{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,19]],"date-time":"2026-10-19T17:56:38Z","timestamp":1792432598917,"version":"4.5.0"},"reference-count":58,"publisher":"Elsevier BV","issue":"37","license":[{"start":{"date-parts":[[2017,9,1]],"date-time":"2017-09-01T00:00:00Z","timestamp":1504224000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,9,3]],"date-time":"2020-09-03T00:00:00Z","timestamp":1599091200000},"content-version":"vor","delay-in-days":1098,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2017,9]]},"DOI":"10.1074\/jbc.m117.791343","type":"journal-article","created":{"date-parts":[[2017,8,5]],"date-time":"2017-08-05T00:30:33Z","timestamp":1501893033000},"page":"15561-15576","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":70,"title":["Pyruvate kinase M knockdown\u2013induced signaling via AMP-activated protein kinase promotes mitochondrial biogenesis, autophagy, and cancer cell survival"],"prefix":"10.1016","volume":"292","author":[{"given":"Gopinath","family":"Prakasam","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rajnish Kumar","family":"Singh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mohammad Askandar","family":"Iqbal","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sunil Kumar","family":"Saini","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ashu Bhan","family":"Tiku","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rameshwar N.K.","family":"Bamezai","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.M117.791343_bib1","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1126\/science.123.3191.309","article-title":"On the origin of cancer cells","volume":"123","author":"Warburg","year":"1956","journal-title":"Science"},{"key":"10.1074\/jbc.M117.791343_bib2","doi-asserted-by":"crossref","first-page":"1029","DOI":"10.1126\/science.1160809","article-title":"Understanding the Warburg effect: The metabolic requirements of cell proliferation","volume":"324","author":"Vander Heiden","year":"2009","journal-title":"Science"},{"key":"10.1074\/jbc.M117.791343_bib3","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1038\/nrc2981","article-title":"Regulation of cancer cell metabolism","volume":"11","author":"Cairns","year":"2011","journal-title":"Nat. Rev. Cancer"},{"key":"10.1074\/jbc.M117.791343_bib4","doi-asserted-by":"crossref","first-page":"230","DOI":"10.1038\/nature06734","article-title":"The M2 splice isoform of pyruvate kinase is important for cancer metabolism and tumour growth","volume":"452","author":"Christofk","year":"2008","journal-title":"Nature"},{"key":"10.1074\/jbc.M117.791343_bib5","doi-asserted-by":"crossref","first-page":"969","DOI":"10.1016\/j.biocel.2010.02.005","article-title":"Pyruvate kinase type M2: A key regulator of the metabolic budget system in tumor cells","volume":"43","author":"Mazurek","year":"2011","journal-title":"Int. J. Biochem. Cell Biol"},{"key":"10.1074\/jbc.M117.791343_bib6","doi-asserted-by":"crossref","first-page":"13807","DOI":"10.1016\/S0021-9258(18)67091-7","article-title":"The M1- and M2-type isozymes of rat pyruvate kinase are produced from the same gene by alternative RNA splicing","volume":"261","author":"Noguchi","year":"1986","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M117.791343_bib7","doi-asserted-by":"crossref","first-page":"1894","DOI":"10.1073\/pnas.0914845107","article-title":"The alternative splicing repressors hnRNP A1\/A2 and PTB influence pyruvate kinase isoform expression and cell metabolism","volume":"107","author":"Clower","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M117.791343_bib8","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1016\/j.tibs.2012.04.003","article-title":"Rocking cell metabolism: Revised functions of the key glycolytic regulator PKM2 in cancer","volume":"37","author":"Chaneton","year":"2012","journal-title":"Trends Biochem. Sci"},{"key":"10.1074\/jbc.M117.791343_bib9","doi-asserted-by":"crossref","first-page":"2685","DOI":"10.1016\/j.febslet.2014.04.011","article-title":"Pyruvate kinase M2 and cancer: An updated assessment","volume":"588","author":"Iqbal","year":"2014","journal-title":"FEBS Lett"},{"key":"10.1074\/jbc.M117.791343_bib10","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1186\/1476-4598-12-72","article-title":"Insulin enhances metabolic capacities of cancer cells by dual regulation of glycolytic enzyme pyruvate kinase M2","volume":"12","author":"Iqbal","year":"2013","journal-title":"Mol. Cancer"},{"key":"10.1074\/jbc.M117.791343_bib11","doi-asserted-by":"crossref","first-page":"300","DOI":"10.1016\/j.semcancer.2005.04.009","article-title":"Pyruvate kinase type M2 and its role in tumor growth and spreading","volume":"15","author":"Mazurek","year":"2005","journal-title":"Semin. Cancer Biol"},{"key":"10.1074\/jbc.M117.791343_bib12","doi-asserted-by":"crossref","first-page":"16864","DOI":"10.1074\/jbc.M109.065029","article-title":"Dominant negative mutations affect oligomerization of human pyruvate kinase M2 isozyme and promote cellular growth and polyploidy","volume":"285","author":"Gupta","year":"2010","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M117.791343_bib13","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1016\/j.canlet.2014.01.031","article-title":"PKM2 contributes to cancer metabolism","volume":"356","author":"Wong","year":"2015","journal-title":"Cancer Lett"},{"key":"10.1074\/jbc.M117.791343_bib14","doi-asserted-by":"crossref","first-page":"732","DOI":"10.1016\/j.cell.2011.03.054","article-title":"Pyruvate kinase M2 is a PHD3-stimulated coactivator for hypoxia-inducible factor 1","volume":"145","author":"Luo","year":"2011","journal-title":"Cell"},{"key":"10.1074\/jbc.M117.791343_bib15","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1038\/nature10598","article-title":"Nuclear PKM2 regulates \u03b2-catenin transactivation upon EGFR activation","volume":"480","author":"Yang","year":"2011","journal-title":"Nature"},{"key":"10.1074\/jbc.M117.791343_bib16","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1186\/s12943-015-0490-2","article-title":"PKM2 promotes tumor angiogenesis by regulating HIF-1\u03b1 through NF-\u03baB activation","volume":"15","author":"Azoitei","year":"2016","journal-title":"Mol. Cancer"},{"key":"10.1074\/jbc.M117.791343_bib17","doi-asserted-by":"crossref","first-page":"598","DOI":"10.1016\/j.molcel.2012.01.001","article-title":"Pyruvate kinase M2 regulates gene transcription by acting as a protein kinase","volume":"45","author":"Gao","year":"2012","journal-title":"Mol. Cell"},{"key":"10.1074\/jbc.M117.791343_bib18","doi-asserted-by":"crossref","first-page":"685","DOI":"10.1016\/j.cell.2012.07.018","article-title":"PKM2 phosphorylates histone H3 and promotes gene transcription and tumorigenesis","volume":"150","author":"Yang","year":"2012","journal-title":"Cell"},{"key":"10.1074\/jbc.M117.791343_bib19","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/j.molcel.2013.11.001","article-title":"PKM2 regulates chromosome segregation and mitosis progression of tumor cells","volume":"53","author":"Jiang","year":"2014","journal-title":"Mol. Cell"},{"key":"10.1074\/jbc.M117.791343_bib20","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1084\/jem.20111487","article-title":"Pyruvate kinase M2-specific siRNA induces apoptosis and tumor regression","volume":"209","author":"Goldberg","year":"2012","journal-title":"J. Exp. Med"},{"key":"10.1074\/jbc.M117.791343_bib21","doi-asserted-by":"crossref","first-page":"4358","DOI":"10.3892\/mmr.2015.3943","article-title":"Knockdown of PKM2 induces apoptosis and autophagy in human A549 alveolar adenocarcinoma cells","volume":"12","author":"Chu","year":"2015","journal-title":"Mol. Med. Rep"},{"key":"10.1074\/jbc.M117.791343_bib22","doi-asserted-by":"crossref","first-page":"24574","DOI":"10.3390\/ijms161024574","article-title":"Knockdown of PKM2 suppresses tumor growth and invasion in lung adenocarcinoma","volume":"16","author":"Sun","year":"2015","journal-title":"Int. J. Mol. Sci"},{"key":"10.1074\/jbc.M117.791343_bib23","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1038\/nchembio.1060","article-title":"Pyruvate kinase M2 activators promote tetramer formation and suppress tumorigenesis","volume":"8","author":"Anastasiou","year":"2012","journal-title":"Nat. Chem. Biol"},{"key":"10.1074\/jbc.M117.791343_bib24","doi-asserted-by":"crossref","first-page":"1453","DOI":"10.1158\/1535-7163.MCT-13-0026","article-title":"Pharmacologic activation of PKM2 slows lung tumor xenograft growth","volume":"12","author":"Parnell","year":"2013","journal-title":"Mol. Cancer Ther"},{"key":"10.1074\/jbc.M117.791343_bib25","series-title":"Probe Reports from the NIH Molecular Libraries Program (online)","article-title":"ML265: A potent PKM2 activator induces tetramerization and reduces tumor formation and size in a mouse xenograft model","author":"Walsh","year":"2010"},{"key":"10.1074\/jbc.M117.791343_bib26","doi-asserted-by":"crossref","first-page":"489","DOI":"10.1073\/pnas.1212780110","article-title":"M2 isoform of pyruvate kinase is dispensable for tumor maintenance and growth","volume":"110","author":"Cort\u00e9s-Cros","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M117.791343_bib27","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1016\/j.cell.2013.09.025","article-title":"PKM2 isoform-specific deletion reveals a differential requirement for pyruvate kinase in tumor cells","volume":"155","author":"Israelsen","year":"2013","journal-title":"Cell"},{"key":"10.1074\/jbc.M117.791343_bib28","doi-asserted-by":"crossref","first-page":"2554","DOI":"10.1073\/pnas.1312570111","article-title":"Loss of the tumor suppressor LKB1 promotes metabolic reprogramming of cancer cells via HIF-1\u03b1","volume":"111","author":"Faubert","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M117.791343_bib29","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/j.ccr.2012.12.008","article-title":"LKB1 inactivation dictates therapeutic response of non-small cell lung cancer to the metabolism drug phenformin","volume":"23","author":"Shackelford","year":"2013","journal-title":"Cancer cell"},{"key":"10.1074\/jbc.M117.791343_bib30","doi-asserted-by":"crossref","first-page":"807","DOI":"10.1038\/nature06030","article-title":"LKB1 modulates lung cancer differentiation and metastasis","volume":"448","author":"Ji","year":"2007","journal-title":"Nature"},{"key":"10.1074\/jbc.M117.791343_bib31","doi-asserted-by":"crossref","first-page":"13875","DOI":"10.1038\/srep13875","article-title":"An optimized method for high-titer lentivirus preparations without ultracentrifugation","volume":"5","author":"Jiang","year":"2015","journal-title":"Sci. Rep"},{"key":"10.1074\/jbc.M117.791343_bib32","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1186\/2045-3701-4-20","article-title":"Activation of Akt protects cancer cells from growth inhibition induced by PKM2 knockdown","volume":"4","author":"Qin","year":"2014","journal-title":"Cell Biosci"},{"key":"10.1074\/jbc.M117.791343_bib33","doi-asserted-by":"crossref","first-page":"11937","DOI":"10.1074\/jbc.M110.203661","article-title":"Reversible high affinity inhibition of phosphofructokinase-1 by acyl-CoA: A mechanism integrating glycolytic flux with lipid metabolism","volume":"286","author":"Jenkins","year":"2011","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M117.791343_bib34","doi-asserted-by":"crossref","first-page":"9404","DOI":"10.1016\/S0021-9258(19)40658-3","article-title":"Interaction of inhibitors with muscle phosphofructokinase","volume":"250","author":"Colombo","year":"1975","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M117.791343_bib35","doi-asserted-by":"crossref","first-page":"7888","DOI":"10.1074\/jbc.M117.779447","article-title":"AMP-activated protein kinase \u03b11 promotes atherogenesis by increasing monocyte-to-macrophage differentiation","volume":"292","author":"Zhang","year":"2017","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M117.791343_bib36","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1038\/ncb2152","article-title":"AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1","volume":"13","author":"Kim","year":"2011","journal-title":"Nat. Cell Biol"},{"key":"10.1074\/jbc.M117.791343_bib37","doi-asserted-by":"crossref","first-page":"1883","DOI":"10.1097\/JTO.0b013e3181fbc28a","article-title":"LKB1 regulated pathways in lung cancer invasion and metastasis","volume":"5","author":"Marcus","year":"2010","journal-title":"J. Thorac. Oncol"},{"key":"10.1074\/jbc.M117.791343_bib38","doi-asserted-by":"crossref","first-page":"6908","DOI":"10.1038\/onc.2008.342","article-title":"LKB1; linking cell structure and tumor suppression","volume":"27","author":"Hezel","year":"2008","journal-title":"Oncogene"},{"key":"10.1074\/jbc.M117.791343_bib39","doi-asserted-by":"crossref","first-page":"1616","DOI":"10.1038\/sj.onc.1209951","article-title":"Dysfunctional AMPK activity, signalling through mTOR and survival in response to energetic stress in LKB1-deficient lung cancer","volume":"26","author":"Carretero","year":"2007","journal-title":"Oncogene"},{"key":"10.1074\/jbc.M117.791343_bib40","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1186\/2049-3002-1-18","article-title":"LKB1 is a central regulator of tumor initiation and pro-growth metabolism in ErbB2-mediated breast cancer","volume":"1","author":"Dupuy","year":"2013","journal-title":"Cancer Metabol"},{"key":"10.1074\/jbc.M117.791343_bib41","doi-asserted-by":"crossref","first-page":"580","DOI":"10.1016\/j.jtcvs.2008.11.029","article-title":"Expression of LKB1 tumor suppressor in non-small cell lung cancer determines sensitivity to 2-deoxyglucose","volume":"137","author":"Inge","year":"2009","journal-title":"J. Thorac. Cardiovasc. Surg"},{"key":"10.1074\/jbc.M117.791343_bib42","doi-asserted-by":"crossref","first-page":"856","DOI":"10.1038\/onc.2015.140","article-title":"LKB1 deficiency enhances sensitivity to energetic stress induced by erlotinib treatment in non-small-cell lung cancer (NSCLC) cells","volume":"35","author":"Whang","year":"2016","journal-title":"Oncogene"},{"key":"10.1074\/jbc.M117.791343_bib43","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1186\/1741-7007-11-36","article-title":"LKB1 and AMPK and the cancer-metabolism link\u2013ten years after","volume":"11","author":"Hardie","year":"2013","journal-title":"BMC Biol"},{"key":"10.1074\/jbc.M117.791343_bib44","doi-asserted-by":"crossref","first-page":"563","DOI":"10.1038\/nrc2676","article-title":"The LKB1-AMPK pathway: Metabolism and growth control in tumour suppression","volume":"9","author":"Shackelford","year":"2009","journal-title":"Nat. Rev. Cancer"},{"key":"10.1074\/jbc.M117.791343_bib45","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1038\/nrm3311","article-title":"AMPK: A nutrient and energy sensor that maintains energy homeostasis","volume":"13","author":"Hardie","year":"2012","journal-title":"Nat. Rev. Mol. Cell Biol"},{"key":"10.1074\/jbc.M117.791343_bib46","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1007\/s10549-010-0900-5","article-title":"Functional implication of TRAIL \u2212716 C\/T promoter polymorphism on its in vitro and in vivo expression and the susceptibility to sporadic breast tumor","volume":"126","author":"Pal","year":"2011","journal-title":"Breast Cancer Res. Treat"},{"key":"10.1074\/jbc.M117.791343_bib47","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1186\/1476-4598-9-303","article-title":"Investigation of DNA damage response and apoptotic gene methylation pattern in sporadic breast tumors using high throughput quantitative DNA methylation analysis technology","volume":"9","author":"Pal","year":"2010","journal-title":"Mol.Cancer"},{"key":"10.1074\/jbc.M117.791343_bib48","doi-asserted-by":"crossref","first-page":"1079","DOI":"10.1093\/abbs\/gmt112","article-title":"A simple protocol for producing high-titer lentivirus","volume":"45","author":"Chu","year":"2013","journal-title":"Acta Biochim. Biophys. Sin"},{"key":"10.1074\/jbc.M117.791343_bib49","doi-asserted-by":"crossref","first-page":"364","DOI":"10.1038\/nature08697","article-title":"HnRNP proteins controlled by c-Myc deregulate pyruvate kinase mRNA splicing in cancer","volume":"463","author":"David","year":"2010","journal-title":"Nature"},{"key":"10.1074\/jbc.M117.791343_bib50","doi-asserted-by":"crossref","first-page":"1402","DOI":"10.1110\/ps.03479604","article-title":"Predicting subcellular localization of proteins for Gram-negative bacteria by support vector machines based on n-peptide compositions","volume":"13","author":"Yu","year":"2004","journal-title":"Protein Sci"},{"key":"10.1074\/jbc.M117.791343_bib51","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1002\/prot.21018","article-title":"Prediction of protein subcellular localization","volume":"64","author":"Yu","year":"2006","journal-title":"Proteins"},{"key":"10.1074\/jbc.M117.791343_bib52","doi-asserted-by":"crossref","first-page":"14427","DOI":"10.1074\/jbc.M411789200","article-title":"SVM-based method for subcellular localization of human proteins using amino acid compositions, their order and similarity search","volume":"280","author":"Garg","year":"2005","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M117.791343_bib53","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1016\/j.ab.2009.07.046","article-title":"A top-down approach to enhance the power of predicting human protein subcellular localization: Hum-mPLoc 2.0","volume":"394","author":"Shen","year":"2009","journal-title":"Anal. Biochem"},{"key":"10.1074\/jbc.M117.791343_bib54","doi-asserted-by":"crossref","first-page":"1006","DOI":"10.1016\/j.bbrc.2007.02.071","article-title":"Hum-mPLoc: An ensemble classifier for large-scale human protein subcellular location prediction by incorporating samples with multiple sites","volume":"355","author":"Shen","year":"2007","journal-title":"Biochem. Biophys. Res. Commun"},{"key":"10.1074\/jbc.M117.791343_bib55","doi-asserted-by":"crossref","first-page":"376","DOI":"10.1093\/bioinformatics\/bti822","article-title":"SubLoc: A server\/client suite for protein subcellular location based on SOAP","volume":"22","author":"Chen","year":"2006","journal-title":"Bioinformatics"},{"key":"10.1074\/jbc.M117.791343_bib56","doi-asserted-by":"crossref","first-page":"1232","DOI":"10.1093\/bioinformatics\/btq115","article-title":"Going from where to why\u2014interpretable prediction of protein subcellular localization","volume":"26","author":"Briesemeister","year":"2010","journal-title":"Bioinformatics"},{"key":"10.1074\/jbc.M117.791343_bib57","doi-asserted-by":"crossref","first-page":"W497","DOI":"10.1093\/nar\/gkq477","article-title":"YLoc\u2014an interpretable web server for predicting subcellular localization","volume":"38","author":"Briesemeister","year":"2010","journal-title":"Nucleic Acids Res"},{"key":"10.1074\/jbc.M117.791343_bib58","doi-asserted-by":"crossref","first-page":"e408","DOI":"10.1093\/bioinformatics\/btl222","article-title":"BaCelLo: A balanced subcellular localization predictor","volume":"22","author":"Pierleoni","year":"2006","journal-title":"Bioinformatics"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820341016?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820341016?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.M117.791343","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,3,26]],"date-time":"2021-03-26T05:13:11Z","timestamp":1616735591000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925820341016"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,9]]},"references-count":58,"journal-issue":{"issue":"37","published-print":{"date-parts":[[2017,9]]}},"alternative-id":["S0021925820341016"],"URL":"https:\/\/doi.org\/10.1074\/jbc.m117.791343","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2017,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Pyruvate kinase M knockdown\u2013induced signaling via AMP-activated protein kinase promotes mitochondrial biogenesis, autophagy, and cancer cell survival","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1074\/jbc.M117.791343","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2017 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}]}}