{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,11]],"date-time":"2026-06-11T10:44:14Z","timestamp":1781174654610,"version":"3.54.1"},"reference-count":42,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2014,11,18]],"date-time":"2014-11-18T00:00:00Z","timestamp":1416268800000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["BMC Bioinformatics"],"published-print":{"date-parts":[[2014,12]]},"DOI":"10.1186\/s12859-014-0379-x","type":"journal-article","created":{"date-parts":[[2014,11,17]],"date-time":"2014-11-17T18:05:09Z","timestamp":1416247509000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":114,"title":["Anatomy of enzyme channels"],"prefix":"10.1186","volume":"15","author":[{"given":"Luk\u00e1\u0161","family":"Pravda","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Karel","family":"Berka","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Radka","family":"Svobodov\u00e1 Va\u0159ekov\u00e1","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David","family":"Sehnal","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pavel","family":"Ban\u00e1\u0161","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Roman A","family":"Laskowski","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jaroslav","family":"Ko\u010da","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michal","family":"Otyepka","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2014,11,18]]},"reference":[{"key":"379_CR1","doi-asserted-by":"publisher","first-page":"149","DOI":"10.1146\/annurev.biochem.70.1.149","volume":"70","author":"X Huang","year":"2001","unstructured":"Huang X, Holden HM, Raushel FM: Channeling of substrates and intermediates in enzyme-catalyzed reactions. Annu Rev Biochem. 2001, 70: 149-180. 10.1146\/annurev.biochem.70.1.149.","journal-title":"Annu Rev Biochem"},{"key":"379_CR2","doi-asserted-by":"publisher","first-page":"2047","DOI":"10.1021\/ci400225w","volume":"53","author":"J Park","year":"2013","unstructured":"Park J, Czapla L, Amaro RE: Molecular simulations of aromatase reveal new insights into the mechanism of ligand binding. J Chem Inf Model. 2013, 53: 2047-2056. 10.1021\/ci400225w.","journal-title":"J Chem Inf Model"},{"key":"379_CR3","doi-asserted-by":"publisher","first-page":"1595","DOI":"10.1021\/ci300151h","volume":"52","author":"J Sgrignani","year":"2012","unstructured":"Sgrignani J, Magistrato A: Influence of the membrane lipophilic environment on the structure and on the substrate access\/egress routes of the human aromatase enzyme. A computational study. J Chem Inf Model. 2012, 52: 1595-1606. 10.1021\/ci300151h.","journal-title":"J Chem Inf Model"},{"key":"379_CR4","doi-asserted-by":"publisher","first-page":"5039","DOI":"10.1021\/bi4006946","volume":"52","author":"Y Madrona","year":"2013","unstructured":"Madrona Y, Hollingsworth SA, Khan B, Poulos TL: P450cin active site water: implications for substrate binding and solvent accessibility. Biochemistry. 2013, 52: 5039-5050. 10.1021\/bi4006946.","journal-title":"Biochemistry"},{"key":"379_CR5","doi-asserted-by":"publisher","first-page":"549","DOI":"10.1002\/chem.201202627","volume":"19","author":"Y-L Cui","year":"2013","unstructured":"Cui Y-L, Zhang J-L, Zheng Q-C, Niu R-J, Xu Y, Zhang H-X, Sun C-C: Structural and dynamic basis of human cytochrome P450 7B1: a survey of substrate selectivity and major active site access channels. Chemistry. 2013, 19: 549-557. 10.1002\/chem.201202627.","journal-title":"Chemistry"},{"key":"379_CR6","doi-asserted-by":"publisher","first-page":"380","DOI":"10.1038\/nature11880","volume":"494","author":"SJ Lee","year":"2013","unstructured":"Lee SJ, McCormick MS, Lippard SJ, Cho U-S: Control of substrate access to the active site in methane monooxygenase. Nature. 2013, 494: 380-384. 10.1038\/nature11880.","journal-title":"Nature"},{"key":"379_CR7","doi-asserted-by":"publisher","first-page":"1600","DOI":"10.1126\/science.1232048","volume":"339","author":"EE Pryor","year":"2013","unstructured":"Pryor EE, Horanyi PS, Clark KM, Fedoriw N, Connelly SM, Koszelak-Rosenblum M, Zhu G, Malkowski MG, Wiener MC, Dumont ME: Structure of the integral membrane protein CAAX protease Ste24p. Science. 2013, 339: 1600-1604. 10.1126\/science.1232048.","journal-title":"Science"},{"key":"379_CR8","doi-asserted-by":"publisher","first-page":"1490","DOI":"10.1016\/j.str.2012.06.003","volume":"20","author":"S Xu","year":"2012","unstructured":"Xu S, Mueser TC, Marnett LJ, Funk MO: Crystal structure of 12-lipoxygenase catalytic-domain-inhibitor complex identifies a substrate-binding channel for catalysis. Structure. 2012, 20: 1490-1497. 10.1016\/j.str.2012.06.003.","journal-title":"Structure"},{"key":"379_CR9","doi-asserted-by":"publisher","first-page":"18459","DOI":"10.1073\/pnas.1210076109","volume":"109","author":"A Guskov","year":"2012","unstructured":"Guskov A, Nordin N, Reynaud A, Engman H, Lundb\u00e4ck A-K, Jong AJO, Cornvik T, Phua T, Eshaghi S: Structural insights into the mechanisms of Mg2+ uptake, transport, and gating by CorA. Proc Natl Acad Sci U S A. 2012, 109: 18459-18464. 10.1073\/pnas.1210076109.","journal-title":"Proc Natl Acad Sci U S A"},{"key":"379_CR10","doi-asserted-by":"publisher","first-page":"130","DOI":"10.2174\/138920012798918372","volume":"13","author":"M Otyepka","year":"2012","unstructured":"Otyepka M, Berka K, Anzenbacher P: Is there a relationship between the substrate preferences and structural flexibility of cytochromes P450?. Curr Drug Metab. 2012, 13: 130-142. 10.2174\/138920012798918372.","journal-title":"Curr Drug Metab"},{"key":"379_CR11","doi-asserted-by":"publisher","first-page":"31093","DOI":"10.1074\/jbc.M113.491415","volume":"288","author":"S Rengachari","year":"2013","unstructured":"Rengachari S, Aschauer P, Schittmayer M, Mayer N, Gruber K, Breinbauer R, Birner-Gruenberger R, Dreveny I, Oberer M: Conformational plasticity and ligand binding of bacterial monoacylglycerol lipase. J Biol Chem. 2013, 288: 31093-31104. 10.1074\/jbc.M113.491415.","journal-title":"J Biol Chem"},{"key":"379_CR12","doi-asserted-by":"publisher","first-page":"33163","DOI":"10.1074\/jbc.M112.392258","volume":"287","author":"MD Salter","year":"2012","unstructured":"Salter MD, Blouin GC, Soman J, Singleton EW, Dewilde S, Moens L, Pesce A, Nardini M, Bolognesi M, Olson JS: Determination of ligand pathways in globins: apolar tunnels versus polar gates. J Biol Chem. 2012, 287: 33163-33178. 10.1074\/jbc.M112.392258.","journal-title":"J Biol Chem"},{"key":"379_CR13","doi-asserted-by":"publisher","first-page":"893","DOI":"10.1016\/j.jmb.2006.05.023","volume":"360","author":"NR Voss","year":"2006","unstructured":"Voss NR, Gerstein M, Steitz TA, Moore PB: The geometry of the ribosomal polypeptide exit tunnel. J Mol Biol. 2006, 360: 893-906. 10.1016\/j.jmb.2006.05.023.","journal-title":"J Mol Biol"},{"key":"379_CR14","doi-asserted-by":"publisher","first-page":"6285","DOI":"10.1021\/cr3000829","volume":"112","author":"D Lemoine","year":"2012","unstructured":"Lemoine D, Jiang R, Taly A, Chataigneau T, Specht A, Grutter T: Ligand-gated Ion channels: new insights into neurological disorders and ligand recognition. Chem Rev. 2012, 112: 6285-6318. 10.1021\/cr3000829.","journal-title":"Chem Rev"},{"key":"379_CR15","doi-asserted-by":"publisher","first-page":"6215","DOI":"10.1021\/cr300444k","volume":"112","author":"JJ Kasianowicz","year":"2012","unstructured":"Kasianowicz JJ: Introduction to Ion channels and disease. Chem Rev. 2012, 112: 6215-6217. 10.1021\/cr300444k.","journal-title":"Chem Rev"},{"key":"379_CR16","doi-asserted-by":"publisher","first-page":"1195","DOI":"10.1021\/cb400030n","volume":"8","author":"AM Knight","year":"2013","unstructured":"Knight AM, Culviner PH, Kurt-Yilmaz N, Zou T, Ozkan SB, Cavagnero S: Electrostatic effect of the ribosomal surface on nascent polypeptide dynamics. ACS Chem Biol. 2013, 8: 1195-1204. 10.1021\/cb400030n.","journal-title":"ACS Chem Biol"},{"key":"379_CR17","doi-asserted-by":"publisher","first-page":"117","DOI":"10.1021\/ar950051e","volume":"4842","author":"B Eisenberg","year":"1998","unstructured":"Eisenberg B: Ionic channels in biological membranes: natural nanotubes. Acc Chem Res. 1998, 4842: 117-123. 10.1021\/ar950051e.","journal-title":"Acc Chem Res"},{"key":"379_CR18","doi-asserted-by":"publisher","first-page":"127","DOI":"10.1146\/annurev.bb.19.060190.001015","volume":"19","author":"B Wallace","year":"1990","unstructured":"Wallace B: Gramicidin channels and pores. Annu Rev Biophys Biophys Chem. 1990, 19: 127-157. 10.1146\/annurev.bb.19.060190.001015.","journal-title":"Annu Rev Biophys Biophys Chem"},{"key":"379_CR19","doi-asserted-by":"publisher","first-page":"366","DOI":"10.1021\/ar010028v","volume":"35","author":"B Roux","year":"2002","unstructured":"Roux B: Computational studies of the gramicidin channel. Acc Chem Res. 2002, 35: 366-375. 10.1021\/ar010028v.","journal-title":"Acc Chem Res"},{"key":"379_CR20","doi-asserted-by":"publisher","first-page":"6250","DOI":"10.1021\/cr3002609","volume":"112","author":"C Maffeo","year":"2012","unstructured":"Maffeo C, Bhattacharya S, Yoo J, Wells D, Aksimentiev A: Modeling and simulation of Ion channels. Chem Rev. 2012, 112: 6250-6284. 10.1021\/cr3002609.","journal-title":"Chem Rev"},{"key":"379_CR21","doi-asserted-by":"publisher","first-page":"517","DOI":"10.1146\/annurev.biochem.72.121801.161617","volume":"72","author":"DA Kraut","year":"2003","unstructured":"Kraut DA, Carroll KS, Herschlag D: Challenges in enzyme mechanism and energetics. Annu Rev Biochem. 2003, 72: 517-571. 10.1146\/annurev.biochem.72.121801.161617.","journal-title":"Annu Rev Biochem"},{"key":"379_CR22","doi-asserted-by":"publisher","first-page":"3210","DOI":"10.1021\/cr0503106","volume":"106","author":"A Warshel","year":"2006","unstructured":"Warshel A, Sharma PK, Kato M, Xiang Y, Liu H, Olsson MHM: Electrostatic basis for enzyme catalysis. Chem Rev. 2006, 106: 3210-3235. 10.1021\/cr0503106.","journal-title":"Chem Rev"},{"key":"379_CR23","doi-asserted-by":"publisher","first-page":"186","DOI":"10.1126\/science.1088172","volume":"303","author":"M Garcia-Viloca","year":"2004","unstructured":"Garcia-Viloca M, Gao J, Karplus M, Truhlar DG: How enzymes work: analysis by modern rate theory and computer simulations. Science. 2004, 303: 186-195. 10.1126\/science.1088172.","journal-title":"Science"},{"key":"379_CR24","doi-asserted-by":"publisher","first-page":"1196","DOI":"10.1126\/science.1085515","volume":"301","author":"S Benkovic","year":"2003","unstructured":"Benkovic S, Hammes-Schiffer S: A perspective on enzyme catalysis. Science. 2003, 301: 1196-1202. 10.1126\/science.1085515.","journal-title":"Science"},{"issue":"Database issue","key":"379_CR25","doi-asserted-by":"publisher","first-page":"D129","DOI":"10.1093\/nar\/gkh028","volume":"32","author":"CT Porter","year":"2004","unstructured":"Porter CT, Bartlett GJ, Thornton JM: The catalytic site atlas: a resource of catalytic sites and residues identified in enzymes using structural data. Nucleic Acids Res. 2004, 32 (Database issue): D129-D133. 10.1093\/nar\/gkh028.","journal-title":"Nucleic Acids Res"},{"key":"379_CR26","doi-asserted-by":"publisher","first-page":"727","DOI":"10.1038\/nchembio.205","volume":"5","author":"M Pavlova","year":"2009","unstructured":"Pavlova M, Klvana M, Prokop Z, Chaloupkova R, Banas P, Otyepka M, Wade RC, Tsuda M, Nagata Y, Damborsky J: Redesigning dehalogenase access tunnels as a strategy for degrading an anthropogenic substrate. Nat Chem Biol. 2009, 5: 727-733. 10.1038\/nchembio.205.","journal-title":"Nat Chem Biol"},{"key":"379_CR27","doi-asserted-by":"publisher","first-page":"890","DOI":"10.1002\/cbic.201200733","volume":"14","author":"V Stepankova","year":"2013","unstructured":"Stepankova V, Khabiri M, Brezovsky J, Pavelka A, Sykora J, Amaro M, Minofar B, Prokop Z, Hof M, Ettrich R, Chaloupkova R, Damborsky J: Expansion of access tunnels and active-site cavities influence activity of haloalkane dehalogenases in organic cosolvents. Chembiochem. 2013, 14: 890-897. 10.1002\/cbic.201200733.","journal-title":"Chembiochem"},{"key":"379_CR28","doi-asserted-by":"publisher","first-page":"8165","DOI":"10.1021\/jp800311c","volume":"112","author":"J Skopal\u00edk","year":"2008","unstructured":"Skopal\u00edk J, Anzenbacher P, Otyepka M: Flexibility of human cytochromes P450: molecular dynamics reveals differences between CYPs 3A4, 2C9, and 2A6, which correlate with their substrate preferences. J Phys Chem B. 2008, 112: 8165-8173. 10.1021\/jp800311c.","journal-title":"J Phys Chem B"},{"key":"379_CR29","doi-asserted-by":"publisher","first-page":"177","DOI":"10.2174\/138920012798918408","volume":"13","author":"T Hendrychov\u00e1","year":"2012","unstructured":"Hendrychov\u00e1 T, Berka K, Navr\u00e1tilov\u00e1 V, Anzenbacher P, Otyepka M: Dynamics and hydration of the active sites of mammalian cytochromes P450 probed by molecular dynamics simulations. Curr Drug Metab. 2012, 13: 177-189. 10.2174\/138920012798918408.","journal-title":"Curr Drug Metab"},{"key":"379_CR30","doi-asserted-by":"publisher","first-page":"39","DOI":"10.1186\/1758-2946-5-39","volume":"5","author":"D Sehnal","year":"2013","unstructured":"Sehnal D, Svobodov\u00e1 Va\u0159ekov\u00e1 R, Berka K, Pravda L, Navr\u00e1tilov\u00e1 V, Ban\u00e1\u0161 P, Ionescu C-M, Otyepka M, Ko\u010da J: MOLE 2.0: advanced approach for analysis of biomacromolecular channels. J Cheminform. 2013, 5: 39-10.1186\/1758-2946-5-39.","journal-title":"J Cheminform"},{"key":"379_CR31","doi-asserted-by":"publisher","first-page":"105","DOI":"10.1016\/0022-2836(82)90515-0","volume":"157","author":"J Kyte","year":"1982","unstructured":"Kyte J, Doolittle RF: A simple method for displaying the hydropathic character of a protein. J Mol Biol. 1982, 157: 105-132. 10.1016\/0022-2836(82)90515-0.","journal-title":"J Mol Biol"},{"key":"379_CR32","doi-asserted-by":"publisher","first-page":"170","DOI":"10.1016\/0022-5193(68)90069-6","volume":"21","author":"JM Zimmerman","year":"1968","unstructured":"Zimmerman JM, Eliezer N, Simha R: The characterization of amino acid sequences in proteins by statistical methods. J Theor Biol. 1968, 21: 170-201. 10.1016\/0022-5193(68)90069-6.","journal-title":"J Theor Biol"},{"issue":"Pt 4","key":"379_CR33","doi-asserted-by":"publisher","first-page":"403","DOI":"10.1107\/S1744309105007931","volume":"61","author":"CJ Webby","year":"2005","unstructured":"Webby CJ, Lott JS, Baker HM, Baker EN, Parker EJ: Crystallization and preliminary X-ray crystallographic analysis of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Mycobacterium tuberculosis. Acta Crystallogr Sect F: Struct Biol Cryst Commun. 2005, 61 (Pt 4): 403-406. 10.1107\/S1744309105007931.","journal-title":"Acta Crystallogr Sect F: Struct Biol Cryst Commun"},{"key":"379_CR34","doi-asserted-by":"publisher","first-page":"989","DOI":"10.1107\/S0907444903006772","volume":"D59","author":"K Houborg","year":"2003","unstructured":"Houborg K, Harris P, Petersen J, Rowland P, Poulsen J-CN, Schneider P, Vind J, Larsen S: Impact of the physical and chemical environment on the molecular structure of Coprinus cinereus peroxidase. Acta Crystallogr Sect D: Biol Crystallogr. 2003, D59: 989-996. 10.1107\/S0907444903006772.","journal-title":"Acta Crystallogr Sect D: Biol Crystallogr"},{"key":"379_CR35","doi-asserted-by":"publisher","first-page":"5","DOI":"10.1002\/jobm.200900338","volume":"50","author":"TK Lundell","year":"2010","unstructured":"Lundell TK, M\u00e4kel\u00e4 MR, Hild\u00e9n K: Lignin-modifying enzymes in filamentous basidiomycetes-ecological, functional and phylogenetic review. J Basic Microbiol. 2010, 50: 5-20. 10.1002\/jobm.200900338.","journal-title":"J Basic Microbiol"},{"key":"379_CR36","doi-asserted-by":"publisher","first-page":"379","DOI":"10.1038\/7939","volume":"17","author":"JR Cherry","year":"1999","unstructured":"Cherry JR, Lamsa MH, Schneider P, Vind J, Svendsen A, Jones A, Pedersen AH: Directed evolution of a fungal peroxidase. Nat Biotechnol. 1999, 17: 379-384. 10.1038\/7939.","journal-title":"Nat Biotechnol"},{"key":"379_CR37","doi-asserted-by":"publisher","first-page":"560","DOI":"10.1016\/j.jmb.2009.05.015","volume":"390","author":"GL Holliday","year":"2009","unstructured":"Holliday GL, Mitchell JBO, Thornton JM: Understanding the functional roles of amino acid residues in enzyme catalysis. J Mol Biol. 2009, 390: 560-577. 10.1016\/j.jmb.2009.05.015.","journal-title":"J Mol Biol"},{"key":"379_CR38","doi-asserted-by":"publisher","first-page":"7133","DOI":"10.1021\/bi00483a001","volume":"29","author":"KA Dill","year":"1990","unstructured":"Dill KA: Dominant forces in protein folding. Biochemistry. 1990, 29: 7133-7155. 10.1021\/bi00483a001.","journal-title":"Biochemistry"},{"key":"379_CR39","doi-asserted-by":"publisher","first-page":"35","DOI":"10.1016\/S1570-9639(04)00063-9","volume":"1699","author":"B Wilkinson","year":"2004","unstructured":"Wilkinson B, Gilbert HF: Protein disulfide isomerase. Biochim Biophys Acta. 2004, 1699: 35-44. 10.1016\/j.bbapap.2004.02.017.","journal-title":"Biochim Biophys Acta"},{"key":"379_CR40","doi-asserted-by":"publisher","first-page":"D485","DOI":"10.1093\/nar\/gkt1243","volume":"42","author":"N Furnham","year":"2014","unstructured":"Furnham N, Holliday GL, de Beer TAP, Jacobsen JOB, Pearson WR, Thornton JM: The catalytic site atlas 2.0: cataloging catalytic sites and residues identified in enzymes. Nucleic Acids Res. 2014, 42: D485-D489. 10.1093\/nar\/gkt1243.","journal-title":"Nucleic Acids Res"},{"issue":"Web Server issu","key":"379_CR41","doi-asserted-by":"publisher","first-page":"W222","DOI":"10.1093\/nar\/gks363","volume":"40","author":"K Berka","year":"2012","unstructured":"Berka K, Han\u00e1k O, Sehnal D, Ban\u00e1\u0161 P, Navr\u00e1tilov\u00e1 V, Jaiswal D, Ionescu C-M, Svobodov\u00e1 Va\u0159ekov\u00e1 R, Ko\u010da J, Otyepka M: MOLEonline 2.0: interactive web-based analysis of biomacromolecular channels. Nucleic Acids Res. 2012, 40 (Web Server issue): W222-W227. 10.1093\/nar\/gks363.","journal-title":"Nucleic Acids Res"},{"issue":"Database issue","key":"379_CR42","doi-asserted-by":"publisher","first-page":"D301","DOI":"10.1093\/nar\/gkl971","volume":"35","author":"H Berman","year":"2007","unstructured":"Berman H, Henrick K, Nakamura H, Markley JL: The worldwide Protein Data Bank (wwPDB): ensuring a single, uniform archive of PDB data. Nucleic Acids Res. 2007, 35 (Database issue): D301-D303. 10.1093\/nar\/gkl971.","journal-title":"Nucleic Acids Res"}],"container-title":["BMC Bioinformatics"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/link.springer.com\/article\/10.1186\/s12859-014-0379-x\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1186\/s12859-014-0379-x.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1186\/s12859-014-0379-x","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1186\/s12859-014-0379-x.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,9,2]],"date-time":"2021-09-02T06:28:46Z","timestamp":1630564126000},"score":1,"resource":{"primary":{"URL":"https:\/\/bmcbioinformatics.biomedcentral.com\/articles\/10.1186\/s12859-014-0379-x"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2014,11,18]]},"references-count":42,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2014,12]]}},"alternative-id":["379"],"URL":"https:\/\/doi.org\/10.1186\/s12859-014-0379-x","relation":{},"ISSN":["1471-2105"],"issn-type":[{"value":"1471-2105","type":"electronic"}],"subject":[],"published":{"date-parts":[[2014,11,18]]},"assertion":[{"value":"19 July 2014","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"5 November 2014","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"18 November 2014","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}}],"article-number":"379"}}