{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,21]],"date-time":"2026-01-21T04:58:11Z","timestamp":1768971491948,"version":"3.49.0"},"reference-count":48,"publisher":"Springer Science and Business Media LLC","issue":"S19","content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["BMC Bioinformatics"],"published-print":{"date-parts":[[2015,12]]},"DOI":"10.1186\/1471-2105-16-s19-s10","type":"journal-article","created":{"date-parts":[[2015,12,17]],"date-time":"2015-12-17T05:01:58Z","timestamp":1450328518000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":20,"title":["Structural studies on molecular mechanisms of Nelfinavir resistance caused by non-active site mutation V77I in HIV-1 protease"],"prefix":"10.1186","volume":"16","author":[{"given":"Ankita","family":"Gupta","sequence":"first","affiliation":[]},{"given":"Salma","family":"Jamal","sequence":"additional","affiliation":[]},{"given":"Sukriti","family":"Goyal","sequence":"additional","affiliation":[]},{"given":"Ritu","family":"Jain","sequence":"additional","affiliation":[]},{"given":"Divya","family":"Wahi","sequence":"additional","affiliation":[]},{"given":"Abhinav","family":"Grover","sequence":"additional","affiliation":[]}],"member":"297","published-online":{"date-parts":[[2015,12,16]]},"reference":[{"issue":"4976","key":"7217_CR1","doi-asserted-by":"publisher","first-page":"1533","DOI":"10.1126\/science.1699273","volume":"249","author":"H Mitsuya","year":"1990","unstructured":"Mitsuya H, Yarchoan R, Broder S: Molecular targets for AIDS therapy. Science. 1990, 249 (4976): 1533-1544.","journal-title":"Science"},{"key":"7217_CR2","doi-asserted-by":"crossref","unstructured":"Krausslich HG, Wimmer E: Viral proteinases. Annu Rev Biochem. 1988, 701-54. 57","DOI":"10.1146\/annurev.bi.57.070188.003413"},{"issue":"13","key":"7217_CR3","doi-asserted-by":"publisher","first-page":"4686","DOI":"10.1073\/pnas.85.13.4686","volume":"85","author":"NE Kohl","year":"1988","unstructured":"Kohl NE, Emini EA, Schleif WA, Davis LJ, Heimbach JC, Dixon RA, et al: Active human immunodeficiency virus protease is required for viral infectivity. Proc Natl Acad Sci USA. 1988, 85 (13): 4686-4690.","journal-title":"Proc Natl Acad Sci USA"},{"issue":"4","key":"7217_CR4","doi-asserted-by":"publisher","first-page":"429","DOI":"10.1002\/prot.10246","volume":"49","author":"J Vondrasek","year":"2002","unstructured":"Vondrasek J, Wlodawer A: HIVdb: a database of the structures of human immunodeficiency virus protease. Proteins. 2002, 49 (4): 429-431.","journal-title":"Proteins"},{"issue":"6208","key":"7217_CR5","doi-asserted-by":"publisher","first-page":"615","DOI":"10.1038\/337615a0","volume":"337","author":"MA Navia","year":"1989","unstructured":"Navia MA, Fitzgerald PM, McKeever BM, Leu CT, Heimbach JC, Herber WK, et al: Three-dimensional structure of aspartyl protease from human immunodeficiency virus HIV-1. Nature. 1989, 337 (6208): 615-620.","journal-title":"Nature"},{"issue":"4918","key":"7217_CR6","doi-asserted-by":"publisher","first-page":"616","DOI":"10.1126\/science.2548279","volume":"245","author":"A Wlodawer","year":"1989","unstructured":"Wlodawer A, Miller M, Jaskolski M, Sathyanarayana BK, Baldwin E, Weber IT, et al: Conserved folding in retroviral proteases: crystal structure of a synthetic HIV-1 protease. Science. 1989, 245 (4918): 616-621.","journal-title":"Science"},{"issue":"8","key":"7217_CR7","doi-asserted-by":"publisher","first-page":"2105","DOI":"10.1021\/bi972059x","volume":"37","author":"JM Louis","year":"1998","unstructured":"Louis JM, Dyda F, Nashed NT, Kimmel AR, Davies DR: Hydrophilic peptides derived from the transframe region of Gag-Pol inhibit the HIV-1 protease. Biochemistry. 1998, 37 (8): 2105-2110.","journal-title":"Biochemistry"},{"issue":"5","key":"7217_CR8","doi-asserted-by":"publisher","first-page":"1207","DOI":"10.1006\/jmbi.2000.4018","volume":"301","author":"M Prabu-Jeyabalan","year":"2000","unstructured":"Prabu-Jeyabalan M, Nalivaika E, Schiffer CA: How does a symmetric dimer recognize an asymmetric substrate? a substrate complex of HIV-1 protease. J Mol Biol. 2000, 301 (5): 1207-1220.","journal-title":"J Mol Biol"},{"issue":"1","key":"7217_CR9","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1006\/jmbi.1998.2354","volume":"285","author":"BG Turner","year":"1999","unstructured":"Turner BG, Summers MF: Structural biology of HIV. J Mol Biol. 1999, 285 (1): 1-32.","journal-title":"J Mol Biol"},{"key":"7217_CR10","doi-asserted-by":"crossref","unstructured":"Wlodawer A, Vondrasek J: Inhibitors of HIV-1 protease: a major success of structure-assisted drug design. Annu Rev Biophys Biomol Struct. 1998, 249-284. 27","DOI":"10.1146\/annurev.biophys.27.1.249"},{"issue":"5","key":"7217_CR11","doi-asserted-by":"publisher","first-page":"633","DOI":"10.2165\/00003495-200565050-00005","volume":"65","author":"C Arvieux","year":"2005","unstructured":"Arvieux C, Tribut O: Amprenavir or fosamprenavir plus ritonavir in HIV infection: pharmacology, efficacy and tolerability profile. Drugs. 2005, 65 (5): 633-659.","journal-title":"Drugs"},{"issue":"6","key":"7217_CR12","doi-asserted-by":"publisher","first-page":"891","DOI":"10.1084\/jem.20041455","volume":"201","author":"A Leslie","year":"2005","unstructured":"Leslie A, Kavanagh D, Honeyborne I, Pfafferott K, Edwards C, Pillay T, et al: Transmission and accumulation of CTL escape variants drive negative associations between HIV polymorphisms and HLA. J Exp Med. 2005, 201 (6): 891-902.","journal-title":"J Exp Med"},{"issue":"1","key":"7217_CR13","doi-asserted-by":"publisher","first-page":"298","DOI":"10.1093\/nar\/gkg100","volume":"31","author":"SY Rhee","year":"2003","unstructured":"Rhee SY, Gonzales MJ, Kantor R, Betts BJ, Ravela J, Shafer RW: Human immunodeficiency virus reverse transcriptase and protease sequence database. Nucleic Acids Res. 2003, 31 (1): 298-303.","journal-title":"Nucleic Acids Res"},{"issue":"7","key":"7217_CR14","doi-asserted-by":"publisher","first-page":"2200","DOI":"10.1128\/JCM.01654-08","volume":"47","author":"S Jallow","year":"2009","unstructured":"Jallow S, Alabi A, Sarge-Njie R, Peterson K, Whittle H, Corrah T, et al: Virological response to highly active antiretroviral therapy in patients infected with human immunodeficiency virus type 2 (HIV-2) and in patients dually infected with HIV-1 and HIV-2 in the Gambia and emergence of drug-resistant variants. J Clin Microbiol. 2009, 47 (7): 2200-2208.","journal-title":"J Clin Microbiol"},{"issue":"18","key":"7217_CR15","doi-asserted-by":"publisher","first-page":"9512","DOI":"10.1128\/JVI.00291-09","volume":"83","author":"H Van Marck","year":"2009","unstructured":"Van Marck H, Dierynck I, Kraus G, Hallenberger S, Pattery T, Muyldermans G, et al: The impact of individual human immunodeficiency virus type 1 protease mutations on drug susceptibility is highly influenced by complex interactions with the background protease sequence. J Virol. 2009, 83 (18): 9512-9520.","journal-title":"J Virol"},{"issue":"3","key":"7217_CR16","doi-asserted-by":"publisher","first-page":"598","DOI":"10.1016\/j.jmb.2007.04.081","volume":"370","author":"H Ode","year":"2007","unstructured":"Ode H, Matsuyama S, Hata M, Neya S, Kakizawa J, Sugiura W, Hoshino T: Computational characterization of structural role of the non-active site mutation M36I of human immunodeficiency virus type 1 protease. J Mol Biol. 2007, 370 (3): 598-607.","journal-title":"J Mol Biol"},{"issue":"1","key":"7217_CR17","doi-asserted-by":"publisher","first-page":"446","DOI":"10.1186\/1756-0500-7-446","volume":"7","author":"S Soni","year":"2014","unstructured":"Soni S, Tyagi C, Grover A, Goswami SK: Molecular modeling and molecular dynamics simulations based structural analysis of the SG2NA protein variants. BMC Res Notes. 2014, 7 (1): 446-","journal-title":"BMC Res Notes"},{"key":"7217_CR18","volume-title":"BioMed Res Int","author":"M Goyal","year":"2013","unstructured":"Goyal M, Grover S, Dhanjal JK, Goyal S, Tyagi C, Chacko S, Grover A: Novel Natural Structure Corrector of ApoE4 for Checking Alzheimer's Disease: Benefits from High Throughput Screening and Molecular Dynamics Simulations. BioMed Res Int. 2013, Article ID 620793 doi:10.1155\/2013\/620793"},{"issue":"1","key":"7217_CR19","doi-asserted-by":"publisher","first-page":"565","DOI":"10.1021\/jp046860+","volume":"109","author":"H Ode","year":"2005","unstructured":"Ode H, Ota M, Neya S, Hata M, Sugiura W, Hoshino T: Resistant mechanism against Nelfinavir of human immunodeficiency virus type 1 proteases. J Phys Chem B. 2005, 109 (1): 565-574.","journal-title":"J Phys Chem B"},{"issue":"19","key":"7217_CR20","doi-asserted-by":"publisher","first-page":"5777","DOI":"10.1021\/jm0605583","volume":"49","author":"T Skalova","year":"2006","unstructured":"Skalova T, Dohnalek J, Duskova J, Petrokova H, Hradilek M, Soucek M, et al: HIV-1 protease mutations and inhibitor modifications monitored on a series of complexes. Structural basis for the effect of the A71V mutation on the active site. J Med Chem. 2006, 49 (19): 5777-5784.","journal-title":"J Med Chem"},{"issue":"10","key":"7217_CR21","doi-asserted-by":"publisher","first-page":"2393","DOI":"10.1110\/ps.0206702","volume":"11","author":"S Piana","year":"2002","unstructured":"Piana S, Carloni P, Rothlisberger U: Drug resistance in HIV-1 protease: Flexibility-assisted mechanism of compensatory mutations. Protein Science. 2002, 11 (10): 2393-2402.","journal-title":"Protein Science"},{"issue":"24","key":"7217_CR22","doi-asserted-by":"publisher","first-page":"7887","DOI":"10.1021\/ja060682b","volume":"128","author":"H Ode","year":"2006","unstructured":"Ode H, Neya S, Hata M, Sugiura W, Hoshino T: Computational simulations of HIV-1 proteases--multi-drug resistance due to nonactive site mutation L90M. J Am Chem Soc. 2006, 128 (24): 7887-7895.","journal-title":"J Am Chem Soc"},{"issue":"2","key":"7217_CR23","doi-asserted-by":"publisher","first-page":"297","DOI":"10.1007\/s00894-006-0121-3","volume":"13","author":"H Meiselbach","year":"2007","unstructured":"Meiselbach H, Horn AH, Harrer T, Sticht H: Insights into amprenavir resistance in E35D HIV-1 protease mutation from molecular dynamics and binding free-energy calculations. J Mol Model. 2007, 13 (2): 297-304.","journal-title":"J Mol Model"},{"issue":"3","key":"7217_CR24","doi-asserted-by":"publisher","first-page":"395","DOI":"10.1385\/CBB:44:3:395","volume":"44","author":"PR Batista","year":"2006","unstructured":"Batista PR, Wilter A, Durham EH, Pascutti PG: Molecular dynamics simulations applied to the study of subtypes of HIV-1 protease common to Brazil, Africa, and Asia. Cell Biochem Biophys. 2006, 44 (3): 395-404.","journal-title":"Cell Biochem Biophys"},{"issue":"8","key":"7217_CR25","doi-asserted-by":"publisher","first-page":"1768","DOI":"10.1021\/jm061158i","volume":"50","author":"H Ode","year":"2007","unstructured":"Ode H, Matsuyama S, Hata M, Hoshino T, Kakizawa J, Sugiura W: Mechanism of drug resistance due to N88S in CRF01_AE HIV-1 protease, analyzed by molecular dynamics simulations. J Med Chem. 2007, 50 (8): 1768-1777.","journal-title":"J Med Chem"},{"issue":"24","key":"7217_CR26","doi-asserted-by":"publisher","first-page":"3979","DOI":"10.1021\/jm9704098","volume":"40","author":"SW Kaldor","year":"1997","unstructured":"Kaldor SW, Kalish VJ, Davies JF, Shetty BV, Fritz JE, Appelt K, et al: Viracept (Nelfinavir mesylate, AG1343): a potent, orally bioavailable inhibitor of HIV-1 protease. J Med Chem. 1997, 40 (24): 3979-3985.","journal-title":"J Med Chem"},{"issue":"1","key":"7217_CR27","doi-asserted-by":"publisher","first-page":"235","DOI":"10.1093\/nar\/28.1.235","volume":"28","author":"HM Berman","year":"2000","unstructured":"Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, et al: The Protein Data Bank. Nucleic Acids Res. 2000, 28 (1): 235-242.","journal-title":"Nucleic Acids Res"},{"key":"7217_CR28","volume-title":"Schrodinger Software Suite","author":"L Schrodinger","year":"2011","unstructured":"Schrodinger L: Schrodinger Software Suite. 2011, New York: Schr\u00f6dinger, LLC"},{"issue":"3","key":"7217_CR29","doi-asserted-by":"publisher","first-page":"221","DOI":"10.1007\/s10822-013-9644-8","volume":"27","author":"GM Sastry","year":"2013","unstructured":"Sastry GM, Adzhigirey M, Day T, Annabhimoju R, Sherman W: Protein and ligand preparation: parameters, protocols, and influence on virtual screening enrichments. J Comput Aided Mol Des. 2013, 27 (3): 221-234.","journal-title":"J Comput Aided Mol Des"},{"issue":"4934","key":"7217_CR30","doi-asserted-by":"publisher","first-page":"1149","DOI":"10.1126\/science.2686029","volume":"246","author":"M Miller","year":"1989","unstructured":"Miller M, Schneider J, Sathyanarayana BK, Toth MV, Marshall GR, Clawson L, et al: Structure of complex of synthetic HIV-1 protease with a substrate-based inhibitor at 2.3 A resolution. Science. 1989, 246 (4934): 1149-1152.","journal-title":"Science"},{"issue":"4","key":"7217_CR31","doi-asserted-by":"publisher","first-page":"915","DOI":"10.1073\/pnas.0508452103","volume":"103","author":"V Hornak","year":"2006","unstructured":"Hornak V, Okur A, Rizzo RC, Simmerling C: HIV-1 protease flaps spontaneously open and reclose in molecular dynamics simulations. Proc Natl Acad Sci USA. 2006, 103 (4): 915-920.","journal-title":"Proc Natl Acad Sci USA"},{"issue":"9","key":"7217_CR32","doi-asserted-by":"publisher","first-page":"1047","DOI":"10.1016\/S0969-2126(99)80172-5","volume":"7","author":"R Ishima","year":"1999","unstructured":"Ishima R, Freedberg DI, Wang YX, Louis JM, Torchia DA: Flap opening and dimer-interface flexibility in the free and inhibitor-bound HIV protease, and their implications for function. Structure. 1999, 7 (9): 1047-1055.","journal-title":"Structure"},{"issue":"4893","key":"7217_CR33","doi-asserted-by":"publisher","first-page":"928","DOI":"10.1126\/science.2537531","volume":"243","author":"IT Weber","year":"1989","unstructured":"Weber IT, Miller M, Jaskolski M, Leis J, Skalka AM, Wlodawer A: Molecular modeling of the HIV-1 protease and its substrate binding site. Science. 1989, 243 (4893): 928-931.","journal-title":"Science"},{"issue":"28","key":"7217_CR34","doi-asserted-by":"publisher","first-page":"6474","DOI":"10.1021\/jp003919d","volume":"105","author":"GA Kaminski","year":"2001","unstructured":"Kaminski GA, Friesner RA, Tirado-Rives J, Jorgensen WL: Evaluation and Reparametrization of the OPLS-AA Force Field for Proteins via Comparison with Accurate Quantum Chemical Calculations on Peptides\u2020. J Phys Chem B. 2001, 105 (28): 6474-6487.","journal-title":"J Phys Chem B"},{"issue":"45","key":"7217_CR35","doi-asserted-by":"publisher","first-page":"11225","DOI":"10.1021\/ja9621760","volume":"118","author":"WL Jorgensen","year":"1996","unstructured":"Jorgensen WL, Maxwell DS, Tirado-Rives J: Development and Testing of the OPLS All-Atom Force Field on Conformational Energetics and Properties of Organic Liquids. J Am Chem Soc. 1996, 118 (45): 11225-11236.","journal-title":"J Am Chem Soc"},{"issue":"3","key":"7217_CR36","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1007\/s00894-014-2099-6","volume":"20","author":"S Goyal","year":"2014","unstructured":"Goyal S, Grover S, Dhanjal JK, Goyal M, Tyagi C, Chacko S, Grover A: Mechanistic insights into mode of actions of novel oligopeptidase B inhibitors for combating leishmaniasis. J Mol Model. 2014, 20 (3): 1-9.","journal-title":"J Mol Model"},{"key":"7217_CR37","volume-title":"Biomed Research International","author":"M Goyal","year":"2014","unstructured":"Goyal M, Dhanjal JK, Goyal S, Tyagi C, Hamid R, Grover A: Development of dual inhibitors against Alzheimer's disease using fragment-based QSAR and molecular docking. Biomed Research International. 2014, Article ID 979606"},{"issue":"Suppl 8","key":"7217_CR38","doi-asserted-by":"publisher","first-page":"S10.","DOI":"10.1186\/1471-2164-14-S8-S10","volume":"14","author":"C Tyagi","year":"2013","unstructured":"Tyagi C, Grover S, Dhanjal JK, Goyal S, Goyal M, Grover A: Mechanistic insights into mode of action of novel natural cathepsin L inhibitors. BMC Genomics. 2013, 14 (Suppl 8): S10.-","journal-title":"BMC Genomics"},{"issue":"3","key":"7217_CR39","doi-asserted-by":"publisher","first-page":"1054","DOI":"10.1016\/j.bbrc.2013.12.088","volume":"443","author":"JK Dhanjal","year":"2014","unstructured":"Dhanjal JK, Goyal S, Sharma S, Hamid R, Grover A: Mechanistic insights into mode of action of potent natural antagonists of BACE-1 for checking Alzheimer's plaque pathology. Biochem Biophys Res Commun. 2014, 443 (3): 1054-1059.","journal-title":"Biochem Biophys Res Commun"},{"issue":"7","key":"7217_CR40","doi-asserted-by":"publisher","first-page":"1739","DOI":"10.1021\/jm0306430","volume":"47","author":"RA Friesner","year":"2004","unstructured":"Friesner RA, Banks JL, Murphy RB, Halgren TA, Klicic JJ, Mainz DT, et al: Glide: a new approach for rapid, accurate docking and scoring. 1. Method and assessment of docking accuracy. J Med Chem. 2004, 47 (7): 1739-1749.","journal-title":"J Med Chem"},{"issue":"7","key":"7217_CR41","doi-asserted-by":"publisher","first-page":"1750","DOI":"10.1021\/jm030644s","volume":"47","author":"TA Halgren","year":"2004","unstructured":"Halgren TA, Murphy RB, Friesner RA, Beard HS, Frye LL, Pollard WT, Banks JL: Glide: a new approach for rapid, accurate docking and scoring. 2. Enrichment factors in database screening. J Med Chem. 2004, 47 (7): 1750-1759.","journal-title":"J Med Chem"},{"issue":"16","key":"7217_CR42","doi-asserted-by":"publisher","first-page":"4805","DOI":"10.1021\/jm060522a","volume":"49","author":"PD Lyne","year":"2006","unstructured":"Lyne PD, Lamb ML, Saeh JC: Accurate prediction of the relative potencies of members of a series of kinase inhibitors using molecular docking and MM-GBSA scoring. J Med Chem. 2006, 49 (16): 4805-4808.","journal-title":"J Med Chem"},{"issue":"2","key":"7217_CR43","doi-asserted-by":"publisher","first-page":"127","DOI":"10.1093\/protein\/8.2.127","volume":"8","author":"AC Wallace","year":"1995","unstructured":"Wallace AC, Laskowski RA, Thornton JM: LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Engineering. 1995, 8 (2): 127-134.","journal-title":"Protein Engineering"},{"issue":"3-4","key":"7217_CR44","doi-asserted-by":"publisher","first-page":"213","DOI":"10.1007\/s002510050595","volume":"50","author":"H Rammensee","year":"1999","unstructured":"Rammensee H, Bachmann J, Emmerich NP, Bachor OA, Stevanovic S: SYFPEITHI: database for MHC ligands and peptide motifs. Immunogenetics. 1999, 50 (3-4): 213-219.","journal-title":"Immunogenetics"},{"issue":"Web Server","key":"7217_CR45","doi-asserted-by":"publisher","first-page":"W116","DOI":"10.1093\/nar\/gkl282","volume":"34","author":"J Dundas","year":"2006","unstructured":"Dundas J, Ouyang Z, Tseng J, Binkowski A, Turpaz Y, Liang J: CASTp: computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues. Nucleic Acids Res. 2006, 34 (Web Server): W116-W118.","journal-title":"Nucleic Acids Res"},{"issue":"9","key":"7217_CR46","doi-asserted-by":"publisher","first-page":"1884","DOI":"10.1002\/pro.5560070905","volume":"7","author":"J Liang","year":"1998","unstructured":"Liang J, Edelsbrunner H, Woodward C: Anatomy of protein pockets and cavities: measurement of binding site geometry and implications for ligand design. Protein Science. 1998, 7 (9): 1884-1897.","journal-title":"Protein Science"},{"issue":"6","key":"7217_CR47","doi-asserted-by":"publisher","first-page":"465","DOI":"10.1016\/j.jmgm.2005.08.008","volume":"24","author":"G Toth","year":"2006","unstructured":"Toth G, Borics A: Flap opening mechanism of HIV-1 protease. J Mol Graphics Modell. 2006, 24 (6): 465-474.","journal-title":"J Mol Graphics Modell"},{"issue":"4","key":"7217_CR48","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1177\/135965350501000409","volume":"10","author":"M John","year":"2005","unstructured":"John M, Moore CB, James IR, Mallal SA: Interactive selective pressures of HLA-restricted immune responses and antiretroviral drugs on HIV-1. Antiviral Therapy. 2005, 10 (4): 551-555.","journal-title":"Antiviral Therapy"}],"container-title":["BMC Bioinformatics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1186\/1471-2105-16-S19-S10.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,5,29]],"date-time":"2022-05-29T15:14:42Z","timestamp":1653837282000},"score":1,"resource":{"primary":{"URL":"https:\/\/bmcbioinformatics.biomedcentral.com\/articles\/10.1186\/1471-2105-16-S19-S10"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2015,12]]},"references-count":48,"journal-issue":{"issue":"S19","published-print":{"date-parts":[[2015,12]]}},"alternative-id":["7217"],"URL":"https:\/\/doi.org\/10.1186\/1471-2105-16-s19-s10","relation":{},"ISSN":["1471-2105"],"issn-type":[{"value":"1471-2105","type":"electronic"}],"subject":[],"published":{"date-parts":[[2015,12]]},"assertion":[{"value":"16 December 2015","order":1,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}}],"article-number":"S10"}}