume":"92","author":"R Li","year":"1995","journal-title":"Proc Natl Acad Sci"},{"key":"ppat.1009355.ref042","doi-asserted-by":"crossref","first-page":"4691","DOI":"10.1111\/febs.12975","article-title":"Collapse of the native structure caused by a single amino acid exchange in human NAD(P)H:Quinone oxidoreductase","volume":"281","author":"WD Lienhart","year":"2014","journal-title":"FEBS J"},{"key":"ppat.1009355.ref043","first-page":"1","article-title":"Conformational dynamics is key to understanding loss-of-function of NQO1 cancer-associated polymorphisms and its correction by pharmacological ligands","volume":"6","author":"MC Encarnaci\u00f3n","year":"2016","journal-title":"Sci Rep"},{"key":"ppat.1009355.ref044","doi-asserted-by":"crossref","first-page":"5729","DOI":"10.1021\/bi034208j","article-title":"Hydroperoxidase II of Escherichia coli exhibits enhanced resistance to proteolytic cleavage compared to other catalases","volume":"42","author":"P Chelikani","year":"2003","journal-title":"Biochemistry"},{"key":"ppat.1009355.ref045","doi-asserted-by":"crossref","first-page":"13207","DOI":"10.1073\/pnas.2135385100","article-title":"The proteome of Saccharomyces cerevisiae mitochondria","volume":"100","author":"A Sickmann","year":"2003","journal-title":"Proc Natl Acad Sci"},{"key":"ppat.1009355.ref046","doi-asserted-by":"crossref","first-page":"1543","DOI":"10.1021\/pr050477f","article-title":"Toward the complete yeast mitochondrial proteome: Multidimensional separation techniques for mitochondrial proteomics","volume":"5","author":"J Reinders","year":"2006","journal-title":"J Proteome Res"},{"key":"ppat.1009355.ref047","doi-asserted-by":"crossref","first-page":"1075","DOI":"10.1083\/jcb.200806035","article-title":"Plasma membrane microdomains regulate turnover of transport proteins in yeast","volume":"183","author":"G Grossmann","year":"2008","journal-title":"J Cell Biol"},{"key":"ppat.1009355.ref048","doi-asserted-by":"crossref","first-page":"30433","DOI":"10.1074\/jbc.R800035200","article-title":"Proteases: Multifunctional enzymes in life and disease","volume":"283","author":"C L\u00f3pez-Ot\u00edn","year":"2008","journal-title":"J Biol Chem"},{"key":"ppat.1009355.ref049","doi-asserted-by":"crossref","first-page":"3072","DOI":"10.4049\/jimmunol.1003730","article-title":"The Facultative intracellular pathogen Candida glabrata subverts macrophage cytokine production and phagolysosome maturation","volume":"187","author":"K Seider","year":"2011","journal-title":"J Immunol"},{"key":"ppat.1009355.ref050","doi-asserted-by":"crossref","first-page":"e1002863","DOI":"10.1371\/journal.ppat.1002863","article-title":"Functional genomic analysis of Candida glabrata-macrophage interaction: role of chromatin remodeling in virulence","volume":"8","author":"MN Rai","year":"2012","journal-title":"PLoS Pathog"},{"key":"ppat.1009355.ref051","doi-asserted-by":"crossref","first-page":"5363","DOI":"10.1016\/S0021-9258(20)81897-3","article-title":"Ubiquinone content and respiratory burst activity of latex-filled phagolysosomes isolated from human neutrophils and evidence for the probable involvement of a third granule","volume":"258","author":"DR Crawford","year":"1983","journal-title":"J Biol Chem"},{"key":"ppat.1009355.ref052","doi-asserted-by":"crossref","first-page":"3129","DOI":"10.1099\/mic.0.27256-0","article-title":"Systematic identification in silico of covalently bound cell wall proteins and analysis of protein-polysaccharide linkages of the human pathogen Candida glabrata","volume":"150","author":"M Weig","year":"2004","journal-title":"Microbiology"},{"key":"ppat.1009355.ref053","doi-asserted-by":"crossref","first-page":"20847","DOI":"10.1074\/jbc.270.35.20847","article-title":"The yeast proprotein convertase encoded by YAP3 is a glycophosphatidylinositol-anchored protein that localizes to the plasma membrane","author":"J Ash","year":"1995","journal-title":"Journal of Biological Chemistry"},{"key":"ppat.1009355.ref054","doi-asserted-by":"crossref","first-page":"1364","DOI":"10.1128\/EC.4.8.1364-1374.2005","article-title":"Yapsins are a family of aspartyl proteases required for cell wall integrity in Saccharomyces cerevisiae","volume":"4","author":"DJ Krysan","year":"2005","journal-title":"Eukaryot Cell"},{"key":"ppat.1009355.ref055","doi-asserted-by":"crossref","first-page":"34311","DOI":"10.1074\/jbc.M111.264671","article-title":"The Rho1 GTPase-activating Protein CgBem2 Is Required for Survival of Azole Stress in Candida glabrata","volume":"286","author":"S Borah","year":"2011","journal-title":"J Biol Chem"},{"key":"ppat.1009355.ref056","doi-asserted-by":"crossref","first-page":"e1008620","DOI":"10.1371\/journal.pgen.1008620","article-title":"Histone H4 dosage modulates DNA damage response in the pathogenic yeast Candida glabrata via homologous recombination pathway","volume":"16","author":"K Kumar","journal-title":"PLoS Genet. 2020"},{"key":"ppat.1009355.ref057","doi-asserted-by":"crossref","first-page":"1281","DOI":"10.1128\/JB.00982-15","article-title":"WrpA is an atypical flavodoxin family protein under regulatory control of the Brucella abortus general stress response system","volume":"198","author":"J Herrou","year":"2016","journal-title":"J Bacteriol"},{"key":"ppat.1009355.ref058","doi-asserted-by":"crossref","first-page":"D442","DOI":"10.1093\/nar\/gky1106","article-title":"The PRIDE database and related tools and resources in 2019: improving support for quantification data","volume":"47","author":"Y Perez-Riverol","year":"2019","journal-title":"Nucleic Acids Res"}],"updated-by":[{"DOI":"10.1371\/journal.ppat.1009355","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2021,3,9]],"date-time":"2021-03-09T00:00:00Z","timestamp":1615248000000}}],"container-title":["PLOS Pathogens"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.ppat.1009355","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,3,9]],"date-time":"2021-03-09T18:39:31Z","timestamp":1615315171000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.ppat.1009355"}},"subtitle":[],"editor":[{"given":"Mira","family":"Edgerton","sequence":"first","affiliation":[],"role":[{"role":"editor","vocabulary":"crossref"}]}],"short-title":[],"issued":{"date-parts":[[2021,2,25]]},"references-count":58,"journal-issue":{"issue":"2","published-online":{"date-parts":[[2021,2,25]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.ppat.1009355","relation":{"new_version":[{"id-type":"doi","id":"10.1371\/journal.ppat.1009355","asserted-by":"object"}]},"ISSN":["1553-7374"],"issn-type":[{"value":"1553-7374","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,2,25]]}}}