{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,17]],"date-time":"2026-01-17T23:56:33Z","timestamp":1768694193818,"version":"3.49.0"},"reference-count":59,"publisher":"Oxford University Press (OUP)","issue":"11","license":[{"start":{"date-parts":[[2013,11,1]],"date-time":"2013-11-01T00:00:00Z","timestamp":1383264000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2013,12,30]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Secreted fungal effectors mediate plant\u2013fungus pathogenic interactions. These proteins are typically N-glycosylated, a common posttranslational modification affecting their location and function. N-glycosylation consists of the addition, and subsequent maturation, of an oligosaccharide core in the endoplasmic reticulum (ER) and Golgi apparatus. In this article, we show that two enzymes catalyzing specific stages of this pathway in maize smut (Ustilago maydis), glucosidase I (Gls1) and glucosidase II \u03b2-subunit (Gas2), are essential for its pathogenic interaction with maize (Zea mays). Gls1 is required for the initial stages of infection following appressorium penetration, and Gas2 is required for efficient fungal spreading inside infected tissues. While U. maydis \u0394gls1 cells induce strong plant defense responses, \u0394gas2 hyphae are able to repress them, showing that slight differences in the N-glycoprotein processing can determine the extent of plant\u2013fungus interactions. Interestingly, the calnexin protein, a central element of the ER quality control system for N-glycoproteins in eukaryotic cells, is essential for avoiding plant defense responses in cells with defective N-glycoproteins processing. Thus, N-glycoprotein maturation and this conserved checkpoint appear to play an important role in the establishment of an initial biotrophic state with the plant, which allows subsequent colonization.<\/jats:p>","DOI":"10.1105\/tpc.113.115691","type":"journal-article","created":{"date-parts":[[2013,11,27]],"date-time":"2013-11-27T04:37:17Z","timestamp":1385527037000},"page":"4676-4690","source":"Crossref","is-referenced-by-count":35,"title":["Endoplasmic Reticulum Glucosidases and Protein Quality Control Factors Cooperate to Establish Biotrophy in<i>Ustilago maydis<\/i>\u00a0"],"prefix":"10.1093","volume":"25","author":[{"given":"Alfonso","family":"Fern\u00e1ndez-\u00c1lvarez","sequence":"first","affiliation":[{"name":"Centro Andaluz de Biolog\u00eda del Desarrollo, Universidad Pablo de Olavide\u2013Consejo Superior de Investigaciones Cient\u00edficas, 41013 Seville, Spain"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Alberto","family":"El\u00edas-Villalobos","sequence":"additional","affiliation":[{"name":"Centro Andaluz de Biolog\u00eda del Desarrollo, Universidad Pablo de Olavide\u2013Consejo Superior de Investigaciones Cient\u00edficas, 41013 Seville, Spain"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Alberto","family":"Jim\u00e9nez-Mart\u00edn","sequence":"additional","affiliation":[{"name":"Centro Andaluz de Biolog\u00eda del Desarrollo, Universidad Pablo de Olavide\u2013Consejo Superior de Investigaciones Cient\u00edficas, 41013 Seville, Spain"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Miriam","family":"Mar\u00edn-Menguiano","sequence":"additional","affiliation":[{"name":"Centro Andaluz de Biolog\u00eda del Desarrollo, Universidad Pablo de Olavide\u2013Consejo Superior de Investigaciones Cient\u00edficas, 41013 Seville, Spain"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jos\u00e9 I.","family":"Ibeas","sequence":"additional","affiliation":[{"name":"Centro Andaluz de Biolog\u00eda del Desarrollo, Universidad Pablo de Olavide\u2013Consejo Superior de Investigaciones Cient\u00edficas, 41013 Seville, Spain"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2013,11,26]]},"reference":[{"key":"2021040912221624100_b1","doi-asserted-by":"crossref","first-page":"4","DOI":"10.1016\/S0304-4165(99)00165-8","article-title":"On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database","volume":"1473","author":"Apweiler","year":"1999","journal-title":"Biochim. Biophys. Acta"},{"key":"2021040912221624100_b2","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1093\/glycob\/10.5.487","article-title":"Two distinct domains of the beta-subunit of glucosidase II interact with the catalytic alpha-subunit","volume":"10","author":"Arendt","year":"2000","journal-title":"Glycobiology"},{"key":"2021040912221624100_b3","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1146\/annurev.ge.29.120195.001143","article-title":"Genetics of Ustilago maydis, a fungal pathogen that induces tumors in maize","volume":"29","author":"Banuett","year":"1995","journal-title":"Annu. Rev. Genet."},{"key":"2021040912221624100_b5","doi-asserted-by":"crossref","first-page":"2965","DOI":"10.1242\/dev.122.10.2965","article-title":"Discrete developmental stages during teliospore formation in the corn smut fungus, Ustilago maydis","volume":"122","author":"Banuett","year":"1996","journal-title":"Development"},{"key":"2021040912221624100_b6","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1007\/BF02423450","article-title":"Tagging pathogenicity genes in Ustilago maydis by restriction enzyme-mediated integration (REMI)","volume":"248","author":"B\u00f6lker","year":"1995","journal-title":"Mol. Gen. Genet."},{"key":"2021040912221624100_b7","doi-asserted-by":"crossref","first-page":"1717","DOI":"10.1002\/j.1460-2075.1992.tb05223.x","article-title":"Manipulating disulfide bond formation and protein folding in the endoplasmic reticulum","volume":"11","author":"Braakman","year":"1992","journal-title":"EMBO J."},{"key":"2021040912221624100_b8","doi-asserted-by":"crossref","first-page":"216","DOI":"10.1007\/s00438-004-1047-z","article-title":"A reverse genetic approach for generating gene replacement mutants in Ustilago maydis","volume":"272","author":"Brachmann","year":"2004","journal-title":"Mol. Genet. Genomics"},{"key":"2021040912221624100_b9","doi-asserted-by":"crossref","first-page":"2199","DOI":"10.1093\/emboj\/cdg198","article-title":"An unusual MAP kinase is required for efficient penetration of the plant surface by Ustilago maydis","volume":"22","author":"Brachmann","year":"2003","journal-title":"EMBO J."},{"key":"2021040912221624100_b10","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1146\/annurev-phyto-080508-081923","article-title":"Ustilago maydis as a pathogen","volume":"47","author":"Brefort","year":"2009","journal-title":"Annu. Rev. Phytopathol."},{"key":"2021040912221624100_b11","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1038\/nature10454","article-title":"Metabolic priming by a secreted fungal effector","volume":"478","author":"Djamei","year":"2011","journal-title":"Nature"},{"key":"2021040912221624100_b12","doi-asserted-by":"crossref","first-page":"e1000290","DOI":"10.1371\/journal.ppat.1000290","article-title":"Pep1, a secreted effector protein of Ustilago maydis, is required for successful invasion of plant cells","volume":"5","author":"Doehlemann","year":"2009","journal-title":"PLoS Pathog."},{"key":"2021040912221624100_b13","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1111\/j.1365-313X.2008.03590.x","article-title":"Reprogramming a maize plant: Transcriptional and metabolic changes induced by the fungal biotroph Ustilago maydis","volume":"56","author":"Doehlemann","year":"2008","journal-title":"Plant J."},{"key":"2021040912221624100_b14","doi-asserted-by":"crossref","first-page":"628","DOI":"10.1038\/sj.embor.embor864","article-title":"O-mannosylation precedes and potentially controls the N-glycosylation of a yeast cell wall glycoprotein","volume":"4","author":"Ecker","year":"2003","journal-title":"EMBO Rep."},{"key":"2021040912221624100_b15","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1038\/nrm1052","article-title":"Quality control in the endoplasmic reticulum","volume":"4","author":"Ellgaard","year":"2003","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"2021040912221624100_b16","doi-asserted-by":"crossref","first-page":"30701","DOI":"10.1016\/S0021-9258(18)43870-7","article-title":"Purification to homogeneity of UDP-glucose:glycoprotein glucosyltransferase from Schizosaccharomyces pombe and apparent absence of the enzyme for Saccharomyces cerevisiae","volume":"269","author":"Fern\u00e1ndez","year":"1994","journal-title":"J. Biol. Chem."},{"key":"2021040912221624100_b17","doi-asserted-by":"crossref","first-page":"3397","DOI":"10.1105\/tpc.109.065839","article-title":"The O-mannosyltransferase PMT4 is essential for normal appressorium formation and penetration in Ustilago maydis","volume":"21","author":"Fern\u00e1ndez-Alvarez","year":"2009","journal-title":"Plant Cell"},{"key":"2021040912221624100_b18","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1016\/j.fgb.2010.06.004","article-title":"Protein glycosylation in the phytopathogen Ustilago maydis: From core oligosaccharide synthesis to the ER glycoprotein quality control system, a genomic analysis","volume":"47","author":"Fern\u00e1ndez-Alvarez","year":"2010","journal-title":"Fungal Genet. Biol."},{"key":"2021040912221624100_b19","doi-asserted-by":"crossref","first-page":"e1002563","DOI":"10.1371\/journal.ppat.1002563","article-title":"Identification of O-mannosylated virulence factors in Ustilago maydis","volume":"8","author":"Fern\u00e1ndez-\u00c1lvarez","year":"2012","journal-title":"PLoS Pathog."},{"key":"2021040912221624100_b20","doi-asserted-by":"crossref","first-page":"647","DOI":"10.1016\/0092-8674(92)90141-X","article-title":"A two-component regulatory system for self\/non-self recognition in Ustilago maydis","volume":"68","author":"Gillissen","year":"1992","journal-title":"Cell"},{"key":"2021040912221624100_b21","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1146\/annurev.phyto.43.040204.135923","article-title":"Contrasting mechanisms of defense against biotrophic and necrotrophic pathogens","volume":"43","author":"Glazebrook","year":"2005","journal-title":"Annu. Rev. Phytopathol."},{"key":"2021040912221624100_b22","doi-asserted-by":"crossref","first-page":"913","DOI":"10.1073\/pnas.91.3.913","article-title":"Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control","volume":"91","author":"Hammond","year":"1994","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2021040912221624100_b23","doi-asserted-by":"crossref","first-page":"1019","DOI":"10.1146\/annurev.biochem.73.011303.073752","article-title":"Roles of N-linked glycans in the endoplasmic reticulum","volume":"73","author":"Helenius","year":"2004","journal-title":"Annu. Rev. Biochem."},{"key":"2021040912221624100_b24","doi-asserted-by":"crossref","first-page":"e1002684","DOI":"10.1371\/journal.ppat.1002684","article-title":"The Ustilago maydis effector Pep1 suppresses plant immunity by inhibition of host peroxidase activity","volume":"8","author":"Hemetsberger","year":"2012","journal-title":"PLoS Pathog."},{"key":"2021040912221624100_b25","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1016\/S0304-4165(98)00129-9","article-title":"Processing glycosidases of Saccharomyces cerevisiae","volume":"1426","author":"Herscovics","year":"1999","journal-title":"Biochim. Biophys. Acta"},{"key":"2021040912221624100_b26","doi-asserted-by":"crossref","first-page":"815","DOI":"10.1016\/j.femsyr.2004.04.002","article-title":"DER7, encoding alpha-glucosidase I is essential for degradation of malfolded glycoproteins of the endoplasmic reticulum","volume":"4","author":"Hitt","year":"2004","journal-title":"FEMS Yeast Res."},{"key":"2021040912221624100_b27","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1016\/0378-1119(87)90131-4","article-title":"A ten-minute DNA preparation from yeast efficiently releases autonomous plasmids for transformation of Escherichia coli","volume":"57","author":"Hoffman","year":"1987","journal-title":"Gene"},{"key":"2021040912221624100_b28","doi-asserted-by":"crossref","first-page":"49894","DOI":"10.1074\/jbc.M410121200","article-title":"The Lec23 Chinese hamster ovary mutant is a sensitive host for detecting mutations in alpha-glucosidase I that give rise to congenital disorder of glycosylation IIb (CDG IIb)","volume":"279","author":"Hong","year":"2004","journal-title":"J. Biol. Chem."},{"key":"2021040912221624100_b29","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1038\/nature05248","article-title":"Insights from the genome of the biotrophic fungal plant pathogen Ustilago maydis","volume":"444","author":"K\u00e4mper","year":"2006","journal-title":"Nature"},{"key":"2021040912221624100_b30","doi-asserted-by":"crossref","first-page":"1862","DOI":"10.1002\/pro.5560021108","article-title":"Kinetics of folding and association of differently glycosylated variants of invertase from Saccharomyces cerevisiae","volume":"2","author":"Kern","year":"1993","journal-title":"Protein Sci."},{"key":"2021040912221624100_b31","doi-asserted-by":"crossref","first-page":"1204","DOI":"10.1016\/j.cub.2011.06.044","article-title":"A secreted fungal effector of Glomus intraradices promotes symbiotic biotrophy","volume":"21","author":"Kloppholz","year":"2011","journal-title":"Curr. Biol."},{"key":"2021040912221624100_b32","doi-asserted-by":"crossref","first-page":"512","DOI":"10.1002\/pmic.201200414","article-title":"Glycocapture-based proteomics for secretome analysis","volume":"13","author":"Lai","year":"2013","journal-title":"Proteomics"},{"key":"2021040912221624100_b33","doi-asserted-by":"crossref","first-page":"3850","DOI":"10.1105\/tpc.109.072363","article-title":"Class I alpha-mannosidases are required for N-glycan processing and root development in Arabidopsis thaliana","volume":"21","author":"Liebminger","year":"2009","journal-title":"Plant Cell"},{"key":"2021040912221624100_b34","doi-asserted-by":"crossref","first-page":"27615","DOI":"10.1074\/jbc.271.44.27615","article-title":"Role of the cysteine residues in the alpha1,2-mannosidase involved in N-glycan biosynthesis in Saccharomyces cerevisiae. The conserved Cys340 and Cys385 residues form an essential disulfide bond","volume":"271","author":"Lipari","year":"1996","journal-title":"J. Biol. Chem."},{"key":"2021040912221624100_b35","doi-asserted-by":"crossref","first-page":"500","DOI":"10.1016\/j.semcdb.2010.03.006","article-title":"Protein quality control in the ER: The recognition of misfolded proteins","volume":"21","author":"M\u00e4\u00e4tt\u00e4nen","year":"2010","journal-title":"Semin. Cell Dev. Biol."},{"key":"2021040912221624100_b36","doi-asserted-by":"crossref","first-page":"895","DOI":"10.1111\/j.1365-2958.2008.06567.x","article-title":"Physical-chemical plant-derived signals induce differentiation in Ustilago maydis","volume":"71","author":"Mendoza-Mendoza","year":"2009","journal-title":"Mol. Microbiol."},{"key":"2021040912221624100_b37","doi-asserted-by":"crossref","first-page":"2293","DOI":"10.1105\/tpc.107.052332","article-title":"An Ustilago maydis gene involved in H2O2 detoxification is required for virulence","volume":"19","author":"Molina","year":"2007","journal-title":"Plant Cell"},{"key":"2021040912221624100_b38","doi-asserted-by":"crossref","first-page":"2184","DOI":"10.1128\/EC.00350-07","article-title":"Endoplasmic reticulum alpha-glycosidases of Candida albicans are required for N glycosylation, cell wall integrity, and normal host-fungus interaction","volume":"6","author":"Mora-Montes","year":"2007","journal-title":"Eukaryot. Cell"},{"key":"2021040912221624100_b39","doi-asserted-by":"crossref","first-page":"e1003177","DOI":"10.1371\/journal.ppat.1003177","article-title":"Compatibility in the Ustilago maydis-maize interaction requires inhibition of host cysteine proteases by the fungal effector Pit2","volume":"9","author":"Mueller","year":"2013","journal-title":"PLoS Pathog."},{"issue":"Suppl 1","key":"2021040912221624100_b40","doi-asserted-by":"crossref","first-page":"S63","DOI":"10.1016\/j.fgb.2008.03.012","article-title":"The secretome of the maize pathogen Ustilago maydis","volume":"45","author":"Mueller","year":"2008","journal-title":"Fungal Genet. Biol."},{"key":"2021040912221624100_b41","doi-asserted-by":"crossref","first-page":"1348","DOI":"10.1111\/j.1365-2958.2008.06242.x","article-title":"Systematic functional analysis of calcium-signalling proteins in the genome of the rice-blast fungus, Magnaporthe oryzae, using a high-throughput RNA-silencing system","volume":"68","author":"Nguyen","year":"2008","journal-title":"Mol. Microbiol."},{"key":"2021040912221624100_b42","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1146\/annurev.genet.37.110801.142628","article-title":"Recognition and response in the plant immune system","volume":"37","author":"Nimchuk","year":"2003","journal-title":"Annu. Rev. Genet."},{"key":"2021040912221624100_b43","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1146\/annurev.biochem.69.1.69","article-title":"Protein glucosylation and its role in protein folding","volume":"69","author":"Parodi","year":"2000","journal-title":"Annu. Rev. Biochem."},{"key":"2021040912221624100_b44","doi-asserted-by":"crossref","first-page":"e28865","DOI":"10.1371\/journal.pone.0028865","article-title":"Impact of the lectin chaperone calnexin on the stress response, virulence and proteolytic secretome of the fungal pathogen Aspergillus fumigatus","volume":"6","author":"Powers-Fletcher","year":"2011","journal-title":"PLoS ONE"},{"key":"2021040912221624100_b45","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1093\/glycob\/7.3.399","article-title":"Structure-function relationships in glucosidase I: Amino acids involved in binding the substrate to the enzyme","volume":"7","author":"Romaniouk","year":"1997","journal-title":"Glycobiology"},{"key":"2021040912221624100_b46","doi-asserted-by":"crossref","first-page":"11071","DOI":"10.1074\/jbc.275.15.11071","article-title":"Mutation of Arg(273) to Leu alters the specificity of the yeast N-glycan processing class I alpha1,2-mannosidase","volume":"275","author":"Romero","year":"2000","journal-title":"J. Biol. Chem."},{"key":"2021040912221624100_b47","doi-asserted-by":"crossref","first-page":"3532","DOI":"10.1105\/tpc.105.036285","article-title":"Endoplasmic reticulum glucosidase II is required for pathogenicity of Ustilago maydis","volume":"17","author":"Schirawski","year":"2005","journal-title":"Plant Cell"},{"key":"2021040912221624100_b48","doi-asserted-by":"crossref","first-page":"1546","DOI":"10.1126\/science.1195330","article-title":"Pathogenicity determinants in smut fungi revealed by genome comparison","volume":"330","author":"Schirawski","year":"2010","journal-title":"Science"},{"key":"2021040912221624100_b49","doi-asserted-by":"crossref","first-page":"576","DOI":"10.1016\/j.sbi.2011.08.005","article-title":"Mechanisms and principles of N-linked protein glycosylation","volume":"21","author":"Schwarz","year":"2011","journal-title":"Curr. Opin. Struct. Biol."},{"key":"2021040912221624100_b50","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1126\/science.1185775","article-title":"Maize tumors caused by Ustilago maydis require organ-specific genes in host and pathogen","volume":"328","author":"Skibbe","year":"2010","journal-title":"Science"},{"key":"2021040912221624100_b52","doi-asserted-by":"crossref","first-page":"582","DOI":"10.1016\/j.cbpa.2009.09.011","article-title":"Chemical approaches toward understanding glycan-mediated protein quality control","volume":"13","author":"Takeda","year":"2009","journal-title":"Curr. Opin. Chem. Biol."},{"key":"2021040912221624100_b53","doi-asserted-by":"crossref","first-page":"1596","DOI":"10.1093\/molbev\/msm092","article-title":"MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0","volume":"24","author":"Tamura","year":"2007","journal-title":"Mol. Biol. Evol."},{"key":"2021040912221624100_b54","doi-asserted-by":"crossref","first-page":"27509","DOI":"10.1074\/jbc.271.44.27509","article-title":"Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit","volume":"271","author":"Trombetta","year":"1996","journal-title":"J. Biol. Chem."},{"key":"2021040912221624100_b55","doi-asserted-by":"crossref","first-page":"1948","DOI":"10.1105\/tpc.108.059394","article-title":"The Cladosporium fulvum virulence protein Avr2 inhibits host proteases required for basal defense","volume":"20","author":"van Esse","year":"2008","journal-title":"Plant Cell"},{"key":"2021040912221624100_b56","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1093\/glycob\/cwf050","article-title":"Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb)","volume":"12","author":"V\u00f6lker","year":"2002","journal-title":"Glycobiology"},{"key":"2021040912221624100_b57","doi-asserted-by":"crossref","first-page":"6325","DOI":"10.1074\/jbc.M510455200","article-title":"Yeast GTB1 encodes a subunit of glucosidase II required for glycoprotein processing in the endoplasmic reticulum","volume":"281","author":"Wilkinson","year":"2006","journal-title":"J. Biol. Chem."},{"key":"2021040912221624100_b59","doi-asserted-by":"crossref","first-page":"681","DOI":"10.1042\/bj3220681","article-title":"Oxidative burst: An early plant response to pathogen infection","volume":"322","author":"Wojtaszek","year":"1997","journal-title":"Biochem. J."},{"key":"2021040912221624100_b60","doi-asserted-by":"crossref","first-page":"3121","DOI":"10.1074\/jbc.R400036200","article-title":"Unraveling the mechanism of protein N-glycosylation","volume":"280","author":"Yan","year":"2005","journal-title":"J. Biol. Chem."},{"key":"2021040912221624100_b61","doi-asserted-by":"crossref","first-page":"5021","DOI":"10.1074\/jbc.274.8.5021","article-title":"The Ost1p subunit of yeast oligosaccharyl transferase recognizes the peptide glycosylation site sequence, -Asn-X-Ser\/Thr-","volume":"274","author":"Yan","year":"1999","journal-title":"J. Biol. Chem."},{"key":"2021040912221624100_b62","doi-asserted-by":"crossref","first-page":"2157","DOI":"10.1099\/mic.0.027490-0","article-title":"Comparative proteomic analysis of an Aspergillus fumigatus mutant deficient in glucosidase I (AfCwh41)","volume":"155","author":"Zhang","year":"2009","journal-title":"Microbiology"}],"container-title":["The Plant Cell"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/academic.oup.com\/plcell\/article-pdf\/25\/11\/4676\/36999705\/plcell_v25_11_4676.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"http:\/\/academic.oup.com\/plcell\/article-pdf\/25\/11\/4676\/36999705\/plcell_v25_11_4676.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,3,17]],"date-time":"2022-03-17T19:05:46Z","timestamp":1647543946000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/plcell\/article\/25\/11\/4676\/6096779"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2013,11,1]]},"references-count":59,"journal-issue":{"issue":"11","published-online":{"date-parts":[[2013,11,26]]},"published-print":{"date-parts":[[2013,12,30]]}},"URL":"https:\/\/doi.org\/10.1105\/tpc.113.115691","relation":{},"ISSN":["1532-298X","1040-4651"],"issn-type":[{"value":"1532-298X","type":"electronic"},{"value":"1040-4651","type":"print"}],"subject":[],"published-other":{"date-parts":[[2013,11,1]]},"published":{"date-parts":[[2013,11,1]]}}}