{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T02:15:35Z","timestamp":1790734535107,"version":"4.1.0"},"reference-count":33,"publisher":"National Academy of Sciences","issue":"25","license":[{"start":{"date-parts":[[2020,12,8]],"date-time":"2020-12-08T00:00:00Z","timestamp":1607385600000},"content-version":"vor","delay-in-days":183,"URL":"https:\/\/www.pnas.org\/site\/aboutpnas\/licenses.xhtml"}],"funder":[{"DOI":"10.13039\/100000002","name":"HHS | National Institutes of Health","doi-asserted-by":"publisher","award":["1ZIAHD008893-09"],"award-info":[{"award-number":["1ZIAHD008893-09"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000024","name":"Gouvernement du Canada | Canadian Institutes of Health Research","doi-asserted-by":"publisher","award":["MOP-48370"],"award-info":[{"award-number":["MOP-48370"]}],"id":[{"id":"10.13039\/501100000024","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100006710","name":"Wayne State University","doi-asserted-by":"publisher","award":["Startup funding"],"award-info":[{"award-number":["Startup funding"]}],"id":[{"id":"10.13039\/100006710","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2020,6,23]]},"abstract":"<jats:p>\n                    During infection, the bacterial pathogen\n                    <jats:italic>Legionella pneumophila<\/jats:italic>\n                    manipulates a variety of host cell signaling pathways, including the Hippo pathway which controls cell proliferation and differentiation in eukaryotes. Our previous studies revealed that\n                    <jats:italic>L. pneumophila<\/jats:italic>\n                    encodes the effector kinase LegK7 which phosphorylates MOB1A, a highly conserved scaffold protein of the Hippo pathway. Here, we show that MOB1A, in addition to being a substrate of LegK7, also functions as an allosteric activator of its kinase activity. A crystallographic analysis of the LegK7\u2013MOB1A complex revealed that the N-terminal half of LegK7 is structurally similar to eukaryotic protein kinases, and that MOB1A directly binds to the LegK7 kinase domain. Substitution of interface residues critical for complex formation abrogated allosteric activation of LegK7 both in vitro and within cells and diminished MOB1A phosphorylation. Importantly, the N-terminal extension (NTE) of MOB1A not only regulated complex formation with LegK7 but also served as a docking site for downstream substrates such as the transcriptional coregulator YAP1. Deletion of the NTE from MOB1A or addition of NTE peptides as binding competitors attenuated YAP1 recruitment to and phosphorylation by LegK7. By providing mechanistic insight into the formation and regulation of the LegK7\u2013MOB1A complex, our study unravels a sophisticated molecular mimicry strategy that is used by\n                    <jats:italic>L. pneumophila<\/jats:italic>\n                    to take control of the host cell Hippo pathway.\n                  <\/jats:p>","DOI":"10.1073\/pnas.2000497117","type":"journal-article","created":{"date-parts":[[2020,6,8]],"date-time":"2020-06-08T20:35:24Z","timestamp":1591648524000},"page":"14433-14443","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":20,"title":["The\n                    <i>Legionella<\/i>\n                    kinase LegK7 exploits the Hippo pathway scaffold protein MOB1A for allostery and substrate phosphorylation"],"prefix":"10.1073","volume":"117","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-8352-7152","authenticated-orcid":false,"given":"Pei-Chung","family":"Lee","sequence":"first","affiliation":[{"name":"Division of Molecular and Cellular Biology, Eunice Kennedy Shriver National Institute of Child Health and Human Development, NIH, Bethesda, MD 20892;"},{"name":"Department of Biological Sciences, College of Liberal Arts and Sciences, Wayne State University, Detroit, MI 48202;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4260-4414","authenticated-orcid":false,"given":"Ksenia","family":"Beyrakhova","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, University of Saskatchewan, Saskatoon, SK S7N5E5, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Caishuang","family":"Xu","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, University of Saskatchewan, Saskatoon, SK S7N5E5, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0854-0891","authenticated-orcid":false,"given":"Michal T.","family":"Boniecki","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, University of Saskatchewan, Saskatoon, SK S7N5E5, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mitchell H.","family":"Lee","sequence":"additional","affiliation":[{"name":"Division of Molecular and Cellular Biology, Eunice Kennedy Shriver National Institute of Child Health and Human Development, NIH, Bethesda, MD 20892;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3338-5141","authenticated-orcid":false,"given":"Chisom J.","family":"Onu","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, College of Liberal Arts and Sciences, Wayne State University, Detroit, MI 48202;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrey M.","family":"Grishin","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, University of Saskatchewan, Saskatoon, SK S7N5E5, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6971-7451","authenticated-orcid":false,"given":"Matthias P.","family":"Machner","sequence":"additional","affiliation":[{"name":"Division of Molecular and Cellular Biology, Eunice Kennedy Shriver National Institute of Child Health and Human Development, NIH, Bethesda, MD 20892;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Miroslaw","family":"Cygler","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, University of Saskatchewan, Saskatoon, SK S7N5E5, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2020,6,8]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"crossref","first-page":"1912","DOI":"10.1126\/science.1075762","article-title":"The protein kinase complement of the human genome","volume":"298","author":"Manning G.","year":"2002","unstructured":"G. Manning, D. B. Whyte, R. Martinez, T. Hunter, S. Sudarsanam, The protein kinase complement of the human genome. Science 298, 1912\u20131934 (2002).","journal-title":"Science"},{"key":"e_1_3_4_2_2","doi-asserted-by":"crossref","first-page":"S6","DOI":"10.1186\/1477-5956-9-S1-S6","article-title":"Prediction of 492 human protein kinase substrate specificities","volume":"9","author":"Safaei J.","year":"2011","unstructured":"J. Safaei, J. Ma\u0148uch, A. Gupta, L. Stacho, S. Pelech, Prediction of 492 human protein kinase substrate specificities. Proteome Sci. 9 (suppl. 1), S6 (2011).","journal-title":"Proteome Sci."},{"key":"e_1_3_4_3_2","doi-asserted-by":"crossref","first-page":"604","DOI":"10.1002\/pro.2636","article-title":"Structural insight into effector proteins of gram-negative bacterial pathogens that modulate the phosphoproteome of their host","volume":"24","author":"Grishin A. M.","year":"2015","unstructured":"A. M. Grishin, K. A. Beyrakhova, M. Cygler, Structural insight into effector proteins of gram-negative bacterial pathogens that modulate the phosphoproteome of their host. Protein Sci. 24, 604\u2013620 (2015).","journal-title":"Protein Sci."},{"key":"e_1_3_4_4_2","doi-asserted-by":"crossref","first-page":"749","DOI":"10.1002\/iub.2040","article-title":"Thinking outside of the cell: Secreted protein kinases in bacteria, parasites, and mammals","volume":"71","author":"Park B. C.","year":"2019","unstructured":"B. C. Park, M. Reese, V. S. Tagliabracci, Thinking outside of the cell: Secreted protein kinases in bacteria, parasites, and mammals. IUBMB Life 71, 749\u2013759 (2019).","journal-title":"IUBMB Life"},{"key":"e_1_3_4_5_2","doi-asserted-by":"crossref","first-page":"1433","DOI":"10.1016\/j.cellsig.2011.04.007","article-title":"MOB control: Reviewing a conserved family of kinase regulators","volume":"23","author":"Hergovich A.","year":"2011","unstructured":"A. Hergovich, MOB control: Reviewing a conserved family of kinase regulators. Cell. Signal. 23, 1433\u20131440 (2011).","journal-title":"Cell. Signal."},{"key":"e_1_3_4_6_2","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1101\/gad.274027.115","article-title":"Mechanisms of Hippo pathway regulation","volume":"30","author":"Meng Z.","year":"2016","unstructured":"Z. Meng, T. Moroishi, K. L. Guan, Mechanisms of Hippo pathway regulation. Genes Dev. 30, 1\u201317 (2016).","journal-title":"Genes Dev."},{"key":"e_1_3_4_7_2","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1016\/j.cub.2008.02.006","article-title":"MOBKL1A\/MOBKL1B phosphorylation by MST1 and MST2 inhibits cell proliferation","volume":"18","author":"Praskova M.","year":"2008","unstructured":"M. Praskova, F. Xia, J. Avruch, MOBKL1A\/MOBKL1B phosphorylation by MST1 and MST2 inhibits cell proliferation. Curr. Biol. 18, 311\u2013321 (2008).","journal-title":"Curr. Biol."},{"key":"e_1_3_4_8_2","doi-asserted-by":"crossref","first-page":"1416","DOI":"10.1101\/gad.264929.115","article-title":"Structural basis for Mob1-dependent activation of the core Mst-Lats kinase cascade in Hippo signaling","volume":"29","author":"Ni L.","year":"2015","unstructured":"L. Ni, Y. Zheng, M. Hara, D. Pan, X. Luo, Structural basis for Mob1-dependent activation of the core Mst-Lats kinase cascade in Hippo signaling. Genes Dev. 29, 1416\u20131431 (2015).","journal-title":"Genes Dev."},{"key":"e_1_3_4_9_2","doi-asserted-by":"crossref","first-page":"695","DOI":"10.1038\/s41467-017-00795-y","article-title":"Stable MOB1 interaction with Hippo\/MST is not essential for development and tissue growth control","volume":"8","author":"Kulaberoglu Y.","year":"2017","unstructured":"Y. Kulaberoglu ., Stable MOB1 interaction with Hippo\/MST is not essential for development and tissue growth control. Nat. Commun. 8, 695 (2017).","journal-title":"Nat. Commun."},{"key":"e_1_3_4_10_2","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1186\/2045-3701-3-32","article-title":"Regulation and functions of mammalian LATS\/NDR kinases: Looking beyond canonical Hippo signalling","volume":"3","author":"Hergovich A.","year":"2013","unstructured":"A. Hergovich, Regulation and functions of mammalian LATS\/NDR kinases: Looking beyond canonical Hippo signalling. Cell Biosci. 3, 32 (2013).","journal-title":"Cell Biosci."},{"key":"e_1_3_4_11_2","doi-asserted-by":"crossref","first-page":"4505","DOI":"10.1172\/JCI63735","article-title":"Cancer susceptibility and embryonic lethality in Mob1a\/1b double-mutant mice","volume":"122","author":"Nishio M.","year":"2012","unstructured":"M. Nishio ., Cancer susceptibility and embryonic lethality in Mob1a\/1b double-mutant mice. J. Clin. Invest. 122, 4505\u20134518 (2012).","journal-title":"J. Clin. Invest."},{"key":"e_1_3_4_12_2","doi-asserted-by":"crossref","first-page":"28488","DOI":"10.1038\/srep28488","article-title":"Structural basis for autoinhibition and its relief of MOB1 in the Hippo pathway","volume":"6","author":"Kim S.-Y.","year":"2016","unstructured":"S.-Y. Kim, Y. Tachioka, T. Mori, T. Hakoshima, Structural basis for autoinhibition and its relief of MOB1 in the Hippo pathway. Sci. Rep. 6, 28488 (2016).","journal-title":"Sci. Rep."},{"key":"e_1_3_4_13_2","doi-asserted-by":"crossref","first-page":"429","DOI":"10.1016\/j.chom.2018.08.004","article-title":"The Legionella effector kinase LegK7 hijacks the host Hippo pathway to promote infection","volume":"24","author":"Lee P.-C.","year":"2018","unstructured":"P.-C. Lee, M. P. Machner, The Legionella effector kinase LegK7 hijacks the host Hippo pathway to promote infection. Cell Host Microbe 24, 429\u2013438.e6 (2018).","journal-title":"Cell Host Microbe"},{"key":"e_1_3_4_14_2","doi-asserted-by":"crossref","first-page":"1189","DOI":"10.1056\/NEJM197712012972201","article-title":"Legionnaires\u2019 disease: Description of an epidemic of pneumonia","volume":"297","author":"Fraser D. W.","year":"1977","unstructured":"D. W. Fraser ., Legionnaires\u2019 disease: Description of an epidemic of pneumonia. N. Engl. J. Med. 297, 1189\u20131197 (1977).","journal-title":"N. Engl. J. Med."},{"key":"e_1_3_4_15_2","doi-asserted-by":"crossref","first-page":"1197","DOI":"10.1056\/NEJM197712012972202","article-title":"Legionnaires\u2019 disease: Isolation of a bacterium and demonstration of its role in other respiratory disease","volume":"297","author":"McDade J. E.","year":"1977","unstructured":"J. E. McDade ., Legionnaires\u2019 disease: Isolation of a bacterium and demonstration of its role in other respiratory disease. N. Engl. J. Med. 297, 1197\u20131203 (1977).","journal-title":"N. Engl. J. Med."},{"key":"e_1_3_4_16_2","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1038\/nmeth1048","article-title":"A semisynthetic epitope for kinase substrates","volume":"4","author":"Allen J. J.","year":"2007","unstructured":"J. J. Allen ., A semisynthetic epitope for kinase substrates. Nat. Methods 4, 511\u2013516 (2007).","journal-title":"Nat. Methods"},{"key":"e_1_3_4_17_2","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1016\/j.bbrc.2006.03.244","article-title":"The human tumour suppressor LATS1 is activated by human MOB1 at the membrane","volume":"345","author":"Hergovich A.","year":"2006","unstructured":"A. Hergovich, D. Schmitz, B. A. Hemmings, The human tumour suppressor LATS1 is activated by human MOB1 at the membrane. Biochem. Biophys. Res. Commun. 345, 50\u201358 (2006).","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"e_1_3_4_18_2","doi-asserted-by":"crossref","first-page":"1163","DOI":"10.1016\/S0969-2126(03)00182-5","article-title":"Crystal structure of a human Mob1 protein: Toward understanding Mob-regulated cell cycle pathways","volume":"11","author":"Stavridi E. S.","year":"2003","unstructured":"E. S. Stavridi ., Crystal structure of a human Mob1 protein: Toward understanding Mob-regulated cell cycle pathways. Structure 11, 1163\u20131170 (2003).","journal-title":"Structure"},{"key":"e_1_3_4_19_2","doi-asserted-by":"crossref","first-page":"1098","DOI":"10.1074\/mcp.M116.065490","article-title":"MOB1 mediated phospho-recognition in the core mammalian Hippo pathway","volume":"16","author":"Couzens A. L.","year":"2017","unstructured":"A. L. Couzens ., MOB1 mediated phospho-recognition in the core mammalian Hippo pathway. Mol. Cell. Proteomics 16, 1098\u20131110 (2017).","journal-title":"Mol. Cell. Proteomics"},{"key":"e_1_3_4_20_2","doi-asserted-by":"crossref","first-page":"576","DOI":"10.1096\/fasebj.9.8.7768349","article-title":"Protein kinases 6. The eukaryotic protein kinase superfamily: Kinase (catalytic) domain structure and classification","volume":"9","author":"Hanks S. K.","year":"1995","unstructured":"S. K. Hanks, T. Hunter, Protein kinases 6. The eukaryotic protein kinase superfamily: Kinase (catalytic) domain structure and classification. FASEB J. 9, 576\u2013596 (1995).","journal-title":"FASEB J."},{"key":"e_1_3_4_21_2","doi-asserted-by":"crossref","first-page":"2209","DOI":"10.1021\/cr000225s","article-title":"Structural basis for control by phosphorylation","volume":"101","author":"Johnson L. N.","year":"2001","unstructured":"L. N. Johnson, R. J. Lewis, Structural basis for control by phosphorylation. Chem. Rev. 101, 2209\u20132242 (2001).","journal-title":"Chem. Rev."},{"key":"e_1_3_4_22_2","doi-asserted-by":"crossref","first-page":"2780","DOI":"10.1093\/bioinformatics\/btn507","article-title":"Searching protein structure databases with DaliLite v.3","volume":"24","author":"Holm L.","year":"2008","unstructured":"L. Holm, S. K\u00e4\u00e4ri\u00e4inen, P. Rosenstr\u00f6m, A. Schenkel, Searching protein structure databases with DaliLite v.3. Bioinformatics 24, 2780\u20132781 (2008).","journal-title":"Bioinformatics"},{"key":"e_1_3_4_23_2","doi-asserted-by":"crossref","first-page":"6130","DOI":"10.1074\/jbc.M409123200","article-title":"Structural basis of constitutive activity and a unique nucleotide binding mode of human Pim-1 kinase","volume":"280","author":"Qian K. C.","year":"2005","unstructured":"K. C. Qian ., Structural basis of constitutive activity and a unique nucleotide binding mode of human Pim-1 kinase. J. Biol. Chem. 280, 6130\u20136137 (2005).","journal-title":"J. Biol. Chem."},{"key":"e_1_3_4_24_2","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1016\/j.molcel.2016.04.001","article-title":"Structural basis for noncanonical substrate recognition of cofilin\/ADF proteins by LIM kinases","volume":"62","author":"Hamill S.","year":"2016","unstructured":"S. Hamill, H. J. Lou, B. E. Turk, T. J. Boggon, Structural basis for noncanonical substrate recognition of cofilin\/ADF proteins by LIM kinases. Mol. Cell 62, 397\u2013408 (2016).","journal-title":"Mol. Cell"},{"key":"e_1_3_4_25_2","doi-asserted-by":"crossref","first-page":"942","DOI":"10.1021\/acsmedchemlett.5b00279","article-title":"Discovery and structure enabled synthesis of 2,6-diaminopyrimidin-4-one IRAK4 inhibitors","volume":"6","author":"Seganish W. M.","year":"2015","unstructured":"W. M. Seganish ., Discovery and structure enabled synthesis of 2,6-diaminopyrimidin-4-one IRAK4 inhibitors. ACS Med. Chem. Lett. 6, 942\u2013947 (2015).","journal-title":"ACS Med. Chem. Lett."},{"key":"e_1_3_4_26_2","doi-asserted-by":"crossref","first-page":"2256","DOI":"10.1107\/S0907444904026460","article-title":"Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions","volume":"60","author":"Krissinel E.","year":"2004","unstructured":"E. Krissinel, K. Henrick, Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr. D Biol. Crystallogr. 60, 2256\u20132268 (2004).","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"e_1_3_4_27_2","doi-asserted-by":"crossref","first-page":"E2096","DOI":"10.1073\/pnas.1620813114","article-title":"Structural basis of autoregulatory scaffolding by apoptosis signal-regulating kinase 1","volume":"114","author":"Weijman J. F.","year":"2017","unstructured":"J. F. Weijman ., Structural basis of autoregulatory scaffolding by apoptosis signal-regulating kinase 1. Proc. Natl. Acad. Sci. U.S.A. 114, E2096\u2013E2105 (2017).","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"e_1_3_4_28_2","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1042\/BJ20040025","article-title":"Regulation of the MST1 kinase by autophosphorylation, by the growth inhibitory proteins, RASSF1 and NORE1, and by Ras","volume":"381","author":"Praskova M.","year":"2004","unstructured":"M. Praskova, A. Khoklatchev, S. Ortiz-Vega, J. Avruch, Regulation of the MST1 kinase by autophosphorylation, by the growth inhibitory proteins, RASSF1 and NORE1, and by Ras. Biochem. J. 381, 453\u2013462 (2004).","journal-title":"Biochem. J."},{"key":"e_1_3_4_29_2","first-page":"352ra108","article-title":"Pharmacological targeting of kinases MST1 and MST2 augments tissue repair and regeneration","volume":"8","author":"Fan F.","year":"2016","unstructured":"F. Fan ., Pharmacological targeting of kinases MST1 and MST2 augments tissue repair and regeneration. Sci. Transl. Med. 8, 352ra108 (2016).","journal-title":"Sci. Transl. Med."},{"key":"e_1_3_4_30_2","doi-asserted-by":"crossref","first-page":"4281","DOI":"10.1038\/onc.2008.66","article-title":"Threonine 74 of MOB1 is a putative key phosphorylation site by MST2 to form the scaffold to activate nuclear Dbf2-related kinase 1","volume":"27","author":"Hirabayashi S.","year":"2008","unstructured":"S. Hirabayashi ., Threonine 74 of MOB1 is a putative key phosphorylation site by MST2 to form the scaffold to activate nuclear Dbf2-related kinase 1. Oncogene 27, 4281\u20134292 (2008).","journal-title":"Oncogene"},{"key":"e_1_3_4_31_2","doi-asserted-by":"crossref","first-page":"2096","DOI":"10.1016\/j.jmb.2018.05.015","article-title":"Regulation of Shigella effector kinase OspG through modulation of its dynamic properties","volume":"430","author":"Grishin A. M.","year":"2018","unstructured":"A. M. Grishin ., Regulation of Shigella effector kinase OspG through modulation of its dynamic properties. J. Mol. Biol. 430, 2096\u20132112 (2018).","journal-title":"J. Mol. Biol."},{"key":"e_1_3_4_32_2","doi-asserted-by":"crossref","first-page":"878","DOI":"10.1016\/j.str.2014.04.010","article-title":"Structural basis for the inhibition of host protein ubiquitination by Shigella effector kinase OspG","volume":"22","author":"Grishin A. M.","year":"2014","unstructured":"A. M. Grishin ., Structural basis for the inhibition of host protein ubiquitination by Shigella effector kinase OspG. Structure 22, 878\u2013888 (2014).","journal-title":"Structure"},{"key":"e_1_3_4_33_2","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/j.celrep.2011.11.004","article-title":"Premetazoan origin of the Hippo signaling pathway","volume":"1","author":"Seb\u00e9-Pedr\u00f3s A.","year":"2012","unstructured":"A. Seb\u00e9-Pedr\u00f3s, Y. Zheng, I. Ruiz-Trillo, D. Pan, Premetazoan origin of the Hippo signaling pathway. Cell Rep. 1, 13\u201320 (2012).","journal-title":"Cell Rep."}],"container-title":["Proceedings of the National Academy of Sciences"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.pnas.org\/syndication\/doi\/10.1073\/pnas.2000497117","content-type":"unspecified","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pnas.org\/doi\/pdf\/10.1073\/pnas.2000497117","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,6,7]],"date-time":"2022-06-07T17:40:56Z","timestamp":1654623656000},"score":1,"resource":{"primary":{"URL":"https:\/\/pnas.org\/doi\/full\/10.1073\/pnas.2000497117"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,6,8]]},"references-count":33,"journal-issue":{"issue":"25","published-print":{"date-parts":[[2020,6,23]]}},"alternative-id":["10.1073\/pnas.2000497117"],"URL":"https:\/\/doi.org\/10.1073\/pnas.2000497117","relation":{},"ISSN":["0027-8424","1091-6490"],"issn-type":[{"value":"0027-8424","type":"print"},{"value":"1091-6490","type":"electronic"}],"subject":[],"published":{"date-parts":[[2020,6,8]]},"assertion":[{"value":"2020-06-08","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}